|
Name |
Accession |
Description |
Interval |
E-value |
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
5-656 |
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: 1143.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 5 REFWGNIAKEFYWKTPCPGPFlqynfDVTKGKIFTEWMKGATTNICYNVLDRNVHekKLGDKVAFYWEGNEPGETTKITY 84
Cdd:cd05966 15 EEFWGEIAKELDWFKPWDKVL-----DWSKGPPFIKWFEGGKLNISYNCLDRHLK--ERGDKVAIIWEGDEPDQSRTITY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 85 RELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITTDAFY 164
Cdd:cd05966 88 RELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCKLVITADGGY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 165 RGEKLVNLKELADESLEKCrekgFPVRCCIVVKHVGRAelgmndspsqsppvkrqcpdvqISWNEGVDLWWHELMQEAGD 244
Cdd:cd05966 168 RGGKVIPLKEIVDEALEKC----PSVEKVLVVKRTGGE----------------------VPMTEGRDLWWHDLMAKQSP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 245 EFEPEWCDAEDPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGVVHTIGGYMLYVATTFKYVFDFHPEDVF 324
Cdd:cd05966 222 ECEPEWMDSEDPLFILYTSGSTGKPK-------------------------GVVHTTGGYLLYAATTFKYVFDYHPDDIY 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 325 WCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVTKHSRASLQ 404
Cdd:cd05966 277 WCTADIGWITGHSYIVYGPLANGATTVMFEGTPTYPDPGRYWDIVEKHKVTIFYTAPTAIRALMKFGDEWVKKHDLSSLR 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 405 VLGTVGEPINPEAWLWYHRVVGSQHCPIVDTFWQTETGGHMLTPLPGATPMKPGSASFPFFGVAPAILNESGEELEGEAE 484
Cdd:cd05966 357 VLGSVGEPINPEAWMWYYEVIGKERCPIVDTWWQTETGGIMITPLPGATPLKPGSATRPFFGIEPAILDEEGNEVEGEVE 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 485 GYLVFKQPWPGIMRTIYGNHTRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEA 564
Cdd:cd05966 437 GYLVIKRPWPGMARTIYGDHERYEDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPA 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 565 VAEAAVVGHPHPVKGECLYCFVTLCDGHTFSSTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQN 644
Cdd:cd05966 517 VAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKIAAG 596
|
650
....*....|..
gi 1538017002 645 DHDLGDTSTVAD 656
Cdd:cd05966 597 EEELGDTSTLAD 608
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
6-663 |
0e+00 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 1066.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 6 EFWGNIAKEFYWKTPcpgpflqYNFDVTKGKIFTEWMKGATTNICYNVLDRNVHEKklGDKVAFYWEGNEPGETTKITYR 85
Cdd:PRK00174 32 GFWAEQAKRLDWFKP-------FDTVLDWNAPFIKWFEDGELNVSYNCLDRHLKTR--GDKVAIIWEGDDPGDSRKITYR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 86 ELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITTDAFYR 165
Cdd:PRK00174 103 ELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVFGGFSAEALADRIIDAGAKLVITADEGVR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 166 GEKLVNLKELADESLEKCRekgfPVRCCIVVKHVGRAelgmndspsqsppvkrqcpdvqISWNEGVDLWWHELMQEAGDE 245
Cdd:PRK00174 183 GGKPIPLKANVDEALANCP----SVEKVIVVRRTGGD----------------------VDWVEGRDLWWHELVAGASDE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 246 FEPEWCDAEDPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGVVHTIGGYMLYVATTFKYVFDFHPEDVFW 325
Cdd:PRK00174 237 CEPEPMDAEDPLFILYTSGSTGKPK-------------------------GVLHTTGGYLVYAAMTMKYVFDYKDGDVYW 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 326 CTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVTKHSRASLQV 405
Cdd:PRK00174 292 CTADVGWVTGHSYIVYGPLANGATTLMFEGVPNYPDPGRFWEVIDKHKVTIFYTAPTAIRALMKEGDEHPKKYDLSSLRL 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 406 LGTVGEPINPEAWLWYHRVVGSQHCPIVDTFWQTETGGHMLTPLPGATPMKPGSASFPFFGVAPAILNESGEELEGEAEG 485
Cdd:PRK00174 372 LGSVGEPINPEAWEWYYKVVGGERCPIVDTWWQTETGGIMITPLPGATPLKPGSATRPLPGIQPAVVDEEGNPLEGGEGG 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 486 YLVFKQPWPGIMRTIYGNHTRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAV 565
Cdd:PRK00174 452 NLVIKDPWPGMMRTIYGDHERFVKTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKV 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 566 AEAAVVGHPHPVKGECLYCFVTLCDGHTFSSTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQND 645
Cdd:PRK00174 532 AEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRKIAEGE 611
|
650
....*....|....*...
