|
Name |
Accession |
Description |
Interval |
E-value |
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
45-685 |
0e+00 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 1173.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 45 QRYRELHRHSVEEPGEFWGNIAKEFYWKTPCPGPFlqynfDVTKGKIFTEWMKGATTNICYNVLDRNVHekKLGDKVAFY 124
Cdd:cd05966 1 EQYKELYKQSIEDPEEFWGEIAKELDWFKPWDKVL-----DWSKGPPFIKWFEGGKLNISYNCLDRHLK--ERGDKVAII 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 125 WEGNEPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERIL 204
Cdd:cd05966 74 WEGDEPDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRIN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 205 DSSCSLLITTDAFYRGEKLVNLKELADESLEKCrekgFPVRCCIVVKHVGRAelgmndspsqsppvkrqcpdvqISWNEG 284
Cdd:cd05966 154 DAQCKLVITADGGYRGGKVIPLKEIVDEALEKC----PSVEKVLVVKRTGGE----------------------VPMTEG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 285 VDLWWHELMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYVFDFHPEDVFWCTADIGWITG 364
Cdd:cd05966 208 RDLWWHDLMAKQSPECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPDDIYWCTADIGWITG 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 365 HSYVTYGPLANGATSVLFEGIPTYPDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVTKHSRASLQVLGTVGEPINP 444
Cdd:cd05966 288 HSYIVYGPLANGATTVMFEGTPTYPDPGRYWDIVEKHKVTIFYTAPTAIRALMKFGDEWVKKHDLSSLRVLGSVGEPINP 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 445 EAWLWYHRVVGSQHCPIVDTFWQTETGGHMLTPLPGATPMKPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPG 524
Cdd:cd05966 368 EAWMWYYEVIGKERCPIVDTWWQTETGGIMITPLPGATPLKPGSATRPFFGIEPAILDEEGNEVEGEVEGYLVIKRPWPG 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 525 IMRTIYGNHTRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPH 604
Cdd:cd05966 448 MARTIYGDHERYEDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPH 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 605 PVKGECLYCFVTLCDGHTFSSTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQNDHDLGDTSTVA 684
Cdd:cd05966 528 DIKGEAIYAFVTLKDGEEPSDELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKIAAGEEELGDTSTLA 607
|
.
gi 625195332 685 D 685
Cdd:cd05966 608 D 608
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
31-692 |
0e+00 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 1105.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 31 PPPEVRRSAHVSsLQRYRELHRHSVEEPGEFWGNIAKEFYWKTPcpgpflqYNFDVTKGKIFTEWMKGATTNICYNVLDR 110
Cdd:PRK00174 4 PPAEFAANALID-MEQYKALYQESVEDPEGFWAEQAKRLDWFKP-------FDTVLDWNAPFIKWFEDGELNVSYNCLDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 111 NVHEKklGDKVAFYWEGNEPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIV 190
Cdd:PRK00174 76 HLKTR--GDKVAIIWEGDDPGDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 191 FAGFSAESLCERILDSSCSLLITTDAFYRGEKLVNLKELADESLEKCRekgfPVRCCIVVKHVGRAelgmndspsqsppv 270
Cdd:PRK00174 154 FGGFSAEALADRIIDAGAKLVITADEGVRGGKPIPLKANVDEALANCP----SVEKVIVVRRTGGD-------------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 271 krqcpdvqISWNEGVDLWWHELMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYVFDFHPE 350
Cdd:PRK00174 216 --------VDWVEGRDLWWHELVAGASDECEPEPMDAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTMKYVFDYKDG 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 351 DVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVTKHSRA 430
Cdd:PRK00174 288 DVYWCTADVGWVTGHSYIVYGPLANGATTLMFEGVPNYPDPGRFWEVIDKHKVTIFYTAPTAIRALMKEGDEHPKKYDLS 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 431 SLQVLGTVGEPINPEAWLWYHRVVGSQHCPIVDTFWQTETGGHMLTPLPGATPMKPGSASFPFFGVAPAILNESGEELEG 510
Cdd:PRK00174 368 SLRLLGSVGEPINPEAWEWYYKVVGGERCPIVDTWWQTETGGIMITPLPGATPLKPGSATRPLPGIQPAVVDEEGNPLEG 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 511 EAEGYLVFKQPWPGIMRTIYGNHTRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVE 590
Cdd:PRK00174 448 GEGGNLVIKDPWPGMMRTIYGDHERFVKTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVA 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 591 HEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSSTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKI 670
Cdd:PRK00174 528 HPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRKI 607
|
650 660
....*....|....*....|..
gi 625195332 671 AQNDHDLGDTSTVADPSVINHL 692
Cdd:PRK00174 608 AEGEEILGDTSTLADPSVVEKL 629
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
41-692 |
0e+00 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 1031.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 41 VSSLQRYRELHRHSVEEPGEFWGNIAKE-FYWKTPcPGPFLQYNFDVtkgkiFTEWMKGATTNICYNVLDRnvHEKKLGD 119
Cdd:TIGR02188 1 IANLEQYKELYEESIEDPDKFWAKLARElLDWFKP-FTKVLDWSFPP-----FYKWFVGGELNVSYNCVDR--HLEARPD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 120 KVAFYWEGNEPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESL 199
Cdd:TIGR02188 73 KVAIIWEGDEPGEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 200 CERILDSSCSLLITTDAFYRGEKLVNLKELADESLEKCREKgfpVRCCIVVKHVGraelgmndspsqsppvkrqcpDVQI 279
Cdd:TIGR02188 153 ADRINDAGAKLVITADEGLRGGKVIPLKAIVDEALEKCPVS---VEHVLVVRRTG---------------------NPVV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 280 SWNEGVDLWWHELMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYVFDFHPEDVFWCTADI 359
Cdd:TIGR02188 209 PWVEGRDVWWHDLMAKASAYCEPEPMDSEDPLFILYTSGSTGKPKGVLHTTGGYLLYAAMTMKYVFDIKDGDIFWCTADV 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 360 GWITGHSYVTYGPLANGATSVLFEGIPTYPDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVTKHSRASLQVLGTVG 439
Cdd:TIGR02188 289 GWITGHSYIVYGPLANGATTVMFEGVPTYPDPGRFWEIIEKHKVTIFYTAPTAIRALMRLGDEWVKKHDLSSLRLLGSVG 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 440 EPINPEAWLWYHRVVGSQHCPIVDTFWQTETGGHMLTPLPGATPMKPGSASFPFFGVAPAILNES-GEELEGEAEGYLVF 518
Cdd:TIGR02188 369 EPINPEAWMWYYKVVGKERCPIVDTWWQTETGGIMITPLPGATPTKPGSATLPFFGIEPAVVDEEgNPVEGPGEGGYLVI 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 519 KQPWPGIMRTIYGNHTRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAA 598
Cdd:TIGR02188 449 KQPWPGMLRTIYGDHERFVDTYFSPFPGYYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAA 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 599 VVGHPHPVKGECLYCFVTLCDGHTFSSTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQNDHD-L 677
Cdd:TIGR02188 529 VVGIPDDIKGQAIYAFVTLKDGYEPDDELRKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRRLLRKIAAGEAEiL 608
|
650
....*....|....*
gi 625195332 678 GDTSTVADPSVINHL 692
Cdd:TIGR02188 609 GDTSTLEDPSVVEEL 623
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
31-692 |
0e+00 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 891.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 31 PPPEVRRSAHVSSLQRYRELHRHSVEEPGEFWGNIAKEFYWKTP-CPGPFLQYNFDVTKGKIFTEWMKGATTNICYNVLD 109
Cdd:PLN02654 16 PSKDFSAQALVSSPQQYMEMYKRSVDDPAGFWSDIASQFYWKQKwEGDEVCSENLDVRKGPISIEWFKGGKTNICYNCLD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 110 RNVhEKKLGDKVAFYWEGNEPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSI 189
Cdd:PLN02654 96 RNV-EAGNGDKIAIYWEGNEPGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 190 VFAGFSAESLCERILDSSCSLLITTDAFYRGEKLVNLKELADESLEKCREKGFPVRCCIVVKHvgraELGMNDSPSQspp 269
Cdd:PLN02654 175 VFAGFSAESLAQRIVDCKPKVVITCNAVKRGPKTINLKDIVDAALDESAKNGVSVGICLTYEN----QLAMKREDTK--- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 270 vkrqcpdvqisWNEGVDLWWHELMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYVFDFHP 349
Cdd:PLN02654 248 -----------WQEGRDVWWQDVVPNYPTKCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 350 EDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVTKHSR 429
Cdd:PLN02654 317 TDVYWCTADCGWITGHSYVTYGPMLNGATVLVFEGAPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 430 ASLQVLGTVGEPINPEAWLWYHRVVGSQHCPIVDTFWQTETGGHMLTPLPGATPMKPGSASFPFFGVAPAILNESGEELE 509
Cdd:PLN02654 397 KSLRVLGSVGEPINPSAWRWFFNVVGDSRCPISDTWWQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGKEIE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 510 GEAEGYLVFKQPWPGIMRTIYGNHTRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALV 589
Cdd:PLN02654 477 GECSGYLCVKKSWPGAFRTLYGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALV 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 590 EHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSSTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:PLN02654 557 SHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRK 636
|
650 660
....*....|....*....|....
gi 625195332 670 IAQNDHD-LGDTSTVADPSVINHL 692
Cdd:PLN02654 637 IASRQLDeLGDTSTLADPGVVDQL 660
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
94-692 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 872.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 94 EWMKGATTNICYNVLDRNVHEKklGDKVAFYWEGnEPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILEL 173
Cdd:COG0365 1 RWFVGGRLNIAYNCLDRHAEGR--GDKVALIWEG-EDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 174 VVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITTDAFYRGEKLVNLKELADESLEKCREkgfpVRCCIVVKHV 253
Cdd:COG0365 78 VIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALEELPS----LEHVIVVGRT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 254 GrAELGMNDspsqsppvkrqcpdvqiswnegvDLWWHELMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGGY 333
Cdd:COG0365 154 G-ADVPMEG-----------------------DLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGY 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 334 MLYVATTFKYVFDFHPEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDESRLWSIVDKYKVTKFYTAPTAI 413
Cdd:COG0365 210 LVHAATTAKYVLDLKPGDVFWCTADIGWATGHSYIVYGPLLNGATVVLYEGRPDFPDPGRLWELIEKYGVTVFFTAPTAI 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 414 RMLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGsqhCPIVDTFWQTETGGHMLTPLPGaTPMKPGSASFPF 493
Cdd:COG0365 290 RALMKAGDEPLKKYDLSSLRLLGSAGEPLNPEVWEWWYEAVG---VPIVDGWGQTETGGIFISNLPG-LPVKPGSMGKPV 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 494 FGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTIYGNHTRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLN 573
Cdd:COG0365 366 PGYDVAVVDEDGNPVPPGEEGELVIKGPWPGMFRGYWNDPERYRETYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVIN 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 574 VSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSSTLTEELKKQIREKIGPIATPDYIQNAPG 653
Cdd:COG0365 446 VSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSDELAKELQAHVREELGPYAYPREIEFVDE 525
|
570 580 590
....*....|....*....|....*....|....*....
gi 625195332 654 LPKTRSGKIMRRVLRKIAQNDhDLGDTSTVADPSVINHL 692
Cdd:COG0365 526 LPKTRSGKIMRRLLRKIAEGR-PLGDTSTLEDPEALDEI 563
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
47-663 |
0e+00 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 708.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 47 YRELHRHSVEEPGEFWGNIAKEFYWKTPCPGpflQYNFDVTKGKIFTEWMKGATTNICYNVLDRNVHEKklGDKVAFYWE 126
Cdd:cd17634 1 YETKYRQSINDPDTFWGEAGKILDWITPYQK---VKNTSFAPGAPSIKWFEDATLNLAANALDRHLREN--GDRTAIIYE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 127 GNEPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDS 206
Cdd:cd17634 76 GDDTSQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 207 SCSLLITTDAFYRGEKLVNLKELADESLEKcreKGFPVRCCIVVKHVGraelgmndspsqsppvkrqcpdVQISWNEGVD 286
Cdd:cd17634 156 SSRLLITADGGVRAGRSVPLKKNVDDALNP---NVTSVEHVIVLKRTG----------------------SDIDWQEGRD 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 287 LWWHELMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYVFDFHPEDVFWCTADIGWITGHS 366
Cdd:cd17634 211 LWWRDLIAKASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHS 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 367 YVTYGPLANGATSVLFEGIPTYPDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVTKHSRASLQVLGTVGEPINPEA 446
Cdd:cd17634 291 YLLYGPLACGATTLLYEGVPNWPTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIEGTDRSSLRILGSVGEPINPEA 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 447 WLWYHRVVGSQHCPIVDTFWQTETGGHMLTPLPGATPMKPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIM 526
Cdd:cd17634 371 YEWYWKKIGKEKCPVVDTWWQTETGGFMITPLPGAIELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPWPGQT 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 527 RTIYGNHTRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPV 606
Cdd:cd17634 451 RTLFGDHERFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAI 530
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 625195332 607 KGECLYCFVTLCDGHTFSSTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIM 663
Cdd:cd17634 531 KGQAPYAYVVLNHGVEPSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
47-692 |
0e+00 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 598.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 47 YRELHRHSVEEPGEFWGNIAKEFYWKTPcpgpfLQYNFDVTKGKiFTEWMKGATTNICYNVLDRNVhEKKLGDKVAFYWE 126
Cdd:cd05967 1 YEEVYARSIAEPEAFWAEQARLIDWFKP-----PEKILDNSNPP-FTRWFVGGRLNTCYNALDRHV-EAGRGDQIALIYD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 127 GNEPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDS 206
Cdd:cd05967 74 SPVTGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 207 SCSLLITTDAFYRGEKLVNLKELADESLEKCREKgfPVRCCIVvkhvgraelgmndspsQSPPVKRQCPDVqiswneGVD 286
Cdd:cd05967 154 KPKLIVTASCGIEPGKVVPYKPLLDKALELSGHK--PHHVLVL----------------NRPQVPADLTKP------GRD 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 287 LWWHELMQEAGdEFEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYVFDFHPEDVFWCTADIGWITGHS 366
Cdd:cd05967 210 LDWSELLAKAE-PVDCVPVAATDPLYILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVWWAASDVGWVVGHS 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 367 YVTYGPLANGATSVLFEGIPT-YPDESRLWSIVDKYKVTKFYTAPTAIRMLMKF--GDEPVTKHSRASLQVLGTVGEPIN 443
Cdd:cd05967 289 YIVYGPLLHGATTVLYEGKPVgTPDPGAFWRVIEKYQVNALFTAPTAIRAIRKEdpDGKYIKKYDLSSLRTLFLAGERLD 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 444 PEAWLWYHRVVGSqhcPIVDTFWQTETGGHMLTPLPG--ATPMKPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQP 521
Cdd:cd05967 369 PPTLEWAENTLGV---PVIDHWWQTETGWPITANPVGlePLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKLP 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 522 W-PGIMRTIYGNHTRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVV 600
Cdd:cd05967 446 LpPGCLLTLWKNDERFKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVV 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 601 GHPHPVKGECLYCFVTLCDGHTFSS-TLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQNDhDLGD 679
Cdd:cd05967 526 GVRDELKGQVPLGLVVLKEGVKITAeELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIADGE-DYTI 604
|
650
....*....|...
gi 625195332 680 TSTVADPSVINHL 692
Cdd:cd05967 605 PSTIEDPSVLDEI 617
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
45-689 |
0e+00 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 564.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 45 QRYRELHRHSVEEPGEFWGNIAKEFYWKTPcPGPFLQYNfdvtkGKIFTEWMKGATTNICYNVLDRnvHEKKLGDKVAFY 124
Cdd:PRK10524 2 MSYSEFYQRSIDDPEAFWAEQARRIDWQTP-FTQVLDYS-----NPPFARWFVGGRTNLCHNAVDR--HLAKRPEQLALI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 125 WEGNEPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERIL 204
Cdd:PRK10524 74 AVSTETDEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARID 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 205 DSSCSLLITTDAFYRGEKLVNLKELADESLEKCREKgfPvrccivvKHVGRAELGMNDSPsqsppvkrqcpdvqisWNEG 284
Cdd:PRK10524 154 DAKPVLIVSADAGSRGGKVVPYKPLLDEAIALAQHK--P-------RHVLLVDRGLAPMA----------------RVAG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 285 VDLWWHELMQEAGDEFEP-EWCDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYVFDFHPEDVFWCTADIGWIT 363
Cdd:PRK10524 209 RDVDYATLRAQHLGARVPvEWLESNEPSYILYTSGTTGKPKGVQRDTGGYAVALATSMDTIFGGKAGETFFCASDIGWVV 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 364 GHSYVTYGPLANGATSVLFEGIPTYPDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVTKHSRASLQVLGTVGEPIN 443
Cdd:PRK10524 289 GHSYIVYAPLLAGMATIMYEGLPTRPDAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDPALLRKHDLSSLRALFLAGEPLD 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 444 PEAWLWYHRVVGSqhcPIVDTFWQTETGGHMLTPLPG--ATPMKPGSASFPFFGVAPAILNESGEELEGEAEG-YLVFKQ 520
Cdd:PRK10524 369 EPTASWISEALGV---PVIDNYWQTETGWPILAIARGveDRPTRLGSPGVPMYGYNVKLLNEVTGEPCGPNEKgVLVIEG 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 521 PW-PGIMRTIYGNHTRFETTYFKKF-PGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAA 598
Cdd:PRK10524 446 PLpPGCMQTVWGDDDRFVKTYWSLFgRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVA 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 599 VVGHPHPVKGECLYCFVTLCDGHTFSST-----LTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQn 673
Cdd:PRK10524 526 VVGVKDALKGQVAVAFVVPKDSDSLADRearlaLEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQAIAE- 604
|
650
....*....|....*.
gi 625195332 674 DHDLGDTSTVADPSVI 689
Cdd:PRK10524 605 GRDPGDLTTIEDPAAL 620
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
94-685 |
0e+00 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 528.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 94 EWMKGATTNICYNVLDRNVHEKkLGDKVAFYWEGNEPGEttKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILEL 173
Cdd:PRK04319 35 SWLETGKVNIAYEAIDRHADGG-RKDKVALRYLDASRKE--KYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 174 VVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITTDAFYRGEKLVNLKELadeslekcrekgfpvrccivvKHV 253
Cdd:PRK04319 112 YFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLERKPADDLPSL---------------------KHV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 254 graeLGMNDSPSQSPPVkrqcpdvqiswnegVDLWwhELMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGGY 333
Cdd:PRK04319 171 ----LLVGEDVEEGPGT--------------LDFN--ALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNAM 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 334 MLYVATTfKYVFDFHPEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGiptYPDESRLWSIVDKYKVTKFYTAPTAI 413
Cdd:PRK04319 231 LQHYQTG-KYVLDLHEDDVYWCTADPGWVTGTSYGIFAPWLNGATNVIDGG---RFSPERWYRILEDYKVTVWYTAPTAI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 414 RMLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGSqhcPIVDTFWQTETGGHMLTPLPgATPMKPGSASFPF 493
Cdd:PRK04319 307 RMLMGAGDDLVKKYDLSSLRHILSVGEPLNPEVVRWGMKVFGL---PIHDNWWMTETGGIMIANYP-AMDIKPGSMGKPL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 494 FGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTIYGNHTRFETtYFKkfPGYYVTGDGCRRDQDGYYWITGRIDDMLN 573
Cdd:PRK04319 383 PGIEAAIVDDQGNELPPNRMGNLAIKKGWPSMMRGIWNNPEKYES-YFA--GDWYVSGDSAYMDEDGYFWFQGRVDDVIK 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 574 VSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSSTLTEELKKQIREKIGPIATPDYIQNAPG 653
Cdd:PRK04319 460 TSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEELKEEIRGFVKKGLGAHAAPREIEFKDK 539
|
570 580 590
....*....|....*....|....*....|..
gi 625195332 654 LPKTRSGKIMRRVLrKIAQNDHDLGDTSTVAD 685
Cdd:PRK04319 540 LPKTRSGKIMRRVL-KAWELGLPEGDLSTMED 570
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
44-686 |
1.48e-178 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 522.44 E-value: 1.48e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 44 LQRYRELHRHSVEEPGEFWGNIAKEF-YWKTPCPGPFLqynfDVTKGKIFTEWMKGATTNICYNVLDRnvHEKKLGDKVA 122
Cdd:cd05968 6 IPDLEAFLERSAEDNAWFWGEFVKDVgIEWYEPPYQTL----DLSGGKPWAAWFVGGRMNIVEQLLDK--WLADTRTRPA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 123 FYWEGnEPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCER 202
Cdd:cd05968 80 LRWEG-EDGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 203 ILDSSCSLLITTDAFYRGEKLVNLKELADESLEKCrekgFPVRCCIVVKHVGRAELgmndspsqsppvkrqcpdvqisWN 282
Cdd:cd05968 159 LQDAEAKALITADGFTRRGREVNLKEEADKACAQC----PTVEKVVVVRHLGNDFT----------------------PA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 283 EGVDLWWHELMQEAGDEFEPewCDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYVFDFHPED-VFWCTaDIGW 361
Cdd:cd05968 213 KGRDLSYDEEKETAGDGAER--TESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDlLTWFT-DLGW 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 362 ITGhSYVTYGPLANGATSVLFEGIPTYPDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVTKHSRASLQVLGTVGEP 441
Cdd:cd05968 290 MMG-PWLIFGGLILGATMVLYDGAPDHPKADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSLRVLGSTGEP 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 442 INPEAWLWYHRVVGSQHCPIVDTFWQTETGGHMLTPLPgATPMKPGSASFPFFGVAPAILNESGEELEGEAEGyLVFKQP 521
Cdd:cd05968 369 WNPEPWNWLFETVGKGRNPIINYSGGTEISGGILGNVL-IKPIKPSSFNGPVPGMKADVLDESGKPARPEVGE-LVLLAP 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 522 WPGIMRTIYGNHTRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVG 601
Cdd:cd05968 447 WPGMTRGFWRDEDRYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIG 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 602 HPHPVKGECLYCFVTLCDGHTFSSTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKiAQNDHDLGDTS 681
Cdd:cd05968 527 VPHPVKGEAIVCFVVLKPGVTPTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRA-AYLGKELGDLS 605
|
....*
gi 625195332 682 TVADP 686
Cdd:cd05968 606 SLENP 610
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
137-671 |
2.21e-135 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 405.73 E-value: 2.21e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 137 TYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITTDA 216
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 217 FYRgeklvnlkeladeslekcrekgfpvrccivvkhvgraelgmndspsqsppvKRqcpdvqiswnegvdlwwhelmqea 296
Cdd:cd05969 82 LYE---------------------------------------------------RT------------------------ 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 297 gdefepewcDAEDPLFILYTSGSTGKPKGVVHtIGGYMLYVATTFKYVFDFHPEDVFWCTADIGWITGHSYVTYGPLANG 376
Cdd:cd05969 87 ---------DPEDPTLLHYTSGTTGTPKGVLH-VHDAMIFYYFTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNG 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 377 ATSVLFEGiptYPDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGs 456
Cdd:cd05969 157 VTNVVYEG---RFDAESWYGIIERVKVTVWYTAPTAIRMLMKEGDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFG- 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 457 qhCPIVDTFWQTETGGHMLTPLPGaTPMKPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTIYGNHTRF 536
Cdd:cd05969 233 --VPIHDTWWQTETGSIMIANYPC-MPIKPGSMGKPLPGVKAAVVDENGNELPPGTKGILALKPGWPSMFRGIWNDEERY 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 537 ETtYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVT 616
Cdd:cd05969 310 KN-SFID--GWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFIS 386
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 625195332 617 LCDGHTFSSTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 671
Cdd:cd05969 387 LKEGFEPSDELKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLKAKE 441
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
108-575 |
6.06e-109 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 336.59 E-value: 6.06e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 108 LDRNVheKKLGDKVAFywegnEPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALH 187
Cdd:pfam00501 1 LERQA--ARTPDKTAL-----EVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 188 SIVFAGFSAESLCERILDSSCSLLITTDAFYrgeklvnlkelaDESLEKCREKGFPVRCCIVVKHVGRAELGMNDSPSQS 267
Cdd:pfam00501 74 VPLNPRLPAEELAYILEDSGAKVLITDDALK------------LEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 268 PPVkrqcpdvqiswnegvdlwwhelmqeagDEFEPEWCDAEDPLFILYTSGSTGKPKGVVHTIgGYMLYVATTFKYV--- 344
Cdd:pfam00501 142 ADV---------------------------PPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTH-RNLVANVLSIKRVrpr 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 345 -FDFHPEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTyPDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEP 423
Cdd:pfam00501 194 gFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFPA-LDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPK 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 424 VTKHSraSLQVLGTVGEPINPEAWLWYHRVVGsqhCPIVDTFWQTETGGHMLTPLPGATPM-KPGSASFPFFGVAPAILN 502
Cdd:pfam00501 273 RALLS--SLRLVLSGGAPLPPELARRFRELFG---GALVNGYGLTETTGVVTTPLPLDEDLrSLGSVGRPLPGTEVKIVD 347
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 625195332 503 ESGEELEGEAEG-YLVFKQpwPGIMRTIYGNHTRFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVS 575
Cdd:pfam00501 348 DETGEPVPPGEPgELCVRG--PGVMKGYLNDPELTAEAFDED--GWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
137-669 |
1.64e-106 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 330.45 E-value: 1.64e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 137 TYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLIttda 216
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIV---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 217 fyrgeklvnlkeladeslekcrekgfpvrccivvkhvgraelgmndspsqsppvkrqcpdvqiswnegvdlwwhelmqea 296
Cdd:cd05972 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 297 gdefepewCDAEDPLFILYTSGSTGKPKGVVHTIGgYMLYVATTFKYVFDFHPEDVFWCTADIGWITGHSYVTYGPLANG 376
Cdd:cd05972 78 --------TDAEDPALIYFTSGTTGLPKGVLHTHS-YPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLG 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 377 ATSVLFEGIPTypDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEpvtKHSRASLQVLGTVGEPINPEAWLWYHRVVGS 456
Cdd:cd05972 149 ATVFVYEGPRF--DAERILELLERYGVTSFCGPPTAYRMLIKQDLS---SYKFSHLRLVVSAGEPLNPEVIEWWRAATGL 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 457 qhcPIVDTFWQTETGgHMLTPLPGaTPMKPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTIYGNHTRF 536
Cdd:cd05972 224 ---PIRDGYGQTETG-LTVGNFPD-MPVKPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKLPPPGLFLGYVGDPEKT 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 537 ETTYFKkfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVT 616
Cdd:cd05972 299 EASIRG---DYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVV 375
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 625195332 617 LCDGHTFSSTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:cd05972 376 LTSGYEPSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
43-670 |
7.61e-92 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 298.80 E-value: 7.61e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 43 SLQRYRELHRHSVEEPGEFWGNIAKefYWKTPCPGPflqYNFDVTKGKIF--TEWMKGATTNICYNVLDRNVHEkklgDK 120
Cdd:cd05943 15 SLADYAALHRWSVDDPGAFWAAVWD--FSGVRGSKP---YDVVVVSGRIMpgARWFPGARLNYAENLLRHADAD----DP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 121 VAFYweGNEPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLC 200
Cdd:cd05943 86 AAIY--AAEDGERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 201 ERILDSSCSLLITTDAFYRGEKLVNLkeladesLEKCRE--KGFPVRCCIVVkhvgraelgmndspsqsppVKRQCPDVQ 278
Cdd:cd05943 164 DRFGQIEPKVLFAVDAYTYNGKRHDV-------REKVAElvKGLPSLLAVVV-------------------VPYTVAAGQ 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 279 ISWNEGVD-LWWHE-LMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYVFDFHPEDVFWCT 356
Cdd:cd05943 218 PDLSKIAKaLTLEDfLATGAAGELEFEPLPFDHPLYILYSSGTTGLPKCIVHGAGGTLLQHLKEHILHCDLRPGDRLFYY 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 357 ADIGWITGHSYVTYgpLANGATSVLFEGIPTYPDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVTKHSRASLQVLG 436
Cdd:cd05943 298 TTCGWMMWNWLVSG--LAVGATIVLYDGSPFYPDTNALWDLADEEGITVFGTSAKYLDALEKAGLKPAETHDLSSLRTIL 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 437 TVGEPINPEAWLWYHRVVGSqhcpivDTFWQTETGGhmlTPLPGA-------TPMKPGSASFPFFGVAPAILNESGEELE 509
Cdd:cd05943 376 STGSPLKPESFDYVYDHIKP------DVLLASISGG---TDIISCfvggnplLPVYRGEIQCRGLGMAVEAFDEEGKPVW 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 510 GEAEGyLVFKQPWPGIMRTIYG--NHTRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESA 587
Cdd:cd05943 447 GEKGE-LVCTKPFPSMPVGFWNdpDGSRYRAAYFAKYPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRV 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 588 LVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSSTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 667
Cdd:cd05943 526 VEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVELDDELRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKVEVAV 605
|
...
gi 625195332 668 RKI 670
Cdd:cd05943 606 KKI 608
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
309-663 |
5.02e-87 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 276.47 E-value: 5.02e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 309 DPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYvFDFHPEDVFWCTADIGWItGHSYVTYGPLANGATSVLFEGipty 388
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAAS-GGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPK---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 389 PDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPvtKHSRASLQVLGTVGEPINPEAWLWYHRVVGsqhCPIVDTFWQT 468
Cdd:cd04433 75 FDPEAALELIEREKVTILLGVPTLLARLLKAPESA--GYDLSSLRALVSGGAPLPPELLERFEEAPG---IKLVNGYGLT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 469 ETGGHMLTPLPGATPMKPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPgiMRTIYGNhtrFETTYFKKFPGYY 548
Cdd:cd04433 150 ETGGTVATGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSV--MKGYWNN---PEATAAVDEDGWY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 549 VTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSStlt 628
Cdd:cd04433 225 RTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDA--- 301
|
330 340 350
....*....|....*....|....*....|....*
gi 625195332 629 EELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIM 663
Cdd:cd04433 302 EELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
107-675 |
9.62e-84 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 272.07 E-value: 9.62e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 107 VLDRNVheKKLGDKVAFYWEGnepgetTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGAL 186
Cdd:COG0318 4 LLRRAA--ARHPDRPALVFGG------RRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 187 HSIVFAGFSAESLcERIL-DSSCSLLITtdafyrgeklvnlkeladeslekcrekgfpvrccivvkhvgraelgmndsps 265
Cdd:COG0318 76 VVPLNPRLTAEEL-AYILeDSGARALVT---------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 266 qsppvkrqcpdvqiswnegvdlwwhelmqeagdefepewcdaedpLFILYTSGSTGKPKGVVHTIGGyMLYVATTFKYVF 345
Cdd:COG0318 103 ---------------------------------------------ALILYTSGTTGRPKGVMLTHRN-LLANAAAIAAAL 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 346 DFHPEDVFWCTADIGWITGHSYVTYGPLANGATSVLfegiPTYPDESRLWSIVDKYKVTKFYTAPTAIRMLMKfgDEPVT 425
Cdd:COG0318 137 GLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVL----LPRFDPERVLELIERERVTVLFGVPTMLARLLR--HPEFA 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 426 KHSRASLQVLGTVGEPINPEAWlwyHRVVGSQHCPIVDTFWQTETGGHMLTPLPGATPMKPGSASFPFFGVAPAILNESG 505
Cdd:COG0318 211 RYDLSSLRLVVSGGAPLPPELL---ERFEERFGVRIVEGYGLTETSPVVTVNPEDPGERRPGSVGRPLPGVEVRIVDEDG 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 506 EELEGEAEGYLVFKQPWpgIMRTIYGNHTRFEttyfKKFP-GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEV 584
Cdd:COG0318 288 RELPPGEVGEIVVRGPN--VMKGYWNDPEATA----EAFRdGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEV 361
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 585 ESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSstlTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMR 664
Cdd:COG0318 362 EEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELD---AEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDR 438
|
570
....*....|.
gi 625195332 665 RVLRKIAQNDH 675
Cdd:COG0318 439 RALRERYAAGA 449
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
29-691 |
1.95e-81 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 271.67 E-value: 1.95e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 29 WSPPPEVRRSAHVSSLQR------------YRELHRHSVEEPGEFWGNIAkEFY---WKTPcPGPFLQYNfdvtkGKIFT 93
Cdd:PRK03584 6 WTPSAERIAASRMTAFIRwlaarrglsfddYAALWRWSVEDLEAFWQSVW-DFFgviGSTP-YTVVLAGR-----RMPGA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 94 EWMKGATTNICYNVLdRNvhekKLGDKVAFYWEGnEPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILEL 173
Cdd:PRK03584 79 RWFPGARLNYAENLL-RH----RRDDRPAIIFRG-EDGPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPET 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 174 VVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITTDAFYRGEKLVN----LKELADE--SLEKcrekgfpvrcC 247
Cdd:PRK03584 153 VVAMLATASLGAIWSSCSPDFGVQGVLDRFGQIEPKVLIAVDGYRYGGKAFDrrakVAELRAAlpSLEH----------V 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 248 IVVKHVGraelgmndspsqSPPVKRQCPDVQIswnegvdlwWHELMQEAGD-EFEPEWCDAEDPLFILYTSGSTGKPKGV 326
Cdd:PRK03584 223 VVVPYLG------------PAAAAAALPGALL---------WEDFLAPAEAaELEFEPVPFDHPLWILYSSGTTGLPKCI 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 327 VHTIGGYMLYVATTFKYVFDFHPED-VFWCTAdIGWITGHSYVtyGPLANGATSVLFEGIPTYPDESRLWSIVDKYKVTK 405
Cdd:PRK03584 282 VHGHGGILLEHLKELGLHCDLGPGDrFFWYTT-CGWMMWNWLV--SGLLVGATLVLYDGSPFYPDPNVLWDLAAEEGVTV 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 406 FYTAPTAIRMLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGSqhcpivDTFWQTETGG-HMLTPLPGATPM 484
Cdd:PRK03584 359 FGTSAKYLDACEKAGLVPGETHDLSALRTIGSTGSPLPPEGFDWVYEHVKA------DVWLASISGGtDICSCFVGGNPL 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 485 KP---GSASFPFFGVAPAILNESGEELEGEAEGyLVFKQPWPGiMRTIYGNH---TRFETTYFKKFPGYYVTGDGCRRDQ 558
Cdd:PRK03584 433 LPvyrGEIQCRGLGMAVEAWDEDGRPVVGEVGE-LVCTKPFPS-MPLGFWNDpdgSRYRDAYFDTFPGVWRHGDWIEITE 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 559 DGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSSTLTEELKKQIREK 638
Cdd:PRK03584 511 HGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLAEGVTLDDALRARIRTTIRTN 590
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 625195332 639 IGPIATPDYIQNAPGLPKTRSGKIM----RRVLR----KIAQNdhdlgdTSTVADPSVINH 691
Cdd:PRK03584 591 LSPRHVPDKIIAVPDIPRTLSGKKVelpvKKLLHgrpvKKAVN------RDALANPEALDW 645
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
57-669 |
4.19e-81 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 270.84 E-value: 4.19e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 57 EPGEFWGNIAKEF-YWKTpcpgpflQYNFDVTKGKIFTEWMKGATTNICYNVLDRNVHEKKLGDKVAFYWEGNEPGETTK 135
Cdd:PTZ00237 20 NPESFWDEVAKKYvHWDK-------MYDKVYSGDEIYPDWFKGGELNTCYNVLDIHVKNPLKRDQDALIYECPYLKKTIK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 136 ITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITTD 215
Cdd:PTZ00237 93 LTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLIITTN 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 216 AFYRGEKLV----NLKELADESLEKcrekgfPvrccivvKHVgrAELGMNDSPSQSPPVKRQcpDVQISWNEgvdLWWHE 291
Cdd:PTZ00237 173 YGILNDEIItftpNLKEAIELSTFK------P-------SNV--ITLFRNDITSESDLKKIE--TIPTIPNT---LSWYD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 292 LMQEAGD-------EFEPewCDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYVFDFHPEDVFWCTADIGWITG 364
Cdd:PTZ00237 233 EIKKIKEnnqspfyEYVP--VESSHPLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSF 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 365 HSYVtYGPLANGATSVLFEGIPTYPD--ESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVTKHSR---ASLQVLGTVG 439
Cdd:PTZ00237 311 HGFL-YGSLSLGNTFVMFEGGIIKNKhiEDDLWNTIEKHKVTHTLTLPKTIRYLIKTDPEATIIRSKydlSNLKEIWCGG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 440 EPINPEAWLWYHRVVGSQhCPIVdtFWQTETGghMLTPLPGATPMKPGSAS-FPFFGVAPAILNESGEELEGEAEGYLVF 518
Cdd:PTZ00237 390 EVIEESIPEYIENKLKIK-SSRG--YGQTEIG--ITYLYCYGHINIPYNATgVPSIFIKPSILSEDGKELNVNEIGEVAF 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 519 KQPWP-GIMRTIYGNHTRFETTyFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEA 597
Cdd:PTZ00237 465 KLPMPpSFATTFYKNDEKFKQL-FSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLEC 543
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 625195332 598 AVVGHPHPVKGECLYCFVTLCDGHTFSSTLTEELKKQIRE----KIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:PTZ00237 544 CSIGIYDPDCYNVPIGLLVLKQDQSNQSIDLNKLKNEINNiitqDIESLAVLRKIIIVNQLPKTKTGKIPRQIISK 619
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
136-669 |
9.69e-79 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 258.22 E-value: 9.69e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 136 ITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERiLDSSCSLLITTD 215
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHR-LRTSGARLVVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 216 AFYRgeklvnlkeladeslekcrekgfpvrccivvkhvgraelgmndspsqsppvkrqcpdvqiswnegvdlwwHELmqe 295
Cdd:cd05973 80 AANR----------------------------------------------------------------------HKL--- 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 296 agdefepewcdAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATtFKYVFDFHPEDVFWCTADIGWITGHSYVTYGPLAN 375
Cdd:cd05973 87 -----------DSDPFVMMFTSGTTGLPKGVPVPLRALAAFGAY-LRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLAL 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 376 GATSVLFEGIPTYPDesrLWSIVDKYKVTKFYTAPTAIRMLMKFGdEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVG 455
Cdd:cd05973 155 GHPTILLEGGFSVES---TWRVIERLGVTNLAGSPTAYRLLMAAG-AEVPARPKGRLRRVSSAGEPLTPEVIRWFDAALG 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 456 SqhcPIVDTFWQTETGGHMLTPLPGATPMKPGSASFPFFGVAPAILNESGeelegeaegylvfKQPWPGIMRTI------ 529
Cdd:cd05973 231 V---PIHDHYGQTELGMVLANHHALEHPVHAGSAGRAMPGWRVAVLDDDG-------------DELGPGEPGRLaidian 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 530 -----YGNHTRFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPH 604
Cdd:cd05973 295 splmwFRGYQLPDTPAIDG--GYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPD 372
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 625195332 605 PVKGECLYCFVTLCDGHTFSSTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:cd05973 373 PERTEVVKAFVVLRGGHEGTPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
131-668 |
4.54e-68 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 230.01 E-value: 4.54e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 131 GETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSL 210
Cdd:cd05971 2 GTPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 211 LITtdafyrgeklvnlkelaDESlekcrekgfpvrccivvkhvgraelgmndspsqsppvkrqcpdvqiswnegvdlwwh 290
Cdd:cd05971 82 LVT-----------------DGS--------------------------------------------------------- 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 291 elmqeagdefepewcdaEDPLFILYTSGSTGKPKGVVHT-------IGGYMLYvattfkyvFDFHP--EDVFWCTADIGW 361
Cdd:cd05971 88 -----------------DDPALIIYTSGTTGPPKGALHAhrvllghLPGVQFP--------FNLFPrdGDLYWTPADWAW 142
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 362 ItghsyvtyGPLANGATSVLFEGIP------TYPDESRLWSIVDKYKVTKFYTAPTAIRMlMKFGDEPVtKHSRASLQVL 435
Cdd:cd05971 143 I--------GGLLDVLLPSLYFGVPvlahrmTKFDPKAALDLMSRYGVTTAFLPPTALKM-MRQQGEQL-KHAQVKLRAI 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 436 GTVGEPINPEAWLWYHRVVGSqhcPIVDTFWQTEtGGHMLTPLPGATPMKPGSASFPFFGVAPAILNESGEELEGEAEGY 515
Cdd:cd05971 213 ATGGESLGEELLGWAREQFGV---EVNEFYGQTE-CNLVIGNCSALFPIKPGSMGKPIPGHRVAIVDDNGTPLPPGEVGE 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 516 LVFKQPWPGIMRTIYGNHTRFEttyfKKFPG-YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAV 594
Cdd:cd05971 289 IAVELPDPVAFLGYWNNPSATE----KKMAGdWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAV 364
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 625195332 595 AEAAVVGHPHPVKGECLYCFVTLCDGHTFSSTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:cd05971 365 LMAAVVGIPDPIRGEIVKAFVVLNPGETPSDALAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| ac_ac_CoA_syn |
TIGR01217 |
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of ... |
39-672 |
3.98e-67 |
|
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of IPP biosynthesis. Most bacteria do not use this pathway, but rather the deoxyxylulose pathway. [Central intermediary metabolism, Other]
Pssm-ID: 273507 [Multi-domain] Cd Length: 652 Bit Score: 233.23 E-value: 3.98e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 39 AHVSSLQRYRELHRHSVEEPGEFWGNIAKEFywKTPCPGPFLQYnFDVTKGkIFTEWMKGATTNICYNVLdrnvhEKKLG 118
Cdd:TIGR01217 29 HHGAAEGGYDALHRWSVDELDTFWKAVWEWF--DVRFSTPCARV-VDDRTM-PGAQWFPGARLNYAENLL-----RAAGT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 119 DKVAFYWegNEPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAES 198
Cdd:TIGR01217 100 EPALLYV--DETHEPAPVTWAELRRQVASLAAALRALGVRPGDRVSGYLPNIPQAVVAMLATASVGAIWSSCSPDFGARG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 199 LCERILDSSCSLLITTDAFYRGEKlvnlKELADESLEKCReKGFP-VRCCIVVKHVGraelgmnDSPSQSPPVkrqcpdv 277
Cdd:TIGR01217 178 VLDRFQQIEPKLLFTVDGYRYNGK----EHDRRDKVAEVR-KELPtLRAVVHIPYLG-------PRETEAPKI------- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 278 qiswnEGvDLWWHELMQEAGD-EFEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYVFDFHPEDVFWCT 356
Cdd:TIGR01217 239 -----DG-ALDLEDFTAAAQAaELVFEQLPFDHPLWILFSSGTTGLPKCIVHSAGGTLVQHLKEHGLHCDLGPGDRLFYY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 357 ADIGWITGHSYVTygPLANGATSVLFEGIPTYPDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVTKHSRASLQVLG 436
Cdd:TIGR01217 313 TTTGWMMWNWLVS--GLATGATLVLYDGSPGFPATNVLWDIAERTGATLFGTSAKYVMACRKAGVHPARTHDLSALQCVA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 437 TVGEPINPEAWLWYHRVVGSqhcpivDTFWQTETGG-HMLTPLPGATPMKP---GSASFPFFGVAPAILNESGEELEGEA 512
Cdd:TIGR01217 391 STGSPLPPDGFRWVYDEIKA------DVWLASISGGtDICSCFAGANPTLPvhiGEIQAPGLGTAVQSWDPEGKPVTGEV 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 513 EGyLVFKQPWPGiMRTIYGNH---TRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALV 589
Cdd:TIGR01217 465 GE-LVCTNPMPS-MPIRFWNDpdgSKYRDAYFDTYPGVWRHGDWITLTPRGGIVIHGRSDSTLNPQGVRMGSAEIYNAVE 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 590 EHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSSTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:TIGR01217 543 RLDEVRESLCIGQEQPDGGYRVVLFVHLAPGATLDDALLDRIKRTIRAGLSPRHVPDEIIEVPGIPHTLTGKRVEVAVKR 622
|
...
gi 625195332 670 IAQ 672
Cdd:TIGR01217 623 VLQ 625
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
102-669 |
1.40e-64 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 223.11 E-value: 1.40e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 102 NICYNVLDRNVHEKKLGDKV---AFYWEgNEPGETTKITYRELLVQVCQFSNVLRKQ-GIQKGDRVAIYMPMILELVVAM 177
Cdd:cd05928 6 NFASDVLDQWADKEKAGKRPpnpALWWV-NGKGDEVKWSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 178 LACARLGAlhsivfagfsaeslcerILDSSCSLLITTDAFYRgeklvnlkeladesLEKCREKgfpvrcCIVVKHVGRAE 257
Cdd:cd05928 85 VACIRTGL-----------------VFIPGTIQLTAKDILYR--------------LQASKAK------CIVTSDELAPE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 258 LgmnDSpsqsppVKRQCPDVQI-------SWNEGVDLwwHELMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPKGVVHTI 330
Cdd:cd05928 128 V---DS------VASECPSLKTkllvsekSRDGWLNF--KELLNEASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSH 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 331 GGYMLYVATTFKYVFDFHPEDVFWCTADIGWITGHSYVTYGPLANGATsVLFEGIPTYpDESRLWSIVDKYKVTKFYTAP 410
Cdd:cd05928 197 SSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWIQGAC-VFVHHLPRF-DPLVILKTLSSYPITTFCGAP 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 411 TAIRMLMKfgdEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGSQhcpIVDTFWQTETGghMLTPLPGATPMKPGS-- 488
Cdd:cd05928 275 TVYRMLVQ---QDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLD---IYEGYGQTETG--LICANFKGMKIKPGSmg 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 489 ASFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTIY-GNHTRFETTYFKKFpgyYVTGDGCRRDQDGYYWITGR 567
Cdd:cd05928 347 KASPPYDVQIIDDNGNVLPPGTEGDIGIRVKPIRPFGLFSGYvDNPEKTAATIRGDF---YLTGDRGIMDEDGYFWFMGR 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 568 IDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDghTFSS----TLTEELKKQIREKIGPIA 643
Cdd:cd05928 424 ADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAP--QFLShdpeQLTKELQQHVKSVTAPYK 501
|
570 580
....*....|....*....|....*.
gi 625195332 644 TPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:cd05928 502 YPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
105-668 |
7.87e-63 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 218.01 E-value: 7.87e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 105 YN---VLDRNVhEKKLGDKVAFYwegnepGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACA 181
Cdd:cd05959 3 YNaatLVDLNL-NEGRGDKTAFI------DDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 182 RLGALHSIVFAGFSAESLCERILDSSCSLLITTDAFYrgeklvnlkELADESLEKCREKgfpVRCCIVVkhvgraelgmN 261
Cdd:cd05959 76 RAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGELA---------PVLAAALTKSEHT---LVVLIVS----------G 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 262 DSPSQSPpvkrqcpdvqiswnegvDLWWHELMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGGyMLYVATTF 341
Cdd:cd05959 134 GAGPEAG-----------------ALLLAELVAAEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHAD-IYWTAELY 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 342 -KYVFDFHPEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTyPDesRLWSIVDKYKVTKFYTAPTAIRMLMKfg 420
Cdd:cd05959 196 aRNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERPT-PA--AVFKRIRRYRPTVFFGVPTLYAAMLA-- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 421 DEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGsqhCPIVDTFWQTETGGHMLTPLPGAtpMKPGSASFPFFGVAPAI 500
Cdd:cd05959 271 APNLPSRDLSSLRLCVSAGEALPAEVGERWKARFG---LDILDGIGSTEMLHIFLSNRPGR--VRYGTTGKPVPGYEVEL 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 501 LNESGEELEGEAEGYLVFKQPWPGIMrtiYGNhtRFETTYfKKFPGYYV-TGDGCRRDQDGYYWITGRIDDMLNVSGHLL 579
Cdd:cd05959 346 RDEDGGDVADGEPGELYVRGPSSATM---YWN--NRDKTR-DTFQGEWTrTGDKYVRDDDGFYTYAGRADDMLKVSGIWV 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 580 STAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSSTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRS 659
Cdd:cd05959 420 SPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTAT 499
|
....*....
gi 625195332 660 GKIMRRVLR 668
Cdd:cd05959 500 GKIQRFKLR 508
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
102-674 |
1.48e-59 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 209.66 E-value: 1.48e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 102 NICYNVLDRNVHEKKlgDKVAFYWeGNEPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACA 181
Cdd:cd05970 17 NFAYDVVDAMAKEYP--DKLALVW-CDDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 182 RLGAlhsivfagfsaeslcerILDSSCSLLITTDAFYRGEKlvnlkelADESLEKCREKGfpvrccIVVKHV--GRAELG 259
Cdd:cd05970 94 KLGA-----------------IAIPATHQLTAKDIVYRIES-------ADIKMIVAIAED------NIPEEIekAAPECP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 260 mndspsqSPPVKRQC-PDVQISWNEgvdlwWHELMQEAGDEFE-PEWCDA---EDPLFILYTSGSTGKPKGVVHTIGgYM 334
Cdd:cd05970 144 -------SKPKLVWVgDPVPEGWID-----FRKLIKNASPDFErPTANSYpcgEDILLVYFSSGTTGMPKMVEHDFT-YP 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 335 LYVATTFKYVFDFHPEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDesRLWSIVDKYKVTKFYTAPTAIR 414
Cdd:cd05970 211 LGHIVTAKYWQNVREGGLHLTVADTGWGKAVWGKIYGQWIAGAAVFVYDYDKFDPK--ALLEKLSKYGVTTFCAPPTIYR 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 415 MLMKfgdEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGSQhcpIVDTFWQTETGGHMLTpLPGATPmKPGSASFPFF 494
Cdd:cd05970 289 FLIR---EDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIK---LMEGFGQTETTLTIAT-FPWMEP-KPGSMGKPAP 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 495 GVAPAILNESGEELEGEAEGYLVF----KQPWpGIMRTIYGNHTRFETTYFKkfpGYYVTGDGCRRDQDGYYWITGRIDD 570
Cdd:cd05970 361 GYEIDLIDREGRSCEAGEEGEIVIrtskGKPV-GLFGGYYKDAEKTAEVWHD---GYYHTGDAAWMDEDGYLWFVGRTDD 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 571 MLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSSTLTEELKKQIREKIGPIATPDYIQN 650
Cdd:cd05970 437 LIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEELKKELQDHVKKVTAPYKYPRIVEF 516
|
570 580
....*....|....*....|....
gi 625195332 651 APGLPKTRSGKImRRVlrKIAQND 674
Cdd:cd05970 517 VDELPKTISGKI-RRV--EIRERD 537
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
105-668 |
5.57e-58 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 205.04 E-value: 5.57e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 105 YNVLDRNVheKKLGDKVAFYWEGnepgetTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLG 184
Cdd:PRK06187 9 GRILRHGA--RKHPDKEAVYFDG------RRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 185 A-LHSI-VFagFSAESLcERIL-DSSCSLLITTDAFyrgEKLV-NLKELADEslekcrekgfpvrccivVKHVgraeLGM 260
Cdd:PRK06187 81 AvLHPInIR--LKPEEI-AYILnDAEDRVVLVDSEF---VPLLaAILPQLPT-----------------VRTV----IVE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 261 NDSPSQSPPVKRQCpdvqiswnegvdlwWHELMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPKGVVHT---IGGYMLYV 337
Cdd:PRK06187 134 GDGPAAPLAPEVGE--------------YEELLAAASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLShrnLFLHSLAV 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 338 ATtfkyVFDFHPEDVF-----------WctadiGWitghsyvTYGPLANGATSVlfegiptYPDE---SRLWSIVDKYKV 403
Cdd:PRK06187 200 CA----WLKLSRDDVYlvivpmfhvhaW-----GL-------PYLALMAGAKQV-------IPRRfdpENLLDLIETERV 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 404 TKFYTAPTAIRMLMKFGDEPVTKHSRASLQVLGtvGEPINPEAWLWYHRVVGsqhCPIVDTFWQTETGG--HMLTPLPGA 481
Cdd:PRK06187 257 TFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYG--GAALPPALLREFKEKFG---IDLVQGYGMTETSPvvSVLPPEDQL 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 482 TPM--KPGSASFPFFGVAPAILNESGEELEGEAEGY--LVFKQPWpgIMRTIYGNHTRFETTYFKkfpGYYVTGDGCRRD 557
Cdd:PRK06187 332 PGQwtKRRSAGRPLPGVEARIVDDDGDELPPDGGEVgeIIVRGPW--LMQGYWNRPEATAETIDG---GWLHTGDVGYID 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 558 QDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSStltEELKKQIRE 637
Cdd:PRK06187 407 EDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLDA---KELRAFLRG 483
|
570 580 590
....*....|....*....|....*....|.
gi 625195332 638 KIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:PRK06187 484 RLAKFKLPKRIAFVDELPRTSVGKILKRVLR 514
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
118-664 |
8.42e-56 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 196.68 E-value: 8.42e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 118 GDKVAFYWEGNEpgettkITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAE 197
Cdd:cd17631 9 PDRTALVFGGRS------LTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 198 SLCERILDSSCSLLIttdafyrgeklvnlkeladeslekcrekgfpvrccivvkhvgraelgmndspsqsppvkrqcpdv 277
Cdd:cd17631 83 EVAYILADSGAKVLF----------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 278 qiswnegvdlwwhelmqeagdefepewcdaEDPLFILYTSGSTGKPKGVVHTIGGyMLYVATTFKYVFDFHPEDVFWCTA 357
Cdd:cd17631 98 ------------------------------DDLALLMYTSGTTGRPKGAMLTHRN-LLWNAVNALAALDLGPDDVLLVVA 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 358 DIGWITGHSYVTYGPLANGATSVLFEGiptyPDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVTKHSraSLQVLGT 437
Cdd:cd17631 147 PLFHIGGLGVFTLPTLLRGGTVVILRK----FDPETVLDLIERHRVTSFFLVPTMIQALLQHPRFATTDLS--SLRAVIY 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 438 VGEPInPEAWLwyhRVVGSQHCPIVDTFWQTETGGHMLTPLPGATPMKPGSASFPFFGVAPAILNESGEELEGEAEGYLV 517
Cdd:cd17631 221 GGAPM-PERLL---RALQARGVKFVQGYGMTETSPGVTFLSPEDHRRKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIV 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 518 FKQPwpGIMRtiyGNHTRFETT--YFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVA 595
Cdd:cd17631 297 VRGP--HVMA---GYWNRPEATaaAFRD--GWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVA 369
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 596 EAAVVGHPHPVKGECLYCFVTLCDGhtfsSTLTE-ELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMR 664
Cdd:cd17631 370 EVAVIGVPDEKWGEAVVAVVVPRPG----AELDEdELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
136-668 |
2.04e-55 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 195.76 E-value: 2.04e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 136 ITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITtd 215
Cdd:cd05919 11 VTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVT-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 216 afyrgeklvnlkeladeslekcrekgfpvrccivvkhvgraelgmndspsqsppvkrqcpdvqiswnegvdlwwhelmqe 295
Cdd:cd05919 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 296 agdefepewcDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYVFDFHPEDVFWCTADI--GWITGHSyvTYGPL 373
Cdd:cd05919 89 ----------SADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREALGLTPGDRVFSSAKMffGYGLGNS--LWFPL 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 374 ANGATSVLFegiPTYPDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPvtKHSRASLQVLGTVGEPInPEAwLWYhRV 453
Cdd:cd05919 157 AVGASAVLN---PGWPTAERVLATLARFRPTVLYGVPTFYANLLDSCAGS--PDALRSLRLCVSAGEAL-PRG-LGE-RW 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 454 VGSQHCPIVDTFWQTETGGHMLTPLPGAtpMKPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMrtiYGNh 533
Cdd:cd05919 229 MEHFGGPILDGIGATEVGHIFLSNRPGA--WRLGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVG---YWN- 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 534 tRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYC 613
Cdd:cd05919 303 -NPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTA 381
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 625195332 614 FVTLCDGHTFSSTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:cd05919 382 FVVLKSPAAPQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
105-668 |
2.10e-55 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 196.63 E-value: 2.10e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 105 YNVLDRNVheKKLGDKVAFYWEGnepgetTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLG 184
Cdd:cd05936 2 ADLLEEAA--RRFPDKTALIFMG------RKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 185 AlhsIVFagfsaeslcerildsscsllittdafyrgekLVNLKELADEslekcrekgfpvrccivVKHVgraelgMNDSP 264
Cdd:cd05936 74 A---VVV-------------------------------PLNPLYTPRE-----------------LEHI------LNDSG 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 265 SQsppvkrqcpdVQIswnegVDLWWHELMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYV 344
Cdd:cd05936 97 AK----------ALI-----VAVSFTDLLAAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWL 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 345 FDFH-PEDVFWCTADIgwitghsYVTYG-------PLANGATSVLfegIPTYPDESRLWSIvDKYKVTKFYTAPTAIRML 416
Cdd:cd05936 162 EDLLeGDDVVLAALPL-------FHVFGltvalllPLALGATIVL---IPRFRPIGVLKEI-RKHRVTIFPGVPTMYIAL 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 417 MKFGDepVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGsqhCPIVDTFWQTETG--GHmLTPLPGatPMKPGSASFPFF 494
Cdd:cd05936 231 LNAPE--FKKRDFSSLRLCISGGAPLPVEVAERFEELTG---VPIVEGYGLTETSpvVA-VNPLDG--PRKPGSIGIPLP 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 495 GVAPAILNESGEELEGEAEGYLVFKQPwpGIMRtiyGNHTRFETT--YFKKfpGYYVTGDGCRRDQDGYYWITGRIDDML 572
Cdd:cd05936 303 GTEVKIVDDDGEELPPGEVGELWVRGP--QVMK---GYWNRPEETaeAFVD--GWLRTGDIGYMDEDGYFFIVDRKKDMI 375
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 573 NVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSstlTEELKKQIREKIGPIATPDYIQNAP 652
Cdd:cd05936 376 IVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLT---EEEIIAFCREQLAGYKVPRQVEFRD 452
|
570
....*....|....*.
gi 625195332 653 GLPKTRSGKIMRRVLR 668
Cdd:cd05936 453 ELPKSAVGKILRRELR 468
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
130-669 |
5.42e-53 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 190.60 E-value: 5.42e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 130 PGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLcERILDSSCS 209
Cdd:cd05926 9 PGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEF-EFYLADLGS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 210 LLITTDAFYRGEKLVNLKELADESLEKCREKGFPVRCCIVVKHVGRAELGMNDSPSQSPpvkrqcpdvqiswnegvdlww 289
Cdd:cd05926 88 KLVLTPKGELGPASRAASKLGLAILELALDVGVLIRAPSAESLSNLLADKKNAKSEGVP--------------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 290 helmqeagdefepewcDAEDPLFILYTSGSTGKPKGV--VHT-IGGYMLYVATTFKYVFD---------FHpedvfwcta 357
Cdd:cd05926 147 ----------------LPDDLALILHTSGTTGRPKGVplTHRnLAASATNITNTYKLTPDdrtlvvmplFH--------- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 358 digwITGHSYVTYGPLANGATSVlfegIPTYPDESRLWSIVDKYKVTkFYTA-PTAIRMLMKFgDEPVTKHSRASLQVLG 436
Cdd:cd05926 202 ----VHGLVASLLSTLAAGGSVV----LPPRFSASTFWPDVRDYNAT-WYTAvPTIHQILLNR-PEPNPESPPPKLRFIR 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 437 TVGEPINPEAwlwYHRVVGSQHCPIVDTFWQTETGGHM-LTPLPgATPMKPGSASFPFfGVAPAILNESGEELEGEAEGY 515
Cdd:cd05926 272 SCSASLPPAV---LEALEATFGAPVLEAYGMTEAAHQMtSNPLP-PGPRKPGSVGKPV-GVEVRILDEDGEILPPGVVGE 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 516 LVFKQPwpGIMRTIYGNHT-RFEttYFKKFpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAV 594
Cdd:cd05926 347 ICLRGP--NVTRGYLNNPEaNAE--AAFKD-GWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAV 421
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 625195332 595 AEAAVVGHPHPVKGECLYCFVTLCDGHTFSStltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:cd05926 422 LEAVAFGVPDEKYGEEVAAAVVLREGASVTE---EELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
307-668 |
6.18e-49 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 178.06 E-value: 6.18e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 307 AEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYVFDFHPEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGip 386
Cdd:cd05958 96 SDDICILAFTSGTTGAPKATMHFHRDPLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEE-- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 387 TYPDEsrLWSIVDKYKVTKFYTAPTAIRMLMKFGDEpvTKHSRASLQVLGTVGEPINPEAWLWYHRVVGSqhcPIVDTFW 466
Cdd:cd05958 174 ATPDL--LLSAIARYKPTVLFTAPTAYRAMLAHPDA--AGPDLSSLRKCVSAGEALPAALHRAWKEATGI---PIIDGIG 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 467 QTETGGHMLTPLPGAtpMKPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpgimrTIY-GNHTRFETTYFKKfp 545
Cdd:cd05958 247 STEMFHIFISARPGD--ARPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGP------TGCrYLADKRQRTYVQG-- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 546 GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSS 625
Cdd:cd05958 317 GWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGP 396
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 625195332 626 TLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:cd05958 397 VLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
136-671 |
7.42e-48 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 174.68 E-value: 7.42e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 136 ITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERIldsscsllittd 215
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRV------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 216 afyrgeklvnlkeladeslekcrEKGFPVRCCIVvkhvgraelgmndspsqsppvkrqcpdvqiswnegvdlwwhelmqe 295
Cdd:cd05974 69 -----------------------DRGGAVYAAVD---------------------------------------------- 79
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 296 agdefepEWCDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFkYVFDFHPEDVFWCTADIGWiTGHSYVT-YGPLA 374
Cdd:cd05974 80 -------ENTHADDPMLLYFTSGTTSKPKLVEHTHRSYPVGHLSTM-YWIGLKPGDVHWNISSPGW-AKHAWSCfFAPWN 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 375 NGATSVLFegipTYP--DESRLWSIVDKYKVTKFYTAPTAIRMLMKfgdEPVTKHSRASLQVLGTvGEPINPEAwlwYHR 452
Cdd:cd05974 151 AGATVFLF----NYArfDAKRVLAALVRYGVTTLCAPPTVWRMLIQ---QDLASFDVKLREVVGA-GEPLNPEV---IEQ 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 453 VVGSQHCPIVDTFWQTETgghmlTPLPGATP---MKPGSASFPFFGVAPAILNESGEELEGEAEGyLVFKQPWP-GIMRT 528
Cdd:cd05974 220 VRRAWGLTIRDGYGQTET-----TALVGNSPgqpVKAGSMGRPLPGYRVALLDPDGAPATEGEVA-LDLGDTRPvGLMKG 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 529 IYGNHTRfetTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKG 608
Cdd:cd05974 294 YAGDPDK---TAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRL 370
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 625195332 609 ECLYCFVTLCDGHTFSSTLTEELKKQIREKIGPIATPDYIQNAPgLPKTRSGKIMRRVLRKIA 671
Cdd:cd05974 371 SVPKAFIVLRAGYEPSPETALEIFRFSRERLAPYKRIRRLEFAE-LPKTISGKIRRVELRRRE 432
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
119-669 |
1.02e-47 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 176.28 E-value: 1.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 119 DKVAFYWEGnepgetTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAES 198
Cdd:PRK08316 26 DKTALVFGD------RSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 199 LCeRILDSSCSLLITTDAfyrgeklvNLKELADESLEKCREKGFPVRCcivvkhvgraelgmndSPSQSPPvkrqcPDVQ 278
Cdd:PRK08316 100 LA-YILDHSGARAFLVDP--------ALAPTAEAALALLPVDTLILSL----------------VLGGREA-----PGGW 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 279 ISWNEgvdlwwhelMQEAGDEFEPE-WCDAEDPLFILYTSGSTGKPKGVVHT----IGGYMLYVATTfkyvfDFHPEDVF 353
Cdd:PRK08316 150 LDFAD---------WAEAGSVAEPDvELADDDLAQILYTSGTESLPKGAMLThralIAEYVSCIVAG-----DMSADDIP 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 354 WCTADIGwitgHS---YVTYGP-LANGATSVLFEGiptyPDESRLWSIVDKYKVTKFYTAPTA-IRMLmkfgdepvtKH- 427
Cdd:PRK08316 216 LHALPLY----HCaqlDVFLGPyLYVGATNVILDA----PDPELILRTIEAERITSFFAPPTVwISLL---------RHp 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 428 --SRASLQVL--GTVGEPINPEAWLWYHRvvgsQHCPIVdTFW----QTETGghmltplPGATPM-------KPGSASFP 492
Cdd:PRK08316 279 dfDTRDLSSLrkGYYGASIMPVEVLKELR----ERLPGL-RFYncygQTEIA-------PLATVLgpeehlrRPGSAGRP 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 493 FFGVAPAILNESGEELEgeaegylvfkqpwPGIMRTIYGNHTRFETTYFKKfP---------GYYVTGDGCRRDQDGYYW 563
Cdd:PRK08316 347 VLNVETRVVDDDGNDVA-------------PGEVGEIVHRSPQLMLGYWDD-PektaeafrgGWFHSGDLGVMDEEGYIT 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 564 ITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSStltEELKKQIREKIGPIA 643
Cdd:PRK08316 413 VVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTE---DELIAHCRARLAGFK 489
|
570 580
....*....|....*....|....*.
gi 625195332 644 TPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:PRK08316 490 VPKRVIFVDELPRNPSGKILKRELRE 515
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
102-669 |
1.02e-47 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 176.18 E-value: 1.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 102 NICYNVLDRNVHEKKlGDKVAFYwegnepGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACA 181
Cdd:TIGR02262 4 NAAEDLLDRNVVEGR-GGKTAFI------DDISSLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 182 RLGALHSIVFAGFSAESLCERILDSSCSLLITTDAFYrgeklvnlkELADESLEKcrekgFPVRCCIVVkhVGRAELGmn 261
Cdd:TIGR02262 77 RAGIVPVALNTLLTADDYAYMLEDSRARVVFVSGALL---------PVIKAALGK-----SPHLEHRVV--VGRPEAG-- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 262 dspsqsppvkrqcpDVQISwnegvdlwwhELMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTF 341
Cdd:TIGR02262 139 --------------EVQLA----------ELLATESEQFKPAATQADDPAFWLYSSGSTGMPKGVVHTHSNPYWTAELYA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 342 KYVFDFHPEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTyPDesRLWSIVDKYKVTKFYTAPTAIRMLMkfGD 421
Cdd:TIGR02262 195 RNTLGIREDDVCFSAAKLFFAYGLGNALTFPMSVGATTVLMGERPT-PD--AVFDRLRRHQPTIFYGVPTLYAAML--AD 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 422 EPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGSQhcpIVDTFWQTETGGHMLTPLPGAtpMKPGSASFPFFGVAPAIL 501
Cdd:TIGR02262 270 PNLPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVD---IVDGIGSTEMLHIFLSNLPGD--VRYGTSGKPVPGYRLRLV 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 502 NESGEELEGEAEGYLVFKQPWPGIMrtIYGNHTRFETTYFKkfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLST 581
Cdd:TIGR02262 345 GDGGQDVADGEPGELLISGPSSATM--YWNNRAKSRDTFQG---EWTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSP 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 582 AEVESALVEHEAVAEAAVVGHPHP---VKGEclyCFVTLCDGHTfssTLTEELKKQIREKIGPIATPDYIQNAPGLPKTR 658
Cdd:TIGR02262 420 FEIESALIQHPAVLEAAVVGVADEdglIKPK---AFVVLRPGQT---ALETELKEHVKDRLAPYKYPRWIVFVDDLPKTA 493
|
570
....*....|.
gi 625195332 659 SGKIMRRVLRK 669
Cdd:TIGR02262 494 TGKIQRFKLRE 504
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
134-668 |
1.83e-47 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 173.25 E-value: 1.83e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 134 TKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALhsivfagfsaeslcerildsscslLIT 213
Cdd:cd05934 2 RRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAV------------------------LVP 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 214 TDAFYRGEKLvnlKELADESlekcrekgfpvRCCIVVKhvgraelgmndspsqsppvkrqcpdvqiswnegvdlwwhelm 293
Cdd:cd05934 58 INTALRGDEL---AYIIDHS-----------GAQLVVV------------------------------------------ 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 294 qeagdefepewcdaeDPLFILYTSGSTGKPKGVV--HTiggYMLYVATTFKYVFDFHPEDVFWCTADIGWITGHSYVTYG 371
Cdd:cd05934 82 ---------------DPASILYTSGTTGPPKGVVitHA---NLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLA 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 372 PLANGATSVLfegIPTYpDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVTKHSRASLqvlgTVGEPINPEAWLWYH 451
Cdd:cd05934 144 ALSVGATLVL---LPRF-SASRFWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDRAHRLRA----AYGAPNPPELHEEFE 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 452 RVVGsqhCPIVDTFWQTETGGHMLTPLPGATPmkPGSASFPFFGVAPAILNESGEELEGEAEGYLVFK-QPWPGIMRTIY 530
Cdd:cd05934 216 ERFG---VRLLEGYGMTETIVGVIGPRDEPRR--PGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIRgLRGWGFFKGYY 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 531 GNhtrfETTYFKKFP-GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGE 609
Cdd:cd05934 291 NM----PEATAEAMRnGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGED 366
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 625195332 610 CLYCFVTLCDGHTFSStltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:cd05934 367 EVKAVVVLRPGETLDP---EELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
132-663 |
2.68e-46 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 171.63 E-value: 2.68e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 132 ETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLL 211
Cdd:cd05911 7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 212 ITTDAFYrgEKLvnlkeladesLEKCREKGFPVRccIVVkhvgraelgMNDSPSQSPPVKrqcpdvqiswnegvDLWWHE 291
Cdd:cd05911 87 FTDPDGL--EKV----------KEAAKELGPKDK--IIV---------LDDKPDGVLSIE--------------DLLSPT 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 292 LMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPKGVV--HTIGGYMLYVATTFKYVfDFHPEDVFWCTADIGWITG-HSYV 368
Cdd:cd05911 130 LGEEDEDLPPPLKDGKDDTAAILYSSGTTGLPKGVClsHRNLIANLSQVQTFLYG-NDGSNDVILGFLPLYHIYGlFTTL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 369 TYgpLANGATSVLFEGiptyPDESRLWSIVDKYKVTKFYTAPTAIRMLMKfgDEPVTKHSRASLQVLGTVGEPINPEAwl 448
Cdd:cd05911 209 AS--LLNGATVIIMPK----FDSELFLDLIEKYKITFLYLVPPIAAALAK--SPLLDKYDLSSLRVILSGGAPLSKEL-- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 449 wYHRV-VGSQHCPIVDTFWQTETGGhMLTPLPGaTPMKPGSASFPFFGVAPAILNESGEELEGEaegylvfKQP---W-- 522
Cdd:cd05911 279 -QELLaKRFPNATIKQGYGMTETGG-ILTVNPD-GDDKPGSVGRLLPNVEAKIVDDDGKDSLGP-------NEPgeiCvr 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 523 -PGIMRTIYGNHTRFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVG 601
Cdd:cd05911 349 gPQVMKGYYNNPEATKETFDED--GWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIG 426
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 625195332 602 HPHPVKGECLYCFVTLCDGhtfsSTLTE-ELKKQIREKIgpiatPDY------IQNAPGLPKTRSGKIM 663
Cdd:cd05911 427 IPDEVSGELPRAYVVRKPG----EKLTEkEVKDYVAKKV-----ASYkqlrggVVFVDEIPKSASGKIL 486
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
136-687 |
3.41e-41 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 159.74 E-value: 3.41e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 136 ITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLAcarlGALHSIVFA---GFSAESLCErildsscsLLI 212
Cdd:PRK07529 59 WTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWG----GEAAGIANPinpLLEPEQIAE--------LLR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 213 TTDAfyrgEKLVNLKELADESL-EKCREKgfpVRCCIVVKHVGRAELGMNDSPSQSPPVKRQCPDVQIswneGVDLWWHE 291
Cdd:PRK07529 127 AAGA----KVLVTLGPFPGTDIwQKVAEV---LAALPELRTVVEVDLARYLPGPKRLAVPLIRRKAHA----RILDFDAE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 292 LMQEAGDE-FEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGGyMLYVATTFKYVFDFHPEDVFWCTADIGWITGhSYVT- 369
Cdd:PRK07529 196 LARQPGDRlFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGN-EVANAWLGALLLGLGPGDTVFCGLPLFHVNA-LLVTg 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 370 YGPLANGAtSVLFEGIPTYPDES---RLWSIVDKYKVTKFYTAPTAIRMLMkfgDEPVTKHSRASLQVLGTVGEPINPEA 446
Cdd:PRK07529 274 LAPLARGA-HVVLATPQGYRGPGviaNFWKIVERYRINFLSGVPTVYAALL---QVPVDGHDISSLRYALCGAAPLPVEV 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 447 WLWYHRVVGsqhCPIVDTFWQTE-TGGHMLTPLPGatPMKPGSASFPFFGVAPAILNESGEELEGEAEGY-----LVFKQ 520
Cdd:PRK07529 350 FRRFEAATG---VRIVEGYGLTEaTCVSSVNPPDG--ERRIGSVGLRLPYQRVRVVILDDAGRYLRDCAVdevgvLCIAG 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 521 P--WPGIMRTIYGNHTRFEttyfkkfPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAA 598
Cdd:PRK07529 425 PnvFSGYLEAAHNKGLWLE-------DGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAA 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 599 VVGHPHPVKGECLYCFVTLCDGHTFSST-LTEELKKQIREkigPIATPDYIQNAPGLPKTRSGKI---------MRRVLR 668
Cdd:PRK07529 498 AVGRPDAHAGELPVAYVQLKPGASATEAeLLAFARDHIAE---RAAVPKHVRILDALPKTAVGKIfkpalrrdaIRRVLR 574
|
570 580
....*....|....*....|
gi 625195332 669 K-IAQNDHDLGDTSTVADPS 687
Cdd:PRK07529 575 AaLRDAGVEAEVVDVVEDGR 594
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
132-667 |
5.13e-41 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 155.76 E-value: 5.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 132 ETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGAlhsiVFAGFSAESLCERIL----DSS 207
Cdd:cd05930 9 GDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGA----AYVPLDPSYPAERLAyileDSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 208 CSLLITtdafyrgeklvnlkeladeslekcrekgfpvrccivvkhvgraelgmndspsqsppvkrqcpdvqiswnegvdl 287
Cdd:cd05930 85 AKLVLT-------------------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 288 wwhelmqeagdefepewcDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATtFKYVFDFHPEDVFWCTADIGWItGHSY 367
Cdd:cd05930 91 ------------------DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLW-MQEAYPLTPGDRVLQFTSFSFD-VSVW 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 368 VTYGPLANGATSVLfegIP--TYPDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVtkhsRASLQVLGTVGEPINPE 445
Cdd:cd05930 151 EIFGALLAGATLVV---LPeeVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELAA----LPSLRLVLVGGEALPPD 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 446 AW------LWYHRVV---GSQHCPIVDTFWQTETGGHMLTPLP-GAtpmkpgsasfPFFGVAPAILNESGeelegeaegy 515
Cdd:cd05930 224 LVrrwrelLPGARLVnlyGPTEATVDATYYRVPPDDEEDGRVPiGR----------PIPNTRVYVLDENL---------- 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 516 lvfkQPWP-GIMRTIY--------GNHTRFETTYFK-----KFPG--YYVTGDGCRRDQDG--YYwiTGRIDDMLNVSGH 577
Cdd:cd05930 284 ----RPVPpGVPGELYiggaglarGYLNRPELTAERfvpnpFGPGerMYRTGDLVRWLPDGnlEF--LGRIDDQVKIRGY 357
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 578 LLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSstlTEELKKQIREKIGPIATPDYIQNAPGLPKT 657
Cdd:cd05930 358 RIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELD---EEELRAHLAERLPDYMVPSAFVVLDALPLT 434
|
570
....*....|
gi 625195332 658 RSGKIMRRVL 667
Cdd:cd05930 435 PNGKVDRKAL 444
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
115-669 |
1.05e-40 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 156.22 E-value: 1.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 115 KKLGDKVAfYWEGNEpgettKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGF 194
Cdd:PRK07656 16 RRFGDKEA-YVFGDQ-----RLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 195 SAESLCERILDSSCSLLITTDAFyrgeklVNLKELADESLEkcrekgfpvrcciVVKHVGRAElgmndsPSQSPPVKRQC 274
Cdd:PRK07656 90 TADEAAYILARGDAKALFVLGLF------LGVDYSATTRLP-------------ALEHVVICE------TEEDDPHTEKM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 275 pdvqiswnegvdLWWHELMQEA-GDEFEPEwCDAEDPLFILYTSGSTGKPKGVVHTIGG-YMLY--VATTFKYVFD---- 346
Cdd:PRK07656 145 ------------KTFTDFLAAGdPAERAPE-VDPDDVADILFTSGTTGRPKGAMLTHRQlLSNAadWAEYLGLTEGdryl 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 347 -----FHpedVFWCTAdiGWITghsyvtygPLANGATSVLfegIPTYpDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGD 421
Cdd:PRK07656 212 aanpfFH---VFGYKA--GVNA--------PLMRGATILP---LPVF-DPDEVFRLIETERITVLPGPPTMYNSLLQHPD 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 422 EpvTKHSRASLQVLGTVGEPInPEAWLwyHRVVGSQHCPIVDT-FWQTETGGHM-LTPLPGATPMKPGSASFPFFGVAPA 499
Cdd:PRK07656 275 R--SAEDLSSLRLAVTGAASM-PVALL--ERFESELGVDIVLTgYGLSEASGVTtFNRLDDDRKTVAGTIGTAIAGVENK 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 500 ILNESGEELEGEAEGYLVFKQPwpGIMRTIYGNHTrfETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLL 579
Cdd:PRK07656 350 IVNELGEEVPVGEVGELLVRGP--NVMKGYYDDPE--ATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNV 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 580 STAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfsSTLTEE-LKKQIREKIGPIATPDYIQNAPGLPKTR 658
Cdd:PRK07656 426 YPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPG----AELTEEeLIAYCREHLAKYKVPRSIEFLDELPKNA 501
|
570
....*....|.