gi 1538017002 646 HDLGDTSTVADPSVINHL 663
Cdd:PRK00174 612 EILGDTSTLADPSVVEKL 629
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
7-663 |
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: 999.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 7 FWGNIAKE-FYWKTPcPGPFLQYNFDVtkgkiFTEWMKGATTNICYNVLDRnvHEKKLGDKVAFYWEGNEPGETTKITYR 85
Cdd:TIGR02188 21 FWAKLARElLDWFKP-FTKVLDWSFPP-----FYKWFVGGELNVSYNCVDR--HLEARPDKVAIIWEGDEPGEVRKITYR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 86 ELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITTDAFYR 165
Cdd:TIGR02188 93 ELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALADRINDAGAKLVITADEGLR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 166 GEKLVNLKELADESLEKCREKgfpVRCCIVVKHVGraelgmndspsqsppvkrqcpDVQISWNEGVDLWWHELMQEAGDE 245
Cdd:TIGR02188 173 GGKVIPLKAIVDEALEKCPVS---VEHVLVVRRTG---------------------NPVVPWVEGRDVWWHDLMAKASAY 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 246 FEPEWCDAEDPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGVVHTIGGYMLYVATTFKYVFDFHPEDVFW 325
Cdd:TIGR02188 229 CEPEPMDSEDPLFILYTSGSTGKPK-------------------------GVLHTTGGYLLYAAMTMKYVFDIKDGDIFW 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 326 CTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVTKHSRASLQV 405
Cdd:TIGR02188 284 CTADVGWITGHSYIVYGPLANGATTVMFEGVPTYPDPGRFWEIIEKHKVTIFYTAPTAIRALMRLGDEWVKKHDLSSLRL 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 406 LGTVGEPINPEAWLWYHRVVGSQHCPIVDTFWQTETGGHMLTPLPGATPMKPGSASFPFFGVAPAILNES-GEELEGEAE 484
Cdd:TIGR02188 364 LGSVGEPINPEAWMWYYKVVGKERCPIVDTWWQTETGGIMITPLPGATPTKPGSATLPFFGIEPAVVDEEgNPVEGPGEG 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 485 GYLVFKQPWPGIMRTIYGNHTRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEA 564
Cdd:TIGR02188 444 GYLVIKQPWPGMLRTIYGDHERFVDTYFSPFPGYYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPA 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 565 VAEAAVVGHPHPVKGECLYCFVTLCDGHTFSSTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQN 644
Cdd:TIGR02188 524 VAEAAVVGIPDDIKGQAIYAFVTLKDGYEPDDELRKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRRLLRKIAAG 603
|
650 660
....*....|....*....|
gi 1538017002 645 DHD-LGDTSTVADPSVINHL 663
Cdd:TIGR02188 604 EAEiLGDTSTLEDPSVVEEL 623
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
40-663 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 860.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 40 EWMKGATTNICYNVLDRNVHEKklGDKVAFYWEGnEPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILEL 119
Cdd:COG0365 1 RWFVGGRLNIAYNCLDRHAEGR--GDKVALIWEG-EDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 120 VVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITTDAFYRGEKLVNLKELADESLEKCREkgfpVRCCIVVKHV 199
Cdd:COG0365 78 VIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALEELPS----LEHVIVVGRT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 200 GrAELGMNDspsqsppvkrqcpdvqiswnegvDLWWHELMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPKlcagsicws 279
Cdd:COG0365 154 G-ADVPMEG-----------------------DLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPK--------- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 280 vemdtkpqpedpfspqGVVHTIGGYMLYVATTFKYVFDFHPEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTY 359