gi 625195332 659 SGKIMRRVLRK 669
Cdd:PRK07656 502 TGKVLKRALRE 512
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
28-669 |
1.84e-40 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 158.32 E-value: 1.84e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 28 GWSPPPEVRRSAHVSSLQRYR-----------------ELHRHSVEEPGEFWGNIAKEF--YWKTPcPGPFLQYNFDVTK 88
Cdd:PLN03052 86 AWFPSPEIAKLTNLGRLLEARgkellgskykdpissfsEFQRFSVENPEVYWSIVLDELslVFSVP-PRCILDTSDESNP 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 89 GKiftEWMKGATTNICYNVLDRNVHEKklGDKVAFYW--EGNEPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIY 166
Cdd:PLN03052 165 GG---QWLPGAVLNVAECCLTPKPSKT--DDSIAIIWrdEGSDDLPVNRMTLSELRSQVSRVANALDALGFEKGDAIAID 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 167 MPMILELVVAMLAcarlgalhsIVFAG---------FSAESLCERILDSSCSLLITTDAFYRGEKLVNLKEladeslekc 237
Cdd:PLN03052 240 MPMNVHAVIIYLA---------IILAGcvvvsiadsFAPSEIATRLKISKAKAIFTQDVIVRGGKSIPLYS--------- 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 238 rekgfpvRcciVVKhvgraelgmndspSQSP-----PVKRQCPDVQIswNEGvDLWWHELMQEA-----GDEFEPEWCDA 307
Cdd:PLN03052 302 -------R---VVE-------------AKAPkaivlPADGKSVRVKL--REG-DMSWDDFLARAnglrrPDEYKAVEQPV 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 308 EDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYVfDFHPEDVF-WCTaDIGWITGHsYVTYGPLANGATSVLFEGIP 386
Cdd:PLN03052 356 EAFTNILFSSGTTGEPKAIPWTQLTPLRAAADAWAHL-DIRKGDIVcWPT-NLGWMMGP-WLVYASLLNGATLALYNGSP 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 387 TYPDESRLwsiVDKYKVTKFYTAPTAIRMLMKFGdePVTKHSRASLQVLGTVGEPINPEAWLWYhrVVGSQHCPIVDTFW 466
Cdd:PLN03052 433 LGRGFAKF---VQDAKVTMLGTVPSIVKTWKNTN--CMAGLDWSSIRCFGSTGEASSVDDYLWL--MSRAGYKPIIEYCG 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 467 QTETGGHMLTplpgATPMKP---GSASFPFFGVAPAILNESGeelegeaegylvfkQPWP---------GIMRTIYGNHT 534
Cdd:PLN03052 506 GTELGGGFVT----GSLLQPqafAAFSTPAMGCKLFILDDSG--------------NPYPddapctgelALFPLMFGASS 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 535 RF-----ETTYFKKFPGYYVT-----GDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVE----SAlveHEAVAEAAVV 600
Cdd:PLN03052 568 TLlnadhYKVYFKGMPVFNGKilrrhGDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIErvcnAA---DESVLETAAI 644
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 625195332 601 GHPHPVKGECLYCFVTLCDGHTFSSTLTEELKK----QIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:PLN03052 645 GVPPPGGGPEQLVIAAVLKDPPGSNPDLNELKKifnsAIQKKLNPLFKVSAVVIVPSFPRTASNKVMRRVLRQ 717
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
167-668 |
4.94e-39 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 151.12 E-value: 4.94e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 167 MPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITTDAFYRGEKLVnlkELADESLEKCREKgfpvrc 246
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGGRAL---PLYSKVVEAAPAK------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 247 CIVVKHVGRaelgmndspSQSPPVKRQCPdvqiSWNE--GVDLWWHelmQEAGDEFEPEWCDAEDPLFILYTSGSTGKPK 324
Cdd:PLN03051 72 AIVLPAAGE---------PVAVPLREQDL----SWCDflGVAAAQG---SVGGNEYSPVYAPVESVTNILFSSGTTGEPK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 325 GVVHTIGGYMLYVATTFKYVfDFHPEDVFWCTADIGWITGhSYVTYGPLANGATSVLFEGIPTYPDesrLWSIVDKYKVT 404
Cdd:PLN03051 136 AIPWTHLSPLRCASDGWAHM-DIQPGDVVCWPTNLGWMMG-PWLLYSAFLNGATLALYGGAPLGRG---FGKFVQDAGVT 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 405 KFYTAPTAIRMLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGSQHcPIVDTFWQTETGGHML--TPLpgaT 482
Cdd:PLN03051 211 VLGLVPSIVKAWRHTGAFAMEGLDWSKLRVFASTGEASAVDDVLWLSSVRGYYK-PVIEYCGGTELASGYIssTLL---Q 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 483 PMKPGSASFPFFGVAPAILNESGEELEGEAEGY--LVFKQPWPGIM-RTIYGNHtrfETTYFKKFPGYYVTGDGCRRDQD 559
Cdd:PLN03051 287 PQAPGAFSTASLGTRFVLLNDNGVPYPDDQPCVgeVALAPPMLGASdRLLNADH---DKVYYKGMPMYGSKGMPLRRHGD 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 560 -------GYYWITGRIDDMLNVSGHLLSTAEVESALVE-HEAVAEAAVVGHPHPVKG-ECLYCFVTLCD-GHTFSSTLTE 629
Cdd:PLN03051 364 imkrtpgGYFCVQGRADDTMNLGGIKTSSVEIERACDRaVAGIAETAAVGVAPPDGGpELLVIFLVLGEeKKGFDQARPE 443
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 625195332 630 ELKKQ----IREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:PLN03051 444 ALQKKfqeaIQTNLNPLFKVSRVKIVPELPRNASNKLLRRVLR 486
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
136-672 |
4.18e-38 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 149.14 E-value: 4.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 136 ITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHsiVFAGFS-----AESLCERildSSCSL 210
Cdd:COG1021 51 LSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIP--VFALPAhrraeISHFAEQ---SEAVA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 211 LITTDAfYRGeklVNLKELADESLEKCREkgfpVRCCIVVkhvGRAElgmndspsqsppvkrqcpdvqiswnEGVDLwwH 290
Cdd:COG1021 126 YIIPDR-HRG---FDYRALARELQAEVPS----LRHVLVV---GDAG-------------------------EFTSL--D 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 291 ELMQEAGDEFEPEwCDAEDPLFILYTSGSTGKPKGVVHTIGGYmLYVATTFKYVFDFHPEDVFWCTADIGwitgHSY--- 367
Cdd:COG1021 168 ALLAAPADLSEPR-PDPDDVAFFQLSGGTTGLPKLIPRTHDDY-LYSVRASAEICGLDADTVYLAALPAA----HNFpls 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 368 --VTYGPLANGATSVLFEGipTYPDEsrLWSIVDKYKVTkfYTA--PTAIRMLMKFGDEpvTKHSRASLQVLGTVGEPIN 443
Cdd:COG1021 242 spGVLGVLYAGGTVVLAPD--PSPDT--AFPLIERERVT--VTAlvPPLALLWLDAAER--SRYDLSSLRVLQVGGAKLS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 444 PEA----------WLW-----------Y-------HRVVGSQHCP--------IVDtfwqtETGghmlTPLPgatpmkPG 487
Cdd:COG1021 314 PELarrvrpalgcTLQqvfgmaeglvnYtrlddpeEVILTTQGRPispddevrIVD-----EDG----NPVP------PG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 488 SAsfpffGVapailnesgeelegeaegyLVFKQPWpgimrTIYGnhtrfettYFKKfP----------GYYVTGDGCRRD 557
Cdd:COG1021 379 EV-----GE-------------------LLTRGPY-----TIRG--------YYRA-PehnaraftpdGFYRTGDLVRRT 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 558 QDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGE--CLycFVTLcDGHTFSstlTEELKKQI 635
Cdd:COG1021 421 PDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGErsCA--FVVP-RGEPLT---LAELRRFL 494
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 625195332 636 REKiGpIAT---PDYIQNAPGLPKTRSGKIMRRVLRKIAQ 672
Cdd:COG1021 495 RER-G-LAAfklPDRLEFVDALPLTAVGKIDKKALRAALA 532
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
101-667 |
3.49e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 146.64 E-value: 3.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 101 TNICYNVldrNVHEKKLGDKVAFYWEGNEpgettkITYRELLVQVCQFSNVL-RKQGIQKGDRVAIYMPMILELVVAMLA 179
Cdd:PRK08314 10 TSLFHNL---EVSARRYPDKTAIVFYGRA------ISYRELLEEAERLAGYLqQECGVRKGDRVLLYMQNSPQFVIAYYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 180 CARLGALHSIVFAGFSAESLCERILDSSCSLLITTDAFY-RGEKLVNLKELAdeslekcrekgfpvrcCIVVKHVGRAel 258
Cdd:PRK08314 81 ILRANAVVVPVNPMNREEELAHYVTDSGARVAIVGSELApKVAPAVGNLRLR----------------HVIVAQYSDY-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 259 gMNDSPSQSPPVK-RQCPDVQISWNEGVDLWwhELMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYV 337
Cdd:PRK08314 143 -LPAEPEIAVPAWlRAEPPLQALAPGGVVAW--KEALAAGLAPPPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 338 ATTFKYvFDFHPEDVFWCTADIGWITGHSYVTYGPLANGATSVLfegIPTYpDESRLWSIVDKYKVTKFYTAPTairMLM 417
Cdd:PRK08314 220 VGSVLW-SNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVL---MPRW-DREAAARLIERYRVTHWTNIPT---MVV 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 418 KFGDEP-VTKHSRASLQVLGTVGEPInPEAwlwyhrvVGS---QHC--PIVDTFWQTETGGHMLTPLPGATpmKPGSASF 491
Cdd:PRK08314 292 DFLASPgLAERDLSSLRYIGGGGAAM-PEA-------VAErlkELTglDYVEGYGLTETMAQTHSNPPDRP--KLQCLGI 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 492 PFFGVAPAILNESGEELEGEAEG--YLVFKqpwPGIMRTIYGNHTRFETTyFKKFPG--YYVTGDGCRRDQDGYYWITGR 567
Cdd:PRK08314 362 PTFGVDARVIDPETLEELPPGEVgeIVVHG---PQVFKGYWNRPEATAEA-FIEIDGkrFFRTGDLGRMDEEGYFFITDR 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 568 IDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTfSSTLTEELKKQIREKIGPIATPDY 647
Cdd:PRK08314 438 LKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEAR-GKTTEEEIIAWAREHMAAYKYPRI 516
|
570 580
....*....|....*....|
gi 625195332 648 IQNAPGLPKTRSGKIMRRVL 667
Cdd:PRK08314 517 VEFVDSLPKSGSGKILWRQL 536
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
132-667 |
6.11e-36 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 141.29 E-value: 6.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 132 ETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLL 211
Cdd:cd17643 9 EDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILADSGPSLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 212 ITtdafyrgeklvnlkeladeslekcrekgfpvrccivvkhvgraelgmndspsqsppvkrqcpdvqiswnegvdlwwhe 291
Cdd:cd17643 89 LT------------------------------------------------------------------------------ 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 292 lmqeagdefepewcDAEDPLFILYTSGSTGKPKGVVHTIGGYM-LYVATTfkYVFDFHPEDVfwctadigWITGHSYV-- 368
Cdd:cd17643 91 --------------DPDDLAYVIYTSGSTGRPKGVVVSHANVLaLFAATQ--RWFGFNEDDV--------WTLFHSYAfd 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 369 -----TYGPLANGATSVlfegIPTYP---DESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVTKHSRASLQVLGtvGE 440
Cdd:cd17643 147 fsvweIWGALLHGGRLV----VVPYEvarSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFG--GE 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 441 PINPeAWL--WYHRVvGSQHCPIVDTFWQTETGGHM----LTP--LPGATpMKPGSASFPFFGVAPAILNESGEELEGEA 512
Cdd:cd17643 221 ALEA-AMLrpWAGRF-GLDRPQLVNMYGITETTVHVtfrpLDAadLPAAA-ASPIGRPLPGLRVYVLDADGRPVPPGVVG 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 513 EGYLVFKQPWPGIMRTIYGNHTRFETTYFKKfPG--YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVE 590
Cdd:cd17643 298 ELYVSGAGVARGYLGRPELTAERFVANPFGG-PGsrMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALAT 376
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 591 HEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFsstLTEELKKQIREKIgpiatPDYIQNA-----PGLPKTRSGKIMRR 665
Cdd:cd17643 377 HPSVRDAAVIVREDEPGDTRLVAYVVADDGAAA---DIAELRALLKELL-----PDYMVPAryvplDALPLTVNGKLDRA 448
|
..
gi 625195332 666 VL 667
Cdd:cd17643 449 AL 450
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
119-668 |
1.48e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 135.50 E-value: 1.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 119 DKVAFYWEGnepgetTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLG----ALHSIVfagf 194
Cdd:PRK06188 27 DRPALVLGD------TRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGlrrtALHPLG---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 195 SAESLCERILDSSCSLLITTDAFYRgeklvnlkELADESLEKCREkgfpvrccivVKHVgraeLGMNDSPsqsppvkrqc 274
Cdd:PRK06188 97 SLDDHAYVLEDAGISTLIVDPAPFV--------ERALALLARVPS----------LKHV----LTLGPVP---------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 275 pdvqiswnEGVDLWwhelmqEAGDEFEPE----WCDAEDPLFILYTSGSTGKPKGVVHT---IGGYMLYVATTFKYvfdf 347
Cdd:PRK06188 145 --------DGVDLL------AAAAKFGPAplvaAALPPDIAGLAYTGGTTGKPKGVMGThrsIATMAQIQLAEWEW---- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 348 hPEDV-FWCTADIGWITGHSYVtygP-LANGATSVLFEGIptypDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVT 425
Cdd:PRK06188 207 -PADPrFLMCTPLSHAGGAFFL---PtLLRGGTVIVLAKF----DPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTR 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 426 KHSraSLQVLGTVGEPINP----EAwlwyHRVVGsqhcPI-VDTFWQTETGgHMLTPLP-----GATPMKPGSASFPFFG 495
Cdd:PRK06188 279 DLS--SLETVYYGASPMSPvrlaEA----IERFG----PIfAQYYGQTEAP-MVITYLRkrdhdPDDPKRLTSCGRPTPG 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 496 VAPAILNESGEELEGEAEGYLVFKQPwpGIMRtiyGNHTRFETT--YFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLN 573
Cdd:PRK06188 348 LRVALLDEDGREVAQGEVGEICVRGP--LVMD---GYWNRPEETaeAFRD--GWLHTGDVAREDEDGFYYIVDRKKDMIV 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 574 VSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSstlTEELKKQIREKIGPIATPDYIQNAPG 653
Cdd:PRK06188 421 TGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVD---AAELQAHVKERKGSVHAPKQVDFVDS 497
|
570
....*....|....*
gi 625195332 654 LPKTRSGKIMRRVLR 668
Cdd:PRK06188 498 LPLTALGKPDKKALR 512
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
137-599 |
1.56e-33 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 133.16 E-value: 1.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 137 TYRELLVQVCQFSNVLRKQ-GIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLcERIL-DSSCSLLITT 214
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERL-AFILeDAGARLLLTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 215 DAFyrgeklvnlkeladesLEKCREKGFPVRCCivvkhVGRAELGMNDSPSQSPPVKRQCPDvqiswnegvdlwwhelmq 294
Cdd:TIGR01733 80 SAL----------------ASRLAGLVLPVILL-----DPLELAALDDAPAPPPPDAPSGPD------------------ 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 295 eagdefepewcdaeDPLFILYTSGSTGKPKGVVHTIGGyMLYVATTFKYVFDFHPEDVfwctadigWITGHSYV------ 368
Cdd:TIGR01733 121 --------------DLAYVIYTSGSTGRPKGVVVTHRS-LVNLLAWLARRYGLDPDDR--------VLQFASLSfdasve 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 369 -TYGPLANGATSVLFEGIPTYPDESRLWSIVDKYKVTKFYTAPTAIRMLMkfgDEPVTkhSRASLQVLGTVGEPINPEAW 447
Cdd:TIGR01733 178 eIFGALLAGATLVVPPEDEERDDAALLAALIAEHPVTVLNLTPSLLALLA---AALPP--ALASLRLVILGGEALTPALV 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 448 LWYHRVVGSqhCPIVDTFWQTETG---GHMLTPLPGATPMKPGSASFPFFGVAPAILNESGeelegeaegylvfkQPWP- 523
Cdd:TIGR01733 253 DRWRARGPG--ARLINLYGPTETTvwsTATLVDPDDAPRESPVPIGRPLANTRLYVLDDDL--------------RPVPv 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 524 GIMRTIY--------GNHTRFETT--YFKKFPGY-------YVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVES 586
Cdd:TIGR01733 317 GVVGELYiggpgvarGYLNRPELTaeRFVPDPFAggdgarlYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEA 396
|
490
....*....|...
gi 625195332 587 ALVEHEAVAEAAV 599
Cdd:TIGR01733 397 ALLRHPGVREAVV 409
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
136-667 |
2.22e-33 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 134.67 E-value: 2.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 136 ITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITTD 215
Cdd:cd05904 33 LTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 216 AFYrgeklvnlkeladeslEKCREKGFPVRCC-IVVKHVGRAELGMNDSPSQSPPVkrqcpdVQISwnegvdlwwhelmq 294
Cdd:cd05904 113 ELA----------------EKLASLALPVVLLdSAEFDSLSFSDLLFEADEAEPPV------VVIK-------------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 295 eagdefepewcdAEDPLFILYTSGSTGKPKGVVHTIGGYmlyVATTFKYVFDF----HPEDVFWCTADIGWITGHSYVTY 370
Cdd:cd05904 157 ------------QDDVAALLYSSGTTGRSKGVMLTHRNL---IAMVAQFVAGEgsnsDSEDVFLCVLPMFHIYGLSSFAL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 371 GPLANGATSVLfegIPTYpDESRLWSIVDKYKVTKFYTAPTAIRMLMKfgDEPVTKHSRASLQVLGTVGEPINPEAWLWY 450
Cdd:cd05904 222 GLLRLGATVVV---MPRF-DLEELLAAIERYKVTHLPVVPPIVLALVK--SPIVDKYDLSSLRQIMSGAAPLGKELIEAF 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 451 HRVVGsqHCPIVDTFWQTETGG--HMlTPLPGATPMKPGSASFPFFGVAPAILNESGEELegeaegyLVFKQP---W--- 522
Cdd:cd05904 296 RAKFP--NVDLGQGYGMTESTGvvAM-CFAPEKDRAKYGSVGRLVPNVEAKIVDPETGES-------LPPNQTgelWirg 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 523 PGIMRTIYGNHTRFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGH 602
Cdd:cd05904 366 PSIMKGYLNNPEATAATIDKE--GWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPY 443
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 625195332 603 PHPVKGECLYCFVTLCDGhtfsSTLTE-ELKKQIREKIGP------IATPDYIqnapglPKTRSGKIMRRVL 667
Cdd:cd05904 444 PDEEAGEVPMAFVVRKPG----SSLTEdEIMDFVAKQVAPykkvrkVAFVDAI------PKSPSGKILRKEL 505
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
118-669 |
1.12e-32 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 132.75 E-value: 1.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 118 GDKVAFYWEGnePGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGA-LHSI---VFAg 193
Cdd:cd12119 10 GDREIVSRTH--EGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAvLHTInprLFP- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 194 fsaeslcERILdsscslLITTDAfyrGEKLVnlkeLADESLEKCREKGFPVrcCIVVKHVGRAELGmNDSPSQSPPvkrq 273
Cdd:cd12119 87 -------EQIA------YIINHA---EDRVV----FVDRDFLPLLEAIAPR--LPTVEHVVVMTDD-AAMPEPAGV---- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 274 cpdvqiswneGVDLWWHELMQEAGDEFEPEWcDAEDPLFILYTSGSTGKPKGVV--------HTIGGYMlyvattfKYVF 345
Cdd:cd12119 140 ----------GVLAYEELLAAESPEYDWPDF-DENTAAAICYTSGTTGNPKGVVyshrslvlHAMAALL-------TDGL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 346 DFHPEDVF-----------WCTADIGWITGHSYVTYGPLANGATsvlfegiptypdesrLWSIVDKYKVTKFYTAPTAIR 414
Cdd:cd12119 202 GLSESDVVlpvvpmfhvnaWGLPYAAAMVGAKLVLPGPYLDPAS---------------LAELIEREGVTFAAGVPTVWQ 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 415 MLMKFGDEpvTKHSRASLQVLgtvgepinpeawlwyhrVVGSQHCP----------IVDTF--W-QTETG--GHMLTPLP 479
Cdd:cd12119 267 GLLDHLEA--NGRDLSSLRRV-----------------VIGGSAVPrslieafeerGVRVIhaWgMTETSplGTVARPPS 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 480 GATP----------MKPGsasFPFFGVAPAILNESGEELEGEAEGY--LVFKQPWpgIMRTIYGNHtrfETTYFKKFPGY 547
Cdd:cd12119 328 EHSNlsedeqlalrAKQG---RPVPGVELRIVDDDGRELPWDGKAVgeLQVRGPW--VTKSYYKND---EESEALTEDGW 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 548 YVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSStl 627
Cdd:cd12119 400 LRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTA-- 477
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 625195332 628 tEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:cd12119 478 -EELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
115-669 |
3.04e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 131.70 E-value: 3.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 115 KKLGDKVAFYWegnepGETTkITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALhsIVFAGF 194
Cdd:PRK07470 18 RRFPDRIALVW-----GDRS-WTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAV--WVPTNF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 195 S---------AESlcerildSSCSLLITTDAFyrgeklvnlkelaDESLEKCREKGFPVRCCIVVkhvGRAELGmndsps 265
Cdd:PRK07470 90 RqtpdevaylAEA-------SGARAMICHADF-------------PEHAAAVRAASPDLTHVVAI---GGARAG------ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 266 qsppvkrqcPDVQiswnegvdlwwHELMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPKGVVHTiGGYMLYVATTfkyvf 345
Cdd:PRK07470 141 ---------LDYE-----------ALVARHLGARVANAAVDHDDPCWFFFTSGTTGRPKAAVLT-HGQMAFVITN----- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 346 dfHPEDVFWCTadigwiTGH--SYVTyGPL------------ANGATSVLFEGIPTYPDEsrLWSIVDKYKVTKFYTAPT 411
Cdd:PRK07470 195 --HLADLMPGT------TEQdaSLVV-APLshgagihqlcqvARGAATVLLPSERFDPAE--VWALVERHRVTNLFTVPT 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 412 AIRMLMKfgDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGSQhcpIVDTFWQTETGGHMlTPLPGA------TPM- 484
Cdd:PRK07470 264 ILKMLVE--HPAVDRYDHSSLRYVIYAGAPMYRADQKRALAKLGKV---LVQYFGLGEVTGNI-TVLPPAlhdaedGPDa 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 485 KPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQP--WPGIMRTIYGNHTRFETTYFKkfpgyyvTGDGCRRDQDGYY 562
Cdd:PRK07470 338 RIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPavFAGYYNNPEANAKAFRDGWFR-------TGDLGHLDARGFL 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 563 WITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSStltEELKKQIREKIGPI 642
Cdd:PRK07470 411 YITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDE---AELLAWLDGKVARY 487
|
570 580
....*....|....*....|....*..
gi 625195332 643 ATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:PRK07470 488 KLPKRFFFWDALPKSGYGKITKKMVRE 514
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
315-671 |
6.72e-32 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 127.60 E-value: 6.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 315 YTSGSTGKPKGVVHTIGGyMLYVATTFKYVFDFHPEDVFWCTADIGWITGhSYVTYG-PLANGAtSVLFEGIPTYPDES- 392
Cdd:cd05944 9 HTGGTTGTPKLAQHTHSN-EVYNAWMLALNSLFDPDDVLLCGLPLFHVNG-SVVTLLtPLASGA-HVVLAGPAGYRNPGl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 393 --RLWSIVDKYKVTKFYTAPTAIRMLMKfgdEPVTKhSRASLQVLGTVGEPINPEAwlwYHRVVGSQHCPIVDTFWQTE- 469
Cdd:cd05944 86 fdNFWKLVERYRITSLSTVPTVYAALLQ---VPVNA-DISSLRFAMSGAAPLPVEL---RARFEDATGLPVVEGYGLTEa 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 470 TGGHMLTPlPGaTPMKPGSAS--FPFFGVAPAILNESGEELEGEAEGYLvfkqpWPGIM--RTIYGNHTRFETTYFKKF- 544
Cdd:cd05944 159 TCLVAVNP-PD-GPKRPGSVGlrLPYARVRIKVLDGVGRLLRDCAPDEV-----GEICVagPGVFGGYLYTEGNKNAFVa 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 545 PGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFS 624
Cdd:cd05944 232 DGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVE 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 625195332 625 stlTEELKKQIREKIGP-IATPDYIQNAPGLPKTRSGKIMRRVLRKIA 671
Cdd:cd05944 312 ---EEELLAWARDHVPErAAVPKHIEVLEELPVTAVGKVFKPALRADA 356
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
137-669 |
8.36e-32 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 128.65 E-value: 8.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 137 TYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALhsivfagfsaeslcerildsSCSLLittdA 216
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAV--------------------TNPIL----P 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 217 FYRGEKLVNLkeladesLEKCREKGFPVrccivvkhvgraelgmndspsqsPPVKRQcpdvqiswnegvdlwwhelmqea 296
Cdd:cd05903 59 FFREHELAFI-------LRRAKAKVFVV-----------------------PERFRQ----------------------- 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 297 gdeFEPEwCDAEDPLFILYTSGSTGKPKGVVHTiGGYMLYVATTFKYVFDFHPEDVFWCTADIGWITGHSYVTYGPLANG 376
Cdd:cd05903 86 ---FDPA-AMPDAVALLLFTSGTTGEPKGVMHS-HNTLSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLG 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 377 ATSVLFEGIptypDESRLWSIVDKYKVTKFYTAPTAIRMLMK---FGDEPVtkhsrASLQVLGTVGEPINP----EAWlw 449
Cdd:cd05903 161 APVVLQDIW----DPDKALALMREHGVTFMMGATPFLTDLLNaveEAGEPL-----SRLRTFVCGGATVPRslarRAA-- 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 450 yhRVVGSQHCPIvdtFWQTETGGHMLTPLPGATPMKPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpgimRTI 529
Cdd:cd05903 230 --ELLGAKVCSA---YGSTECPGAVTSITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEGELLSRGP-----SVF 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 530 YGNHTRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGE 609
Cdd:cd05903 300 LGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGE 379
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 625195332 610 CLYCFVTLCDGHTFS-STLTEELKKQ--IREKIgpiatPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:cd05903 380 RACAVVVTKSGALLTfDELVAYLDRQgvAKQYW-----PERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
131-668 |
2.00e-31 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 128.62 E-value: 2.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 131 GETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLcERILDSSCSL 210
Cdd:cd17651 16 AEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERL-AFMLADAGPV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 211 LITTDAFYRGEklvnlkeladeslekcrekgFPVRccivvkhvgraelgmndspsqsppvkrqcpdvqiswnEGVDLWWH 290
Cdd:cd17651 95 LVLTHPALAGE--------------------LAVE-------------------------------------LVAVTLLD 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 291 ELMQEAGDEFEPEW-CDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTfKYVFDFHPEDVFWCTADIGWITGHSYVt 369
Cdd:cd17651 118 QPGAAAGADAEPDPaLDADDLAYVIYTSGSTGRPKGVVMPHRSLANLVAWQ-ARASSLGPGARTLQFAGLGFDVSVQEI- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 370 YGPLANGATSVLfegIPTY--PDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVTKHsrASLQVLGTVGEPINPE-- 445
Cdd:cd17651 196 FSTLCAGATLVL---PPEEvrTDPPALAAWLDEQRISRVFLPTVALRALAEHGRPLGVRL--AALRYLLTGGEQLVLTed 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 446 -----AWLWYHRVVgsqhcpivDTFWQTET---GGHMLTPLPGATPMKPgSASFPFFGVAPAILNEsgeelegeaegylv 517
Cdd:cd17651 271 lrefcAGLPGLRLH--------NHYGPTEThvvTALSLPGDPAAWPAPP-PIGRPIDNTRVYVLDA-------------- 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 518 FKQPWP------------GIMRtiyGNHTRFETTYfKKF------PG--YYVTGDGCRRDQDGYYWITGRIDDMLNVSGH 577
Cdd:cd17651 328 ALRPVPpgvpgelyiggaGLAR---GYLNRPELTA-ERFvpdpfvPGarMYRTGDLARWLPDGELEFLGRADDQVKIRGF 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 578 LLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTlcdGHTFSSTLTEELKKQIREKIGPIATPDYIQNAPGLPKT 657
Cdd:cd17651 404 RIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVV---GDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLT 480
|
570
....*....|.
gi 625195332 658 RSGKIMRRVLR 668
Cdd:cd17651 481 PNGKLDRRALP 491
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
119-670 |
2.41e-30 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 125.07 E-value: 2.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 119 DKVAFYWEGnepgetTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGAlhSIVFAG--FSA 196
Cdd:PRK03640 17 DRTAIEFEE------KKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGA--VAVLLNtrLSR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 197 ESLCERILDSSCSLLITTDAFyrgeklvnlkeladeslekcrekgfpvrccivvkhvgraelgmndspsqsppVKRQCPD 276
Cdd:PRK03640 89 EELLWQLDDAEVKCLITDDDF----------------------------------------------------EAKLIPG 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 277 VQISWNEgvdlwwheLMQEAGDEFEP-EWCDAEDPLFILYTSGSTGKPKGVVHTIGGYmLYVATTFKYVFDFHPEDVFWC 355
Cdd:PRK03640 117 ISVKFAE--------LMNGPKEEAEIqEEFDLDEVATIMYTSGTTGKPKGVIQTYGNH-WWSAVGSALNLGLTEDDCWLA 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 356 TADIGWITGHSYVTygplangaTSVLFeGIPTYP----DESRLWSIVDKYKVTKFYTAPTAI-RMLMKFGDEPVTKHSRA 430
Cdd:PRK03640 188 AVPIFHISGLSILM--------RSVIY-GMRVVLvekfDAEKINKLLQTGGVTIISVVSTMLqRLLERLGEGTYPSSFRC 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 431 SLqvLGtvGEPInPEAWLwyhrvvgsQHC-----PIVDTFWQTETGGHMLTPLPGATPMKPGSASFPFFGVAPAILNESG 505
Cdd:PRK03640 259 ML--LG--GGPA-PKPLL--------EQCkekgiPVYQSYGMTETASQIVTLSPEDALTKLGSAGKPLFPCELKIEKDGV 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 506 EELEGEAEGYLVfKQP--WPGIMRTIYGNHTRFETTYFKkfpgyyvTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAE 583
Cdd:PRK03640 326 VVPPFEEGEIVV-KGPnvTKGYLNREDATRETFQDGWFK-------TGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAE 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 584 VESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLcdGHTFSStltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIM 663
Cdd:PRK03640 398 IEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK--SGEVTE---EELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLL 472
|
....*..
gi 625195332 664 RRVLRKI 670
Cdd:PRK03640 473 RHELKQL 479
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
137-668 |
3.82e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 124.92 E-value: 3.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 137 TYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITTDA 216
Cdd:PRK09088 24 TYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLGDDA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 217 fyrgeklvnlkeLADeslekcrekgfpvrccivvkhvGRAElgmndspsqsppvkrqcpdvqiswneGVDLwwhELMQEA 296
Cdd:PRK09088 104 ------------VAA----------------------GRTD--------------------------VEDL---AAFIAS 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 297 GDEFEP---EWCDAEDPLFILYTSGSTGKPKGVVHTIGGyMLYVATTFKYVFDFHPEDVFWCTAD----IGWITGHSYVt 369
Cdd:PRK09088 121 ADALEPadtPSIPPERVSLILFTSGTSGQPKGVMLSERN-LQQTAHNFGVLGRVDAHSSFLCDAPmfhiIGLITSVRPV- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 370 ygpLANGATSVLFEGIPtyPDESRLWSIVDKYKVTKFYTAPtaiRMLMKFGDEPVTKHSR-ASLQVLGTVGEPiNPE--- 445
Cdd:PRK09088 199 ---LAVGGSILVSNGFE--PKRTLGRLGDPALGITHYFCVP---QMAQAFRAQPGFDAAAlRHLTALFTGGAP-HAAedi 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 446 -AWLwyhrvvgSQHCPIVDTFWQTETGGHMLTPL-PGATPMKPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQP-- 521
Cdd:PRK09088 270 lGWL-------DDGIPMVDGFGMSEAGTVFGMSVdCDVIRAKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPnl 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 522 WPGIMRTIYGNHTRFETTyfkkfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVG 601
Cdd:PRK09088 343 SPGYWRRPQATARAFTGD------GWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVG 416
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 625195332 602 HPHPVKGECLYCFVTLCDGhtfSSTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:PRK09088 417 MADAQWGEVGYLAIVPADG---APLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLR 480
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
119-667 |
1.08e-29 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 122.74 E-value: 1.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 119 DKVAFYWEGnepgetTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAES 198
Cdd:cd05945 6 DRPAVVEGG------RTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 199 LcERILD-SSCSLLITTDAfyrgeklvnlkeladeslekcrekgfpvrccivvkhvgraelgmndspsqsppvkrqcpdv 277
Cdd:cd05945 80 I-REILDaAKPALLIADGD------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 278 qiswnegvdlwwhelmqeagdefepewcdaeDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYvFDFHPEDVFWCTA 357
Cdd:cd05945 98 -------------------------------DNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSD-FPLGPGDVFLNQA 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 358 ---------DIgwitghsyvtYGPLANGATSV------------LFEGIPTYPdesrlwsivdkykVTKFYTAPTAIRML 416
Cdd:cd05945 146 pfsfdlsvmDL----------YPALASGATLVpvprdatadpkqLFRFLAEHG-------------ITVWVSTPSFAAMC 202
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 417 MkfGDEPVTKHSRASL-QVLgTVGEPI-NPEAWLWYHRVvgsQHCPIVDTFWQTET----GGHMLTPLPGATpMKPGSAS 490
Cdd:cd05945 203 L--LSPTFTPESLPSLrHFL-FCGEVLpHKTARALQQRF---PDARIYNTYGPTEAtvavTYIEVTPEVLDG-YDRLPIG 275
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 491 FPFFGVAPAILNESGEELEGEAEGYLVFKQP--WPGIMRTiYGNHTRFettyFKKFPGY--YVTGDGCRRDQDGYYWITG 566
Cdd:cd05945 276 YAKPGAKLVILDEDGRPVPPGEKGELVISGPsvSKGYLNN-PEKTAAA----FFPDEGQraYRTGDLVRLEADGLLFYRG 350
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 567 RIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSstLTEELKKQIREKIGPIATPD 646
Cdd:cd05945 351 RLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEAG--LTKAIKAELAERLPPYMIPR 428
|
570 580
....*....|....*....|.
gi 625195332 647 YIQNAPGLPKTRSGKIMRRVL 667
Cdd:cd05945 429 RFVYLDELPLNANGKIDRKAL 449
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
145-668 |
1.75e-29 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 122.16 E-value: 1.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 145 VCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAEslcerILDSSCSLLITtdafYRGEKLV 224
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFVPLNPT-----LKESVLRYLVA----DAGGRIV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 225 nlkeLADESLekcrekgfpvrccivvkhVGRAELGMNDSPSqsppvkrqcPDVQISwnegVDLWWHELMQEAGDEFEPEw 304
Cdd:cd05922 74 ----LADAGA------------------ADRLRDALPASPD---------PGTVLD----ADGIRAARASAPAHEVSHE- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 305 cdaeDPLFILYTSGSTGKPKGVV--HTiggYMLYVATTFKYVFDFHPEDVFWCTADIGWITGHSYVTYGpLANGATSVLF 382
Cdd:cd05922 118 ----DLALLLYTSGSTGSPKLVRlsHQ---NLLANARSIAEYLGITADDRALTVLPLSYDYGLSVLNTH-LLRGATLVLT 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 383 EGipTYPDESrLWSIVDKYKVTKFYTAPTAIRML--MKFGDEPVtkhsrASLQVLGTVGEPInPEAWLWYHR--VVGSQh 458
Cdd:cd05922 190 ND--GVLDDA-FWEDLREHGATGLAGVPSTYAMLtrLGFDPAKL-----PSLRYLTQAGGRL-PQETIARLRelLPGAQ- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 459 cpIVDTFWQTETGGHMLTPLPGATPMKPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPWpgIMRTiYGNHTRFET 538
Cdd:cd05922 260 --VYVMYGQTEATRRMTYLPPERILEKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPN--VMKG-YWNDPPYRR 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 539 TYfKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVkGECLYCFVTLC 618
Cdd:cd05922 335 KE-GRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPL-GEKLALFVTAP 412
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 625195332 619 DGHTFSstlteELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:cd05922 413 DKIDPK-----DVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
137-667 |
3.71e-29 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 121.63 E-value: 3.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 137 TYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLcERIL-DSSCSLLITTD 215
Cdd:cd12116 14 SYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRL-RYILeDAEPALVLTDD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 216 AfyrgeklvnlkeLADeslekcrekgfPVRCCIVVKHVGRAELGMNDSPSQSPPVkrqcPDvqiswnegvdlwwhelmqe 295
Cdd:cd12116 93 A------------LPD-----------RLPAGLPVLLLALAAAAAAPAAPRTPVS----PD------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 296 agdefepewcdaeDPLFILYTSGSTGKPKGVVHTIGGY------------------MLYVATtfkYVFDFHPEDVFWcta 357
Cdd:cd12116 127 -------------DLAYVIYTSGSTGRPKGVVVSHRNLvnflhsmrerlglgpgdrLLAVTT---YAFDISLLELLL--- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 358 digwitghsyvtygPLANGATSVLFEGIPTYpDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPvtkhsRASLQVL-G 436
Cdd:cd12116 188 --------------PLLAGARVVIAPRETQR-DPEALARLIEAHSITVMQATPATWRMLLDAGWQG-----RAGLTALcG 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 437 tvGEPINPEawlwyhrvVGSQHCPIVDTFWQ----TETgghmlTPLPGATPMKPGSASFPffgVAPAILNESGeelegea 512
Cdd:cd12116 248 --GEALPPD--------LAARLLSRVGSLWNlygpTET-----TIWSTAARVTAAAGPIP---IGRPLANTQV------- 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 513 egYLV--FKQPWP-GIMRTIY--------GNHTRFETTyFKKF-------PG--YYVTGDGCRRDQDGYYWITGRIDDML 572
Cdd:cd12116 303 --YVLdaALRPVPpGVPGELYiggdgvaqGYLGRPALT-AERFvpdpfagPGsrLYRTGDLVRRRADGRLEYLGRADGQV 379
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 573 NVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGEcLYCFVTLCDGHTFSstlTEELKKQIREKIGPIATPDYIQNAP 652
Cdd:cd12116 380 KIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRR-LVAYVVLKAGAAPD---AAALRAHLRATLPAYMVPSAFVRLD 455
|
570
....*....|....*
gi 625195332 653 GLPKTRSGKIMRRVL 667
Cdd:cd12116 456 ALPLTANGKLDRKAL 470
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
119-672 |
3.87e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 122.84 E-value: 3.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 119 DKVAFYWEGNEpgettkITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAES 198
Cdd:PRK06178 48 QRPAIIFYGHV------ITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 199 LCERILDSSCSLLITTDAFYrgeKLVNlkeladeslekcrekgfPVRCCIVVKHVGRAELG--MNDSPSQSPPVKRQCPD 276
Cdd:PRK06178 122 LSYELNDAGAEVLLALDQLA---PVVE-----------------QVRAETSLRHVIVTSLAdvLPAEPTLPLPDSLRAPR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 277 VQISWnegvdlwWHELMQ--EAGDEFEPEWCDAEDPLFIL-YTSGSTGKPKGVVHTiGGYMLYVATTFKYVFDFHPED-V 352
Cdd:PRK06178 182 LAAAG-------AIDLLPalRACTAPVPLPPPALDALAALnYTGGTTGMPKGCEHT-QRDMVYTAAAAYAVAVVGGEDsV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 353 FWCTADIGWITGHSYVTYGPLANGATSVLFegipTYPDESRLWSIVDKYKVTK-FYTAPTAIRMLmkfgDEP-VTKHSRA 430
Cdd:PRK06178 254 FLSFLPEFWIAGENFGLLFPLFSGATLVLL----ARWDAVAFMAAVERYRVTRtVMLVDNAVELM----DHPrFAEYDLS 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 431 SLQVLGTVG--EPINPEAWLWYHRVVGSQhcpIVDTFW-QTET------------GGHMLT--------PLPGA----TP 483
Cdd:PRK06178 326 SLRQVRVVSfvKKLNPDYRQRWRALTGSV---LAEAAWgMTEThtcdtftagfqdDDFDLLsqpvfvglPVPGTefkiCD 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 484 MKPGsASFPFfGV-------APAILnesgeelegeaegylvfkqpwpgimrTIYGNHTRFETTYFKKfpGYYVTGDGCRR 556
Cdd:PRK06178 403 FETG-ELLPL-GAegeivvrTPSLL--------------------------KGYWNKPEATAEALRD--GWLHTGDIGKI 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 557 DQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSStltEELKKQIR 636
Cdd:PRK06178 453 DEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTA---AALQAWCR 529
|
570 580 590
....*....|....*....|....*....|....*..
gi 625195332 637 EKIGPIATPD-YIQNApgLPKTRSGKIMRRVLRKIAQ 672
Cdd:PRK06178 530 ENMAVYKVPEiRIVDA--LPMTATGKVRKQDLQALAE 564
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
583-661 |
1.15e-28 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 109.17 E-value: 1.15e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 625195332 583 EVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfSSTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGK 661
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPG---VELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
136-667 |
1.60e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 120.91 E-value: 1.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 136 ITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITTD 215
Cdd:PRK06710 50 ITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 216 AFYrgEKLVNLKELAD-ESLEKCREKGF-PVRCCIVVKHVGRaelgmndspsqsppvKRQCPDVQISWNEGVDLWwHELM 293
Cdd:PRK06710 130 LVF--PRVTNVQSATKiEHVIVTRIADFlPFPKNLLYPFVQK---------------KQSNLVVKVSESETIHLW-NSVE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 294 QEAGDEFEPEwCDAEDPLFIL-YTSGSTGKPKGVVHTIGGYMLYVATTFKYVFD-FHPEDVFWCTADIGWITGHSYVTYG 371
Cdd:PRK06710 192 KEVNTGVEVP-CDPENDLALLqYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNcKEGEEVVLGVLPFFHVYGMTAVMNL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 372 PLANGATSVLfegIPTYpDESRLWSIVDKYKVTKFYTAPTAIRMLMkfgDEPVTK-HSRASLQVLGTVGEPINPEAWLWY 450
Cdd:PRK06710 271 SIMQGYKMVL---IPKF-DMKMVFEAIKKHKVTLFPGAPTIYIALL---NSPLLKeYDISSIRACISGSAPLPVEVQEKF 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 451 HRVVGSQhcpIVDTFWQTETgghmlTPLPGATPM----KPGSASFPFFGVAPAILNESGEELEGEAEG-YLVFKQPwpGI 525
Cdd:PRK06710 344 ETVTGGK---LVEGYGLTES-----SPVTHSNFLwekrVPGSIGVPWPDTEAMIMSLETGEALPPGEIgEIVVKGP--QI 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 526 MRtiyGNHTRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHP 605
Cdd:PRK06710 414 MK---GYWNKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDP 490
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 625195332 606 VKGECLYCFVTLCDGHTFSStltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 667
Cdd:PRK06710 491 YRGETVKAFVVLKEGTECSE---EELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
136-669 |
2.37e-28 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 119.89 E-value: 2.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 136 ITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITTD 215
Cdd:TIGR03098 26 LTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLLVTSS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 216 AfyrgekLVNLKELADESLEKCREkgfpvrccivVKHVGRAELGMNDSPSQSPpvkrqcpdvqISWNEgvdlwwhelMQE 295
Cdd:TIGR03098 106 E------RLDLLHPALPGCHDLRT----------LIIVGDPAHASEGHPGEEP----------ASWPK---------LLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 296 AGDEFEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYVfDFHPEDVFWCTADIGWITGHSYVTYGpLAN 375
Cdd:TIGR03098 151 LGDADPPHPVIDSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYL-ENRPDDRLLAVLPLSFDYGFNQLTTA-FYV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 376 GATSVLF--------------EGIPTYPDESRLWSIV--DKYKVTKF----YTAPTAIRMLMKfgdepVTKHSRASLqvl 435
Cdd:TIGR03098 229 GATVVLHdyllprdvlkalekHGITGLAAVPPLWAQLaqLDWPESAApslrYLTNSGGAMPRA-----TLSRLRSFL--- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 436 gtvgepinPEAWLwyHRVVGsqhcpIVDTFWQTetgghmlTPLPGATPMKPGS--ASFPFFGVapAILNESGEELEGEAE 513
Cdd:TIGR03098 301 --------PNARL--FLMYG-----LTEAFRST-------YLPPEEVDRRPDSigKAIPNAEV--LVLREDGSECAPGEE 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 514 GYLVFKQPwpgIMRTIYGNHTRFETTYFKKFPGYYV----------TGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAE 583
Cdd:TIGR03098 357 GELVHRGA---LVAMGYWNDPEKTAERFRPLPPFPGelhlpelavwSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTE 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 584 VESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSStltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIM 663
Cdd:TIGR03098 434 VEEVAYATGLVAEAVAFGVPDPTLGQAIVLVVTPPGGEELDR---AALLAECRARLPNYMVPALIHVRQALPRNANGKID 510
|
....*.
gi 625195332 664 RRVLRK 669
Cdd:TIGR03098 511 RKALAK 516
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
119-674 |
4.65e-28 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 119.00 E-value: 4.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 119 DKVAFYWEGNEPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAES 198
Cdd:PRK13295 39 DKTAVTAVRLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 199 LCERILDSSCSLLITTDAFyrgeklvnlkeladeslekcreKGFpvrccivvkhvgraelgmnDSPSQSPPVKRQCPDVQ 278
Cdd:PRK13295 119 LSFMLKHAESKVLVVPKTF----------------------RGF-------------------DHAAMARRLRPELPALR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 279 ---ISWNEGVDLW--------WhELMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPKGVVHT----IGGYMLYVATtfky 343
Cdd:PRK13295 158 hvvVVGGDGADSFeallitpaW-EQEPDAPAILARLRPGPDDVTQLIYTSGTTGEPKGVMHTantlMANIVPYAER---- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 344 vFDFHPEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEgiptYPDESRLWSIVDKYKVTkFYTAPTAirMLMKFGDep 423
Cdd:PRK13295 233 -LGLGADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQD----IWDPARAAELIRTEGVT-FTMASTP--FLTDLTR-- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 424 VTKHSR---ASLQVLGTVGEPINP----EAWlwyhRVVGSQhcpIVDTFWQTETGGHMLTpLPGATPMKPG-SASFPFFG 495
Cdd:PRK13295 303 AVKESGrpvSSLRTFLCAGAPIPGalveRAR----AALGAK---IVSAWGMTENGAVTLT-KLDDPDERAStTDGCPLPG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 496 VAPAILNESGEELEGEAEGYLVFKQPwpgimrTIYGNHTRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVS 575
Cdd:PRK13295 375 VEVRVVDADGAPLPAGQIGRLQVRGC------SNFGGYLKRPQLNGTDADGWFDTGDLARIDADGYIRISGRSKDVIIRG 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 576 GHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFS-STLTEELKKQireKIGPIATPDYIQNAPGL 654
Cdd:PRK13295 449 GENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDfEEMVEFLKAQ---KVAKQYIPERLVVRDAL 525
|
570 580
....*....|....*....|
gi 625195332 655 PKTRSGKIMRRVLRKIAQND 674
Cdd:PRK13295 526 PRTPSGKIQKFRLREMLRGE 545
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
136-667 |
5.25e-28 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 117.58 E-value: 5.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 136 ITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITTd 215
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 216 afyrgeklvnlkeladeslekcrekgfpvrccivvkhvgrAELgmndspsqsppvkrqcpdvqiswnegvdlwwhelmqe 295
Cdd:cd05935 81 ----------------------------------------SEL------------------------------------- 83
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 296 agdefepewcdaEDPLFILYTSGSTGKPKGVVHTiGGYMLYVATTFKYVFDFHPEDVFWCTADIGWITGHSYVTYGPLAN 375
Cdd:cd05935 84 ------------DDLALIPYTSGTTGLPKGCMHT-HFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYV 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 376 GATSVLFegipTYPDESRLWSIVDKYKVTKFYTAPTAIRMLMkfGDEPVTKHSRASLQVLGTVGEPInPEAWLwyHRVVG 455
Cdd:cd05935 151 GGTYVLM----ARWDRETALELIEKYKVTFWTNIPTMLVDLL--ATPEFKTRDLSSLKVLTGGGAPM-PPAVA--EKLLK 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 456 SQHCPIVDTFWQTETGGHMLTPLPGAtpMKPGSASFPFFGVAPAILNESGEELEGEAEG-YLVFKQPwpGIMRTiYGNHT 534
Cdd:cd05935 222 LTGLRFVEGYGLTETMSQTHTNPPLR--PKLQCLGIP*FGVDARVIDIETGRELPPNEVgEIVVRGP--QIFKG-YWNRP 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 535 RFETTYFKKFPG--YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLY 612
Cdd:cd05935 297 EETEESFIEIKGrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVK 376
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 625195332 613 CFVTLCDGhtFSSTLTEE-LKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 667
Cdd:cd05935 377 AFIVLRPE--YRGKVTEEdIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
112-668 |
9.47e-28 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 117.87 E-value: 9.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 112 VHEKKLGDKVAFYWegnePGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVF 191
Cdd:PRK13391 5 IHAQTTPDKPAVIM----ASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 192 AGFSAESLCERILDSSCSLLITTDAFYrgeklvnlkELADESLEKCrekgfP-VRCCIVVKHVGRAElGMNDSPsqspPV 270
Cdd:PRK13391 81 SHLTPAEAAYIVDDSGARALITSAAKL---------DVARALLKQC-----PgVRHRLVLDGDGELE-GFVGYA----EA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 271 KRQCPDVQI-SWNEGVDLwwhelmqeagdefepewcdaedplfiLYTSGSTGKPKGVV----HTIGGYMLYVATTFKYVF 345
Cdd:PRK13391 142 VAGLPATPIaDESLGTDM--------------------------LYSSGTTGRPKGIKrplpEQPPDTPLPLTAFLQRLW 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 346 DFHPEDVFWCTADIGwitgHSyvtyGPLA-------NGATSVLFEGIptypDESRLWSIVDKYKVTKFYTAPTA-IRMLm 417
Cdd:PRK13391 196 GFRSDMVYLSPAPLY----HS----APQRavmlvirLGGTVIVMEHF----DAEQYLALIEEYGVTHTQLVPTMfSRML- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 418 KFGDEPVTKHSRASLQVLGTVGEPINPE------AWlWyhrvvgsqhCPIVDTFWQTETGGhmltplpGATPM------- 484
Cdd:PRK13391 263 KLPEEVRDKYDLSSLEVAIHAAAPCPPQvkeqmiDW-W---------GPIIHEYYAATEGL-------GFTACdseewla 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 485 KPGSASFPFFGVaPAILNESGeelegeaegylvfkQPWP-GIMRTIYgnhtrFET-TYFKKF-------------PGYYV 549
Cdd:PRK13391 326 HPGTVGRAMFGD-LHILDDDG--------------AELPpGEPGTIW-----FEGgRPFEYLndpaktaearhpdGTWST 385
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 550 TGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSSTLTE 629
Cdd:PRK13391 386 VGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPALAA 465
|
570 580 590
....*....|....*....|....*....|....*....
gi 625195332 630 ELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:PRK13391 466 ELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLR 504
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
119-668 |
1.31e-27 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 116.70 E-value: 1.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 119 DKVAFYWEGNEpgettkITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAES 198
Cdd:cd17649 2 DAVALVFGDQS------LSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 199 LCERILDSSCSLLITtdafyrgeklvnlkeladeslekcrekgfpvrccivvkhvgraelgmndspsQSPpvkrqcpdvq 278
Cdd:cd17649 76 LRYMLEDSGAGLLLT----------------------------------------------------HHP---------- 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 279 iswnegvdlwwhelmqeagdefepewcdaEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYvFDFHPEDVFWCTAD 358
Cdd:cd17649 94 -----------------------------RQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAER-YGLTPGDRELQFAS 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 359 IGWITGHSYVtYGPLANGAtSVLFEGIPTYPDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEpVTKHSRASLQVLGTV 438
Cdd:cd17649 144 FNFDGAHEQL-LPPLICGA-CVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEADR-TGDGRPPSLRLYIFG 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 439 GEPINPE-AWLWyhrvvGSQHCPIVDTFWQTETgghMLTPL--PGATPMKPGSASFP----FFGVAPAILNESGEELEGE 511
Cdd:cd17649 221 GEALSPElLRRW-----LKAPVRLFNAYGPTEA---TVTPLvwKCEAGAARAGASMPigrpLGGRSAYILDADLNPVPVG 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 512 AEGYLVFKQPwpGIMRtiyGNHTRFETTYfKKF-------PG--YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTA 582
Cdd:cd17649 293 VTGELYIGGE--GLAR---GYLGRPELTA-ERFvpdpfgaPGsrLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELG 366
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 583 EVESALVEHEAVAEAAVVGHPHPVkGECLYCFVTLCDGHTFSSTLtEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKI 662
Cdd:cd17649 367 EIEAALLEHPGVREAAVVALDGAG-GKQLVAYVVLRAAAAQPELR-AQLRTALRASLPDYMVPAHLVFLARLPLTPNGKL 444
|
....*.
gi 625195332 663 MRRVLR 668
Cdd:cd17649 445 DRKALP 450
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
115-667 |
3.30e-27 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 115.76 E-value: 3.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 115 KKLGDKVAFYWEGnepgetTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGF 194
Cdd:cd12117 8 ARTPDAVAVVYGD------RSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 195 SAESLCERILDSSCSLLITtdafyrgeklvnlkelaDESLEKcrekGFPVRCCIVVKHVGRAElgmndSPSQSPPVKrqc 274
Cdd:cd12117 82 PAERLAFMLADAGAKVLLT-----------------DRSLAG----RAGGLEVAVVIDEALDA-----GPAGNPAVP--- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 275 pdvqiswnegvdlwwhelmqeagdefepewCDAEDPLFILYTSGSTGKPKGVVHTIGGyMLYVATTFKYVfDFHPEDVFW 354
Cdd:cd12117 133 ------------------------------VSPDDLAYVMYTSGSTGRPKGVAVTHRG-VVRLVKNTNYV-TLGPDDRVL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 355 CTADIGWiTGHSYVTYGPLANGATSVLFEGiPTYPDESRLWSIVDKYKVTK-FYTAP-------TAIRMLmkfgdepvtk 426
Cdd:cd12117 181 QTSPLAF-DASTFEIWGALLNGARLVLAPK-GTLLDPDALGALIAEEGVTVlWLTAAlfnqladEDPECF---------- 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 427 hsrASLQVLGTVGEPINPEawlWYHRVVgsQHCP---IVDTFWQTETGG----HMLTPL-PGATPMKPGSasfPFFGVAP 498
Cdd:cd12117 249 ---AGLRELLTGGEVVSPP---HVRRVL--AACPglrLVNGYGPTENTTfttsHVVTELdEVAGSIPIGR---PIANTRV 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 499 AILNesgeelegeaegylVFKQPWP-GIMRTIY--------GNHTRFETTYfKKF------PG--YYVTGDGCRRDQDGY 561
Cdd:cd12117 318 YVLD--------------EDGRPVPpGVPGELYvggdglalGYLNRPALTA-ERFvadpfgPGerLYRTGDLARWLPDGR 382
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 562 YWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTfsstlTEELKKQIREKIGP 641
Cdd:cd12117 383 LEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGALD-----AAELRAFLRERLPA 457
|
570 580
....*....|....*....|....*.
gi 625195332 642 IATPDYIQNAPGLPKTRSGKIMRRVL 667
Cdd:cd12117 458 YMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
130-667 |
6.68e-27 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 114.91 E-value: 6.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 130 PGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERI-LDSSC 208
Cdd:cd05923 23 PARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIeRGEMT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 209 SLLITTDAfyrgeklvnlkELADESlekcreKGFPVRCCIVVKHVGraeLGMNDSpsqsppvkrqcpdvqiswnegvdlw 288
Cdd:cd05923 103 AAVIAVDA-----------QVMDAI------FQSGVRVLALSDLVG---LGEPES------------------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 289 whelmqeAGDEFEPEWCDAEDPLFILYTSGSTGKPKGVV---HTIGGYMLYVATTFKYVFDFHpeDVFWCTADIGWITGH 365
Cdd:cd05923 138 -------AGPLIEDPPREPEQPAFVFYTSGTTGLPKGAVipqRAAESRVLFMSTQAGLRHGRH--NVVLGLMPLYHVIGF 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 366 SYVTYGPLANGATSVLfegiPTYPDESRLWSIVDKYKVTKFYTAPTAIRMLMkfGDEPVTKHSRASLQVLGTVGEPInPE 445
Cdd:cd05923 209 FAVLVAALALDGTYVV----VEEFDPADALKLIEQERVTSLFATPTHLDALA--AAAEFAGLKLSSLRHVTFAGATM-PD 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 446 AWLwyHRVVGSQHCPIVDTFWQTETGGHMLTPLPGA-TPMKPGsasfpFFG---VAPaILNESGEELEGEAEGYLVFKQP 521
Cdd:cd05923 282 AVL--ERVNQHLPGEKVNIYGTTEAMNSLYMRDARTgTEMRPG-----FFSevrIVR-IGGSPDEALANGEEGELIVAAA 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 522 ----WPGIMRtiygnhtRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEA 597
Cdd:cd05923 354 adaaFTGYLN-------QPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEV 426
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 625195332 598 AVVGHPHPVKGECLYCFVTLCDGhtfssTLTEELKKQ--IREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 667
Cdd:cd05923 427 VVIGVADERWGQSVTACVVPREG-----TLSADELDQfcRASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
313-669 |
7.37e-27 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 113.60 E-value: 7.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 313 ILYTSGSTGKPKGVVHTIGGYmLYVATTFKYVFDFHPEDVFWCTADIGWITGHSYVTYGpLANGATSVLFEGIptypDES 392
Cdd:cd05912 82 IMYTSGTTGKPKGVQQTFGNH-WWSAIGSALNLGLTEDDNWLCALPLFHISGLSILMRS-VIYGMTVYLVDKF----DAE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 393 RLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVTKHSRASLqvLGtvGEPInPEAWLwyhrvvgsQHC-----PIVDTFWQ 467
Cdd:cd05912 156 QVLHLINSGKVTIISVVPTMLQRLLEILGEGYPNNLRCIL--LG--GGPA-PKPLL--------EQCkekgiPVYQSYGM 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 468 TETGGHMLTPLPGATPMKPGSASFPFFGVAPAILNESGEELEGEAegyLVFKQPwpGIMRTIYG----NHTRFETTYFKk 543
Cdd:cd05912 223 TETCSQIVTLSPEDALNKIGSAGKPLFPVELKIEDDGQPPYEVGE---ILLKGP--NVTKGYLNrpdaTEESFENGWFK- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 544 fpgyyvTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLcdghtf 623
Cdd:cd05912 297 ------TGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVS------ 364
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 625195332 624 SSTLT-EELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:cd05912 365 ERPISeEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
118-667 |
1.08e-26 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 114.29 E-value: 1.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 118 GDKVAFYWEGnepgetTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAE 197
Cdd:cd17646 12 PDAPAVVDEG------RTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 198 SLCERILDSSCSLLITT-DAFYRGEKLVNLKELADESLekcrekgfpvrccivvkhvgraelgmnDSPSQSPPVKRQCPD 276
Cdd:cd17646 86 RLAYMLADAGPAVVLTTaDLAARLPAGGDVALLGDEAL---------------------------AAPPATPPLVPPRPD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 277 vqiswnegvdlwwhelmqeagdefepewcdaeDPLFILYTSGSTGKPKGVV---HTIGGYMLYvattFKYVFDFHPEDVF 353
Cdd:cd17646 139 --------------------------------NLAYVIYTSGSTGRPKGVMvthAGIVNRLLW----MQDEYPLGPGDRV 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 354 WCTADIG-----WitghsyVTYGPLANGATSVLFE----GIPTYpdesrLWSIVDKYKVTKFYTAPTairMLMKFGDEPv 424
Cdd:cd17646 183 LQKTPLSfdvsvW------ELFWPLVAGARLVVARpgghRDPAY-----LAALIREHGVTTCHFVPS---MLRVFLAEP- 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 425 TKHSRASLQVLGTVGEPINPEAWLWYHRVVgsqHCPIVDTFWQTET----------GGHMLTPLPGATPMkPGSASFpff 494
Cdd:cd17646 248 AAGSCASLRRVFCSGEALPPELAARFLALP---GAELHNLYGPTEAaidvthwpvrGPAETPSVPIGRPV-PNTRLY--- 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 495 gVAPAILNEsgeelegeaegylvfkQPwPGIMRTIY--------GNHTRFETTYfKKF------PG--YYVTGDGCRRDQ 558
Cdd:cd17646 321 -VLDDALRP----------------VP-VGVPGELYlggvqlarGYLGRPALTA-ERFvpdpfgPGsrMYRTGDLARWRP 381
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 559 DGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTfsSTLTEELKKQIREK 638
Cdd:cd17646 382 DGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAA--GPDTAALRAHLAER 459
|
570 580
....*....|....*....|....*....
gi 625195332 639 IGPIATPDYIQNAPGLPKTRSGKIMRRVL 667
Cdd:cd17646 460 LPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
119-669 |
1.56e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 114.49 E-value: 1.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 119 DKVAFYWEGNEpgettkITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAES 198
Cdd:PRK07786 32 DAPALRFLGNT------TTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 199 LCERILDSSCSLLITTDAfyrgekLVNLKELADESLekcrekgfPVRCCIVVkhVGRAelgmndspsqsppvkrqcpdvq 278
Cdd:PRK07786 106 IAFLVSDCGAHVVVTEAA------LAPVATAVRDIV--------PLLSTVVV--AGGS---------------------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 279 iswNEGVDLWWHELMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPKGVV--HT-IGGYMLYVATTFKYvfdFHPEDVFWC 355
Cdd:PRK07786 148 ---SDDSVLGYEDLLAEAGPAHAPVDIPNDSPALIMYTSGTTGRPKGAVltHAnLTGQAMTCLRTNGA---DINSDVGFV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 356 TADIGWITGhsyvtygpLANGATSVLFeGIPT--YP----DESRLWSIVDKYKVTKFYTAPTAIRMLMkfgDEPVTKHSR 429
Cdd:PRK07786 222 GVPLFHIAG--------IGSMLPGLLL-GAPTviYPlgafDPGQLLDVLEAEKVTGIFLVPAQWQAVC---AEQQARPRD 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 430 ASLQVLGTVGEPiNPEAWL--WYHRVVGSQhcpIVDTFWQTEtgghmLTPLpgaTPM--------KPGSASFPFFGVAPA 499
Cdd:PRK07786 290 LALRVLSWGAAP-ASDTLLrqMAATFPEAQ---ILAAFGQTE-----MSPV---TCMllgedairKLGSVGKVIPTVAAR 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 500 ILNESGEELEGEAEGYLVFKQPwpgIMRTIYGNHTRFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLL 579
Cdd:PRK07786 358 VVDENMNDVPVGEVGEIVYRAP---TLMSGYWNNPEATAEAFAG--GWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENI 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 580 STAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfSSTLT-EELKKQIREKIGPIATPDYIQNAPGLPKTR 658
Cdd:PRK07786 433 YCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRND---DAALTlEDLAEFLTDRLARYKHPKALEIVDALPRNP 509
|
570
....*....|.
gi 625195332 659 SGKIMRRVLRK 669
Cdd:PRK07786 510 AGKVLKTELRE 520
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
135-671 |
1.92e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 114.48 E-value: 1.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 135 KITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITT 214
Cdd:PRK12583 45 RYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 215 DAFyRGEKLVN-----LKELADESLEKCREKGFPVRCCIVVkhvgraeLGMNDSPSQsppvkrqcpdvqiswnegvdLWW 289
Cdd:PRK12583 125 DAF-KTSDYHAmlqelLPGLAEGQPGALACERLPELRGVVS-------LAPAPPPGF--------------------LAW 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 290 HELmQEAGDEFEPE-------WCDAEDPLFILYTSGSTGKPKGVV---HTI--GGYMLYVAttfkyvFDFHPEDVFWCTA 357
Cdd:PRK12583 177 HEL-QARGETVSREalaerqaSLDRDDPINIQYTSGTTGFPKGATlshHNIlnNGYFVAES------LGLTEHDRLCVPV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 358 DIGWITGHSYVTYGPLANGATsVLFEGIPTYPDESrlWSIVDKYKVTKFYTAPTairMLMKFGDEPvtKHSRASLQVLGT 437
Cdd:PRK12583 250 PLYHCFGMVLANLGCMTVGAC-LVYPNEAFDPLAT--LQAVEEERCTALYGVPT---MFIAELDHP--QRGNFDLSSLRT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 438 ---VGEPINPEAwlwYHRVVGSQHCP-IVDTFWQTETGGhmLTPLPGAT-PMKPGSASF----PFFGVApaILNESGEEL 508
Cdd:PRK12583 322 gimAGAPCPIEV---MRRVMDEMHMAeVQIAYGMTETSP--VSLQTTAAdDLERRVETVgrtqPHLEVK--VVDPDGATV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 509 EGEAEGYLVFKqpwpG--IMRTIYGNHTRFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVES 586
Cdd:PRK12583 395 PRGEIGELCTR----GysVMKGYWNNPEATAESIDED--GWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEE 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 587 ALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSStltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRV 666
Cdd:PRK12583 469 FLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASE---EELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFR 545
|
....*
gi 625195332 667 LRKIA 671
Cdd:PRK12583 546 MREIS 550
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
132-605 |
2.48e-26 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 115.72 E-value: 2.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 132 ETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGAlhsivfA------GFSAESLcERIL- 204
Cdd:COG1020 498 GDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGA------AyvpldpAYPAERL-AYMLe 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 205 DSSCSLLITTDAFyrgeklvnLKELADESLEkcrekgfpvrcCIVVkhvgrAELGMNDSPSQSPPVKRqcpdvqiswneg 284
Cdd:COG1020 571 DAGARLVLTQSAL--------AARLPELGVP-----------VLAL-----DALALAAEPATNPPVPV------------ 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 285 vdlwwhelmqeagdefepewcDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYvFDFHPEDVF-WCTA---DIG 360
Cdd:COG1020 615 ---------------------TPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRR-YGLGPGDRVlQFASlsfDAS 672
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 361 witghsyVT--YGPLANGATSVLfegiptYPDESR-----LWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVtkhsrASLQ 433
Cdd:COG1020 673 -------VWeiFGALLSGATLVL------APPEARrdpaaLAELLARHRVTVLNLTPSLLRALLDAAPEAL-----PSLR 734
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 434 VLGTVGEPINPEAWLWYHRVVGsqHCPIVDTFWQTETG----GHMLTPLPGATPMKP-GSasfPFFGVAPAILNEsgeel 508
Cdd:COG1020 735 LVLVGGEALPPELVRRWRARLP--GARLVNLYGPTETTvdstYYEVTPPDADGGSVPiGR---PIANTRVYVLDA----- 804
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 509 egeaegylvFKQPWP-GIMRTIY--------GNHTRFETT--YF----KKFPG--YYVTGDGCRRDQDG---YywiTGRI 568
Cdd:COG1020 805 ---------HLQPVPvGVPGELYiggaglarGYLNRPELTaeRFvadpFGFPGarLYRTGDLARWLPDGnleF---LGRA 872
|
490 500 510
....*....|....*....|....*....|....*..
gi 625195332 569 DDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHP 605
Cdd:COG1020 873 DDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDA 909
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
132-667 |
1.08e-25 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 110.87 E-value: 1.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 132 ETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLL 211
Cdd:cd12115 21 GDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 212 ITtdafyrgeklvnlkeladeslekcrekgfpvrccivvkhvgraelgmndspsqsppvkrqcpdvqiswnegvdlwwhe 291
Cdd:cd12115 101 LT------------------------------------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 292 lmqeagdefepewcDAEDPLFILYTSGSTGKPKGVVHTIGGymlyvATTFkyvfdfhpedVFWCTADIG--WITGHSYVT 369
Cdd:cd12115 103 --------------DPDDLAYVIYTSGSTGRPKGVAIEHRN-----AAAF----------LQWAAAAFSaeELAGVLAST 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 370 -----------YGPLANGATSVLFEGIPTYPDESRLwsivdkYKVTKFYTAPTAIRMLMKFGDEPvtkhsrASLQVLGTV 438
Cdd:cd12115 154 sicfdlsvfelFGPLATGGKVVLADNVLALPDLPAA------AEVTLINTVPSAAAELLRHDALP------ASVRVVNLA 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 439 GEPINPEAwlwYHRVVGSQHC--------PIVDTFWQTetgGHMLTPLPGATPmkpgSASFPFFGVAPAILNEsgeeleg 510
Cdd:cd12115 222 GEPLPRDL---VQRLYARLQVervvnlygPSEDTTYST---VAPVPPGASGEV----SIGRPLANTQAYVLDR------- 284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 511 eaegylvFKQPWP-GIMRTIY-GNHT--------------RFETTYFkkFPG--YYVTGDGCRRDQDGYYWITGRIDDML 572
Cdd:cd12115 285 -------ALQPVPlGVPGELYiGGAGvargylgrpgltaeRFLPDPF--GPGarLYRTGDLVRWRPDGLLEFLGRADNQV 355
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 573 NVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfSSTLTEELKKQIREKIGPIATPDYIQNAP 652
Cdd:cd12115 356 KVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPG---AAGLVEDLRRHLGTRLPAYMVPSRFVRLD 432
|
570
....*....|....*
gi 625195332 653 GLPKTRSGKIMRRVL 667
Cdd:cd12115 433 ALPLTPNGKIDRSAL 447
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
291-669 |
1.48e-25 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 110.85 E-value: 1.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 291 ELMQEAGDEFEPEWCDAE-DPLFILYTSGSTGKPKGVVHTIGGYMLyVATTFKYVFDFHPEDVFWCTADI----GWItgh 365
Cdd:cd12118 115 DLLAEGDPDFEWIPPADEwDPIALNYTSGTTGRPKGVVYHHRGAYL-NALANILEWEMKQHPVYLWTLPMfhcnGWC--- 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 366 syVTYGPLANGATSVLFEGIptypDESRLWSIVDKYKVTKFYTAPTAIRMLMKfGDEPVTKHSRASLQVLgTVGEPiNPE 445
Cdd:cd12118 191 --FPWTVAAVGGTNVCLRKV----DAKAIYDLIEKHKVTHFCGAPTVLNMLAN-APPSDARPLPHRVHVM-TAGAP-PPA 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 446 AWLWYHRVVGSQhcpIVDTFWQTETGGhmltplPGAT-PMKPGSASFPffGVAPAILNESGEELEGEAEGYLVFKQ---- 520
Cdd:cd12118 262 AVLAKMEELGFD---VTHVYGLTETYG------PATVcAWKPEWDELP--TEERARLKARQGVRYVGLEEVDVLDPetmk 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 521 --PWPG------------IMRTIYGNHtrfETTYfKKFP-GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVE 585
Cdd:cd12118 331 pvPRDGktigeivfrgniVMKGYLKNP---EATA-EAFRgGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVE 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 586 SALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfSSTLTEELKKQIREKIGPIATPDYIQNAPgLPKTRSGKIMRR 665
Cdd:cd12118 407 GVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEG---AKVTEEEIIAFCREHLAGFMVPKTVVFGE-LPKTSTGKIQKF 482
|
....
gi 625195332 666 VLRK 669
Cdd:cd12118 483 VLRD 486
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
131-670 |
2.03e-25 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 110.72 E-value: 2.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 131 GETTKITYRELLVQVCQFSNVLRKQ-GIQKGDRVAIYMPMILELVVAMLACARLGALhSIVFagfsaeslcerildsscs 209
Cdd:PRK06839 23 TEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECI-AVPL------------------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 210 llittdafyrgeklvNLKELADESLEKCREKGFPVRCCivVKHVGRAELGMNDSPSQSPPVkrqcpdvqisWNEGVDlww 289
Cdd:PRK06839 84 ---------------NIRLTENELIFQLKDSGTTVLFV--EKTFQNMALSMQKVSYVQRVI----------SITSLK--- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 290 hELMQEAGDEFEPEwcDAEDPLFILYTSGSTGKPKGVVHTIGGyMLYVATTFKYVFDFHPEDVFWCTADIGWITGHSYVT 369
Cdd:PRK06839 134 -EIEDRKIDNFVEK--NESASFIICYTSGTTGKPKGAVLTQEN-MFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 370 YGPLANGATSVlfegIPTYPDESRLWSIVDKYKVTKFYTAPT---AIRMLMKFgdepvTKHSRASLQVLGTVGEPInPEA 446
Cdd:PRK06839 210 FPTLFAGGVII----VPRKFEPTKALSMIEKHKVTVVMGVPTihqALINCSKF-----ETTNLQSVRWFYNGGAPC-PEE 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 447 WLwyhRVVGSQHCPIVDTFWQTETGGHMLTPLPGATPMKPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpGIM 526
Cdd:PRK06839 280 LM---REFIDRGFLFGQGFGMTETSPTVFMLSEEDARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGP--NVM 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 527 RTIYGNHTRFETTYFKkfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPV 606
Cdd:PRK06839 355 KEYWNRPDATEETIQD---GWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVK 431
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 625195332 607 KGECLYCFVTLCDGhtfSSTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKI 670
Cdd:PRK06839 432 WGEIPIAFIVKKSS---SVLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQ 492
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
131-601 |
2.03e-25 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 109.99 E-value: 2.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 131 GETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESlCERIL-DSSCS 209
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQ-IAYILnDSEAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 210 LLITTDAfyrgeklvnlkeladeslekcrekgfpvrccivvkhvgraelgmndspsqsppvkrqcpdvqiswnegvdlww 289
Cdd:cd05907 80 ALFVEDP------------------------------------------------------------------------- 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 290 helmqeagdefepewcdaEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYVfDFHPEDVFWCTADIGWITGHSYVT 369
Cdd:cd05907 87 ------------------DDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERL-PATEGDRHLSFLPLAHVFERRAGL 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 370 YGPLANGATSVLFEGIPTYPDESRlwsivdKYKVTKFYTAPT---AIRMLMKFGDEP------VTKHSRASLQVLGTVGE 440
Cdd:cd05907 148 YVPLLAGARIYFASSAETLLDDLS------EVRPTVFLAVPRvweKVYAAIKVKAVPglkrklFDLAVGGRLRFAASGGA 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 441 PINPEAWLWYHRvVGsqhCPIVDTFWQTETGGHMLTPLPGATpmKPGSASFPFFGVAPAILNESGeelegeaegyLVFKQ 520
Cdd:cd05907 222 PLPAELLHFFRA-LG---IPVYEGYGLTETSAVVTLNPPGDN--RIGTVGKPLPGVEVRIADDGE----------ILVRG 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 521 pwPGIMRTIYGN--HTRFETTYfkkfPGYYVTGDGCRRDQDGYYWITGRIDDML-NVSGHLLSTAEVESALVEHEAVAEA 597
Cdd:cd05907 286 --PNVMLGYYKNpeATAEALDA----DGWLHTGDLGEIDEDGFLHITGRKKDLIiTSGGKNISPEPIENALKASPLISQA 359
|
....
gi 625195332 598 AVVG 601
Cdd:cd05907 360 VVIG 363
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
107-602 |
2.05e-25 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 111.35 E-value: 2.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 107 VLDRNVheKKLGDKVAFYWEGNepGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGAL 186
Cdd:COG1022 16 LLRRRA--ARFPDRVALREKED--GIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 187 HSIVFAGFSAESLcERIL-DSSCSLLITTDAfyrgEKLVNLKELADE--SLEKcrekgfpvrccIVVkhvgraelgMNds 263
Cdd:COG1022 92 TVPIYPTSSAEEV-AYILnDSGAKVLFVEDQ----EQLDKLLEVRDElpSLRH-----------IVV---------LD-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 264 psqsPPVKRQCPDVqiswnegvdLWWHELMQEAGDEFEPEW-------CDAEDPLFILYTSGSTGKPKGVVHTIGGyMLY 336
Cdd:COG1022 145 ----PRGLRDDPRL---------LSLDELLALGREVADPAElearraaVKPDDLATIIYTSGTTGRPKGVMLTHRN-LLS 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 337 VATTFKYVFDFHPEDVF-----WCtadigWITGHSyVTYGPLANGATSVLFEGI-----------PTY----PdesRLW- 395
Cdd:COG1022 211 NARALLERLPLGPGDRTlsflpLA-----HVFERT-VSYYALAAGATVAFAESPdtlaedlrevkPTFmlavP---RVWe 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 396 SIVDKYkVTKFYTAPTAIRML----MKFGdepvTKHSRASLQvlgtvGEPINPEAWLWY---HRVVGSQhcpivdtfWQT 468
Cdd:COG1022 282 KVYAGI-QAKAEEAGGLKRKLfrwaLAVG----RRYARARLA-----GKSPSLLLRLKHalaDKLVFSK--------LRE 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 469 ETGGHMLTPLPGATPMKPGSASFpFFGV--------------APAILNESGEelegeaegylvFK-----QPWPG----- 524
Cdd:COG1022 344 ALGGRLRFAVSGGAALGPELARF-FRALgipvlegygltetsPVITVNRPGD-----------NRigtvgPPLPGvevki 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 525 ------------IMRtiyGnhtrfettYFKKfP----------GYYVTGD-GcRRDQDGYYWITGRIDDMLNVS-GHLLS 580
Cdd:COG1022 412 aedgeilvrgpnVMK---G--------YYKN-PeataeafdadGWLHTGDiG-ELDEDGFLRITGRKKDLIVTSgGKNVA 478
|
570 580
....*....|....*....|..
gi 625195332 581 TAEVESALVEHEAVAEAAVVGH 602
Cdd:COG1022 479 PQPIENALKASPLIEQAVVVGD 500
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
131-672 |
3.32e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 110.22 E-value: 3.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 131 GETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSL 210
Cdd:PRK06164 31 DEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARW 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 211 LITTDAFyRGEKLVN-LKELADESLEkcrekgfPVRCCIVVkhvgraELGMNDSPSQSPPVKRQCPDVqiswnegvdlww 289
Cdd:PRK06164 111 LVVWPGF-KGIDFAAiLAAVPPDALP-------PLRAIAVV------DDAADATPAPAPGARVQLFAL------------ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 290 hELMQEAGDEFEPEwcDAEDPLFILY-TSGSTGKPKGVVHTIGGyMLYVATTFKYVFDFHPEDVFWCTADIGWITGHSYV 368
Cdd:PRK06164 165 -PDPAPPAAAGERA--ADPDAGALLFtTSGTTSGPKLVLHRQAT-LLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 369 TyGPLANGATSVLfegIPTYpDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPvtkHSRASLQVLGTVGepINPeAWL 448
Cdd:PRK06164 241 L-GALAGGAPLVC---EPVF-DAARTARALRRHRVTHTFGNDEMLRRILDTAGER---ADFPSARLFGFAS--FAP-ALG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 449 WYHRVVGSQHCPIVDTFWQTE-----TGGHMLTP-----LPGATPMKPGSASFPFFGVAPAILNESGEELEGEAEgylvf 518
Cdd:PRK06164 310 ELAALARARGVPLTGLYGSSEvqalvALQPATDPvsvriEGGGRPASPEARVRARDPQDGALLPDGESGEIEIRA----- 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 519 kqpwPGIMRTIYGN--HTRFETTYfkkfPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAE 596
Cdd:PRK06164 385 ----PSLMRGYLDNpdATARALTD----DGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAA 456
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 625195332 597 AAVVGHPHPVKGEClYCFVTLCDGhtfSSTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSG---KIMRRVLRKIAQ 672
Cdd:PRK06164 457 AQVVGATRDGKTVP-VAFVIPTDG---ASPDEAGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLREMAQ 531
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
131-668 |
3.65e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 109.99 E-value: 3.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 131 GETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSL 210
Cdd:PRK08276 7 PSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 211 LITTDAFyrgekLVNLKELADESlekcrEKGFPVRccivvkHVGRAELgmndspsqsppvkrqcpdvqiswnEGVDLWWH 290
Cdd:PRK08276 87 LIVSAAL-----ADTAAELAAEL-----PAGVPLL------LVVAGPV------------------------PGFRSYEE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 291 ELMQEAGDEFEPEWCDAEdplfILYTSGSTGKPKGV--------VHTIGGYMLYVATTFkyvFDFHPEDVFWCTADIGwi 362
Cdd:PRK08276 127 ALAAQPDTPIADETAGAD----MLYSSGTTGRPKGIkrplpgldPDEAPGMMLALLGFG---MYGGPDSVYLSPAPLY-- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 363 tgHSYVT-YG--PLANGATSVLFEGIptypDESRLWSIVDKYKVTKFYTAPTA-IRMLmKFGDEPVTKHSRASLQVLGTV 438
Cdd:PRK08276 198 --HTAPLrFGmsALALGGTVVVMEKF----DAEEALALIERYRVTHSQLVPTMfVRML-KLPEEVRARYDVSSLRVAIHA 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 439 GEPINPE------AWlWyhrvvGsqhcPIVD-TFWQTETGGHMLtplpgATPM----KPGSASFPFFGVApAILNESGEE 507
Cdd:PRK08276 271 AAPCPVEvkramiDW-W-----G----PIIHeYYASSEGGGVTV-----ITSEdwlaHPGSVGKAVLGEV-RILDEDGNE 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 508 LEGEAEGYLVFKQPWPGImrTIYGNHTRFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLnVSGHL-LSTAEVES 586
Cdd:PRK08276 335 LPPGEIGTVYFEMDGYPF--EYHNDPEKTAAARNPH--GWVTVGDVGYLDEDGYLYLTDRKSDMI-ISGGVnIYPQEIEN 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 587 ALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSSTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRV 666
Cdd:PRK08276 410 LLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRR 489
|
..
gi 625195332 667 LR 668
Cdd:PRK08276 490 LR 491
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
134-667 |
6.31e-25 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 108.95 E-value: 6.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 134 TKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALhsIVFAGFSaeslcerildsscsllit 213
Cdd:cd05920 39 RRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAV--PVLALPS------------------ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 214 tdafYRGEKLVNLKELADeslekcrekgfpvrcciVVKHVGRAELGMNDSPSQSPPVKRQCPDVQiswnegvdlwwhelm 293
Cdd:cd05920 99 ----HRRSELSAFCAHAE-----------------AVAYIVPDRHAGFDHRALARELAESIPEVA--------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 294 qeagdefepewcdaedplFILYTSGSTGKPKGVVHTIGGYmLYVATTFKYVFDFHPEDVFWCTADIGwitgHSYVTYGP- 372
Cdd:cd05920 143 ------------------LFLLSGGTTGTPKLIPRTHNDY-AYNVRASAEVCGLDQDTVYLAVLPAA----HNFPLACPg 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 373 ----LANGATSVLfegiPTYPDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPvtKHSRASLQVLGTVGEPINPEAWL 448
Cdd:cd05920 200 vlgtLLAGGRVVL----APDPSPDAAFPLIEREGVTVTALVPALVSLWLDAAASR--RADLSSLRLLQVGGARLSPALAR 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 449 WYHRVVGsqhCPIVDTFWQTE-----------------TGGHMLTPL-------PGATPMKPGSASfpffgvapailnes 504
Cdd:cd05920 274 RVPPVLG---CTLQQVFGMAEgllnytrlddpdeviihTQGRPMSPDdeirvvdEEGNPVPPGEEG-------------- 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 505 geelegeaegYLVFKQPWpgimrTIYG-------NHTRFETTyfkkfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGH 577
Cdd:cd05920 337 ----------ELLTRGPY-----TIRGyyrapehNARAFTPD------GFYRTGDLVRRTPDGYLVVEGRIKDQINRGGE 395
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 578 LLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDghtfSSTLTEELKKQIREKigPIAT---PDYIQNAPGL 654
Cdd:cd05920 396 KIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRD----PPPSAAQLRRFLRER--GLAAyklPDRIEFVDSL 469
|
570
....*....|...