Cdd:COG0365 201 ----------------GVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTADIGWATGHSYIVYGPLLNGATVVLYEGRPDF 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 360 PDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGsqhCPIVDTFWQT 439
Cdd:COG0365 265 PDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDLSSLRLLGSAGEPLNPEVWEWWYEAVG---VPIVDGWGQT 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 440 ETGGHMLTPLPGaTPMKPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTIYGNHTRFETTYFKKFPGYY 519
Cdd:COG0365 342 ETGGIFISNLPG-LPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPWPGMFRGYWNDPERYRETYFGRFPGWY 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 520 VTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSSTLT 599
Cdd:COG0365 421 RTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSDELA 500
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1538017002 600 EELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQNDhDLGDTSTVADPSVINHL 663
Cdd:COG0365 501 KELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEGR-PLGDTSTLEDPEALDEI 563
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
7-663 |
0e+00 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 848.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 7 FWGNIAKEFYWKTP-CPGPFLQYNFDVTKGKIFTEWMKGATTNICYNVLDRNVhEKKLGDKVAFYWEGNEPGETTKITYR 85
Cdd:PLN02654 46 FWSDIASQFYWKQKwEGDEVCSENLDVRKGPISIEWFKGGKTNICYNCLDRNV-EAGNGDKIAIYWEGNEPGFDASLTYS 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 86 ELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITTDAFYR 165
Cdd:PLN02654 125 ELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVITCNAVKR 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 166 GEKLVNLKELADESLEKCREKGFPVRCCIVVKHvgraELGMNDSPSQsppvkrqcpdvqisWNEGVDLWWHELMQEAGDE 245
Cdd:PLN02654 205 GPKTINLKDIVDAALDESAKNGVSVGICLTYEN----QLAMKREDTK--------------WQEGRDVWWQDVVPNYPTK 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 246 FEPEWCDAEDPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGVVHTIGGYMLYVATTFKYVFDFHPEDVFW 325
Cdd:PLN02654 267 CEVEWVDAEDPLFLLYTSGSTGKPK-------------------------GVLHTTGGYMVYTATTFKYAFDYKPTDVYW 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 326 CTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVTKHSRASLQV 405
Cdd:PLN02654 322 CTADCGWITGHSYVTYGPMLNGATVLVFEGAPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKSLRV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 406 LGTVGEPINPEAWLWYHRVVGSQHCPIVDTFWQTETGGHMLTPLPGATPMKPGSASFPFFGVAPAILNESGEELEGEAEG 485
Cdd:PLN02654 402 LGSVGEPINPSAWRWFFNVVGDSRCPISDTWWQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGKEIEGECSG 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 486 YLVFKQPWPGIMRTIYGNHTRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAV 565
Cdd:PLN02654 482 YLCVKKSWPGAFRTLYGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQC 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 566 AEAAVVGHPHPVKGECLYCFVTLCDGHTFSSTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQND 645
Cdd:PLN02654 562 AEAAVVGIEHEVKGQGIYAFVTLVEGVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIASRQ 641
|
650
....*....|....*....