gi 625195332 655 PKTRSGKIMRRVL 667
Cdd:cd05920 470 PLTAVGKIDKKAL 482
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
309-669 |
8.44e-25 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 108.15 E-value: 8.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 309 DPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYvFDFHPEDVFWCTADIGWITGHSYVTYGPLANGATSV-------- 380
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAANVRALVDA-WRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEflpkfdpk 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 381 ------------LFEGIPT-YpdeSRLWSIVDkykvtkfyTAPTAIRMLMKFGDEpvtkhsRASLQVLGTVG--EPINPE 445
Cdd:cd05941 169 evaisrlmpsitVFMGVPTiY---TRLLQYYE--------AHFTDPQFARAAAAE------RLRLMVSGSAAlpVPTLEE 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 446 awlWYHRvvgSQHcPIVDTFWQTETGGHMLTPLPGatPMKPGSASFPFFGVAPAIL-NESGEELEGEAEGYLVFKQPwpg 524
Cdd:cd05941 232 ---WEAI---TGH-TLLERYGMTEIGMALSNPLDG--ERRPGTVGMPLPGVQARIVdEETGEPLPRGEVGEIQVRGP--- 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 525 imrtiygnhTRFETtYFKKfP----------GYYVTGDGCRRDQDGYYWITGRI-DDMLNVSGHLLSTAEVESALVEHEA 593
Cdd:cd05941 300 ---------SVFKE-YWNK-PeatkeeftddGWFKTGDLGVVDEDGYYWILGRSsVDIIKSGGYKVSALEIERVLLAHPG 368
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 625195332 594 VAEAAVVGHPHPVKGECLYCFVTLCDGHTfssTLT-EELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:cd05941 369 VSECAVIGVPDPDWGERVVAVVVLRAGAA---ALSlEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
107-669 |
7.56e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 106.24 E-value: 7.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 107 VLDRNVHEkkLGDKVAFYWEGNEpgettkITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGA- 185
Cdd:PRK05605 37 LYDNAVAR--FGDRPALDFFGAT------TTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAv 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 186 --LHSIVFAGFSAESLCE----RIL---DSSCSLLITTDAFYRGEKLVN---------LKELADE-SLEKCREKgfpvrc 246
Cdd:PRK05605 109 vvEHNPLYTAHELEHPFEdhgaRVAivwDKVAPTVERLRRTTPLETIVSvnmiaamplLQRLALRlPIPALRKA------ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 247 civvkhvgRAELgmndspsqSPPVkrqcPDVqISWNEGVDlwwhELMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPKGV 326
Cdd:PRK05605 183 --------RAAL--------TGPA----PGT-VPWETLVD----AAIGGDGSDVSHPRPTPDDVALILYTSGTTGKPKGA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 327 VHTIGGYMLYVATTFKYVFDF--HPEDV------FwctadigwitgHSY-----VTYGPLAnGATSVLFegiPTyPDESR 393
Cdd:PRK05605 238 QLTHRNLFANAAQGKAWVPGLgdGPERVlaalpmF-----------HAYgltlcLTLAVSI-GGELVLL---PA-PDIDL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 394 LWSIVDKYKVTKFYTAPTAIRMLMKFGDEP-VTKHS-RASLQvlGTVGEPInpeawlwyhrvvgsqhcPIVDTfWQTETG 471
Cdd:PRK05605 302 ILDAMKKHPPTWLPGVPPLYEKIAEAAEERgVDLSGvRNAFS--GAMALPV-----------------STVEL-WEKLTG 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 472 GHM-----LT---PLPGATPM----KPGSASFPFFGVAPAILNESGEELEGEAEGY--LVFKQPwpgimRTIYGNHTRFE 537
Cdd:PRK05605 362 GLLvegygLTetsPIIVGNPMsddrRPGYVGVPFPDTEVRIVDPEDPDETMPDGEEgeLLVRGP-----QVFKGYWNRPE 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 538 TTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTL 617
Cdd:PRK05605 437 ETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVL 516
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 625195332 618 CDGHTFSStltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:PRK05605 517 EPGAALDP---EGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVRE 565
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
288-669 |
9.41e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 105.92 E-value: 9.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 288 WWHELMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPKGVVHT-----IGGYMLyvATTFkyvfDFHPEDVFWCTADI--- 359
Cdd:PRK07867 132 WADELAAHRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCThrkvaSAGVML--AQRF----GLGPDDVCYVSMPLfhs 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 360 -----GWITGhsyvtygpLANGATSVL---FEGiptypdeSRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVTKHSraS 431
Cdd:PRK07867 206 navmaGWAVA--------LAAGASIALrrkFSA-------SGFLPDVRRYGATYANYVGKPLSYVLATPERPDDADN--P 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 432 LQVL-GTVGEPINPEAwlwYHRVVGsqhCPIVDTFWQTEtGGHMLTPLPGaTPmkPGSASFPFFGVA-----------PA 499
Cdd:PRK07867 269 LRIVyGNEGAPGDIAR---FARRFG---CVVVDGFGSTE-GGVAITRTPD-TP--PGALGPLPPGVAivdpdtgtecpPA 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 500 ILNESGEELEGEAEGYLVFKQPwPGIMRTIYGNHtrfETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLL 579
Cdd:PRK07867 339 EDADGRLLNADEAIGELVNTAG-PGGFEGYYNDP---EADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENL 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 580 STAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTF-SSTLTEELKKQirEKIGPIATPDYIQNAPGLPKTR 658
Cdd:PRK07867 415 GTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKFdPDAFAEFLAAQ--PDLGPKQWPSYVRVCAELPRTA 492
|
410
....*....|.
gi 625195332 659 SGKIMRRVLRK 669
Cdd:PRK07867 493 TFKVLKRQLSA 503
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
116-668 |
1.44e-23 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 105.15 E-value: 1.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 116 KLGDKVAFYWEgNEPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFS 195
Cdd:PRK08008 19 VYGHKTALIFE-SSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 196 AESlCERILDSS-CSLLITTDAFYrgeklvnlkELADESLekcREKGFPVRCCIVVKHVGRAELGMND---SPSQSPPVK 271
Cdd:PRK08008 98 REE-SAWILQNSqASLLVTSAQFY---------PMYRQIQ---QEDATPLRHICLTRVALPADDGVSSftqLKAQQPATL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 272 RQCPDVQiswnegvdlwwhelmqeagdefepewcdAEDPLFILYTSGSTGKPKGVVHT-----IGGYmlY----VATTFK 342
Cdd:PRK08008 165 CYAPPLS----------------------------TDDTAEILFTSGTTSRPKGVVIThynlrFAGY--YsawqCALRDD 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 343 YVF-----DFHPEdvFWCTADIGWITGhsyvtygplanGATSVLFEgipTYpDESRLWSIVDKYKVTKFYTAPTAIRMLM 417
Cdd:PRK08008 215 DVYltvmpAFHID--CQCTAAMAAFSA-----------GATFVLLE---KY-SARAFWGQVCKYRATITECIPMMIRTLM 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 418 KfgdEPVTKHSRaslqvlgtvgepinpeawlwyhrvvgsQHC--------PIVD----------------TFWQTETGGH 473
Cdd:PRK08008 278 V---QPPSANDR---------------------------QHClrevmfylNLSDqekdafeerfgvrlltSYGMTETIVG 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 474 MLTPLPGATPMKPgSASFPFFGVAPAILNESGEELEGEAEGYLVFK-QPWPGIMRTIYGNHTrfETTYFKKFPGYYVTGD 552
Cdd:PRK08008 328 IIGDRPGDKRRWP-SIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKgVPGKTIFKEYYLDPK--ATAKVLEADGWLHTGD 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 553 GCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSstlTEELK 632
Cdd:PRK08008 405 TGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLS---EEEFF 481
|
570 580 590
....*....|....*....|....*....|....*.
gi 625195332 633 KQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:PRK08008 482 AFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
136-670 |
3.72e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 103.85 E-value: 3.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 136 ITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITTD 215
Cdd:PRK07788 75 LTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKALVYDD 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 216 AFyrgeklVNLKELADESLEKCRekgfpvrccivvkhvgraelGMNDSPSQSPPVKRQCPDVQiswnegvdlwwhELMQE 295
Cdd:PRK07788 155 EF------TDLLSALPPDLGRLR--------------------AWGGNPDDDEPSGSTDETLD------------DLIAG 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 296 AGDEFEPEWcdAEDPLFILYTSGSTGKPKGVVH-------TIGGYMLYVAttfkyvfdFHPEDVFWCTADIGWITGHSYV 368
Cdd:PRK07788 197 SSTAPLPKP--PKPGGIVILTSGTTGTPKGAPRpepsplaPLAGLLSRVP--------FRAGETTLLPAPMFHATGWAHL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 369 TYGpLANGATSVL---FegiptypDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVTKHSRASLQVLGTVGEPINPE 445
Cdd:PRK07788 267 TLA-MALGSTVVLrrrF-------DPEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKYDTSSLKIIFVSGSALSPE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 446 AWLWYHRVVGsqhcPIVDTFW-QTETGGHMLtplpgATP----MKPGSASFPFFGVAPAILNESGeelegeaegylvfkQ 520
Cdd:PRK07788 339 LATRALEAFG----PVLYNLYgSTEVAFATI-----ATPedlaEAPGTVGRPPKGVTVKILDENG--------------N 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 521 PWP-GIMRTIY-GNHTRFETtYF-----KKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEA 593
Cdd:PRK07788 396 EVPrGVVGRIFvGNGFPFEG-YTdgrdkQIIDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPD 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 625195332 594 VAEAAVVGHPHPVKGECLYCFVTLCDGhtfsSTLTEE-LKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKI 670
Cdd:PRK07788 475 VVEAAVIGVDDEEFGQRLRAFVVKAPG----AALDEDaIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREM 548
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
289-668 |
3.84e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 103.95 E-value: 3.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 289 WHELMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGgyMLYV---ATTFKYvfDFHPEDVFWCTADIGwitgH 365
Cdd:PRK13388 131 YAELVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHG--RLAFagrALTERF--GLTRDDVCYVSMPLF----H 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 366 S---YVTYGP-LANGATSVLfegiPTYPDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPvtKHSRASLQV-LGTVGE 440
Cdd:PRK13388 203 SnavMAGWAPaVASGAAVAL----PAKFSASGFLDDVRRYGATYFNYVGKPLAYILATPERP--DDADNPLRVaFGNEAS 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 441 PINPEAwlwYHRVVGsqhCPIVDTFWQTETGGhMLTPLPGaTPmkPGSASFPFFGVApaILNESGEelegeaegylvfkQ 520
Cdd:PRK13388 277 PRDIAE---FSRRFG---CQVEDGYGSSEGAV-IVVREPG-TP--PGSIGRGAPGVA--IYNPETL-------------T 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 521 PWPgimRTIYGNHTRF-----------ETTYFKKFPGYYV---------------TGDGCRRDQDGYYWITGRIDDMLNV 574
Cdd:PRK13388 332 ECA---VARFDAHGALlnadeaigelvNTAGAGFFEGYYNnpeataermrhgmywSGDLAYRDADGWIYFAGRTADWMRV 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 575 SGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFS-STLTEELKKQirEKIGPIATPDYIQNAPG 653
Cdd:PRK13388 409 DGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATFDpDAFAAFLAAQ--PDLGTKAWPRYVRIAAD 486
|
410
....*....|....*
gi 625195332 654 LPKTRSGKIMRRVLR 668
Cdd:PRK13388 487 LPSTATNKVLKRELI 501
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
136-668 |
4.28e-23 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 103.68 E-value: 4.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 136 ITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITTD 215
Cdd:PRK13382 69 LTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYDE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 216 AFyrgeklvnlKELADESLEKCrekgfpvrccivvkhvgraelgmndspsqsPPVKRQcpdvqISWNEGVDLWWHELMQE 295
Cdd:PRK13382 149 EF---------SATVDRALADC------------------------------PQATRI-----VAWTDEDHDLTVEVLIA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 296 AGDEFEPEWCDAEDPLfILYTSGSTGKPKGVVHT-IGGYMlyvatTFKYVFDFHPedvfwctadigWITGHSYVTYGPL- 373
Cdd:PRK13382 185 AHAGQRPEPTGRKGRV-ILLTSGTTGTPKGARRSgPGGIG-----TLKAILDRTP-----------WRAEEPTVIVAPMf 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 374 -ANGATSVLFEGIPTYP-------DESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVTKHSRASLQVLGTVGEPINPE 445
Cdd:PRK13382 248 hAWGFSQLVLAASLACTivtrrrfDPEATLDLIDRHRATGLAVVPVMFDRIMDLPAEVRNRYSGRSLRFAAASGSRMRPD 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 446 AWLWYHRVVGSQhcpIVDTFWQTETGghMLTPlpgATP----MKPGSASFPFFGVAPAILNESgeelegeaegylvFKQP 521
Cdd:PRK13382 328 VVIAFMDQFGDV---IYNNYNATEAG--MIAT---ATPadlrAAPDTAGRPAEGTEIRILDQD-------------FREV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 522 WPGIMRTIY-GNHTRFE-----TTyfKKF-PGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAV 594
Cdd:PRK13382 387 PTGEVGTIFvRNDTQFDgytsgST--KDFhDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDV 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 625195332 595 AEAAVVGHPHPVKGECLYCFVTLCDGhtfSSTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:PRK13382 465 AEAAVIGVDDEQYGQRLAAFVVLKPG---ASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQ 535
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
134-671 |
4.28e-22 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 100.10 E-value: 4.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 134 TKITYRELLVQVCQFSNVLRKQGIQkGDRVAIYMPMILELVVAMLACARLGALhsIVFAGFSAEslcERILDSSCSL--- 210
Cdd:cd05909 6 TSLTYRKLLTGAIALARKLAKMTKE-GENVGVMLPPSAGGALANFALALSGKV--PVMLNYTAG---LRELRACIKLagi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 211 --LITTDAFYRGEKLVNLKELADE----SLEKCREK-GFPVRCcivvkhvgRAELGMNDSPSqsppvkrqcpdvqiswne 283
Cdd:cd05909 80 ktVLTSKQFIEKLKLHHLFDVEYDarivYLEDLRAKiSKADKC--------KAFLAGKFPPK------------------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 284 gvdlWWHELMQEAGDefepewcDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKyVFDFHPEDVFWCTADIGWIT 363
Cdd:cd05909 134 ----WLLRIFGVAPV-------QPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITA-IFDPNPEDVVFGALPFFHSF 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 364 GHSYVTYGPLANGAtSVLFEGIPTYPDesRLWSIVDKYKVTKFYTAPTAIRMLMKFgdepVTKHSRASLQVLGTVGEPIN 443
Cdd:cd05909 202 GLTGCLWLPLLSGI-KVVFHPNPLDYK--KIPELIYDKKATILLGTPTFLRGYARA----AHPEDFSSLRLVVAGAEKLK 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 444 PEAW-LWYHRvvgsQHCPIVDTFWQTETGGHMLTPLPgATPMKPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPw 522
Cdd:cd05909 275 DTLRqEFQEK----FGIRILEGYGTTECSPVISVNTP-QSPNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRG- 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 523 PGIMRTIYGNHtrfETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAV-AEAAVVG 601
Cdd:cd05909 349 PNVMLGYLNEP---ELTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEdNEVAVVS 425
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 625195332 602 HPHPVKGECLYCFVTLcdghtfSSTLTEELKKQIRE-KIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 671
Cdd:cd05909 426 VPDGRKGEKIVLLTTT------TDTDPSSLNDILKNaGISNLAKPSYIHQVEEIPLLGTGKPDYVTLKALA 490
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
132-673 |
2.55e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 97.93 E-value: 2.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 132 ETTKITYRELLVQVCQFSNVLRKQGiQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLL 211
Cdd:PRK07638 23 NDRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 212 ITtDAFYrgeklvnlkeladeslekcrekgfpvrccivvkhvgraelgMNDSPSQSPPVkrqcpdvqISWNEgvdlwWHE 291
Cdd:PRK07638 102 VT-ERYK-----------------------------------------LNDLPDEEGRV--------IEIDE-----WKR 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 292 LMQEAGDEFEPEwCDAE-DPLFILYTSGSTGKPKGVVHTIGGYMLYVATTfkyVFDFH--PEDVFWctadigwITG---H 365
Cdd:PRK07638 127 MIEKYLPTYAPI-ENVQnAPFYMGFTSGSTGKPKAFLRAQQSWLHSFDCN---VHDFHmkREDSVL-------IAGtlvH 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 366 SYVTYGplangATSVLFEG-----IPTY-PDESRLWsiVDKYKVTKFYTAPTAIRMLMK---FGDEPVT------KHSRA 430
Cdd:PRK07638 196 SLFLYG-----AISTLYVGqtvhlMRKFiPNQVLDK--LETENISVMYTVPTMLESLYKenrVIENKMKiissgaKWEAE 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 431 SLQVLGTvgepINPEAWLWyhrvvgsqhcpivdTFWQTETGGHMLTPLPGATPMKPGSASFPFFGVAPAILNESGeeleg 510
Cdd:PRK07638 269 AKEKIKN----IFPYAKLY--------------EFYGASELSFVTALVDEESERRPNSVGRPFHNVQVRICNEAG----- 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 511 eaegylvfKQPWPGIMRTIYGNHTRFettyfkkFPGYYVTGDGCRR---------------DQDGYYWITGRIDDMLNVS 575
Cdd:PRK07638 326 --------EEVQKGEIGTVYVKSPQF-------FMGYIIGGVLARElnadgwmtvrdvgyeDEEGFIYIVGREKNMILFG 390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 576 GHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLycfVTLCDGHTFSstltEELKKQIREKIGPIATPDYIQNAPGLP 655
Cdd:PRK07638 391 GINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKP---VAIIKGSATK----QQLKSFCLQRLSSFKIPKEWHFVDEIP 463
|
570
....*....|....*...
gi 625195332 656 KTRSGKIMRRVLRKIAQN 673
Cdd:PRK07638 464 YTNSGKIARMEAKSWIEN 481
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
309-671 |
2.56e-21 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 95.48 E-value: 2.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 309 DPLFILYTSGSTGKPKGVVHTIGGyMLYVATTFKYVFDFHPEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTY 388
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAAN-LLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLLERNQALA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 389 PDESRlwsivdkYKVTKFYTAPTAIRMLMkfgDEPVTKHSRASLQVLGTVGEPINPEAwlwyHRVVGSQHCPIVDTFWQT 468
Cdd:cd17630 80 EDLAP-------PGVTHVSLVPTQLQRLL---DSGQGPAALKSLRAVLLGGAPIPPEL----LERAADRGIPLYTTYGMT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 469 ETGGHMLTPLPGATpmKPGSASFPFFGVAPAILNESGEelegeaegylvfkqpWPGIMRTIYGNHTRFETTYFKKfPGYY 548
Cdd:cd17630 146 ETASQVATKRPDGF--GRGGVGVLLPGRELRIVEDGEI---------------WVGGASLAMGYLRGQLVPEFNE-DGWF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 549 VTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTfsstlT 628
Cdd:cd17630 208 TTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPAD-----P 282
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 625195332 629 EELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 671
Cdd:cd17630 283 AELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
131-667 |
3.95e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 99.26 E-value: 3.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 131 GETTkITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSL 210
Cdd:PRK12316 533 GEET-LDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQL 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 211 LITTDAFyrGEKLvnlkeladeslekcrekgfPVrccivvkhvgraelgmndspsqSPPVKRQCPDVQISWNEGvdlWWH 290
Cdd:PRK12316 612 LLSQSHL--GRKL-------------------PL----------------------AAGVQVLDLDRPAAWLEG---YSE 645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 291 ElmqeagdefEPEWC-DAEDPLFILYTSGSTGKPKGVVHT---IGGYMLYVATTFK------------YVFDFHPEDVFW 354
Cdd:PRK12316 646 E---------NPGTElNPENLAYVIYTSGSTGKPKGAGNRhraLSNRLCWMQQAYGlgvgdtvlqktpFSFDVSVWEFFW 716
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 355 ctadigwitghsyvtygPLANGATSVLF-EGIPTYPDesRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPvtkhSRASLQ 433
Cdd:PRK12316 717 -----------------PLMSGARLVVAaPGDHRDPA--KLVELINREGVDTLHFVPSMLQAFLQDEDVA----SCTSLR 773
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 434 VLGTVGEPINPEAWLwyhRVVGSQ-HCPIVDTFWQTETGghmlTPLPGATPMKPGSASF----PFFGVAPAILNESGeel 508
Cdd:PRK12316 774 RIVCSGEALPADAQE---QVFAKLpQAGLYNLYGPTEAA----IDVTHWTCVEEGGDSVpigrPIANLACYILDANL--- 843
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 509 egeaegylvfkQPWP-GIMRTIY--------GNHTRFETTYFKKFPGYYV-------TGDGCRRDQDGYYWITGRIDDML 572
Cdd:PRK12316 844 -----------EPVPvGVLGELYlagrglarGYHGRPGLTAERFVPSPFVagermyrTGDLARYRADGVIEYAGRIDHQV 912
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 573 NVSGHLLSTAEVESALVEHEAVAEAAVVGhphpVKGECLYCFVTLCDGhtfSSTLTEELKKQIREKIGPIATPDYIQNAP 652
Cdd:PRK12316 913 KLRGLRIELGEIEARLLEHPWVREAAVLA----VDGKQLVGYVVLESE---GGDWREALKAHLAASLPEYMVPAQWLALE 985
|
570
....*....|....*
gi 625195332 653 GLPKTRSGKIMRRVL 667
Cdd:PRK12316 986 RLPLTPNGKLDRKAL 1000
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
133-667 |
1.38e-20 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 95.23 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 133 TTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLI 212
Cdd:cd17650 10 TRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 213 Ttdafyrgeklvnlkeladeslekcrekgfpvrccivvkhvgraelgmndspsqsppvkrqcpdvqiswnegvdlwwhel 292
Cdd:cd17650 90 T------------------------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 293 mqeagdefepewcDAEDPLFILYTSGSTGKPKGVVHTIGGYM-LYVATTFKYVFDFHPE----------DVFwcTADIGW 361
Cdd:cd17650 91 -------------QPEDLAYVIYTSGTTGKPKGVMVEHRNVAhAAHAWRREYELDSFPVrllqmasfsfDVF--AGDFAR 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 362 itghsyvtygPLANGATSVLfegIP--TYPDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVTKHSRASLQVLGTVG 439
Cdd:cd17650 156 ----------SLLNGGTLVI---CPdeVKLDPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVGSDG 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 440 EPINPEAWLwYHRVvgSQHCPIVDTFWQTET--------GGhmLTPLPGATPMKPGSasfPFFGVAPAILNESGeelege 511
Cdd:cd17650 223 CKAQDFKTL-AARF--GQGMRIINSYGVTEAtidstyyeEG--RDPLGDSANVPIGR---PLPNTAMYVLDERL------ 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 512 aegylvfkQPWP-GIMRTIY--------GNHTRFETTYfKKF------PG--YYVTGDGCRRDQDGYYWITGRIDDMLNV 574
Cdd:cd17650 289 --------QPQPvGVAGELYiggagvarGYLNRPELTA-ERFvenpfaPGerMYRTGDLARWRADGNVELLGRVDHQVKI 359
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 575 SGHLLSTAEVESALVEHEAVAEAAVVGHpHPVKGE---CLYCFVTlcdghtfSSTLTEELKKQIREKIGPIATPDYIQNA 651
Cdd:cd17650 360 RGFRIELGEIESQLARHPAIDEAVVAVR-EDKGGEarlCAYVVAA-------ATLNTAELRAFLAKELPSYMIPSYYVQL 431
|
570
....*....|....*.
gi 625195332 652 PGLPKTRSGKIMRRVL 667
Cdd:cd17650 432 DALPLTPNGKVDRRAL 447
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
132-665 |
3.47e-20 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 94.57 E-value: 3.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 132 ETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGAlhsIVFAgfsaeslceriLDSScslL 211
Cdd:PRK05852 40 DRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADL---VVVP-----------LDPA---L 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 212 ITTDAFYRGEKLVNLKELADeSLEKCREKGFPVRCCIVVKHVGRAELGMNDSPSQSPPVKRQcPDVQISWNEGVdlwwhe 291
Cdd:PRK05852 103 PIAEQRVRSQAAGARVVLID-ADGPHDRAEPTTRWWPLTVNVGGDSGPSGGTLSVHLDAATE-PTPATSTPEGL------ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 292 lmqeagdefepewcdAEDPLFILYTSGSTGKPKGVVHTIGGymlyVATTFKYV---FDFHPEDVfwCTADIGWITGHSYV 368
Cdd:PRK05852 175 ---------------RPDDAMIMFTGGTTGLPKMVPWTHAN----IASSVRAIitgYRLSPRDA--TVAVMPLYHGHGLI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 369 T--YGPLANGATSVLfegiptyPDESRL-----WSIVDKYKVTKFYTAPTAIRMLMKFGDEPVTKHSRASLQVLGTVGEP 441
Cdd:PRK05852 234 AalLATLASGGAVLL-------PARGRFsahtfWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKPAALRFIRSCSAP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 442 INPEAWLWYHRVVGSqhcPIVDTFWQTET---------GGHMLTPLPGATPMKPGSASFPFFGVA--------PAILNes 504
Cdd:PRK05852 307 LTAETAQALQTEFAA---PVVCAFGMTEAthqvtttqiEGIGQTENPVVSTGLVGRSTGAQIRIVgsdglplpAGAVG-- 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 505 geelegeaegylvfkQPW---PGIMRTIYGNHtrfETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLST 581
Cdd:PRK05852 382 ---------------EVWlrgTTVVRGYLGDP---TITAANFTDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISP 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 582 AEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSStltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGK 661
Cdd:PRK05852 444 ERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTA---EELVQFCRERLAAFEIPASFQEASGLPHTAKGS 520
|
....
gi 625195332 662 IMRR 665
Cdd:PRK05852 521 LDRR 524
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
115-667 |
4.99e-20 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 93.93 E-value: 4.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 115 KKLGDKVAFYWEGNepgettKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGF 194
Cdd:cd17655 8 EKTPDHTAVVFEDQ------TLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 195 SAESLcERIL-DSSCSLLITTDAFYRGEKlvnlkeladeslekcrekgfpvrccivvkHVGRAELgMNDSPSQSppvkrq 273
Cdd:cd17655 82 PEERI-QYILeDSGADILLTQSHLQPPIA-----------------------------FIGLIDL-LDEDTIYH------ 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 274 cpdvqiswnegvdlwwhelmqEAGDEFEPEwCDAEDPLFILYTSGSTGKPKGV----------VHTIGGYM-----LYVA 338
Cdd:cd17655 125 ---------------------EESENLEPV-SKSDDLAYVIYTSGSTGKPKGVmiehrgvvnlVEWANKVIyqgehLRVA 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 339 TTFKYVFDFHPEDVFwctadigwitghsyvtyGPLANGATSVLfegiptYPDESR-----LWSIVDKYKVTKFYTAPTAI 413
Cdd:cd17655 183 LFASISFDASVTEIF-----------------ASLLSGNTLYI------VRKETVldgqaLTQYIRQNRITIIDLTPAHL 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 414 RMLMKFGDEPvtkhsRASLQVLGTVGEPINPE-AWLWYHRVVGSqhCPIVDTFWQTETG-GHMLTPLpgaTPMKPGSASF 491
Cdd:cd17655 240 KLLDAADDSE-----GLSLKHLIVGGEALSTElAKKIIELFGTN--PTITNAYGPTETTvDASIYQY---EPETDQQVSV 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 492 PffgVAPAILNESGeelegeaegYLVFK--QPWP-GIMRTIY--------GNHTRFETTYfKKF------PG--YYVTGD 552
Cdd:cd17655 310 P---IGKPLGNTRI---------YILDQygRPQPvGVAGELYiggegvarGYLNRPELTA-EKFvddpfvPGerMYRTGD 376
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 553 GCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTlCDGHTFSSTLTEELK 632
Cdd:cd17655 377 LARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIV-SEKELPVAQLREFLA 455
|
570 580 590
....*....|....*....|....*....|....*
gi 625195332 633 KQIREKIgpiaTPDYIQNAPGLPKTRSGKIMRRVL 667
Cdd:cd17655 456 RELPDYM----IPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
117-670 |
7.11e-20 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 93.67 E-value: 7.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 117 LGDKVAFYWEGnepgetTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSA 196
Cdd:PRK06155 34 YPDRPLLVFGG------TRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 197 ESLcERILDSSCSLLITTDAfyrgeKLVNLKELADESLEKCREKGFpvrccIVVKHVGRAELGMNDSPSqsPPVKRQCPD 276
Cdd:PRK06155 108 PQL-EHILRNSGARLLVVEA-----ALLAALEAADPGDLPLPAVWL-----LDAPASVSVPAGWSTAPL--PPLDAPAPA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 277 VQISwnegvdlwwhelmqeagdefepewcdAEDPLFILYTSGSTGKPKGVVHTiggymlyvattfkyvfdfHPEDVFW-- 354
Cdd:PRK06155 175 AAVQ--------------------------PGDTAAILYTSGTTGPSKGVCCP------------------HAQFYWWgr 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 355 -CTADIGWITGHSYVTYGPL-------------ANGATSVLFEGIPTypdeSRLWSIVDKYKVTKFYTAPTAIRMLMKfg 420
Cdd:PRK06155 211 nSAEDLEIGADDVLYTTLPLfhtnalnaffqalLAGATYVLEPRFSA----SGFWPAVRRHGATVTYLLGAMVSILLS-- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 421 dEPVTKHSRAS-LQV-LGTVGEPINPEAWLWYHRVvgsqhcPIVDTFWQTETGGHMLTPLPGAtpmKPGSASFPFFGVAP 498
Cdd:PRK06155 285 -QPARESDRAHrVRVaLGPGVPAALHAAFRERFGV------DLLDGYGSTETNFVIAVTHGSQ---RPGSMGRLAPGFEA 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 499 AILNESGEELEGEAEGYLVFKQPWPGIMRTIYGNHTRFETTYFKKFpgYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHL 578
Cdd:PRK06155 355 RVVDEHDQELPDGEPGELLLRADEPFAFATGYFGMPEKTVEAWRNL--WFHTGDRVVRDADGWFRFVDRIKDAIRRRGEN 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 579 LSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSStltEELKKQIREKIGPIATPDYIQNAPGLPKTR 658
Cdd:PRK06155 433 ISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEP---VALVRHCEPRLAYFAVPRYVEFVAALPKTE 509
|
570
....*....|..
gi 625195332 659 SGKIMRRVLRKI 670
Cdd:PRK06155 510 NGKVQKFVLREQ 521
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
313-668 |
1.60e-19 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 92.06 E-value: 1.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 313 ILYTSGSTGKPKGVVHTIGGYMLYVATTFKYVFDFHP--EDVFWCTADIGWITGHSyVTYGPLANGATSVLFEGIptypD 390
Cdd:cd05929 130 MLYSGGTTGRPKGIKRGLPGGPPDNDTLMAAALGFGPgaDSVYLSPAPLYHAAPFR-WSMTALFMGGTLVLMEKF----D 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 391 ESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVTKHSRASLQVLGTVGEPINP---EAWL-WYHrvvgsqhcPIVDTFW 466
Cdd:cd05929 205 PEEFLRLIERYRVTFAQFVPTMFVRLLKLPEAVRNAYDLSSLKRVIHAAAPCPPwvkEQWIdWGG--------PIIWEYY 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 467 Q-TETGGhmLTPLPGATPMK-PGSASFPFFGVApAILNESGEelegeaegylvfKQPwPGIMRTIY--GNHTRFETTYFK 542
Cdd:cd05929 277 GgTEGQG--LTIINGEEWLThPGSVGRAVLGKV-HILDEDGN------------EVP-PGEIGEVYfaNGPGFEYTNDPE 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 543 KFP------GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVT 616
Cdd:cd05929 341 KTAaarnegGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQ 420
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 625195332 617 LCDGHTFSSTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:cd05929 421 PAPGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
309-664 |
2.22e-19 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 89.77 E-value: 2.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 309 DPLFILYTSGSTGKPKGVVHTiggYMLYVATtfkyvfdfhpedvFWCTADIGWITGHSYVTY-GPLA-----NGATSVLF 382
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRS---ERSWIES-------------FVCNEDLFNISGEDAILApGPLShslflYGAISALY 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 383 EG----IPTYPDESRLWSIVDKYKVTKFYTAPTAIRMLMKFgDEPVTKhsrasLQVLGTVGEPINPEAwlwyHRVV--GS 456
Cdd:cd17633 65 LGgtfiGQRKFNPKSWIRKINQYNATVIYLVPTMLQALART-LEPESK-----IKSIFSSGQKLFEST----KKKLknIF 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 457 QHCPIVDTFWQTETGghMLTPLPGATPMKPGSASFPFFGVAPAILNESGeelegeaegylvfkqpwpGIMRTIYGNHTRF 536
Cdd:cd17633 135 PKANLIEFYGTSELS--FITYNFNQESRPPNSVGRPFPNVEIEIRNADG------------------GEIGKIFVKSEMV 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 537 ETTY----FKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGEcLY 612
Cdd:cd17633 195 FSGYvrggFSNPDGWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGE-IA 273
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 625195332 613 CFVTLCDGHTFSSTLTEELKKQIREKIgpiatPDYIQNAPGLPKTRSGKIMR 664
Cdd:cd17633 274 VALYSGDKLTYKQLKRFLKQKLSRYEI-----PKKIIFVDSLPYTSSGKIAR 320
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
137-669 |
2.24e-18 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 89.04 E-value: 2.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 137 TYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITTDA 216
Cdd:PRK06087 51 TYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 217 FYRGEKLVNLKELADEslekcrekgfpvrccivVKHVGRAELGMNDSPSQSPPVKRQCpdvqISWNEGVDlwwhelmqea 296
Cdd:PRK06087 131 FKQTRPVDLILPLQNQ-----------------LPQLQQIVGVDKLAPATSSLSLSQI----IADYEPLT---------- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 297 gdefEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGGyMLYVATTFKYVFDFHPEDVFWCTADIGWITGHSYVTYGPLANG 376
Cdd:PRK06087 180 ----TAITTHGDELAAVLFTSGTEGLPKGVMLTHNN-ILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 377 ATSVLFEGIPtyPDESrlWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVTKHSraSLQVLGTVGEPInPEawlwyhRVVgs 456
Cdd:PRK06087 255 ARSVLLDIFT--PDAC--LALLEQQRCTCMLGATPFIYDLLNLLEKQPADLS--ALRFFLCGGTTI-PK------KVA-- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 457 QHC-----PIVDTFWQTETGGHMLTPLPGATPMKPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPWpgiMRTIYG 531
Cdd:PRK06087 320 RECqqrgiKLLSVYGSTESSPHAVVNLDDPLSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPN---VFMGYL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 532 NHTRfETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECL 611
Cdd:PRK06087 397 DEPE-LTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERS 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 625195332 612 YCFVTLcDGHTFSSTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:PRK06087 476 CAYVVL-KAPHHSLTLEEVVAFFSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
89-670 |
2.97e-18 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 88.74 E-value: 2.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 89 GKIFTEWMKGATTNICYNVLDRnvhEKKLGDKVAFYWEGNEpgetTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMP 168
Cdd:cd17642 5 PGPFYPLEDGTAGEQLHKAMKR---YASVPGTIAFTDAHTG----VNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 169 MILELVVAMLACARLGalhsiVFAGFSAESLCERILDSSCSLLITTDAFYRGEKLvnlkeladESLEKCREKGFPVRCCI 248
Cdd:cd17642 78 NSLQFFLPVIAGLFIG-----VGVAPTNDIYNERELDHSLNISKPTIVFCSKKGL--------QKVLNVQKKLKIIKTII 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 249 VVKhvGRAELGmndspsqsppvKRQCPDVQISWNEGVDLWWHELMQEAGDEfepewcdAEDPLFILYTSGSTGKPKGVVH 328
Cdd:cd17642 145 ILD--SKEDYK-----------GYQCLYTFITQNLPPGFNEYDFKPPSFDR-------DEQVALIMNSSGSTGLPKGVQL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 329 T--------------IGGYMLYVATTFKYVFDFHpeDVFWCTADIGWITGhsyvtygplanGATSVLfegIPTYPDESRL 394
Cdd:cd17642 205 ThknivarfshardpIFGNQIIPDTAILTVIPFH--HGFGMFTTLGYLIC-----------GFRVVL---MYKFEEELFL 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 395 WSIVDkYKVTKFYTAPTAIRMLMKfgDEPVTKHSRASLQVLGTVGEPINPEawlwyhrvVGSQ-----HCPIV-DTFWQT 468
Cdd:cd17642 269 RSLQD-YKVQSALLVPTLFAFFAK--STLVDKYDLSNLHEIASGGAPLSKE--------VGEAvakrfKLPGIrQGYGLT 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 469 ETGGHML-TPlpgATPMKPGSAS--FPFFGvAPAILNESGEELEGEAEGYLVFKQpwPGIMRTIYGNHTRFETTYFKKfp 545
Cdd:cd17642 338 ETTSAILiTP---EGDDKPGAVGkvVPFFY-AKVVDLDTGKTLGPNERGELCVKG--PMIMKGYVNNPEATKALIDKD-- 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 546 GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfsS 625
Cdd:cd17642 410 GWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAG----K 485
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 625195332 626 TLTEelkKQIREKIGPIATPDY-----IQNAPGLPKTRSGKIMRRVLRKI 670
Cdd:cd17642 486 TMTE---KEVMDYVASQVSTAKrlrggVKFVDEVPKGLTGKIDRRKIREI 532
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
136-667 |
4.09e-18 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 87.71 E-value: 4.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 136 ITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLcERIL-DSSCSLLITt 214
Cdd:cd12114 13 LTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARR-EAILaDAGARLVLT- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 215 dafyrgeklvnlkeladeslekcrekgfpvrccivvkhvgraelgmndspsQSPPVKrQCPDVQISWNEGVDLwwhelmQ 294
Cdd:cd12114 91 ---------------------------------------------------DGPDAQ-LDVAVFDVLILDLDA------L 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 295 EAGDEFEPEWCDAEDPLFILYTSGSTGKPKGVV--H-----TIGgymlyvATTFKYVFDfhPEDVFWCTA---------D 358
Cdd:cd12114 113 AAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMisHraalnTIL------DINRRFAVG--PDDRVLALSslsfdlsvyD 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 359 IgwitghsyvtYGPLANGATSVLfegiptyPDESRL-----W-SIVDKYKVTKFYTAPTAIRMLMKF-GDEPVTKHSRAs 431
Cdd:cd12114 185 I----------FGALSAGATLVL-------PDEARRrdpahWaELIERHGVTLWNSVPALLEMLLDVlEAAQALLPSLR- 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 432 LQVLGtvGEPINPEawlwyhrvvgsqhcpIVDTFWQTETGGHmLTPLPGAT------------PMKPGSASFPFfGVAPA 499
Cdd:cd12114 247 LVLLS--GDWIPLD---------------LPARLRALAPDAR-LISLGGATeasiwsiyhpidEVPPDWRSIPY-GRPLA 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 500 -----ILNESgeelegeaegylvfKQPWP------------GIMRTIYGNHTRFETTYFKKFPG--YYVTGD-GCRRDqD 559
Cdd:cd12114 308 nqryrVLDPR--------------GRDCPdwvpgelwiggrGVALGYLGDPELTAARFVTHPDGerLYRTGDlGRYRP-D 372
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 560 GYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPvKGECLYCFVTLCDGHTfsSTLTEELKKQIREKI 639
Cdd:cd12114 373 GTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDP-GGKRLAAFVVPDNDGT--PIAPDALRAFLAQTL 449
|
570 580
....*....|....*....|....*...
gi 625195332 640 GPIATPDYIQNAPGLPKTRSGKIMRRVL 667
Cdd:cd12114 450 PAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
289-669 |
6.27e-18 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 87.49 E-value: 6.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 289 WHELMQEAGDEFEP-EWCDAEDPLFILYTSGSTGKPKGVVHT-IGGYMLYVATTFKYVFDFHPEDVFWCTADIGWITGHS 366
Cdd:cd05915 133 GYLAYEEALGEEADpVRVPERAACGMAYTTGTTGLPKGVVYShRALVLHSLAASLVDGTALSEKDVVLPVVPMFHVNAWC 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 367 YVtYGPLANGATSVLFEGIPTypDESRLWSIVdKYKVTKFYTAPTAIRMLMKFGDEpVTKHSRASLQVLGTVGEPinPEA 446
Cdd:cd05915 213 LP-YAATLVGAKQVLPGPRLD--PASLVELFD-GEGVTFTAGVPTVWLALADYLES-TGHRLKTLRRLVVGGSAA--PRS 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 447 WL-----WYHRVVGSQHCPIV-----DTFWQTEtgghmLTPLPGATPMK-PGSASFPFFGVAPAILNESGEELEGEAEGY 515
Cdd:cd05915 286 LIarferMGVEVRQGYGLTETspvvvQNFVKSH-----LESLSEEEKLTlKAKTGLPIPLVRLRVADEEGRPVPKDGKAL 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 516 LVFKQPWPGIMRTIYGNHTRFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVA 595
Cdd:cd05915 361 GEVQLKGPWITGGYYGNEEATRSALTPD--GFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVK 438
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 625195332 596 EAAVVGHPHPVKGECLYCFVTLCDghtfSSTLTEELKKQIREKIGPIAT-PDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:cd05915 439 EAAVVAIPHPKWQERPLAVVVPRG----EKPTPEELNEHLLKAGFAKWQlPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
546-668 |
8.96e-18 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 85.41 E-value: 8.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 546 GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSS 625
Cdd:cd05917 230 GWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTE 309
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 625195332 626 tltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:cd05917 310 ---EDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
119-684 |
1.07e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 88.48 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 119 DKVAFYWEGNEpgettkITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAES 198
Cdd:PRK12316 3072 DAVALAFGEQR------LSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEER 3145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 199 LCERILDSSCSLLITTDAFyrgeklvnlkeladeslekcrekgfpvrccivvkhvgraelgmndSPSQSPPVKRQCPDVQ 278
Cdd:PRK12316 3146 LAYMLEDSGAQLLLSQSHL---------------------------------------------RLPLAQGVQVLDLDRG 3180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 279 iswnegvdlwwhelMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPKGVV--------HTIGGYMLYVATTFKYVFDFHPE 350
Cdd:PRK12316 3181 --------------DENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGirhsalsnHLCWMQQAYGLGVGDRVLQFTTF 3246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 351 DvfwctadigwITGHSYVTYGPLANGATSVLfEGIPTYPDESRLWSIVDKYKVTKFYTAPTAIRMLMkfgdEPVTKHSRA 430
Cdd:PRK12316 3247 S----------FDVFVEELFWPLMSGARVVL-AGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFL----EEEDAHRCT 3311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 431 SLQVLGTVGEPINPEAwlwYHRVVGSQhcPIVDTFWQTETgghmlTPLPGATPMKPGSASFPFFGVAPAILNESGEELEG 510
Cdd:PRK12316 3312 SLKRIVCGGEALPADL---QQQVFAGL--PLYNLYGPTEA-----TITVTHWQCVEEGKDAVPIGRPIANRACYILDGSL 3381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 511 EAEGYLVFKQPWPGIMRTIYGNHTR-------FETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAE 583
Cdd:PRK12316 3382 EPVPVGALGELYLGGEGLARGYHNRpgltaerFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGE 3461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 584 VESALVEHEAVAEAAVVGhphpVKGECLYCFVTLCDGhtfSSTLTEELKKQIREKIgpiatPDYIQNA-----PGLPKTR 658
Cdd:PRK12316 3462 IEARLLEHPWVREAVVLA----VDGRQLVAYVVPEDE---AGDLREALKAHLKASL-----PEYMVPAhllflERMPLTP 3529
|
570 580
....*....|....*....|....*.
gi 625195332 659 SGKIMRRVLRKIaqnDHDLGDTSTVA 684
Cdd:PRK12316 3530 NGKLDRKALPRP---DAALLQQDYVA 3552
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
132-674 |
1.19e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 86.92 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 132 ETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGA-LH---------SIVFagfsaeslce 201
Cdd:PRK08162 40 GDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAvLNtlntrldaaSIAF---------- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 202 rILDSSCS-LLITTDAFyrgeklvnlKELADESLEKCRekgfpvRCCIVVKHVGRAELGMNDSPSqsppvkrqcpdvqis 280
Cdd:PRK08162 110 -MLRHGEAkVLIVDTEF---------AEVAREALALLP------GPKPLVIDVDDPEYPGGRFIG--------------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 281 wnegvDLWWHELMQEAGDEFEPEWCDAE-DPLFILYTSGSTGKPKGVV-HTIGGYMLYVATTFKYVFDFHPE-----DVF 353
Cdd:PRK08162 159 -----ALDYEAFLASGDPDFAWTLPADEwDAIALNYTSGTTGNPKGVVyHHRGAYLNALSNILAWGMPKHPVylwtlPMF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 354 WCTadiGWitGHSY-VTygplANGATSVLFEGIptypDESRLWSIVDKYKVTKFYTAPTAIRMLMkfgDEPVTKHSRASL 432
Cdd:PRK08162 234 HCN---GW--CFPWtVA----ARAGTNVCLRKV----DPKLIFDLIREHGVTHYCGAPIVLSALI---NAPAEWRAGIDH 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 433 QVLGTVGEPINPEAWLWYHRVVGSQhcpIVDTFWQTETGGHmltplpgAT--PMKPGSASFPFfgVAPAILNESGEELEG 510
Cdd:PRK08162 298 PVHAMVAGAAPPAAVIAKMEEIGFD---LTHVYGLTETYGP-------ATvcAWQPEWDALPL--DERAQLKARQGVRYP 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 511 EAEGYLVFK----QPWPGIMRTI-----YGN-----HTRFETTYFKKFP-GYYVTGDGCRRDQDGYYWITGRIDDMLNVS 575
Cdd:PRK08162 366 LQEGVTVLDpdtmQPVPADGETIgeimfRGNivmkgYLKNPKATEEAFAgGWFHTGDLAVLHPDGYIKIKDRSKDIIISG 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 576 GHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSstlTEELKKQIREKIGPIATPDYIQNAPgLP 655
Cdd:PRK08162 446 GENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGASAT---EEEIIAHCREHLAGFKVPKAVVFGE-LP 521
|
570
....*....|....*....
gi 625195332 656 KTRSGKIMRRVLRKIAQND 674
Cdd:PRK08162 522 KTSTGKIQKFVLREQAKSL 540
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
113-668 |
1.22e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 86.48 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 113 HEKKLGDKVAFYWEGNEpgettkITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFA 192
Cdd:PRK06145 11 HARRTPDRAALVYRDQE------ISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 193 GFSAESLCERILDSSCSLLittdafyrgeklvnlkeLADESLEKCREKGFPVrccIVVkhvgraelgmnDSPSQSppvkr 272
Cdd:PRK06145 85 RLAADEVAYILGDAGAKLL-----------------LVDEEFDAIVALETPK---IVI-----------DAAAQA----- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 273 qcpDVQIswnegvdlwwhelMQEAGDEFEPEWCDAEDPLF-ILYTSGSTGKPKGVVHTIGgymlyvattfkyvfdfhpeD 351
Cdd:PRK06145 129 ---DSRR-------------LAQGGLEIPPQAAVAPTDLVrLMYTSGTTDRPKGVMHSYG-------------------N 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 352 VFWCTAD----IGWITGHSYVTYGPLAN-GA-----TSVLFEG-----IPTYPDESRLWSIvDKYKVTKFYTAPTAI-RM 415
Cdd:PRK06145 174 LHWKSIDhviaLGLTASERLLVVGPLYHvGAfdlpgIAVLWVGgtlriHREFDPEAVLAAI-ERHRLTCAWMAPVMLsRV 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 416 LMkfgdepVTKHSRASLQVLGTV--GEPINPEAWLwyhRVVGS--QHCPIVDTFWQTET-GGHMLTPlPGATPMKPGSAS 490
Cdd:PRK06145 253 LT------VPDRDRFDLDSLAWCigGGEKTPESRI---RDFTRvfTRARYIDAYGLTETcSGDTLME-AGREIEKIGSTG 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 491 FPFFGVAPAILNESGEELEGEAEGYLVFKQPwpgimRTIYGNHTRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDD 570
Cdd:PRK06145 323 RALAHVEIRIADGAGRWLPPNMKGEICMRGP-----KVTKGYWKDPEKTAEAFYGDWFRSGDVGYLDEEGFLYLTDRKKD 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 571 MLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSstlTEELKKQIREKIGPIATPDYIQN 650
Cdd:PRK06145 398 MIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLT---LEALDRHCRQRLASFKVPRQLKV 474
|
570
....*....|....*...
gi 625195332 651 APGLPKTRSGKIMRRVLR 668
Cdd:PRK06145 475 RDELPRNPSGKVLKRVLR 492
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
306-672 |
1.31e-17 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 86.61 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 306 DAEDPLFILYTSGSTGKPKGVV--HTiGGYMLYVATTFKYVFDFHPedVFWCTADIGWITGHSYvTYGPLANGATSVLFE 383
Cdd:PLN03102 184 DEHDPISLNYTSGTTADPKGVVisHR-GAYLSTLSAIIGWEMGTCP--VYLWTLPMFHCNGWTF-TWGTAARGGTSVCMR 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 384 GIpTYPDesrLWSIVDKYKVTKFYTAPTAIRMLMKfGDEPVTKHSRASLQVLgTVGEPiNPEAWLWYHRVVGSQhcpIVD 463
Cdd:PLN03102 260 HV-TAPE---IYKNIEMHNVTHMCCVPTVFNILLK-GNSLDLSPRSGPVHVL-TGGSP-PPAALVKKVQRLGFQ---VMH 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 464 TFWQTETGGHML--------TPLPGATPMK-PGSASFPFFGVAPAILNESGEELEG----EAEGYLVFKQPwpGIMRTiY 530
Cdd:PLN03102 330 AYGLTEATGPVLfcewqdewNRLPENQQMElKARQGVSILGLADVDVKNKETQESVprdgKTMGEIVIKGS--SIMKG-Y 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 531 GNHTRFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGEC 610
Cdd:PLN03102 407 LKNPKATSEAFKH--GWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGET 484
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 625195332 611 LYCFVTLCDGHTFSS-------TLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQ 672
Cdd:PLN03102 485 PCAFVVLEKGETTKEdrvdklvTRERDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRDIAK 553
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
546-668 |
2.32e-17 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 85.88 E-value: 2.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 546 GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDghtfsS 625
Cdd:PRK08974 432 GWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKD-----P 506
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 625195332 626 TLT-EELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:PRK08974 507 SLTeEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
107-668 |
2.65e-17 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 86.24 E-value: 2.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 107 VLDRNVHEKKLGDKVAFYwegnepgETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGAL 186
Cdd:PRK06060 9 LLAEQASEAGWYDRPAFY-------AADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 187 HSIVFAGFSAESLCERILDSSCSLLITTDAF---YRGEKLVNLKELADESlekcrekgfpvrccivvkhvGRAElgmnds 263
Cdd:PRK06060 82 AFLANPELHRDDHALAARNTEPALVVTSDALrdrFQPSRVAEAAELMSEA--------------------ARVA------ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 264 PSQSPPVkrqcpdvqiswnegvdlwwhelmqeAGDEFEpewcdaedplFILYTSGSTGKPKGVVHTIGGYMLYVATTFKY 343
Cdd:PRK06060 136 PGGYEPM-------------------------GGDALA----------YATYTSGTTGPPKAAIHRHADPLTFVDAMCRK 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 344 VFDFHPEDVFWCTADIGWITGHSYVTYGPLANGATSVLfEGIPTYPDESRLWSIvdKYKVTKFYTAPTAIRMLMkfgdEP 423
Cdd:PRK06060 181 ALRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVI-NSAPVTPEAAAILSA--RFGPSVLYGVPNFFARVI----DS 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 424 VTKHSRASLQVLGTVGEPINPEAWLWYHRVVGSqhCPIVDTFWQTETGGHMLTPlpGATPMKPGSAS--FPFFG---VAP 498
Cdd:PRK06060 254 CSPDSFRSLRCVVSAGEALELGLAERLMEFFGG--IPILDGIGSTEVGQTFVSN--RVDEWRLGTLGrvLPPYEirvVAP 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 499 AILNESgeelegeaegylvfkqpwPGIMRTIYGNHTRFETTYFKKfP-------GYYVTGDGCRRDQDGYYWITGRIDDM 571
Cdd:PRK06060 330 DGTTAG------------------PGVEGDLWVRGPAIAKGYWNR-PdspvaneGWLDTRDRVCIDSDGWVTYRCRADDT 390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 572 LNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSSTLTEELKKQIREKIGPIATPDYIQNA 651
Cdd:PRK06060 391 EVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRDLHRGLLNRLSAFKVPHRFAVV 470
|
570
....*....|....*..
gi 625195332 652 PGLPKTRSGKIMRRVLR 668
Cdd:PRK06060 471 DRLPRTPNGKLVRGALR 487
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
135-669 |
2.88e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 86.93 E-value: 2.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 135 KITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITT 214
Cdd:PRK12316 4576 KLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQ 4655
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 215 DAFYrgEKLVNLKELADESLEKCRE-KGFPvrccivvkhvgraelgmndspSQSPPVKrqcpdvqiswnegvdlwwhelm 293
Cdd:PRK12316 4656 SHLL--QRLPIPDGLASLALDRDEDwEGFP---------------------AHDPAVR---------------------- 4690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 294 qeagdefepewCDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYvFDFHPED-VFWCTA---DI---GWitghs 366
Cdd:PRK12316 4691 -----------LHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGER-YELTPDDrVLQFMSfsfDGsheGL----- 4753
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 367 yvtYGPLANGAtSVLFEGiPTYPDESRLWSIVDKYKVTKFYTAPTAIRMLMKfGDEPVTKHSRASLQVLGtvGEPINPEA 446
Cdd:PRK12316 4754 ---YHPLINGA-SVVIRD-DSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAE-HAERDGEPPSLRVYCFG--GEAVAQAS 4825
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 447 W-LWY--------HRVVGSQHCPIVDTFWQTETGghmltPLPGATPMKPGSasfPFFGVAPAILNESGEELEGEAEGYLV 517
Cdd:PRK12316 4826 YdLAWralkpvylFNGYGPTETTVTVLLWKARDG-----DACGAAYMPIGT---PLGNRSGYVLDGQLNPLPVGVAGELY 4897
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 518 FKQPwpGIMRtiyGNH-------TRFETTYFKKfPG--YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESAL 588
Cdd:PRK12316 4898 LGGE--GVAR---GYLerpaltaERFVPDPFGA-PGgrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARL 4971
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 589 VEHEAVAEAAVVGHPHPVkGECLYCFVTLCDGHTFSSTLTE-ELKKQIREKIGPiATPDYIQNA-----PGLPKTRSGKI 662
Cdd:PRK12316 4972 REHPAVREAVVIAQEGAV-GKQLVGYVVPQDPALADADEAQaELRDELKAALRE-RLPEYMVPAhlvflARMPLTPNGKL 5049
|
....*..
gi 625195332 663 MRRVLRK 669
Cdd:PRK12316 5050 DRKALPQ 5056
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
129-668 |
3.05e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 85.45 E-value: 3.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 129 EPGETtkITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSC 208
Cdd:PRK13390 20 ETGEQ--VSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 209 SLLITTDAfyrgeklvnLKELAdeslekcrekgfpvrccivvkhvgrAELGmNDSPsqsppvkrqcpdVQISWNEGVDLW 288
Cdd:PRK13390 98 RVLVASAA---------LDGLA-------------------------AKVG-ADLP------------LRLSFGGEIDGF 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 289 --WHELMQEAGDEFEPEWCDAedplFILYTSGSTGKPKGV--------VHTIGGYMLYVATTFkyvFDFHPEDVFWCTAD 358
Cdd:PRK13390 131 gsFEAALAGAGPRLTEQPCGA----VMLYSSGTTGFPKGIqpdlpgrdVDAPGDPIVAIARAF---YDISESDIYYSSAP 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 359 IGwitgHSyvtyGPL-------ANGATSVLFEGIptypDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVTKHSRAS 431
Cdd:PRK13390 204 IY----HA----APLrwcsmvhALGGTVVLAKRF----DAQATLGHVERYRITVTQMVPTMFVRLLKLDADVRTRYDVSS 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 432 LQVLGTVGEPINPEA------WLWyhrvvgsqhcPIVDTFWQTeTGGHMLTPL-PGATPMKPGSASFPFFGVApAILNES 504
Cdd:PRK13390 272 LRAVIHAAAPCPVDVkhamidWLG----------PIVYEYYSS-TEAHGMTFIdSPDWLAHPGSVGRSVLGDL-HICDDD 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 505 GEELEGEAEGYLVFKQPwpgimRTIYGNHTRFETTYFKKFPG---YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLST 581
Cdd:PRK13390 340 GNELPAGRIGTVYFERD-----RLPFRYLNDPEKTAAAQHPAhpfWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYP 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 582 AEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSSTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGK 661
Cdd:PRK13390 415 QETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGK 494
|
....*..
gi 625195332 662 IMRRVLR 668
Cdd:PRK13390 495 LVKGLLR 501
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
136-668 |
3.58e-17 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 85.46 E-value: 3.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 136 ITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITTD 215
Cdd:PRK07059 49 ITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVVLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 216 AFYRGEKLV----NLKELADESL-EKCREKGFPVRccIVVKHVGRAelgmndSPSQSPPVKRQCPDVqiswnegvdlwwh 290
Cdd:PRK07059 129 NFATTVQQVlaktAVKHVVVASMgDLLGFKGHIVN--FVVRRVKKM------VPAWSLPGHVRFNDA------------- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 291 eLMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPKGVVHT---IGGYMLYVATTFKYVFDF--HPEDVFWCTA----DIGW 361
Cdd:PRK07059 188 -LAEGARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLhrnIVANVLQMEAWLQPAFEKkpRPDQLNFVCAlplyHIFA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 362 ITGHSYVTygpLANGATSVLfegIPTYPDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVTKHSRASLQVLG--TVG 439
Cdd:PRK07059 267 LTVCGLLG---MRTGGRNIL---IPNPRDIPGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKLDFSKLIVANGGgmAVQ 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 440 EPInpeAWLWYHRVvgsqHCPIVDTFWQTETGGhMLTPLPGATPMKPGSASFPFFGVAPAILNESGEElegeaegyLVFK 519
Cdd:PRK07059 341 RPV---AERWLEMT----GCPITEGYGLSETSP-VATCNPVDATEFSGTIGLPLPSTEVSIRDDDGND--------LPLG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 520 QPW------PGIMRtiyGNHTRFETTYFKKFP-GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHE 592
Cdd:PRK07059 405 EPGeicirgPQVMA---GYWNRPDETAKVMTAdGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHP 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 625195332 593 AVAEAAVVGHPHPVKGECLYCFVTLCDghtfsSTLTEE-LKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:PRK07059 482 GVLEVAAVGVPDEHSGEAVKLFVVKKD-----PALTEEdVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
135-670 |
3.82e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 86.37 E-value: 3.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 135 KITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITT 214
Cdd:PRK12467 3120 QLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQ 3199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 215 DAFyrgeklvnlkeladesLEKcrekgfpvrccIVVKHVGRAELGMNDSPSQSPPvkrQCPDVQIswnegvdlwwhelmq 294
Cdd:PRK12467 3200 AHL----------------LEQ-----------LPAPAGDTALTLDRLDLNGYSE---NNPSTRV--------------- 3234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 295 eagdefepewcDAEDPLFILYTSGSTGKPKGVVHTIGG-----------YMLYVATT----FKYVFDFHPEDVFWctadi 359
Cdd:PRK12467 3235 -----------MGENLAYVIYTSGSTGKPKGVGVRHGAlanhlcwiaeaYELDANDRvllfMSFSFDGAQERFLW----- 3298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 360 gwitghsyvtygPLANGATSVLFEGIPTYPDEsrLWSIVDKYKVTKFYTAPTAIRMLMKFGDepvtKHSRASLQVLGTVG 439
Cdd:PRK12467 3299 ------------TLICGGCLVVRDNDLWDPEE--LWQAIHAHRISIACFPPAYLQQFAEDAG----GADCASLDIYVFGG 3360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 440 EPINPEAWLWYHRVV---------GSQHCPIVDTFWQTETGGhmlTPLPGATPMkpgsaSFPFFGVAPAILNESGeeleg 510
Cdd:PRK12467 3361 EAVPPAAFEQVKRKLkprgltngyGPTEAVVTVTLWKCGGDA---VCEAPYAPI-----GRPVAGRSIYVLDGQL----- 3427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 511 eaegylvfkQPWP-GIMRTIY--------GNH-------TRFETTYFKKFPG-YYVTGDGCRRDQDGYYWITGRIDDMLN 573
Cdd:PRK12467 3428 ---------NPVPvGVAGELYiggvglarGYHqrpsltaERFVADPFSGSGGrLYRTGDLARYRADGVIEYLGRIDHQVK 3498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 574 VSGHLLSTAEVESALVEHEAVAEAAVVGHPhPVKGECLYCFVTLcdgHTFSSTLTEELKKQIREKIgpiatPDYIQNA-- 651
Cdd:PRK12467 3499 IRGFRIELGEIEARLLQHPSVREAVVLARD-GAGGKQLVAYVVP---ADPQGDWRETLRDHLAASL-----PDYMVPAql 3569
|
570 580
....*....|....*....|..
gi 625195332 652 ---PGLPKTRSGKIMRRVLRKI 670
Cdd:PRK12467 3570 lvlAAMPLGPNGKVDRKALPDP 3591
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
115-671 |
3.98e-17 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 85.31 E-value: 3.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 115 KKLGDKVAFYWEGnepgetTKITYRELLVQVCQF-SNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAG 193
Cdd:PRK08751 36 AKFADRPAYHSFG------KTITYREADQLVEQFaAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 194 FSAESLCERILDSSCSLLITTDAFYRGEKLVnlkeLADESLEKCREK------GFPVRCCI--VVKHVgraelgmndsps 265
Cdd:PRK08751 110 YTPRELKHQLIDSGASVLVVIDNFGTTVQQV----IADTPVKQVITTglgdmlGFPKAALVnfVVKYV------------ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 266 qsppvKRQCPDVQISwneGVDLWWHELMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPKGVvhtiggyMLyvatTFKYVF 345
Cdd:PRK08751 174 -----KKLVPEYRIN---GAIRFREALALGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGA-------ML----THRNLV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 346 DFHPEDVFWCTADIGWITGHSYV-TYGPL-------ANGATSVLFEGIPTYPDESR-LWSIVDKYKVTKFyTAPTAIRML 416
Cdd:PRK08751 235 ANMQQAHQWLAGTGKLEEGCEVViTALPLyhifaltANGLVFMKIGGCNHLISNPRdMPGFVKELKKTRF-TAFTGVNTL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 417 M-KFGDEP-VTKHSRASLQVLGTVGEPINPEAWLWYHRVVGsqhCPIVDTFWQTETgghmlTPLPGATPMK----PGSAS 490
Cdd:PRK08751 314 FnGLLNTPgFDQIDFSSLKMTLGGGMAVQRSVAERWKQVTG---LTLVEAYGLTET-----SPAACINPLTlkeyNGSIG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 491 FPFFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRTIYGNHTrfETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDD 570
Cdd:PRK08751 386 LPIPSTDACIKDDAGTVLAIGEIGELCIKGP--QVMKGYWKRPE--ETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKD 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 571 MLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDghtfsSTLT-EELKKQIREKIGPIATPDYIQ 649
Cdd:PRK08751 462 MILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVKKD-----PALTaEDVKAHARANLTGYKQPRIIE 536
|
570 580
....*....|....*....|..
gi 625195332 650 NAPGLPKTRSGKIMRRVLRKIA 671
Cdd:PRK08751 537 FRKELPKTNVGKILRRELRDAA 558
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
308-664 |
5.53e-17 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 82.69 E-value: 5.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 308 EDPLFILYTSGSTGKPKGVvhtiggyMLYVATTFKYVFDFHPEDVFWCTADIGWITGHSYVTYGpLANGATSVLFEG-IP 386
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAV-------LLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGG-LWWILTCLIHGGlCV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 387 TYPDESRLWS---IVDKYKVTKFYTAPTAIRMLMKfgdepVTKHSRA---SLQVLGTVGE-PINPEA--WLWYHRVVGSQ 457
Cdd:cd17635 73 TGGENTTYKSlfkILTTNAVTTTCLVPTLLSKLVS-----ELKSANAtvpSLRLIGYGGSrAIAADVrfIEATGLTNTAQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 458 HcpivdtFWQTETGGHMLTPLpGATPMKPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPWpgIMRTIYGNHTRFE 537
Cdd:cd17635 148 V------YGLSETGTALCLPT-DDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPA--NMLGYWNNPERTA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 538 TTYFKkfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGEcLYCFVTL 617
Cdd:cd17635 219 EVLID---GWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGE-LVGLAVV 294
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 625195332 618 CDGHTFSSTLTeELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMR 664
Cdd:cd17635 295 ASAELDENAIR-ALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
137-667 |
7.34e-17 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 83.46 E-value: 7.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 137 TYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITTda 216
Cdd:cd17652 14 TYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLLTT-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 217 fyrgeklvnlkeladeslekcrekgfpvrccivvkhvgraelgmndspsqsppvkrqcpdvqiswnegvdlwwhelmqea 296
Cdd:cd17652 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 297 gdefepewcdAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYvFDFHPEDVFWCTADIGWITGHSYVTYGPLAnG 376
Cdd:cd17652 92 ----------PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAA-FDVGPGSRVLQFASPSFDASVWELLMALLA-G 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 377 ATSVLFEGIPTYPDESrLWSIVDKYKVTkFYTAPTAIRMLMKFGDEPvtkhsraSLQVLGTVGEPINPE-AWLWyhrvvg 455
Cdd:cd17652 160 ATLVLAPAEELLPGEP-LADLLREHRIT-HVTLPPAALAALPPDDLP-------DLRTLVVAGEACPAElVDRW------ 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 456 SQHCPIVDTFWQTET--GGHMLTPLPGATPMKPGSasfPFFGVAPAILNESGeelegeaegylvfkQPWP-GIMRTIY-- 530
Cdd:cd17652 225 APGRRMINAYGPTETtvCATMAGPLPGGGVPPIGR---PVPGTRVYVLDARL--------------RPVPpGVPGELYia 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 531 ------GNHTRFETTYfKKF-------PG--YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVA 595
Cdd:cd17652 288 gaglarGYLNRPGLTA-ERFvadpfgaPGsrMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVA 366
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 625195332 596 EAAVVGHPHPVKGECLYCFVTLCDGhtfSSTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 667
Cdd:cd17652 367 EAVVVVRDDRPGDKRLVAYVVPAPG---AAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
136-669 |
1.22e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 85.01 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 136 ITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITTD 215
Cdd:PRK12316 2029 LSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQR 2108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 216 AFYrgEKLVNLKELADESLEkcrekgfpvrccivvkhvgrAELGMNDSPSQSPPVKrqcpdvqiswnegvdlwwhelmqe 295
Cdd:PRK12316 2109 HLL--ERLPLPAGVARLPLD--------------------RDAEWADYPDTAPAVQ------------------------ 2142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 296 agdefepewCDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYvFDFHPEDVFWCTADIGWITGHSYVtYGPLAN 375
Cdd:PRK12316 2143 ---------LAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGER-YELSPADCELQFMSFSFDGAHEQW-FHPLLN 2211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 376 GATSVLFEGipTYPDESRLWSIVDKYKVTKFYTAPTairMLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVG 455
Cdd:PRK12316 2212 GARVLIRDD--ELWDPEQLYDEMERHGVTILDFPPV---YLQQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLAWEALR 2286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 456 SQHcpIVDTFWQTETgghMLTPLP-GATPMKPGSASFPFFGVAPA-----ILNESgeelegeaegylvFKQPWPGIMRTI 529
Cdd:PRK12316 2287 PVY--LFNGYGPTEA---VVTPLLwKCRPQDPCGAAYVPIGRALGnrrayILDAD-------------LNLLAPGMAGEL 2348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 530 YGNHTRFETTYFKKfPG-----------------YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHE 592
Cdd:PRK12316 2349 YLGGEGLARGYLNR-PGltaerfvpdpfsasgerLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHP 2427
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 625195332 593 AVAEAAVVGHPHPvKGECLYCFVTLCDGHTfssTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:PRK12316 2428 AVREAVVVAQDGA-SGKQLVAYVVPDDAAE---DLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPK 2500
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
117-661 |
1.28e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 83.40 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 117 LGDKVAFYWeGNEpgettKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSA 196
Cdd:PRK07798 16 VPDRVALVC-GDR-----RLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 197 ESLCERILDSSCSLLITTDAFyrGEKLVNLKEladeSLEKcrekgfpVRCCIVVkhvgraelgmNDSPSQSPPVkrqcpd 276
Cdd:PRK07798 90 DELRYLLDDSDAVALVYEREF--APRVAEVLP----RLPK-------LRTLVVV----------EDGSGNDLLP------ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 277 vqiswnEGVDlwWHELMQEAGDE--FEPEwcdAEDPLFILYTSGSTGKPKGVV---HTI-----GGYMLYVATTfkyvfd 346
Cdd:PRK07798 141 ------GAVD--YEDALAAGSPErdFGER---SPDDLYLLYTGGTTGMPKGVMwrqEDIfrvllGGRDFATGEP------ 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 347 fhPEDVFWCTADIGWITGHSYVTYGPLANGAT-----SVLFEG--IPTYPDES----RLWSIVDKYKVTkfytaptaiRM 415
Cdd:PRK07798 204 --IEDEEELAKRAAAGPGMRRFPAPPLMHGAGqwaafAALFSGqtVVLLPDVRfdadEVWRTIEREKVN---------VI 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 416 LMkFGD---EPVTKHSRA-------SLQVLGTVGEPINP---EAWLwyhrvvgsQHCP---IVDTFWQTETGGHMLtplp 479
Cdd:PRK07798 273 TI-VGDamaRPLLDALEArgpydlsSLFAIASGGALFSPsvkEALL--------ELLPnvvLTDSIGSSETGFGGS---- 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 480 GATPMKPGSASFPFFGVAPAILnesgeelegeaegylVFK------QPWPGiMRTIYGNHTRFETTYFKK-------FP- 545
Cdd:PRK07798 340 GTVAKGAVHTGGPRFTIGPRTV---------------VLDedgnpvEPGSG-EIGWIARRGHIPLGYYKDpektaetFPt 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 546 --G--YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGH 621
Cdd:PRK07798 404 idGvrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGA 483
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 625195332 622 TFSStltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGK 661
Cdd:PRK07798 484 RPDL---AELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
136-670 |
1.82e-16 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 82.97 E-value: 1.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 136 ITYRELLVQVCQFSNVLRKQ-GIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITt 214
Cdd:PLN02574 67 ISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFT- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 215 dafyrgeklvnlkelADESLEKCREKGFPVrccivvkhVGRAELGMNDSPSQSPPVkrqcpdvqiswnegvdlwWHELMQ 294
Cdd:PLN02574 146 ---------------SPENVEKLSPLGVPV--------IGVPENYDFDSKRIEFPK------------------FYELIK 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 295 EAGDEFEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYVFDFHP----EDVFWCTADIGWITGHSYVTY 370
Cdd:PLN02574 185 EDFDFVPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFEASQYEypgsDNVYLAALPMFHIYGLSLFVV 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 371 GPLANGATSVLFEGIptypDESRLWSIVDKYKVTKFYTAPTAIRMLMKfGDEPVTKHSRASLQVLGTVGEPINPEAWLWY 450
Cdd:PLN02574 265 GLLSLGSTIVVMRRF----DASDMVKVIDRFKVTHFPVVPPILMALTK-KAKGVCGEVLKSLKQVSCGAAPLSGKFIQDF 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 451 HRVVgsQHCPIVDTFWQTETGGHMLTPLPGATPMKPGSASFpffgVAPAILNESGEELEGEAEGYLVFKQPW---PGIMR 527
Cdd:PLN02574 340 VQTL--PHVDFIQGYGMTESTAVGTRGFNTEKLSKYSSVGL----LAPNMQAKVVDWSTGCLLPPGNCGELWiqgPGVMK 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 528 TIYGNHTRFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVK 607
Cdd:PLN02574 414 GYLNNPKATQSTIDKD--GWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKEC 491
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 625195332 608 GECLYCFVTLCDGhtfsSTLTEE-LKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKI 670
Cdd:PLN02574 492 GEIPVAFVVRRQG----STLSQEaVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRS 551
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
107-406 |
1.94e-16 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 83.00 E-value: 1.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 107 VLDRNVHekKLGDKVAFYWEGnepgetTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGAL 186
Cdd:PRK08279 42 VFEEAAA--RHPDRPALLFED------QSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 187 HSIVFAGFSAESL--CERILDSscSLLITtdafyrGEKLVNLKELADESLEKcrekgfPVRCCIVVKHVGRAELGMNDSP 264
Cdd:PRK08279 114 VALLNTQQRGAVLahSLNLVDA--KHLIV------GEELVEAFEEARADLAR------PPRLWVAGGDTLDDPEGYEDLA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 265 SQSppvkRQCPDVQISWNEGVdlwwhelmqeagdefepewcDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVAtTFKYV 344
Cdd:PRK08279 180 AAA----AGAPTTNPASRSGV--------------------TAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMG-GFGGL 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 625195332 345 FDFHPEDVFWCTADIGWITGHSYVTYGPLANGATSVL---FEGiptypdeSRLWSIVDKYKVTKF 406
Cdd:PRK08279 235 LRLTPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALrrkFSA-------SRFWDDVRRYRATAF 292
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
131-673 |
2.07e-16 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 82.72 E-value: 2.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 131 GETTKI-TYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCS 209
Cdd:PLN02246 45 GATGRVyTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 210 LLITTDAFYrgEKLVNLKEladeslekcrEKGFPVRCCivvkhvgraelgmnDSPsqsppvkrqcPDVQISWNEgvdlww 289
Cdd:PLN02246 125 LIITQSCYV--DKLKGLAE----------DDGVTVVTI--------------DDP----------PEGCLHFSE------ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 290 heLMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVAttfKYV------FDFHPEDVFWCTADIGWIT 363
Cdd:PLN02246 163 --LTQADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVA---QQVdgenpnLYFHSDDVILCVLPMFHIY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 364 GHSYVTYGPLANGATSVLfegIPTYpDESRLWSIVDKYKVTkfyTAPTAIRMLMKFGDEP-VTKHSRASLQVLGTVGEPI 442
Cdd:PLN02246 238 SLNSVLLCGLRVGAAILI---MPKF-EIGALLELIQRHKVT---IAPFVPPIVLAIAKSPvVEKYDLSSIRMVLSGAAPL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 443 NPEawlwyhrvvgsqhcpIVDTFW-------------QTETGGHMLTPLPGA---TPMKPGSAsfpffgvAPAILNESGE 506
Cdd:PLN02246 311 GKE---------------LEDAFRaklpnavlgqgygMTEAGPVLAMCLAFAkepFPVKSGSC-------GTVVRNAELK 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 507 ELEGEAEGYLVFKQPW------PGIMRTIYGNHTRFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLS 580
Cdd:PLN02246 369 IVDPETGASLPRNQPGeicirgPQIMKGYLNDPEATANTIDKD--GWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVA 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 581 TAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfsSTLTE-ELK----KQI--REKIGPIATPDYIqnapg 653
Cdd:PLN02246 447 PAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNG----SEITEdEIKqfvaKQVvfYKRIHKVFFVDSI----- 517
|
570 580
....*....|....*....|.
gi 625195332 654 lPKTRSGKIMRRVLR-KIAQN 673
Cdd:PLN02246 518 -PKAPSGKILRKDLRaKLAAG 537
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
115-668 |
2.33e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 82.89 E-value: 2.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 115 KKLGDKVAFywegNEPGETtkITYRELLVQVCQFSNVLRKQ-GIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAG 193
Cdd:PRK05677 35 QRFADKPAF----SNLGKT--LTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 194 FSAESLCERILDSSCSLLITtdafyrgekLVNLKELADESLEKCRekgfpvrccivVKHVGRAELGmndspSQSPPVKRQ 273
Cdd:PRK05677 109 YTAREMEHQFNDSGAKALVC---------LANMAHLAEKVLPKTG-----------VKHVIVTEVA-----DMLPPLKRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 274 CPDVQISWNEGVDLWWH---------ELMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPKGVVHT---IGGYMLYVATTF 341
Cdd:PRK05677 164 LINAVVKHVKKMVPAYHlpqavkfndALAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLThrnLVANMLQCRALM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 342 K-------------------YVFDFHpedvfwCTAdigwitghsyvtygPLANGATSVLfegIPTYPDESRLWSIVDKYK 402
Cdd:PRK05677 244 GsnlnegceiliaplplyhiYAFTFH------CMA--------------MMLIGNHNIL---ISNPRDLPAMVKELGKWK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 403 VTKFYTAPTAIRMLMKfgDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGsqhCPIVDTFWQTETgghmlTPLPGAT 482
Cdd:PRK05677 301 FSGFVGLNTLFVALCN--NEAFRKLDFSALKLTLSGGMALQLATAERWKEVTG---CAICEGYGMTET-----SPVVSVN 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 483 PMK---PGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRTIYGNHTrfETTYFKKFPGYYVTGDGCRRDQD 559
Cdd:PRK05677 371 PSQaiqVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVKGP--QVMKGYWQRPE--ATDEILDSDGWLKTGDIALIQED 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 560 GYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfsSTLTEE-LKKQIREK 638
Cdd:PRK05677 447 GYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPG----ETLTKEqVMEHMRAN 522
|
570 580 590
....*....|....*....|....*....|
gi 625195332 639 IGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:PRK05677 523 LTGYKVPKAVEFRDELPTTNVGKILRRELR 552
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
129-668 |
6.53e-16 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 81.08 E-value: 6.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 129 EPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGAlhsiVF-----AGFSAEsLCERI 203
Cdd:PRK07514 22 ETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGA----VFlplntAYTLAE-LDYFI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 204 LDSSCSLLITTDAfyrgeklvnlkelADESLEKCREK-GfpvrccivVKHVgrAELGMNDSPSQSppvkrqcpdvqiswn 282
Cdd:PRK07514 97 GDAEPALVVCDPA-------------NFAWLSKIAAAaG--------APHV--ETLDADGTGSLL--------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 283 egvdlwwhELMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGGyMLYVATTFKYVFDFHPEDVFWCTADIGWI 362
Cdd:PRK07514 139 --------EAAAAAPDDFETVPRGADDLAAILYTSGTTGRSKGAMLSHGN-LLSNALTLVDYWRFTPDDVLIHALPIFHT 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 363 TGHSYVTYGPLANGA------------------TSVLFEGIPTypdesrlwsivdkykvtkFYTaptaiRMLmkfgDEP- 423
Cdd:PRK07514 210 HGLFVATNVALLAGAsmiflpkfdpdavlalmpRATVMMGVPT------------------FYT-----RLL----QEPr 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 424 ----VTKHSRasLQVLGTVgePINPEAWL-WYHRvvgSQHcPIVDTFWQTETGghMLTPLPGATPMKPGSASFPFFGVAP 498
Cdd:PRK07514 263 ltreAAAHMR--LFISGSA--PLLAETHReFQER---TGH-AILERYGMTETN--MNTSNPYDGERRAGTVGFPLPGVSL 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 499 AILNESGEELEGEAEGYL-------VFKQPW--PGimrtiygnHTRFETTYfkkfPGYYVTGDGCRRDQDGYYWITGRID 569
Cdd:PRK07514 333 RVTDPETGAELPPGEIGMievkgpnVFKGYWrmPE--------KTAEEFRA----DGFFITGDLGKIDERGYVHIVGRGK 400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 570 DMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFS-STLTEELKKQI-REKIgpiatPDY 647
Cdd:PRK07514 401 DLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDeAAILAALKGRLaRFKQ-----PKR 475
|
570 580
....*....|....*....|.
gi 625195332 648 IQNAPGLPKTRSGKIMRRVLR 668
Cdd:PRK07514 476 VFFVDELPRNTMGKVQKNLLR 496
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
135-673 |
6.66e-16 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 81.19 E-value: 6.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 135 KITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGAlhSIVFAGFSAES--LCERILDSSCSLLI 212
Cdd:PRK10946 48 QFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGV--APVNALFSHQRseLNAYASQIEPALLI 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 213 TTdafyRGEKLVNLKELADESLEKCRekgfpvRCCIVVKHvgraelgmNDSPSQSppvkrqcpdvqiswnegVDLWwhel 292
Cdd:PRK10946 126 AD----RQHALFSDDDFLNTLVAEHS------SLRVVLLL--------NDDGEHS-----------------LDDA---- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 293 MQEAGDEFEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKyVFDFHPEDVFWCTADigwiTGHSYVTYGP 372
Cdd:PRK10946 167 INHPAEDFTATPSPADEVAFFQLSGGSTGTPKLIPRTHNDYYYSVRRSVE-ICGFTPQTRYLCALP----AAHNYPMSSP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 373 lanGATSVLFEG----IPTYPDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVTKHSRASLQVLGTVGEPINP---- 444
Cdd:PRK10946 242 ---GALGVFLAGgtvvLAPDPSATLCFPLIEKHQVNVTALVPPAVSLWLQAIAEGGSRAQLASLKLLQVGGARLSEtlar 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 445 -----------------EAWLWYHR-------VVGSQHCPIV--DTFWQTETGGHmltPLPGATP---MKPGSASFPFFG 495
Cdd:PRK10946 319 ripaelgcqlqqvfgmaEGLVNYTRlddsderIFTTQGRPMSpdDEVWVADADGN---PLPQGEVgrlMTRGPYTFRGYY 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 496 VAPAilnesgeelegeaegylvfkqpwpgimrtiyGNHTRFETTyfkkfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVS 575
Cdd:PRK10946 396 KSPQ-------------------------------HNASAFDAN------GFYCSGDLVSIDPDGYITVVGREKDQINRG 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 576 GHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGE--CLYCFVTlcdghtfSSTLTEELKKQIREK-IGPIATPDYIQNAP 652
Cdd:PRK10946 439 GEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEksCAFLVVK-------EPLKAVQLRRFLREQgIAEFKLPDRVECVD 511
|
570 580
....*....|....*....|.
gi 625195332 653 GLPKTRSGKIMRRVLRKIAQN 673
Cdd:PRK10946 512 SLPLTAVGKVDKKQLRQWLAS 532
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
136-669 |
7.02e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 82.52 E-value: 7.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 136 ITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITtd 215
Cdd:PRK12467 538 LSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLT-- 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 216 afyRGEKLVNLKELADESLEKCREKGFPVRccivvkhvGRAELgmNDSPSQSPpvkrqcpdvqiswnegvdlwwhelmqe 295
Cdd:PRK12467 616 ---QSHLLAQLPVPAGLRSLCLDEPADLLC--------GYSGH--NPEVALDP--------------------------- 655
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 296 agdefepewcdaEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYvFDFHPEDVFWCTADIGWITGHsYVTYGPLAN 375
Cdd:PRK12467 656 ------------DNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAER-LQLAADDSMLMVSTFAFDLGV-TELFGALAS 721
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 376 GATsVLFEGIPTYPDESRLWSIVDKYKVTKFYTAPTAIRMLMKfgDEPVTKHSRASLQVLGtvGEpINPEAWLWYHRVVG 455
Cdd:PRK12467 722 GAT-LHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQ--ASRVALPRPQRALVCG--GE-ALQVDLLARVRALG 795
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 456 SQhCPIVDTFWQTETGGHMLT-PLPGATpmKPGSASF---PFFGVAPAILNEsgeelegeaegYLvfkQPWP-GIMRTIY 530
Cdd:PRK12467 796 PG-ARLINHYGPTETTVGVSTyELSDEE--RDFGNVPigqPLANLGLYILDH-----------YL---NPVPvGVVGELY 858
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 531 --------GNHTR--FETTYFKKFPG------YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAV 594
Cdd:PRK12467 859 iggaglarGYHRRpaLTAERFVPDPFgadggrLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGV 938
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 625195332 595 AEAAVVGHPHPVKGECL-YCFVTLCDGHTFSSTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:PRK12467 939 REAVVLAQPGDAGLQLVaYLVPAAVADGAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPK 1014
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
309-664 |
8.22e-16 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 79.24 E-value: 8.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 309 DPLFILYTSGSTGKPKGVVHTIGGyMLYVATTFKYVFDFHPEDVFWCTADIGWITGHSyVTYGPLANGATSVLFEGIpty 388
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGN-LIAANLQLIHAMGLTEADVYLNMLPLFHIAGLN-LALATFHAGGANVVMEKF--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 389 pDESRLWSIVDKYKVTKFYTAPTAIRMLMkfgdEPVTKHSR--ASLQVLGTVGEPINPEAWlwyHRVVGSqhcpivdTFW 466
Cdd:cd17637 76 -DPAEALELIEEEKVTLMGSFPPILSNLL----DAAEKSGVdlSSLRHVLGLDAPETIQRF---EETTGA-------TFW 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 467 ----QTETGGhMLTPLPGATpmKPGSASFPFFGVAPAILNESGEELEGEAEGY------LVFKQPWPGIMRTiygNHTrf 536
Cdd:cd17637 141 slygQTETSG-LVTLSPYRE--RPGSAGRPGPLVRVRIVDDNDRPVPAGETGEivvrgpLVFQGYWNLPELT---AYT-- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 537 ettyFKKfpGYYVTGDGCRRDQDGYYWITGRI--DDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCF 614
Cdd:cd17637 213 ----FRN--GWHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAV 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 625195332 615 VTLCDGHTFSStltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMR 664
Cdd:cd17637 287 CVLKPGATLTA---DELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| ACAS_N |
pfam16177 |
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many ... |
47-107 |
1.19e-15 |
|
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many acetyl-coenzyme A synthetase enzymes.