gi 1538017002 646 HD-LGDTSTVADPSVINHL 663
Cdd:PLN02654 642 LDeLGDTSTLADPGVVDQL 660
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
7-634 |
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: 688.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 7 FWGNIAKEFYWKTPCPGpflQYNFDVTKGKIFTEWMKGATTNICYNVLDRNVHEKklGDKVAFYWEGNEPGETTKITYRE 86
Cdd:cd17634 15 FWGEAGKILDWITPYQK---VKNTSFAPGAPSIKWFEDATLNLAANALDRHLREN--GDRTAIIYEGDDTSQSRTISYRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 87 LLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITTDAFYRG 166
Cdd:cd17634 90 LHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADGGVRA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 167 EKLVNLKELADESLEKcreKGFPVRCCIVVKHVGraelgmndspsqsppvkrqcpdVQISWNEGVDLWWHELMQEAGDEF 246
Cdd:cd17634 170 GRSVPLKKNVDDALNP---NVTSVEHVIVLKRTG----------------------SDIDWQEGRDLWWRDLIAKASPEH 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 247 EPEWCDAEDPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGVVHTIGGYMLYVATTFKYVFDFHPEDVFWC 326
Cdd:cd17634 225 QPEAMNAEDPLFILYTSGTTGKPK-------------------------GVLHTTGGYLVYAATTMKYVFDYGPGDIYWC 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 327 TADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVTKHSRASLQVL 406
Cdd:cd17634 280 TADVGWVTGHSYLLYGPLACGATTLLYEGVPNWPTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIEGTDRSSLRIL 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 407 GTVGEPINPEAWLWYHRVVGSQHCPIVDTFWQTETGGHMLTPLPGATPMKPGSASFPFFGVAPAILNESGEELEGEAEGY 486
Cdd:cd17634 360 GSVGEPINPEAYEWYWKKIGKEKCPVVDTWWQTETGGFMITPLPGAIELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGN 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 487 LVFKQPWPGIMRTIYGNHTRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVA 566
Cdd:cd17634 440 LVITDPWPGQTRTLFGDHERFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVA 519
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1538017002 567 EAAVVGHPHPVKGECLYCFVTLCDGHTFSSTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIM 634
Cdd:cd17634 520 EAAVVGIPHAIKGQAPYAYVVLNHGVEPSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
7-663 |
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: 570.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 7 FWGNIAKEFYWKTPcpgpfLQYNFDVTKGKiFTEWMKGATTNICYNVLDRNVhEKKLGDKVAFYWEGNEPGETTKITYRE 86
Cdd:cd05967 15 FWAEQARLIDWFKP-----PEKILDNSNPP-FTRWFVGGRLNTCYNALDRHV-EAGRGDQIALIYDSPVTGTERTYTYAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 87 LLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITTDAFYRG 166
Cdd:cd05967 88 LLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKLIVTASCGIEP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 167 EKLVNLKELADESLEKCREKgfPVRCCIVvkhvgraelgmndspsQSPPVKRQCPDVqiswneGVDLWWHELMQEAGdEF 246
Cdd:cd05967 168 GKVVPYKPLLDKALELSGHK--PHHVLVL----------------NRPQVPADLTKP------GRDLDWSELLAKAE-PV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 247 EPEWCDAEDPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGVVHTIGGYMLYVATTFKYVFDFHPEDVFWC 326
Cdd:cd05967 223 DCVPVAATDPLYILYTSGTTGKPK-------------------------GVVRDNGGHAVALNWSMRNIYGIKPGDVWWA 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 327 TADIGWITGHSYVTYGPLANGATSVLFEGIPT-YPDESRLWSIVDKYKVTKFYTAPTAIRMLMKF--GDEPVTKHSRASL 403
Cdd:cd05967 278 ASDVGWVVGHSYIVYGPLLHGATTVLYEGKPVgTPDPGAFWRVIEKYQVNALFTAPTAIRAIRKEdpDGKYIKKYDLSSL 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 404 QVLGTVGEPINPEAWLWYHRVVGSqhcPIVDTFWQTETGGHMLTPLPG--ATPMKPGSASFPFFGVAPAILNESGEELEG 481
Cdd:cd05967 358 RTLFLAGERLDPPTLEWAENTLGV---PVIDHWWQTETGWPITANPVGlePLPIKAGSPGKPVPGYQVQVLDEDGEPVGP 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 482 EAEGYLVFKQPW-PGIMRTIYGNHTRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALV 560
Cdd:cd05967 435 NELGNIVIKLPLpPGCLLTLWKNDERFKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVL 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 561 EHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSS-TLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 639
Cdd:cd05967 515 SHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITAeELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLR 594
|
650 660
....*....|....*....|....