Pssm-ID: 465043 [Multi-domain] Cd Length: 55 Bit Score: 71.35 E-value: 1.19e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 625195332 47 YRELHRHSVEEPGEFWGNIAKEFYWKTPCpgpflQYNFDVTKGkIFTEWMKGATTNICYNV 107
Cdd:pfam16177 1 YEALYRRSIEDPEGFWGEVAKELDWFKPF-----DKVLDGSNG-PFAKWFVGGKLNVCYNC 55
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
131-669 |
5.71e-15 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 77.73 E-value: 5.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 131 GETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLcERILDSS-CS 209
Cdd:cd17653 18 SLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARI-QAILRTSgAT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 210 LLITTDAfyrgeklvnlkeladeslekcrekgfpvrccivvkhvgraelgmndspsqsppvkrqcpdvqiswnegvdlww 289
Cdd:cd17653 97 LLLTTDS------------------------------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 290 helmqeagdefepewcdAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATT---------------FKYVFDFhpedvfw 354
Cdd:cd17653 104 -----------------PDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPparldvgpgsrvaqvLSIAFDA------- 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 355 CTADIgwitghsyvtYGPLANGATSVLFEGIPTYPDESRlwsivdkyKVTKFYTAPTAIRMLmkfgdepvtkhSRASLQV 434
Cdd:cd17653 160 CIGEI----------FSTLCNGGTLVLADPSDPFAHVAR--------TVDALMSTPSILSTL-----------SPQDFPN 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 435 LGTV---GEPINP---EAWlWYHRVV----GSQHCPIVDTFWQTETGghmlTPLPGATPMkPGSASFpffgvapaILNES 504
Cdd:cd17653 211 LKTIflgGEAVPPsllDRW-SPGRRLynayGPTECTISSTMTELLPG----QPVTIGKPI-PNSTCY--------ILDAD 276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 505 geelegeaegylvfKQPWP------------GIMRTIYGNH----TRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRI 568
Cdd:cd17653 277 --------------LQPVPegvvgeicisgvQVARGYLGNPaltaSKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGRE 342
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 569 DDMLNVSGHLLSTAEVES-ALVEHEAVAEAAVVGHphpvkGECLYCFVTLcdghtfSSTLTEELKKQIREKIGPIATPDY 647
Cdd:cd17653 343 DNQVKVRGFRINLEEIEEvVLQSQPEVTQAAAIVV-----NGRLVAFVTP------ETVDVDGLRSELAKHLPSYAVPDR 411
|
570 580
....*....|....*....|..
gi 625195332 648 IQNAPGLPKTRSGKIMRRVLRK 669
Cdd:cd17653 412 IIALDSFPLTANGKVDRKALRE 433
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
140-668 |
9.67e-15 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 77.43 E-value: 9.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 140 ELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLIT-TDAFy 218
Cdd:PRK12406 16 ELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAhADLL- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 219 rgeklvnlkeladESLEKCREKGFPVRCCIVVKHVgRAELGMndspsqsPPVKRQCPDVQISWNEgvdlwWheLMQEAGD 298
Cdd:PRK12406 95 -------------HGLASALPAGVTVLSVPTPPEI-AAAYRI-------SPALLTPPAGAIDWEG-----W--LAQQEPY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 299 EFEPewcdAEDPLFILYTSGSTGKPKGVVHTIG------GYMLYVATtfkyVFDFHPEDVFWCTadigwitGHSYVT--- 369
Cdd:PRK12406 147 DGPP----VPQPQSMIYTSGTTGHPKGVRRAAPtpeqaaAAEQMRAL----IYGLKPGIRALLT-------GPLYHSapn 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 370 -YGPLAN--GATSVL---FEgiptyPDEsrLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVTKHSRASLQVLGTVGEPIN 443
Cdd:PRK12406 212 aYGLRAGrlGGVLVLqprFD-----PEE--LLQLIERHRITHMHMVPTMFIRLLKLPEEVRAKYDVSSLRHVIHAAAPCP 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 444 PE------AWlWyhrvvgsqhCPIVDTFW-QTETGGhmltpLPGATP----MKPGSASFPFFGVAPAILNESGEELEGEA 512
Cdd:PRK12406 285 ADvkramiEW-W---------GPVIYEYYgSTESGA-----VTFATSedalSHPGTVGKAAPGAELRFVDEDGRPLPQGE 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 513 EGYLVFKQPwpGIMRTIYGNHTRFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHE 592
Cdd:PRK12406 350 IGEIYSRIA--GNPDFTYHNKPEKRAEIDRG--GFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVP 425
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 625195332 593 AVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSstlTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:PRK12406 426 GVHDCAVFGIPDAEFGEALMAVVEPQPGATLD---EADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLR 498
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
134-667 |
1.16e-14 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 78.16 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 134 TKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLcERIL-DSSCSLLI 212
Cdd:PRK10252 482 YQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRL-KMMLeDARPSLLI 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 213 TTDAFyrGEKLVNLKELADESLekcrekgfpvrccivvkhvgRAELgmndSPSQSPPVKRQCPDvqiswnegvdlwwhel 292
Cdd:PRK10252 561 TTADQ--LPRFADVPDLTSLCY--------------------NAPL----APQGAAPLQLSQPH---------------- 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 293 mqeagdefepewcdaeDPLFILYTSGSTGKPKGVV--HT-IGGYMLYVATTFKyvfdFHPEDVFW----CTADIG----- 360
Cdd:PRK10252 599 ----------------HTAYIIFTSGSTGRPKGVMvgQTaIVNRLLWMQNHYP----LTADDVVLqktpCSFDVSvweff 658
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 361 WitghsyvtygPLANGATSVLFEgiptyPDESR----LWSIVDKYKVTKFYTAPTairMLMKFGDEPVTKHSRASLQVLG 436
Cdd:PRK10252 659 W----------PFIAGAKLVMAE-----PEAHRdplaMQQFFAEYGVTTTHFVPS---MLAAFVASLTPEGARQSCASLR 720
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 437 TV---GEPINPEAWLWYHRVVGSqhcPIVDTFWQTE---------TGGHMLTPLPGAT-PMkpgsaSFPFFGVAPAILNE 503
Cdd:PRK10252 721 QVfcsGEALPADLCREWQQLTGA---PLHNLYGPTEaavdvswypAFGEELAAVRGSSvPI-----GYPVWNTGLRILDA 792
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 504 SGeelegeaegylvfkQPWP-GIMRTIY--------GNHTRFETTYfKKF------PG--YYVTGDGCRRDQDGYYWITG 566
Cdd:PRK10252 793 RM--------------RPVPpGVAGDLYltgiqlaqGYLGRPDLTA-SRFiadpfaPGerMYRTGDVARWLDDGAVEYLG 857
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 567 RIDDMLNVSGHLLSTAEVESALVEH----EAVAEAAVVGHPHPVKGEC--LYCFVTLCDGHTFSStltEELKKQIREKIG 640
Cdd:PRK10252 858 RSDDQLKIRGQRIELGEIDRAMQALpdveQAVTHACVINQAAATGGDArqLVGYLVSQSGLPLDT---SALQAQLRERLP 934
|
570 580
....*....|....*....|....*..
gi 625195332 641 PIATPDYIQNAPGLPKTRSGKIMRRVL 667
Cdd:PRK10252 935 PHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
135-667 |
1.30e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 78.28 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 135 KITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITT 214
Cdd:PRK12467 1599 ELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQ 1678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 215 dafyrgeklvnlKELADEslekcrekgFPVrccivvkhvgraelgmndspsqspPVKRQCPDVqiswnEGVDLWWhelmq 294
Cdd:PRK12467 1679 ------------SHLQAR---------LPL------------------------PDGLRSLVL-----DQEDDWL----- 1703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 295 EAGDEFEPEWCDAEDPL-FILYTSGSTGKPKGVVHTIGGYM-LYVATtfKYVFDFHPEDVfwctadigWITGHSYV---- 368
Cdd:PRK12467 1704 EGYSDSNPAVNLAPQNLaYVIYTSGSTGRPKGAGNRHGALVnRLCAT--QEAYQLSAADV--------VLQFTSFAfdvs 1773
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 369 ---TYGPLANGAtSVLFEGIPTYPDESRLWSIVDKYKVTKFYTAPTAIRMLMKFgDEPVTKHSraSLQVLGTVGEPINPE 445
Cdd:PRK12467 1774 vweLFWPLINGA-RLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQM-DEQVEHPL--SLRRVVCGGEALEVE 1849
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 446 AW-LWYHRVVGSQhcpIVDTFWQTETGGHmLTPLPGATPMKPGSASFPFfGVAPAILNEsgeelegeaegYLVFKQ--PW 522
Cdd:PRK12467 1850 ALrPWLERLPDTG---LFNLYGPTETAVD-VTHWTCRRKDLEGRDSVPI-GQPIANLST-----------YILDASlnPV 1913
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 523 P-GIMRTIY--------GNH-------TRFETTYFKKFPG-YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVE 585
Cdd:PRK12467 1914 PiGVAGELYlggvglarGYLnrpaltaERFVADPFGTVGSrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIE 1993
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 586 SALVEHEAVAEAAVVGHPHPvKGECLYCFVT-----LCDGHTFSSTLTEELKKQIREKIgpiatPDYIQNA-----PGLP 655
Cdd:PRK12467 1994 ARLREQGGVREAVVIAQDGA-NGKQLVAYVVptdpgLVDDDEAQVALRAILKNHLKASL-----PEYMVPAhlvflARMP 2067
|
570
....*....|..
gi 625195332 656 KTRSGKIMRRVL 667
Cdd:PRK12467 2068 LTPNGKLDRKAL 2079
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
115-671 |
1.46e-14 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 77.17 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 115 KKLGDKVAFywegNEPGETtkITYRELLVQVCQFSNVLRKQ-GIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAG 193
Cdd:PRK12492 35 KKFADRPAF----SNLGVT--LSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 194 FSAESLCERILDSSCSLLITTDAFyrgEKLVNlKELADESLEKCRE----------KGFPVRccIVVKHVgraelgmnds 263
Cdd:PRK12492 109 YTAREMRHQFKDSGARALVYLNMF---GKLVQ-EVLPDTGIEYLIEakmgdllpaaKGWLVN--TVVDKV---------- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 264 psqsppvKRQCPDVQISWNEGVDlwwHELMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGGY---MLYVATT 340
Cdd:PRK12492 173 -------KKMVPAYHLPQAVPFK---QALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLvanMLQVRAC 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 341 F-KYVFDFHP-----EDVFWCTADIGWITGHSYVTYGPLANGATSVLFEG---IPTYPDEsrlwsiVDKYKVTKFYTAPT 411
Cdd:PRK12492 243 LsQLGPDGQPlmkegQEVMIAPLPLYHIYAFTANCMCMMVSGNHNVLITNprdIPGFIKE------LGKWRFSALLGLNT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 412 AIRMLMkfgDEPVTKHSRAS-LQVLGTVGEPI---NPEAWlwyHRVVGsqhCPIVDTFWQTETgghmlTPLPGATPM--- 484
Cdd:PRK12492 317 LFVALM---DHPGFKDLDFSaLKLTNSGGTALvkaTAERW---EQLTG---CTIVEGYGLTET-----SPVASTNPYgel 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 485 -KPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRtiyGNHTRFETTY-FKKFPGYYVTGDGCRRDQDGYY 562
Cdd:PRK12492 383 aRLGTVGIPVPGTALKVIDDDGNELPLGERGELCIKGP--QVMK---GYWQQPEATAeALDAEGWFKTGDIAVIDPDGFV 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 563 WITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfsSTLTEELKKQIREKIGPI 642
Cdd:PRK12492 458 RIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDP----GLSVEELKAYCKENFTGY 533
|
570 580
....*....|....*....|....*....
gi 625195332 643 ATPDYIQNAPGLPKTRSGKIMRRVLRKIA 671
Cdd:PRK12492 534 KVPKHIVLRDSLPMTPVGKILRRELRDIA 562
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
546-669 |
2.75e-14 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 75.94 E-value: 2.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 546 GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSS 625
Cdd:PRK06018 410 GFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATR 489
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 625195332 626 tltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:PRK06018 490 ---EEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALRE 530
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
289-606 |
4.24e-14 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 75.58 E-value: 4.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 289 WHELMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGGYMlYVATTFKYVFDFHPEDVFWCTADIGWITGHSYV 368
Cdd:cd05932 118 WDDLIAQHPPLEERPTRFPEQLATLIYTSGTTGQPKGVMLTFGSFA-WAAQAGIEHIGTEENDRMLSYLPLAHVTERVFV 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 369 TYGPLANGATSVLFEGIPTYPDEsrlwsiVDKYKVTKFYTAPtaiRMLMKFGDEPVTKHSRASLQ--------------- 433
Cdd:cd05932 197 EGGSLYGGVLVAFAESLDTFVED------VQRARPTLFFSVP---RLWTKFQQGVQDKIPQQKLNlllkipvvnslvkrk 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 434 -----------VLGTVGEPINPEAWLWYHRVvgsqHCPIVDTFWQTETGGHMLTPLPGATpmKPGSASFPFFGVAPAIln 502
Cdd:cd05932 268 vlkglgldqcrLAGCGSAPVPPALLEWYRSL----GLNILEAYGMTENFAYSHLNYPGRD--KIGTVGNAGPGVEVRI-- 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 503 esgeelegEAEGYLVFKQPwpGIMRTIYGNHTRFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVS-GHLLST 581
Cdd:cd05932 340 --------SEDGEILVRSP--ALMMGYYKDPEATAEAFTAD--GFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAP 407
|
330 340
....*....|....*....|....*..
gi 625195332 582 AEVESALVEHEAVAEAAVVGH--PHPV 606
Cdd:cd05932 408 APIENKLAEHDRVEMVCVIGSglPAPL 434
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
546-664 |
4.39e-14 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 74.07 E-value: 4.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 546 GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfsS 625
Cdd:cd17638 215 GWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPG----V 290
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 625195332 626 TLTEE-LKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMR 664
Cdd:cd17638 291 TLTEEdVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
132-672 |
4.44e-14 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 75.65 E-value: 4.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 132 ETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLL 211
Cdd:PLN02479 42 GSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 212 ITTDAFYrgeklvnlkELADESL---EKCREKGFPVRCCIVVkhvgraelgmnDSPSQSPPvkrqcpDVQISWNEGVdLW 288
Cdd:PLN02479 122 MVDQEFF---------TLAEEALkilAEKKKSSFKPPLLIVI-----------GDPTCDPK------SLQYALGKGA-IE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 289 WHELMQEAGDEF-----EPEWcdaeDPLFILYTSGSTGKPKGVV-HTIGGYMLyvATTFKYVFDFHPEDVFWCTADIGWI 362
Cdd:PLN02479 175 YEKFLETGDPEFawkppADEW----QSIALGYTSGTTASPKGVVlHHRGAYLM--ALSNALIWGMNEGAVYLWTLPMFHC 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 363 TGHSYvTYGPLANGATSVLFEGIPTypdeSRLWSIVDKYKVTKFYTAPTAIRML------------------MKFGDEP- 423
Cdd:PLN02479 249 NGWCF-TWTLAALCGTNICLRQVTA----KAIYSAIANYGVTHFCAAPVVLNTIvnapksetilplprvvhvMTAGAAPp 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 424 ---VTKHSRASLQVLGTVG--EPINPE---AWL--WYH---------------RVVGSQHCPIVDTfwqtetgghmltpl 478
Cdd:PLN02479 324 psvLFAMSEKGFRVTHTYGlsETYGPStvcAWKpeWDSlppeeqarlnarqgvRYIGLEGLDVVDT-------------- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 479 pgaTPMKPGSASFPFFGVAPAILNesgeelegeaegyLVFKqpwpGIMRTIYGNHTRFETtyfkkfpGYYVTGDGCRRDQ 558
Cdd:PLN02479 390 ---KTMKPVPADGKTMGEIVMRGN-------------MVMK----GYLKNPKANEEAFAN-------GWFHSGDLGVKHP 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 559 DGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFS--STLTEELKKQIR 636
Cdd:PLN02479 443 DGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSdeAALAEDIMKFCR 522
|
570 580 590
....*....|....*....|....*....|....*.
gi 625195332 637 EKIGPIATPDYIQNAPgLPKTRSGKIMRRVLRKIAQ 672
Cdd:PLN02479 523 ERLPAYWVPKSVVFGP-LPKTATGKIQKHVLRAKAK 557
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
119-669 |
8.17e-14 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 74.63 E-value: 8.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 119 DKVAFYwegnEPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGAlhsiVFAGFSAES 198
Cdd:PLN02330 43 DKVAFV----EAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGG----VFSGANPTA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 199 LCERILD----SSCSLLITTDAFYrgeklvnlkeladeslEKCREKGFPVrccIVVKHVgraelgmndspsqsppvkrqC 274
Cdd:PLN02330 115 LESEIKKqaeaAGAKLIVTNDTNY----------------GKVKGLGLPV---IVLGEE--------------------K 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 275 PDVQISWNEGVDLwwhelMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPKGVVHTiggYMLYVATTFKYVFDFHPEDVFW 354
Cdd:PLN02330 156 IEGAVNWKELLEA-----ADRAGDTSDNEEILQTDLCALPFSSGTTGISKGVMLT---HRNLVANLCSSLFSVGPEMIGQ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 355 CTAdIGWITG-HSYvtygplanGATSVLFegiPTYPDESRLwSIVDKYKVTKFYTA------------PTAIRMLMKfgd 421
Cdd:PLN02330 228 VVT-LGLIPFfHIY--------GITGICC---ATLRNKGKV-VVMSRFELRTFLNAlitqevsfapivPPIILNLVK--- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 422 EPVTKH---SRASLQVLGTVGEPINPEAWLWYH-RVVGSQhcpIVDTFWQTETGGHMLT---PLPGATPMKPGSASFPFF 494
Cdd:PLN02330 292 NPIVEEfdlSKLKLQAIMTAAAPLAPELLTAFEaKFPGVQ---VQEAYGLTEHSCITLThgdPEKGHGIAKKNSVGFILP 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 495 GVAPAILNESGEelegeaegyLVFKQPWPG--------IMRTIYGNHTRFETTYFKKfpGYYVTGDGCRRDQDGYYWITG 566
Cdd:PLN02330 369 NLEVKFIDPDTG---------RSLPKNTPGelcvrsqcVMQGYYNNKEETDRTIDED--GWLHTGDIGYIDDDGDIFIVD 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 567 RIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSStltEELKKQIREKIGPIATPD 646
Cdd:PLN02330 438 RIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESE---EDILNFVAANVAHYKKVR 514
|
570 580
....*....|....*....|...
gi 625195332 647 YIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:PLN02330 515 VVQFVDSIPKSLSGKIMRRLLKE 537
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
308-667 |
9.44e-14 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 74.01 E-value: 9.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 308 EDPLFILYTSGSTGKPKGVV--------HTIGGYMLYVATTFKYV-------FDFHPEDVFwctadIGWITGHSYVTygp 372
Cdd:cd17644 106 ENLAYVIYTSGSTGKPKGVMiehqslvnLSHGLIKEYGITSSDRVlqfasiaFDVAAEEIY-----VTLLSGATLVL--- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 373 langatsVLFEGIPTYPDesrLWSIVDKYKVTKFYTAPTAIRMLMKFGdEPVTKHSRASLQVLGTVGEPINPEAW-LW-- 449
Cdd:cd17644 178 -------RPEEMRSSLED---FVQYIQQWQLTVLSLPPAYWHLLVLEL-LLSTIDLPSSLRLVIVGGEAVQPELVrQWqk 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 450 -------YHRVVGSQHCPIVDTFwqtetggHMLTPLPGATPMKPGSASfPFFGVAPAILNEsgeelegeaegylvFKQPW 522
Cdd:cd17644 247 nvgnfiqLINVYGPTEATIAATV-------CRLTQLTERNITSVPIGR-PIANTQVYILDE--------------NLQPV 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 523 P-GIMRTIYGNHTRFETTYF-------KKF--------PG--YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEV 584
Cdd:cd17644 305 PvGVPGELHIGGVGLARGYLnrpeltaEKFishpfnssESerLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEI 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 585 ESALVEHEAVAEAAVVGHPHPVKGECLYCFVTlcdGHTFSSTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMR 664
Cdd:cd17644 385 EAVLSQHNDVKTAVVIVREDQPGNKRLVAYIV---PHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDR 461
|
...
gi 625195332 665 RVL 667
Cdd:cd17644 462 RAL 464
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
115-382 |
3.52e-13 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 72.66 E-value: 3.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 115 KKLGDKVAFYWEGNEPGETTKITYRELLVQVCQFSNVLRKQGiQKGDRVAIYMPMILELVVAMLACARLGALHSIVFA-- 192
Cdd:cd05931 4 AARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPpt 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 193 -GFSAESLCERILDSSCSLLITTDAFyrgeklvnlkeladeslekcrekgfpvrccivvkhvgRAELgmndspsqsPPVK 271
Cdd:cd05931 83 pGRHAERLAAILADAGPRVVLTTAAA-------------------------------------LAAV---------RAFA 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 272 RQCPDVQISWNEGVDLwwheLMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKyVFDFHPED 351
Cdd:cd05931 117 ASRPAAGTPRLLVVDL----LPDTSAADWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRR-AYGLDPGD 191
|
250 260 270
....*....|....*....|....*....|....*
gi 625195332 352 --VFW--CTADIGWITGhsyvTYGPLANGATSVLF 382
Cdd:cd05931 192 vvVSWlpLYHDMGLIGG----LLTPLYSGGPSVLM 222
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
131-667 |
3.86e-13 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 73.66 E-value: 3.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 131 GETtkITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSL 210
Cdd:PRK05691 2211 GQT--LSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGL 2288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 211 LITTDAFYRGeklvnLKELADESLEKCREKGFPVRccivvkhvgraelgmnDSPSQSPPVKRQCPDVQIswnegvdlwwh 290
Cdd:PRK05691 2289 LLSDRALFEA-----LGELPAGVARWCLEDDAAAL----------------AAYSDAPLPFLSLPQHQA----------- 2336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 291 elmqeagdefepewcdaedplFILYTSGSTGKPKGVVHTIGGYMLYVATTFKyVFDFHPEDvfwCTADIGWIT--GHSYV 368
Cdd:PRK05691 2337 ---------------------YLIYTSGSTGKPKGVVVSHGEIAMHCQAVIE-RFGMRADD---CELHFYSINfdAASER 2391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 369 TYGPLANGATSVL-FEGiptYPDESRLWSIVDKYKVTKFYTAPTAIRMLMKFgdePVTKHSRASLQVLGTVGEPINPEAW 447
Cdd:PRK05691 2392 LLVPLLCGARVVLrAQG---QWGAEEICQLIREQQVSILGFTPSYGSQLAQW---LAGQGEQLPVRMCITGGEALTGEHL 2465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 448 LWYHRVVGSQHcpIVDTFWQTETgghMLTPLPGATP--MKPGSASFPFFGVAPA----ILNESGEELEGEAEGYLvfkqp 521
Cdd:PRK05691 2466 QRIRQAFAPQL--FFNAYGPTET---VVMPLACLAPeqLEEGAASVPIGRVVGArvayILDADLALVPQGATGEL----- 2535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 522 WPGIMRTIYGNH-------TRFETTYFKKFPG-YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEA 593
Cdd:PRK05691 2536 YVGGAGLAQGYHdrpgltaERFVADPFAADGGrLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPA 2615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 594 VAEAAVVGHPHPvKGECLYCFV---TLCDGHTFSSTLTEELKKQIREKIgpiatPDYIQNA-----PGLPKTRSGKIMRR 665
Cdd:PRK05691 2616 VREAVVLALDTP-SGKQLAGYLvsaVAGQDDEAQAALREALKAHLKQQL-----PDYMVPAhlillDSLPLTANGKLDRR 2689
|
..
gi 625195332 666 VL 667
Cdd:PRK05691 2690 AL 2691
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
133-667 |
6.51e-13 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 71.58 E-value: 6.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 133 TTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESL---CErILDSSCS 209
Cdd:PRK05857 39 TSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIerfCQ-ITDPAAA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 210 LLIttdafyRGEKLvnlkelADESLEKCREKGFPVRCCIVVKHVGRAELGMNDSPSQSPpvkrqcpdvqiswNEGVDlww 289
Cdd:PRK05857 118 LVA------PGSKM------ASSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAGNA-------------DQGSE--- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 290 helmqeagdefepewcdaeDPLFILYTSGSTGKPKGVvhtiggymLYVATTFKYVFD-FHPEDVFWctadIGWITGHSyv 368
Cdd:PRK05857 170 -------------------DPLAMIFTSGTTGEPKAV--------LLANRTFFAVPDiLQKEGLNW----VTWVVGET-- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 369 TYGPLAngATSV---------LFEG---IPTYPDESRLWSIVDKYKVTKFYTAPTAIRML---MKFGDEPVtkhsrASLQ 433
Cdd:PRK05857 217 TYSPLP--ATHIgglwwiltcLMHGglcVTGGENTTSLLEILTTNAVATTCLVPTLLSKLvseLKSANATV-----PSLR 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 434 VLGTVG-EPINPEAwlwyhRVVGSQHCPIVDTFWQTETGGHMLTpLP----GATPMKPGSASFPFFGV----APAILNES 504
Cdd:PRK05857 290 LVGYGGsRAIAADV-----RFIEATGVRTAQVYGLSETGCTALC-LPtddgSIVKIEAGAVGRPYPGVdvylAATDGIGP 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 505 GEELEGEAEGYLVFKQPWPGIMRTIYGNHTRFETTYFKkfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEV 584
Cdd:PRK05857 364 TAPGAGPSASFGTLWIKSPANMLGYWNNPERTAEVLID---GWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEV 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 585 ESALVEHEAVAEAAVVGHPHPVKGECLYCFV---TLCDGHTfsstlTEELKKQI----REKIGPIATPDYIQNAPGLPKT 657
Cdd:PRK05857 441 DRIAEGVSGVREAACYEIPDEEFGALVGLAVvasAELDESA-----ARALKHTIaarfRRESEPMARPSTIVIVTDIPRT 515
|
570
....*....|
gi 625195332 658 RSGKIMRRVL 667
Cdd:PRK05857 516 QSGKVMRASL 525
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
131-374 |
1.22e-12 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 71.30 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 131 GETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSL 210
Cdd:PLN02387 102 GEYEWITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTT 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 211 LITtdafyrGEKlvNLKELAD--ESLEkcrekgfpvrcciVVKHVgraeLGMNDSPSQSPPVKRQCPDVQISWNEGVDlw 288
Cdd:PLN02387 182 VIC------DSK--QLKKLIDisSQLE-------------TVKRV----IYMDDEGVDSDSSLSGSSNWTVSSFSEVE-- 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 289 whELMQEAgdEFEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYVFDFHPEDVfwctadigwitghsYV 368
Cdd:PLN02387 235 --KLGKEN--PVDPDLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVPKLGKNDV--------------YL 296
|
....*.
gi 625195332 369 TYGPLA 374
Cdd:PLN02387 297 AYLPLA 302
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
132-382 |
1.26e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 71.16 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 132 ETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLL 211
Cdd:PTZ00216 118 ETRYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAI 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 212 ITTdafyrGEKLVNLkeladesLEKCREKGFPvRCCIVvkHVGraelgmndspSQSPPVKRQCPDVqISWNEGVDLWWHE 291
Cdd:PTZ00216 198 VCN-----GKNVPNL-------LRLMKSGGMP-NTTII--YLD----------SLPASVDTEGCRL-VAWTDVVAKGHSA 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 292 LMQEAGDEfePEWCDAEdpLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYVFDF--HPEDvfwctadigwitGHSYVT 369
Cdd:PTZ00216 252 GSHHPLNI--PENNDDL--ALIMYTSGTTGDPKGVMHTHGSLTAGILALEDRLNDLigPPEE------------DETYCS 315
|
250
....*....|....*..
gi 625195332 370 YGPLAN----GATSVLF 382
Cdd:PTZ00216 316 YLPLAHimefGVTNIFL 332
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
306-673 |
1.35e-12 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 70.65 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 306 DAEDPLFILYTSGSTGKPKGVV--HtigGYMLYVATTFKYVFDFHPED-VFW--------CTADIgwitghsyvtYGPLA 374
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVVieH---RALSTSALAHGRALGLTSESrVLQfasytfdvSILEI----------FTTLA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 375 NGATSVlfegIPtyPDESRLWSIVD---KYKVTkfyTA---PTAIRMLmkfGDEPVTkhsraSLQVLGTVGEPINPEAW- 447
Cdd:cd05918 171 AGGCLC----IP--SEEDRLNDLAGfinRLRVT---WAfltPSVARLL---DPEDVP-----SLRTLVLGGEALTQSDVd 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 448 LWYHRV------------VGSQHCPIVD-------------TFWQTETGGH-MLTPLpGAT-------PMkpgsasfpff 494
Cdd:cd05918 234 TWADRVrlinaygpaectIAATVSPVVPstdprnigrplgaTCWVVDPDNHdRLVPI-GAVgelliegPI---------- 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 495 gVAPAILNESGEELEgeaegylVFKQPWPGIMRTIYGNHTRFettyfkkfpgyYVTGDGCRRDQDG--YYwiTGRIDDML 572
Cdd:cd05918 303 -LARGYLNDPEKTAA-------AFIEDPAWLKQEGSGRGRRL-----------YRTGDLVRYNPDGslEY--VGRKDTQV 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 573 NVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGEC---LYCFVTLcDGHTFSSTLTEELKKQIREKIGPIAT----- 644
Cdd:cd05918 362 KIRGQRVELGEIEHHLRQSLPGAKEVVVEVVKPKDGSSspqLVAFVVL-DGSSSGSGDGDSLFLEPSDEFRALVAelrsk 440
|
410 420 430
....*....|....*....|....*....|....*....
gi 625195332 645 -----PDY-IQNA----PGLPKTRSGKIMRRVLRKIAQN 673
Cdd:cd05918 441 lrqrlPSYmVPSVflplSHLPLTASGKIDRRALRELAES 479
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
137-671 |
2.14e-12 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 70.22 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 137 TYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGA-LHSIVFAGFSAEslCERILDSS-CSLLITT 214
Cdd:PRK08315 45 TYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAiLVTINPAYRLSE--LEYALNQSgCKALIAA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 215 DAF----YRG--EKLVnlKELADESLEKCREKGFPVrccivVKHVGRaeLGMNDSPSQSPpvkrqcpdvqiswnegvdlw 288
Cdd:PRK08315 123 DGFkdsdYVAmlYELA--PELATCEPGQLQSARLPE-----LRRVIF--LGDEKHPGMLN-------------------- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 289 WHELMqEAGDEFEPEWCDA-------EDPLFILYTSGSTGKPKGVV---HTIG--GYmlYVATTFKYVfdfhPED----- 351
Cdd:PRK08315 174 FDELL-ALGRAVDDAELAArqatldpDDPINIQYTSGTTGFPKGATlthRNILnnGY--FIGEAMKLT----EEDrlcip 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 352 --VFWCtadIGWITGhsyvTYGPLANGATSVlfegiptYPDES----RLWSIVDKYKVTKFYTAPTA-IRMLmkfgDEPv 424
Cdd:PRK08315 247 vpLYHC---FGMVLG----NLACVTHGATMV-------YPGEGfdplATLAAVEEERCTALYGVPTMfIAEL----DHP- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 425 tKHSRASLQVLGT---VGEPINPEAwlwYHRVVGSQHCP-IVDTFWQTETGghmltplPGATPMKP-----------GSA 489
Cdd:PRK08315 308 -DFARFDLSSLRTgimAGSPCPIEV---MKRVIDKMHMSeVTIAYGMTETS-------PVSTQTRTddplekrvttvGRA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 490 sFPFFGVApaILNESGEELEGEAEG-------YLVFKqpwpgimrtiygnhtrfettyfkkfpGYYV------------- 549
Cdd:PRK08315 377 -LPHLEVK--IVDPETGETVPRGEQgelctrgYSVMK--------------------------GYWNdpektaeaidadg 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 550 ---TGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSSt 626
Cdd:PRK08315 428 wmhTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTE- 506
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 625195332 627 ltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 671
Cdd:PRK08315 507 --EDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREMM 549
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
546-668 |
2.47e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 69.63 E-value: 2.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 546 GYYVTGDGCRRDQDGYYWITGRID-DMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTfs 624
Cdd:PRK07787 350 GWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVA-- 427
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 625195332 625 stlTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:PRK07787 428 ---ADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
132-667 |
2.53e-12 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 69.81 E-value: 2.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 132 ETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLL 211
Cdd:cd17656 10 ENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 212 ITtdafyrgeklvnlkeladeslekCREkgfpvrccivvkhvgraelgMNDSPSQSPPVkrqcpdVQISWnegvDLWWHE 291
Cdd:cd17656 90 LT-----------------------QRH--------------------LKSKLSFNKST------ILLED----PSISQE 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 292 LMQEAGDEFEpewcdAEDPLFILYTSGSTGKPKGVV--HTiggymlYVATTFKYVFDFHPEDVFwctADIGWITGHSY-V 368
Cdd:cd17656 117 DTSNIDYINN-----SDDLLYIIYTSGTTGKPKGVQleHK------NMVNLLHFEREKTNINFS---DKVLQFATCSFdV 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 369 TYGPLAngaTSVLFEG----IP--TYPDESRLWSIVDKYKVTKFYTAPTAIRMLmkFGDEPVTKHSRASLQVLGTVGEPI 442
Cdd:cd17656 183 CYQEIF---STLLSGGtlyiIReeTKRDVEQLFDLVKRHNIEVVFLPVAFLKFI--FSEREFINRFPTCVKHIITAGEQL 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 443 ---NPeawlwYHRVVGSQHCPIVDTFWQTETggHMLT--------PLPGATPM-KPGSASFPFfgvapaILNESgeeleg 510
Cdd:cd17656 258 vitNE-----FKEMLHEHNVHLHNHYGPSET--HVVTtytinpeaEIPELPPIgKPISNTWIY------ILDQE------ 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 511 eaegylvfKQPWP-GIMRTIY--------GNHTRFETTYFKKFPG-------YYVTGDGCRRDQDGYYWITGRIDDMLNV 574
Cdd:cd17656 319 --------QQLQPqGIVGELYisgasvarGYLNRQELTAEKFFPDpfdpnerMYRTGDLARYLPDGNIEFLGRADHQVKI 390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 575 SGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVtlCDGHTFSstlTEELKKQIREKIGPIATPDYIQNAPGL 654
Cdd:cd17656 391 RGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYF--VMEQELN---ISQLREYLAKQLPEYMIPSFFVPLDQL 465
|
570
....*....|...
gi 625195332 655 PKTRSGKIMRRVL 667
Cdd:cd17656 466 PLTPNGKVDRKAL 478
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
308-661 |
2.62e-12 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 68.95 E-value: 2.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 308 EDPLFILYTSGSTGKPKGVV---HTIGGYMLYVATTFKYVF----DFHPEDVfwCTADIGW------ITGHSYVTYGPLA 374
Cdd:cd05924 3 ADDLYILYTGGTTGMPKGVMwrqEDIFRMLMGGADFGTGEFtpseDAHKAAA--AAAGTVMfpapplMHGTGSWTAFGGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 375 NGATSVLFEGIPTYPDEsrLWSIVDKYKVTKF------YTAPTaIRMLMKFGDEPVTkhsraSLQVLGTVGEPINPEawl 448
Cdd:cd05924 81 LGGQTVVLPDDRFDPEE--VWRTIEKHKVTSMtivgdaMARPL-IDALRDAGPYDLS-----SLFAISSGGALLSPE--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 449 wyHRVVGSQHCP---IVDTFWQTETGGHMLTPlpgATPMKPGSASFPFFGVAPAILNESgeelegeaegyLVFKQPWPGI 525
Cdd:cd05924 150 --VKQGLLELVPnitLVDAFGSSETGFTGSGH---SAGSGPETGPFTRANPDTVVLDDD-----------GRVVPPGSGG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 526 MRTI----------YGNHTRFETTyFKKFPG--YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEA 593
Cdd:cd05924 214 VGWIarrghiplgyYGDEAKTAET-FPEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPA 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 625195332 594 VAEAAVVGHPHPVKGECLYCFVTLCDGHTFSStltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGK 661
Cdd:cd05924 293 VYDVLVVGRPDERWGQEVVAVVQLREGAGVDL---EELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
133-669 |
4.00e-12 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 68.99 E-value: 4.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 133 TTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLI 212
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 213 TtdafyrgeklvNLKELADESLEKcrekgfpvrccivvkhvgraelgmndspsqSPPVkrqCPDVqiswnegvdlwwhel 292
Cdd:cd05939 81 F-----------NLLDPLLTQSST------------------------------EPPS---QDDV--------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 293 mqeagdefepewcDAEDPLFILYTSGSTGKPKGVVHTIGGYmLYVATTFKYVFDFHPEDVFWCTADIgWITGHSYVTYGP 372
Cdd:cd05939 102 -------------NFRDKLFYIYTSGTTGLPKAAVIVHSRY-YRIAAGAYYAFGMRPEDVVYDCLPL-YHSAGGIMGVGQ 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 373 -LANGATSVLFEGIPTypdeSRLWSIVDKYKVTKF-YTAPTAIRMLMKFGDEPVTKHsraslQVLGTVGEPINPEAWlwy 450
Cdd:cd05939 167 aLLHGSTVVIRKKFSA----SNFWDDCVKYNCTIVqYIGEICRYLLAQPPSEEEQKH-----NVRLAVGNGLRPQIW--- 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 451 HRVVGSQHCPIVDTFWQTETGGHMLTPLPGatpmKPGSASF-PFFG--VAPAIL---NESGEELEGEAEGYLVFKQPW-P 523
Cdd:cd05939 235 EQFVRRFGIPQIGEFYGATEGNSSLVNIDN----HVGACGFnSRILpsVYPIRLikvDEDTGELIRDSDGLCIPCQPGeP 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 524 GIM--RTIYGNHTRFETTY--------------FKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESA 587
Cdd:cd05939 311 GLLvgKIIQNDPLRRFDGYvnegatnkkiardvFKKGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGI 390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 588 LVEHEAVAEAAVVGHPHP-VKGEC----LYCFVTLCDGHTFSSTLTEELKkqirekigPIATPDYIQNAPGLPKTRSGKI 662
Cdd:cd05939 391 LSNVLGLEDVVVYGVEVPgVEGRAgmaaIVDPERKVDLDRFSAVLAKSLP--------PYARPQFIRLLPEVDKTGTFKL 462
|
....*..
gi 625195332 663 MRRVLRK 669
Cdd:cd05939 463 QKTDLQK 469
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
291-669 |
6.22e-12 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 68.67 E-value: 6.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 291 ELMQEAGDEFEPEWCDA-EDPLFILYTSGSTGKPKGVvhTIGGYMLYVATTFKYVF-DFHPEDVFWCTADIGWITGHSYV 368
Cdd:PLN02860 154 MLKQRALGTTELDYAWApDDAVLICFTSGTTGRPKGV--TISHSALIVQSLAKIAIvGYGEDDVYLHTAPLCHIGGLSSA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 369 tygpLAN---GATSVLfegIPTYpDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVTKHSRASLQVL----GTVGEP 441
Cdd:PLN02860 232 ----LAMlmvGACHVL---LPKF-DAKAALQAIKQHNVTSMITVPAMMADLISLTRKSMTWKVFPSVRKIlnggGSLSSR 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 442 INPEAWLWYHRVvgsqhcPIVDTFWQTETGGHM-LTPLPGATPMKPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQ 520
Cdd:PLN02860 304 LLPDAKKLFPNA------KLFSAYGMTEACSSLtFMTLHDPTLESPKQTLQTVNQTKSSSVHQPQGVCVGKPAPHVELKI 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 521 PWPGIMRT----IYGNHT--RF-----ETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALV 589
Cdd:PLN02860 378 GLDESSRVgrilTRGPHVmlGYwgqnsETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLS 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 590 EHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSSTLT-----------EELKKQIREK-IGPIATPD-YIQNAPGLPK 656
Cdd:PLN02860 458 QHPGVASVVVVGVPDSRLTEMVVACVRLRDGWIWSDNEKenakknltlssETLRHHCREKnLSRFKIPKlFVQWRKPFPL 537
|
410
....*....|...
gi 625195332 657 TRSGKIMRRVLRK 669
Cdd:PLN02860 538 TTTGKIRRDEVRR 550
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
520-675 |
3.31e-11 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 66.17 E-value: 3.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 520 QPWPGIMRTIYGNHTRFETT--------YFKKF---PGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESAL 588
Cdd:PRK07445 287 QVLPHAQITIPANQTGNITIqaqslalgYYPQIldsQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAI 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 589 VEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfsSTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 668
Cdd:PRK07445 367 LATGLVQDVCVLGLPDPHWGEVVTAIYVPKDP----SISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQ 442
|
....*..
gi 625195332 669 KIAQNDH 675
Cdd:PRK07445 443 QIAVQRL 449
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
137-669 |
1.68e-10 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 63.99 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 137 TYRELLVQVCQFSNVLRKQ-GIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESL--CERIldSSCSLLIT 213
Cdd:cd05937 7 TYSETYDLVLRYAHWLHDDlGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLihCLKL--SGSRFVIV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 214 TDafyrgeklvnlkeladeslekcrekgfpvrccivvkhvgraelgmndspsqsppvkrqcpdvqiswnegvdlwwhelm 293
Cdd:cd05937 85 DP------------------------------------------------------------------------------ 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 294 qeagdefepewcdaEDPLFILYTSGSTGKPKGVVHTIGgyMLYV-ATTFKYVFDFHPEDVFWCTADIGWITGHSYVTYGP 372
Cdd:cd05937 87 --------------DDPAILIYTSGTTGLPKAAAISWR--RTLVtSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNC 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 373 LANGATSVL---FEGiptypdeSRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVTKHSRaslqVLGTVGEPINPEAWLW 449
Cdd:cd05937 151 LMSGGTLALsrkFSA-------SQFWKDVRDSGATIIQYVGELCRYLLSTPPSPYDRDHK----VRVAWGNGLRPDIWER 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 450 YHRVVGsqhCPIVDTFWQ-TETGGHMLTPLPGAtpmkpgsasfpfFGvAPAILNESGEELEGEAEGYLVFK------QPW 522
Cdd:cd05937 220 FRERFN---VPEIGEFYAaTEGVFALTNHNVGD------------FG-AGAIGHHGLIRRWKFENQVVLVKmdpetdDPI 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 523 ---------------PG--IMRTIYGNHTRFETTY--------------FKKFPGYYVTGDGCRRDQDGYYWITGRIDDM 571
Cdd:cd05937 284 rdpktgfcvrapvgePGemLGRVPFKNREAFQGYLhnedatesklvrdvFRKGDIYFRTGDLLRQDADGRWYFLDRLGDT 363
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 572 LNVSGHLLSTAEVESALVEHEAVAEAAVVG---HPHPVKGECLYCfvTLCDGHTFSSTLT-EELKKQIREKIGPIATPDY 647
Cdd:cd05937 364 FRWKSENVSTTEVADVLGAHPDIAEANVYGvkvPGHDGRAGCAAI--TLEESSAVPTEFTkSLLASLARKNLPSYAVPLF 441
|
570 580
....*....|....*....|..
gi 625195332 648 IQNAPGLPKTRSGKIMRRVLRK 669
Cdd:cd05937 442 LRLTEEVATTDNHKQQKGVLRD 463
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
520-677 |
3.72e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 62.80 E-value: 3.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 520 QPWPGIMrtiYGN-HTR---FETTYFKK-----FPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVE 590
Cdd:PRK07008 377 LPWDGKA---FGDlQVRgpwVIDRYFRGdasplVDGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVA 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 591 HEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSStltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKI 670
Cdd:PRK07008 454 HPAVAEAACIACAHPKWDERPLLVVVKRPGAEVTR---EELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQ 530
|
....*..
gi 625195332 671 AQnDHDL 677
Cdd:PRK07008 531 FR-DYVL 536
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
546-667 |
4.84e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 62.71 E-value: 4.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 546 GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLcdgHTFSS 625
Cdd:PRK13383 396 GMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVL---HPGSG 472
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 625195332 626 TLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 667
Cdd:PRK13383 473 VDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
131-664 |
6.50e-10 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 62.07 E-value: 6.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 131 GETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSL 210
Cdd:cd05914 3 YGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 211 LITTdafyrgeklvnlkeladeslekcrekgfpvrccivvkhvgraelgmndspsqsppvkrqcpdvqiswnegvdlwwh 290
Cdd:cd05914 83 IFVS---------------------------------------------------------------------------- 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 291 elmqeagdefepewcDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYVFdFHPEDVFWCTADIGWITGHSYVTY 370
Cdd:cd05914 87 ---------------DEDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVL-LGKGDKILSILPLHHIYPLTFTLL 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 371 GPLANGATSVLFEGIPTYPDE-------------SRLWSIVDKYKVTKFYTAPTAI---RMLMKFGDEPVTKHSRASLQ- 433
Cdd:cd05914 151 LPLLNGAHVVFLDKIPSAKIIalafaqvtptlgvPVPLVIEKIFKMDIIPKLTLKKfkfKLAKKINNRKIRKLAFKKVHe 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 434 ---------VLGtvGEPINPEAwLWYHRVVGsqhCPIVDTFWQTETGghmltPLPGATP---MKPGSASFPFFGVAPAIL 501
Cdd:cd05914 231 afggnikefVIG--GAKINPDV-EEFLRTIG---FPYTIGYGMTETA-----PIISYSPpnrIRLGSAGKVIDGVEVRID 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 502 NESGEELEGEaegyLVFKQpwPGIMRTIYGNHtrfETTYFKKFP-GYYVTGDGCRRDQDGYYWITGRIDDM-LNVSGHLL 579
Cdd:cd05914 300 SPDPATGEGE----IIVRG--PNVMKGYYKNP---EATAEAFDKdGWFHTGDLGKIDAEGYLYIRGRKKEMiVLSSGKNI 370
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 580 STAEVESALVEHEAVAEAAVV---------GHPHP----VKGECLycfVTLCDghtfssTLTEELKKQIREKigpiaTPD 646
Cdd:cd05914 371 YPEEIEAKINNMPFVLESLVVvqekklvalAYIDPdfldVKALKQ---RNIID------AIKWEVRDKVNQK-----VPN 436
|
570 580
....*....|....*....|....*
gi 625195332 647 Y-------IQNAPgLPKTRSGKIMR 664
Cdd:cd05914 437 YkkiskvkIVKEE-FEKTPKGKIKR 460
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
550-667 |
7.85e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 61.59 E-value: 7.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 550 TGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGE--CLycfvTLCDGHTFSstl 627
Cdd:PRK08308 295 TKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGErvKA----KVISHEEID--- 367
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 625195332 628 TEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 667
Cdd:PRK08308 368 PVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
306-667 |
8.26e-10 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 61.65 E-value: 8.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 306 DAEDPLFILYTSGSTGKPKGVVHTIGGYM--------LY---------VATTFKYVFDFHPEDVFwctadIGWITGHSYV 368
Cdd:cd17648 92 NSTDLAYAIYTSGTTGKPKGVLVEHGSVVnlrtslseRYfgrdngdeaVLFFSNYVFDFFVEQMT-----LALLNGQKLV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 369 TYGPlangatSVLFegiptypDESRLWSIVDKYKVTKFYTAPTAIRMLmKFGdepvtkhSRASLQVLGTVGEPINPEAwl 448
Cdd:cd17648 167 VPPD------EMRF-------DPDRFYAYINREKVTYLSGTPSVLQQY-DLA-------RLPHLKRVDAAGEEFTAPV-- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 449 wYHRVVGSQHCPIVDTFWQTETGGHML-TPLPGATPmKPGSASFPFFGVAPAILNESGeelegeaegylvfkQPWP-GIM 526
Cdd:cd17648 224 -FEKLRSRFAGLIINAYGPTETTVTNHkRFFPGDQR-FDKSLGRPVRNTKCYVLNDAM--------------KRVPvGAV 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 527 RTIY--------GNHTRFETTYFK---------------KFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAE 583
Cdd:cd17648 288 GELYlggdgvarGYLNRPELTAERflpnpfqteqerargRNARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 584 VESALVEHEAVAEAAVVGHPHPVKGEC-----LYCFVTLCDGHtfsstLTE-ELKKQIREKIGPIATPDYIQNAPGLPKT 657
Cdd:cd17648 368 VEAALASYPGVRECAVVAKEDASQAQSriqkyLVGYYLPEPGH-----VPEsDLLSFLRAKLPRYMVPARLVRLEGIPVT 442
|
410
....*....|
gi 625195332 658 RSGKIMRRVL 667
Cdd:cd17648 443 INGKLDVRAL 452
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
545-669 |
1.16e-09 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 60.83 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 545 PGYYVTGDGCRRDqDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLycfVTLCDGHTFS 624
Cdd:PRK07824 233 PGWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRV---VAAVVGDGGP 308
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 625195332 625 STLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:PRK07824 309 APTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVR 353
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
546-669 |
1.54e-09 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 60.95 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 546 GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSS 625
Cdd:PRK05620 430 GWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTR 509
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 625195332 626 TLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 669
Cdd:PRK05620 510 ETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQ 553
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
118-329 |
1.76e-09 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 60.93 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 118 GDKVAFYWEGNEP------GETT--------KITYRELLVQVCQFSNVLR-KQGIQKGDRVAIYMPMILELVVAMLACAR 182
Cdd:cd17632 36 ADRPALGQRATELvtdpatGRTTlrllprfeTITYAELWERVGAVAAAHDpEQPVRPGDFVAVLGFTSPDYATVDLALTR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 183 LGALHSIVFAGFSAESLCErILDSSCSLLITTDAfyrgeklvnlkELADESLEKCREKGFPVRcciVVKHVGRAELGMND 262
Cdd:cd17632 116 LGAVSVPLQAGASAAQLAP-ILAETEPRLLAVSA-----------EHLDLAVEAVLEGGTPPR---LVVFDHRPEVDAHR 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 625195332 263 SPSQSppVKRQCPDVQISWNEGVDLWWHELMQEAGDEFEPEwcDAEDPL-FILYTSGSTGKPKGVVHT 329
Cdd:cd17632 181 AALES--ARERLAAVGIPVTTLTLIAVRGRDLPPAPLFRPE--PDDDPLaLLIYTSGSTGTPKGAMYT 244
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
119-667 |
1.91e-09 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 61.34 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 119 DKVAFYWEGNEpgettkITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAES 198
Cdd:PRK05691 1146 ERIALVWDGGS------LDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAER 1219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 199 LCERILDSSCSLLITTDAFyrgekLVNLKELADeslekcrekgfpvrccivVKHVGRAELGMNDSPSQSPpvkrqcpdvq 278
Cdd:PRK05691 1220 LAYMLADSGVELLLTQSHL-----LERLPQAEG------------------VSAIALDSLHLDSWPSQAP---------- 1266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 279 iswneGVDLWWHELMqeagdefepewcdaedplFILYTSGSTGKPKGVVHT---IGGYMLYVATTfkYVFDfhPEDVFWC 355
Cdd:PRK05691 1267 -----GLHLHGDNLA------------------YVIYTSGSTGQPKGVGNThaaLAERLQWMQAT--YALD--DSDVLMQ 1319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 356 TADIGWITGhSYVTYGPLANGATSVLfEGIPTYPDESRLWSIVDKYKVTKFYTAPTairMLMKFGDEPVTKHSRaSLQVL 435
Cdd:PRK05691 1320 KAPISFDVS-VWECFWPLITGCRLVL-AGPGEHRDPQRIAELVQQYGVTTLHFVPP---LLQLFIDEPLAAACT-SLRRL 1393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 436 GTVGEPINPE---------AWLWYHRVVGSQHCPIVDTFWQTETGGHMLTPLpgatpmkpgsaSFPFFGVAPAILNESGE 506
Cdd:PRK05691 1394 FSGGEALPAElrnrvlqrlPQVQLHNRYGPTETAINVTHWQCQAEDGERSPI-----------GRPLGNVLCRVLDAELN 1462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 507 ELEGEAEGYLVFKQPwpGIMRTIYG----NHTRFETTYFKKfPG--YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLS 580
Cdd:PRK05691 1463 LLPPGVAGELCIGGA--GLARGYLGrpalTAERFVPDPLGE-DGarLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVE 1539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 581 TAEVESALVEHEAVAEAAVVGHpHPVKGECLYCFVTLCDGHtfsSTLTEELKKQIREKIgpiatPDYIQNA-----PGLP 655
Cdd:PRK05691 1540 PEEIQARLLAQPGVAQAAVLVR-EGAAGAQLVGYYTGEAGQ---EAEAERLKAALAAEL-----PEYMVPAqlirlDQMP 1610
|
570
....*....|..
gi 625195332 656 KTRSGKIMRRVL 667
Cdd:PRK05691 1611 LGPSGKLDRRAL 1622
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
548-667 |
3.44e-09 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 60.57 E-value: 3.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 548 YVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAvVGHPHPVKGECLYCFVTLCDGHTFSSTL 627
Cdd:PRK05691 4104 YRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAA-VAVQEGVNGKHLVGYLVPHQTVLAQGAL 4182
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 625195332 628 TEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 667
Cdd:PRK05691 4183 LERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
135-669 |
1.09e-08 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 58.13 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 135 KITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSivfagfsaeslcerildsscslLITT 214
Cdd:cd05940 3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAA----------------------LINY 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 215 DAfyRGEKLVNLKELADeslekcrekgfpVRCCIVvkhvgraelgmndspsqsppvkrqcpdvqiswnegvdlwwhelmq 294
Cdd:cd05940 61 NL--RGESLAHCLNVSS------------AKHLVV--------------------------------------------- 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 295 eagdefepewcdaeDPLFILYTSGSTGKPKGVVHTIGGYmLYVATTFKYVFDFHPEDVFWCTADIGWITGHSYVTYGPLA 374
Cdd:cd05940 82 --------------DAALYIYTSGTTGLPKAAIISHRRA-WRGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLA 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 375 NGATSVLFEGIPTypdeSRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVTK-HsraslQVLGTVGEPINPEAWLWYHRV 453
Cdd:cd05940 147 SGATLVIRKKFSA----SNFWDDIRKYQATIFQYIGELCRYLLNQPPKPTERkH-----KVRMIFGNGLRPDIWEEFKER 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 454 VGsqhCPIVDTFWQTETGGHMLTPLPGatpmKPGSAsfpffGVAPAILnesgeeleGEAEGYLVFK------QPW----- 522
Cdd:cd05940 218 FG---VPRIAEFYAATEGNSGFINFFG----KPGAI-----GRNPSLL--------RKVAPLALVKydlesgEPIrdaeg 277
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 523 ---------PGIMRTIYGNHTRFE-------------TTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLS 580
Cdd:cd05940 278 rcikvprgePGLLISRINPLEPFDgytdpaatekkilRDVFKKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVS 357
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 581 TAEVESALVEHEAVAEAAVVGHPHP-VKGECLYCFVTLCDGHTFSstlTEELKKQIREKIGPIATPDYIQNAPGLPKTRS 659
Cdd:cd05940 358 TTEVAAVLGAFPGVEEANVYGVQVPgTDGRAGMAAIVLQPNEEFD---LSALAAHLEKNLPGYARPLFLRLQPEMEITGT 434
|
570
....*....|
gi 625195332 660 GKIMRRVLRK 669
Cdd:cd05940 435 FKQQKVDLRN 444
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
296-447 |
1.75e-08 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 57.60 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 296 AGDEFEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGgymLYVA--TTFKYVFDFHPEDVFWCTADIgwitghsYVTYGPl 373
Cdd:PRK09274 162 AAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHG---MFEAqiEALREDYGIEPGEIDLPTFPL-------FALFGP- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 374 ANGATSVLFEGIPTYP---DESRLWSIVDKYKVTKFYTAPTAIrmlmkfgdEPVTKHSRASLQVLGTV------GEPINP 444
Cdd:PRK09274 231 ALGMTSVIPDMDPTRPatvDPAKLFAAIERYGVTNLFGSPALL--------ERLGRYGEANGIKLPSLrrvisaGAPVPI 302
|
...
gi 625195332 445 EAW 447
Cdd:PRK09274 303 AVI 305
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
306-672 |
2.26e-08 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 57.63 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 306 DAEDPLFILYTSGSTGKPKGVV---HTIGGYMLYVATtfkyVFDFHPEDVfwctadigwITG-----HSY----VTYGPL 373
Cdd:PRK08633 780 KPDDTATIIFSSGSEGEPKGVMlshHNILSNIEQISD----VFNLRNDDV---------ILSslpffHSFgltvTLWLPL 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 374 ANGATSVlFEGIPTypDESRLWSIVDKYKVTKFYTAPTAIRMLMKfgDEPVTKHSRASLQVLGTVGEPINPEawlwyhrv 453
Cdd:PRK08633 847 LEGIKVV-YHPDPT--DALGIAKLVAKHRATILLGTPTFLRLYLR--NKKLHPLMFASLRLVVAGAEKLKPE-------- 913
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 454 VGSQ-----HCPIVDTFWQTETgghmlTP-----LPGA--------TPMKPGSASFPFFGVAPAILNESGeelegeaegY 515
Cdd:PRK08633 914 VADAfeekfGIRILEGYGATET-----SPvasvnLPDVlaadfkrqTGSKEGSVGMPLPGVAVRIVDPET---------F 979
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 516 LVFKQPWPG--------IMRTIYGNHTRF-ETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVES 586
Cdd:PRK08633 980 EELPPGEDGliliggpqVMKGYLGDPEKTaEVIKDIDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEE 1059
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 587 ALveHEAVAEA----AVVGHPHPVKGECLycfVTLcdgHTFSSTLTEELKKQIRE-KIGPIATPDYIQNAPGLPKTRSGK 661
Cdd:PRK08633 1060 EL--AKALGGEevvfAVTAVPDEKKGEKL---VVL---HTCGAEDVEELKRAIKEsGLPNLWKPSRYFKVEALPLLGSGK 1131
|
410
....*....|.
gi 625195332 662 IMRRVLRKIAQ 672
Cdd:PRK08633 1132 LDLKGLKELAL 1142
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
307-632 |
1.29e-07 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 54.77 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 307 AEDPLFILYTSGSTGKPKGVVHTIGGYMLYVAtTFKYVFDFHPEDVFWCTADIgwitghsYVTYGPlANGATSVLFEGIP 386
Cdd:cd05910 84 ADEPAAILFTSGSTGTPKGVVYRHGTFAAQID-ALRQLYGIRPGEVDLATFPL-------FALFGP-ALGLTSVIPDMDP 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 387 TYP---DESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEpvTKHSRASLQVLGTVGEPINPEAWLWYHRVVgSQHCPIVD 463
Cdd:cd05910 155 TRParaDPQKLVGAIRQYGVSIVFGSPALLERVARYCAQ--HGITLPSLRRVLSAGAPVPIALAARLRKML-SDEAEILT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 464 TFWQTET------GGHMLTPLPGATPMKPGSA--SFPFFGVAPAILNESGEELEGEAEGYLVfkQPW---------PGIM 526
Cdd:cd05910 232 PYGATEAlpvssiGSRELLATTTAATSGGAGTcvGRPIPGVRVRIIEIDDEPIAEWDDTLEL--PRGeigeitvtgPTVT 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 527 RTIYgnhTRFETTYFKKFPG-----YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVG 601
Cdd:cd05910 310 PTYV---NRPVATALAKIDDnsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVG 386
|
330 340 350
....*....|....*....|....*....|.
gi 625195332 602 HPHPVKGECLYCFVTLCDGHTFSSTLTEELK 632
Cdd:cd05910 387 VGKPGCQLPVLCVEPLPGTITPRARLEQELR 417
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
108-326 |
1.87e-07 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 54.36 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 108 LDRNVHEkkLGDKVAFYW---EGNEPGETTKITYRELLVQVCQFSNVLrKQGIQKGDRVAIYMPMILELVVAMLACARLG 184
Cdd:PRK12476 40 IERNIAN--VGDTVAYRYldhSHSAAGCAVELTWTQLGVRLRAVGARL-QQVAGPGDRVAILAPQGIDYVAGFFAAIKAG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 185 ALHSIVFA----GfSAESLCERILDSSCSLLITTDAfyrgeklvnlkelADESLEKCREKgfpvrccivVKHVGRAELGM 260
Cdd:PRK12476 117 TIAVPLFApelpG-HAERLDTALRDAEPTVVLTTTA-------------AAEAVEGFLRN---------LPRLRRPRVIA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 625195332 261 NDspsqsppvkrQCPDvqiswnegvdlwwhelmqEAGDEFEPEWCDAEDPLFILYTSGSTGKPKGV 326
Cdd:PRK12476 174 ID----------AIPD------------------SAGESFVPVELDTDDVSHLQYTSGSTRPPVGV 211
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
546-660 |
2.60e-07 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 53.07 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 546 GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSS 625
Cdd:cd17636 217 GWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTE 296
|
90 100 110
....*....|....*....|....*....|....*
gi 625195332 626 tltEELKKQIREKIGPIATPDYIQNAPGLPKTRSG 660
Cdd:cd17636 297 ---AELIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
115-667 |
3.52e-07 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 53.33 E-value: 3.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 115 KKLGDKVAFYWEGNepgettKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGF 194
Cdd:cd17645 9 ERTPDHVAVVDRGQ------SLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 195 SAESLCERILDSSCSLLITtdafyrgeklvnlkeladeslekcrekgfpvrccivvkhvgraelgmndspsqsppvkrqc 274
Cdd:cd17645 83 PGERIAYMLADSSAKILLT------------------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 275 pdvqiswnegvdlwwhelmqeagdefepewcDAEDPLFILYTSGSTGKPKGVV---HTIGGYMLYvattFKYVFDFHPED 351
Cdd:cd17645 102 -------------------------------NPDDLAYVIYTSGSTGLPKGVMiehHNLVNLCEW----HRPYFGVTPAD 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 352 VFWCTADIGWiTGHSYVTYGPLANGATsvlfegIPTYPDESRLwsivDKYKVTK-FYTAPTAIRMLMKFGDEPVTKHSRA 430
Cdd:cd17645 147 KSLVYASFSF-DASAWEIFPHLTAGAA------LHVVPSERRL----DLDALNDyFNQEGITISFLPTGAAEQFMQLDNQ 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 431 SLQVLGTVGEPINpeawlwyhrVVGSQHCPIVDTFWQTETgghmlTPLPGATPMKPGSASFPFfGVAPA-----ILNESG 505
Cdd:cd17645 216 SLRVLLTGGDKLK---------KIERKGYKLVNNYGPTEN-----TVVATSFEIDKPYANIPI-GKPIDntrvyILDEAL 280
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 506 EELEGEAEGYLVFKQPwpGIMRtiyGNHTRFETTYfKKF------PG--YYVTGDGCRRDQDGYYWITGRIDDMLNVSGH 577
Cdd:cd17645 281 QLQPIGVAGELCIAGE--GLAR---GYLNRPELTA-EKFivhpfvPGerMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGY 354
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 578 LLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTlcdghTFSSTLTEELKKQIREKIGPIATPDYIQNAPGLPKT 657
Cdd:cd17645 355 RIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVT-----APEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLT 429
|
570
....*....|
gi 625195332 658 RSGKIMRRVL 667
Cdd:cd17645 430 ANGKVDRKAL 439
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
131-673 |
5.64e-07 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 52.67 E-value: 5.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 131 GETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACarlgalhsiVFAGFSAeslcerildsscsL 210
Cdd:cd05906 35 GSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWAC---------VLAGFVP-------------A 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 211 LITTDAFYRG-----EKLVNLKELADEslekcrekgfPVrcCIVvkhvgraelgmndSPSQSPPVKRQcpdVQISWNEGV 285
Cdd:cd05906 93 PLTVPPTYDEpnarlRKLRHIWQLLGS----------PV--VLT-------------DAELVAEFAGL---ETLSGLPGI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 286 DLWWHELMQEAGDEfePEW--CDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKyVFDFHPEDVF--WCTADigW 361
Cdd:cd05906 145 RVLSIEELLDTAAD--HDLpqSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQ-HNGLTPQDVFlnWVPLD--H 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 362 ITGHSYVTYGPLANGATSVlfeGIPTyPD---ESRLW-SIVDKYKVTkfYT-APT-AIRMLMKFGDEPVTKH-SRASLQV 434
Cdd:cd05906 220 VGGLVELHLRAVYLGCQQV---HVPT-EEilaDPLRWlDLIDRYRVT--ITwAPNfAFALLNDLLEEIEDGTwDLSSLRY 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 435 LGTVGEPINP---EAWLWYHRVVGSQHCPIVDTFWQTETGGHMLTPLPGATPMKPGSASF-----PFFGVAPAILNESGE 506
Cdd:cd05906 294 LVNAGEAVVAktiRRLLRLLEPYGLPPDAIRPAFGMTETCSGVIYSRSFPTYDHSQALEFvslgrPIPGVSMRIVDDEGQ 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 507 ELEGEAEGYLVFKqpwpGIMRTI--YGNHTRFETTYFKKfpGYYVTGD-GCRRdqDGYYWITGRIDDMLNVSGHLLSTAE 583
Cdd:cd05906 374 LLPEGEVGRLQVR----GPVVTKgyYNNPEANAEAFTED--GWFRTGDlGFLD--NGNLTITGRTKDTIIVNGVNYYSHE 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 584 VESALVEHEAVAE--AAVVGHPHPVKGECLYC--FVTLCDGHTFSSTLTEELKKQIREKIGpiATPDYI----QNApgLP 655
Cdd:cd05906 446 IEAAVEEVPGVEPsfTAAFAVRDPGAETEELAifFVPEYDLQDALSETLRAIRSVVSREVG--VSPAYLiplpKEE--IP 521
|
570
....*....|....*...
gi 625195332 656 KTRSGKIMRRVLRKIAQN 673
Cdd:cd05906 522 KTSLGKIQRSKLKAAFEA 539
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
129-662 |
1.10e-06 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 51.70 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 129 EPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGAlhsiVFAGFSAESLCERILdssc 208
Cdd:cd17654 10 QTTSDTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGA----AYAPIDPASPEQRSL---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 209 SLLITTDAFYrgeKLVNlkeladeslekcrekgfpvrccivvKHVGRAelgmndsPSQSPPVKRqcpdvqiswnegvdlw 288
Cdd:cd17654 82 TVMKKCHVSY---LLQN-------------------------KELDNA-------PLSFTPEHR---------------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 289 wHELMQEAGdefepewCDAedplFILYTSGSTGKPKGV---VHTIGGYMLYvattFKYVFDFHPEDVFWCTadigwitgh 365
Cdd:cd17654 111 -HFNIRTDE-------CLA----YVIHTSGTTGTPKIVavpHKCILPNIQH----FRSLFNITSEDILFLT--------- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 366 SYVTYGP--------LANGATSVlfegipTYPDE-----SRLWSIVDK-YKVTKFYTAPTAIRMLMK--FGDEPVTKHSr 429
Cdd:cd17654 166 SPLTFDPsvveiflsLSSGATLL------IVPTSvkvlpSKLADILFKrHRITVLQATPTLFRRFGSqsIKSTVLSATS- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 430 aSLQVLGTVGE--PINPEAWLWYHRVVGSQHCPIVDTfwqTETGGHMLT--------PLPGATPMkpgsasfpffgVAPA 499
Cdd:cd17654 239 -SLRVLALGGEpfPSLVILSSWRGKGNRTRIFNIYGI---TEVSCWALAykvpeedsPVQLGSPL-----------LGTV 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 500 ILNESGEELEGEAEGYLvfkqpwPGIMRTIY--GNHTRFETTYfkkfpgyYVTGDGCRRdQDGYYWITGRIDDMLNVSGH 577
Cdd:cd17654 304 IEVRDQNGSEGTGQVFL------GGLNRVCIldDEVTVPKGTM-------RATGDFVTV-KDGELFFLGRKDSQIKRRGK 369
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 578 LLSTAEVESALVEHEAVAEAAVVGHphpvKGECLYCFVTlcdGHTFSSTLTEELKKQIREkigPIATPDYIQNAPGLPKT 657
Cdd:cd17654 370 RINLDLIQQVIESCLGVESCAVTLS----DQQRLIAFIV---GESSSSRIHKELQLTLLS---SHAIPDTFVQIDKLPLT 439
|
....*
gi 625195332 658 RSGKI 662
Cdd:cd17654 440 SHGKV 444
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
131-382 |
1.12e-06 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 51.83 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 131 GETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSL 210
Cdd:cd17639 1 GEYKYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 211 LITtdafyrgeklvnlkeladeslekcrekgfpvrccivvkhvgraelgmNDSPsqsppvkrqcpdvqiswnegvdlwwh 290
Cdd:cd17639 81 IFT-----------------------------------------------DGKP-------------------------- 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 291 elmqeagdefepewcdaEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYVFDF-HPEDVfwctadigwitghsYVT 369
Cdd:cd17639 88 -----------------DDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPELlGPDDR--------------YLA 136
|
250
....*....|....*..
gi 625195332 370 YGPLAN----GATSVLF 382
Cdd:cd17639 137 YLPLAHifelAAENVCL 153
|
|
| PRK09188 |
PRK09188 |
serine/threonine protein kinase; Provisional |
587-679 |
7.51e-06 |
|
serine/threonine protein kinase; Provisional
Pssm-ID: 236400 [Multi-domain] Cd Length: 365 Bit Score: 48.61 E-value: 7.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 587 ALVEHEAVAEAAVVGHPHPVKGECLYCFVtlcdgHTFSSTLTEELKKQIREKIGPIAtPDYIQNAPGLPKTRSGKIMRRV 666
Cdd:PRK09188 248 ALKSDPAVSDVAIALFSLPAKGVGLYAFV-----EAELPADEKSLRARLAGAKPPKP-PEHIQPVAALPRDADGTVRDDI 321
|
90
....*....|...
gi 625195332 667 LRKIAQNDHDLGD 679
Cdd:PRK09188 322 LRLIAMNQIDELD 334
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
545-673 |
1.11e-05 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 48.94 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 545 PGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTlcdghtfS 624
Cdd:PRK08043 590 RGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASKGEALVLFTT-------D 662
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 625195332 625 STLT-EELKKQIREKIGP-IATPDYIQNAPGLPKTRSGKIMRRVLRKIAQN 673
Cdd:PRK08043 663 SELTrEKLQQYAREHGVPeLAVPRDIRYLKQLPLLGSGKPDFVTLKSMVDE 713
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
136-648 |
1.66e-05 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 48.06 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 136 ITYRELLVQVCQFSNVLRKQ-GIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITT 214
Cdd:cd05938 6 YTYRDVDRRSNQAARALLAHaGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLVVA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 215 DAfyrgeklvnLKELADESLEKCREKGfpVRCCIVVKHV---GRAELG--MNDSPSQSPPvkrQCPDVQISWNegvdlww 289
Cdd:cd05938 86 PE---------LQEAVEEVLPALRADG--VSVWYLSHTSnteGVISLLdkVDAASDEPVP---ASLRAHVTIK------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 290 helmqeagdefepewcdaeDPLFILYTSGSTGKPKGVVhtIGGYMLYVATTFKYVFDFHPEDVFWCTA----DIGWITGH 365
Cdd:cd05938 145 -------------------SPALYIYTSGTTGLPKAAR--ISHLRVLQCSGFLSLCGVTADDVIYITLplyhSSGFLLGI 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 366 SyvtyGPLANGATSVLFEGIPTypdeSRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVTKHSRASLqvlgTVGEPINPE 445
Cdd:cd05938 204 G----GCIELGATCVLKPKFSA----SQFWDDCRKHNVTVIQYIGELLRYLCNQPQSPNDRDHKVRL----AIGNGLRAD 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 446 AWLWYHRVVGSQHcpIVDTFWQTEtgGHM----LTPLPGATpmkpGSAS------FPF------------------FGVA 497
Cdd:cd05938 272 VWREFLRRFGPIR--IREFYGSTE--GNIgffnYTGKIGAV----GRVSylykllFPFelikfdvekeepvrdaqgFCIP 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 498 -----PAILnesgeelegeaEGYLVFKQPWPGimrtiY-GNHTRFETT----YFKKFPGYYVTGDGCRRDQDGYYWITGR 567
Cdd:cd05938 344 vakgePGLL-----------VAKITQQSPFLG-----YaGDKEQTEKKllrdVFKKGDVYFNTGDLLVQDQQNFLYFHDR 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 568 IDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHP-VKGECLYCFVTLCDGHTFSStltEELKKQIREKIGPIATPD 646
Cdd:cd05938 408 VGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTVPgHEGRIGMAAVKLKPGHEFDG---KKLYQHVREYLPAYARPR 484
|
..
gi 625195332 647 YI 648
Cdd:cd05938 485 FL 486
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
113-374 |
2.37e-05 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 47.79 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 113 HEKKLGDKVAfywEGNEPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARlgalHSIVfa 192
Cdd:PLN02736 59 DYKYLGTRIR---VDGTVGEYKWMTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACSA----YSYV-- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 193 gfsaeslcerildsSCSLLIT--TDAFyrgEKLVNLKELAD--------ESLEKCREKGFPVRCCIVVkhvgraelGMND 262
Cdd:PLN02736 130 --------------SVPLYDTlgPDAV---KFIVNHAEVAAifcvpqtlNTLLSCLSEIPSVRLIVVV--------GGAD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 263 SPSQSPPVKRQCPDVQISwnegvdlwwhELMQEAG---DEFEPEwcDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVAT 339
Cdd:PLN02736 185 EPLPSLPSGTGVEIVTYS----------KLLAQGRsspQPFRPP--KPEDVATICYTSGTTGTPKGVVLTHGNLIANVAG 252
|
250 260 270
....*....|....*....|....*....|....*
gi 625195332 340 TfKYVFDFHPEDVfwctadigwitghsYVTYGPLA 374
Cdd:PLN02736 253 S-SLSTKFYPSDV--------------HISYLPLA 272
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
137-337 |
3.27e-05 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 47.12 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 137 TYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARL-------------GALHSIV------FAgFSAE 197
Cdd:PLN02430 78 TYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHslicvplydtlgpGAVDYIVdhaeidFV-FVQD 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 198 SLCERILDSSCSllittdAFYRGEKLVNLKELADESLEKCREKGFPVRCCIVVKHVGRaelgmnDSPSQSPPVKrqcpdv 277
Cdd:PLN02430 157 KKIKELLEPDCK------SAKRLKAIVSFTSVTEEESDKASQIGVKTYSWIDFLHMGK------ENPSETNPPK------ 218
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 278 qiswnegvdlwwhelmqeagdefepewcdAEDPLFILYTSGSTGKPKGVVHTIGGYMLYV 337
Cdd:PLN02430 219 -----------------------------PLDICTIMYTSGTSGDPKGVVLTHEAVATFV 249
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
119-326 |
5.64e-05 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 46.43 E-value: 5.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 119 DKVAFYWEGnepgetTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGalHSIVFAGFS--A 196
Cdd:PRK04813 17 DFPAYDYLG------EKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAG--HAYIPVDVSspA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 197 ESLcERILDSS-CSLLITTDAFYRGE---KLVNLKELADESLEKcrekgfpvrccivvkhvgraelgmnDSPSQSPPVKr 272
Cdd:PRK04813 89 ERI-EMIIEVAkPSLIIATEELPLEIlgiPVITLDELKDIFATG-------------------------NPYDFDHAVK- 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 625195332 273 qcpdvqiswnegvdlwwhelmqeaGDefepewcdaeDPLFILYTSGSTGKPKGV 326
Cdd:PRK04813 142 ------------------------GD----------DNYYIIFTSGTTGKPKGV 161
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
283-374 |
7.93e-05 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 45.67 E-value: 7.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 283 EGVDLW-WHELMQE-AGDEFEPEWCDAEDPLFILYTSGSTGKPKGVVHTIGGYMLYVATTFKYVFDFH---PEDVfwcta 357
Cdd:cd05927 87 AGVKVYsLEEFEKLgKKNKVPPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNkinPTDV----- 161
|
90
....*....|....*..
gi 625195332 358 digwitghsYVTYGPLA 374
Cdd:cd05927 162 ---------YISYLPLA 169
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
306-388 |
8.86e-05 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 46.11 E-value: 8.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 306 DAEDPLFILYTSGSTGKPKGVV--HTiggYMLYVATTFKYVFDFHPEDVFWCTADIgwitGHSyvtYGpLANGATSVLFE 383
Cdd:PRK06814 791 DPDDPAVILFTSGSEGTPKGVVlsHR---NLLANRAQVAARIDFSPEDKVFNALPV----FHS---FG-LTGGLVLPLLS 859
|
....*
gi 625195332 384 GIPTY 388
Cdd:PRK06814 860 GVKVF 864
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
306-602 |
2.42e-04 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 44.27 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 306 DAEDPLFILYTSGSTGKPKGVVHTIGGyMLYVATTFKYVFDFHPEDVFWCTADIgWitgHSY---VTYGPLANGAtSVLF 382
Cdd:cd17640 86 DSDDLATIIYTSGTTGNPKGVMLTHAN-LLHQIRSLSDIVPPQPGDRFLSILPI-W---HSYersAEYFIFACGC-SQAY 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 383 EGIPTYPDEsrlwsiVDKYKVTKFYTAPTAIRMLMKFGDEPVTKHSRASLQVLGTV---GE---PINPEAWLWYH----- 451
Cdd:cd17640 160 TSIRTLKDD------LKRVKPHYIVSVPRLWESLYSGIQKQVSKSSPIKQFLFLFFlsgGIfkfGISGGGALPPHvdtff 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 452 RVVGsqhCPIVDTFWQTETGghmltplPGATPMKP-----GSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPwPGIM 526
Cdd:cd17640 234 EAIG---IEVLNGYGLTETS-------PVVSARRLkcnvrGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRG-PQVM 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 527 RTIYGNHtrfETTyfKKF---PGYYVTGDGCRRDQDGYYWITGRIDDMLNVS-GHLLSTAEVESALVEHEAVAEAAVVGH 602
Cdd:cd17640 303 KGYYKNP---EAT--SKVldsDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIMVVGQ 377
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
301-445 |
1.49e-03 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 41.71 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 301 EPEWCDAEDPL-FILYTSGSTGKPKGVV---HTIGGYMLYVATTfkyvFDFHPEDVF--W--CTADIGWITGHsyvtYGP 372
Cdd:cd05908 98 EEVLCELADELaFIQFSSGSTGDPKGVMlthENLVHNMFAILNS----TEWKTKDRIlsWmpLTHDMGLIAFH----LAP 169
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 625195332 373 LANGATSVLfegIPT--YPDESRLW-SIVDKYKVTKFYTAPTAIRMLMK-FGDEPVTKHSRASLQVLGTVGEPINPE 445
Cdd:cd05908 170 LIAGMNQYL---MPTrlFIRRPILWlKKASEHKATIVSSPNFGYKYFLKtLKPEKANDWDLSSIRMILNGAEPIDYE 243
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
132-186 |
4.98e-03 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 40.02 E-value: 4.98e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 625195332 132 ETTKITYRELLVQVCQFSNVLR-KQGIQKGDRVAIYMPMILELVVAMLACARLGAL 186
Cdd:cd05905 11 EATTLTWGKLLSRAEKIAAVLQkKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVV 66
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
132-190 |
5.10e-03 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 40.43 E-value: 5.10e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 625195332 132 ETTKITYRellvQVCQFSNV----LRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIV 190
Cdd:TIGR03443 267 KTRSFTYK----QINEASNIlahyLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVI 325
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
136-331 |
5.78e-03 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 39.85 E-value: 5.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 136 ITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGAlhsivfagfsaeslceRILdsscsllittd 215
Cdd:PRK09029 29 LTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGA----------------RVL----------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625195332 216 afyrgekLVNlkeladeslekcrekgfpvrccivvkhvgraelgmndsPsQSPPVKRQ--CPDVQIS--WNEGVDLWWHE 291
Cdd:PRK09029 82 -------PLN--------------------------------------P-QLPQPLLEelLPSLTLDfaLVLEGENTFSA 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 625195332 292 L----MQEAGDEFEPEWcDAEDPLFILYTSGSTGKPKGVVHTIG 331
Cdd:PRK09029 116 LtslhLQLVEGAHAVAW-QPQRLATMTLTSGSTGLPKAAVHTAQ 158
|
|
| |