gi 1538017002 640 KIAQNDhDLGDTSTVADPSVINHL 663
Cdd:cd05967 595 KIADGE-DYTIPSTIEDPSVLDEI 617
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
4-660 |
0e+00 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 531.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 4 RREFWGNIAKEFYWKTPcPGPFLQYNfdvtkGKIFTEWMKGATTNICYNVLDRnvHEKKLGDKVAFYWEGNEPGETTKIT 83
Cdd:PRK10524 15 PEAFWAEQARRIDWQTP-FTQVLDYS-----NPPFARWFVGGRTNLCHNAVDR--HLAKRPEQLALIAVSTETDEERTYT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 84 YRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITTDAF 163
Cdd:PRK10524 87 FRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARIDDAKPVLIVSADAG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 164 YRGEKLVNLKELADESLEKCREKgfPvrccivvKHVGRAELGMNDSPsqsppvkrqcpdvqisWNEGVDLWWHELMQEAG 243
Cdd:PRK10524 167 SRGGKVVPYKPLLDEAIALAQHK--P-------RHVLLVDRGLAPMA----------------RVAGRDVDYATLRAQHL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 244 DEFEP-EWCDAEDPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGVVHTIGGYMLYVATTFKYVFDFHPED 322
Cdd:PRK10524 222 GARVPvEWLESNEPSYILYTSGTTGKPK-------------------------GVQRDTGGYAVALATSMDTIFGGKAGE 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 323 VFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVTKHSRAS 402
Cdd:PRK10524 277 TFFCASDIGWVVGHSYIVYAPLLAGMATIMYEGLPTRPDAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDPALLRKHDLSS 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 403 LQVLGTVGEPINPEAWLWYHRVVGSqhcPIVDTFWQTETGGHMLTPLPG--ATPMKPGSASFPFFGVAPAILNESGEELE 480
Cdd:PRK10524 357 LRALFLAGEPLDEPTASWISEALGV---PVIDNYWQTETGWPILAIARGveDRPTRLGSPGVPMYGYNVKLLNEVTGEPC 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 481 GEAEG-YLVFKQPW-PGIMRTIYGNHTRFETTYFKKF-PGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVES 557
Cdd:PRK10524 434 GPNEKgVLVIEGPLpPGCMQTVWGDDDRFVKTYWSLFgRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEE 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 558 ALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSST-----LTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGK 632
Cdd:PRK10524 514 SISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLADRearlaLEKEIMALVDSQLGAVARPARVWFVSALPKTRSGK 593
|
650 660
....*....|....*....|....*...
gi 1538017002 633 IMRRVLRKIAQnDHDLGDTSTVADPSVI 660
Cdd:PRK10524 594 LLRRAIQAIAE-GRDPGDLTTIEDPAAL 620
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
40-656 |
3.61e-177 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 516.37 E-value: 3.61e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 40 EWMKGATTNICYNVLDRNVHEKkLGDKVAFYWEGNEPGEttKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILEL 119
Cdd:PRK04319 35 SWLETGKVNIAYEAIDRHADGG-RKDKVALRYLDASRKE--KYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 120 VVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITTDAFYRGEKLVNLKELadeslekcrekgfpvrccivvKHV 199
Cdd:PRK04319 112 YFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLERKPADDLPSL---------------------KHV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 200 graeLGMNDSPSQSPPVkrqcpdvqiswnegVDLWwhELMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPKlcagsicws 279
Cdd:PRK04319 171 ----LLVGEDVEEGPGT--------------LDFN--ALMEQASDEFDIEWTDREDGAILHYTSGSTGKPK--------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 280 vemdtkpqpedpfspqGVVHTIGGYMLYVATTfKYVFDFHPEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGiptY 359
Cdd:PRK04319 222 ----------------GVLHVHNAMLQHYQTG-KYVLDLHEDDVYWCTADPGWVTGTSYGIFAPWLNGATNVIDGG---R 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 360 PDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGSqhcPIVDTFWQT 439
Cdd:PRK04319 282 FSPERWYRILEDYKVTVWYTAPTAIRMLMGAGDDLVKKYDLSSLRHILSVGEPLNPEVVRWGMKVFGL---PIHDNWWMT 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 440 ETGGHMLTPLPgATPMKPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTIYGNHTRFETtYFKkfPGYY 519
Cdd:PRK04319 359 ETGGIMIANYP-AMDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIKKGWPSMMRGIWNNPEKYES-YFA--GDWY 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 520 VTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSSTLT 599
Cdd:PRK04319 435 VSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEELK 514
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1538017002 600 EELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLrKIAQNDHDLGDTSTVAD 656
Cdd:PRK04319 515 EEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVL-KAWELGLPEGDLSTMED 570
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
7-657 |
8.87e-170 |
|
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: 498.94 E-value: 8.87e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 7 FWGNIAKEF-YWKTPCPGPFLqynfDVTKGKIFTEWMKGATTNICYNVLDRnvHEKKLGDKVAFYWEGnEPGETTKITYR 85
Cdd:cd05968 23 FWGEFVKDVgIEWYEPPYQTL----DLSGGKPWAAWFVGGRMNIVEQLLDK--WLADTRTRPALRWEG-EDGTSRTLTYG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 86 ELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITTDAFYR 165
Cdd:cd05968 96 ELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITADGFTR 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 166 GEKLVNLKELADESLEKCrekgFPVRCCIVVKHVGRAELgmndspsqsppvkrqcpdvqisWNEGVDLWWHELMQEAGDE 245
Cdd:cd05968 176 RGREVNLKEEADKACAQC----PTVEKVVVVRHLGNDFT----------------------PAKGRDLSYDEEKETAGDG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 246 FEPewCDAEDPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGVVHTIGGYMLYVATTFKYVFDFHPED-VF 324
Cdd:cd05968 230 AER--TESEDPLMIIYTSGTTGKPK-------------------------GTVHVHAGFPLKAAQDMYFQFDLKPGDlLT 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 325 WCTaDIGWITGhSYVTYGPLANGATSVLFEGIPTYPDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVTKHSRASLQ 404
Cdd:cd05968 283 WFT-DLGWMMG-PWLIFGGLILGATMVLYDGAPDHPKADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSLR 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 405 VLGTVGEPINPEAWLWYHRVVGSQHCPIVDTFWQTETGGHMLTPLPgATPMKPGSASFPFFGVAPAILNESGEELEGEAE 484
Cdd:cd05968 361 VLGSTGEPWNPEPWNWLFETVGKGRNPIINYSGGTEISGGILGNVL-IKPIKPSSFNGPVPGMKADVLDESGKPARPEVG 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 485 GyLVFKQPWPGIMRTIYGNHTRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEA 564
Cdd:cd05968 440 E-LVLLAPWPGMTRGFWRDEDRYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPA 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 565 VAEAAVVGHPHPVKGECLYCFVTLCDGHTFSSTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKiAQN 644
Cdd:cd05968 519 VLESAAIGVPHPVKGEAIVCFVVLKPGVTPTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRA-AYL 597
|
650
....*....|...
gi 1538017002 645 DHDLGDTSTVADP 657
Cdd:cd05968 598 GKELGDLSSLENP 610
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
83-642 |
9.19e-131 |
|
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: 392.64 E-value: 9.19e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 83 TYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITTDA 162
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 163 FYRgeklvnlkeladeslekcrekgfpvrccivvkhvgraelgmndspsqsppvKRqcpdvqiswnegvdlwwhelmqea 242
Cdd:cd05969 82 LYE---------------------------------------------------RT------------------------ 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 243 gdefepewcDAEDPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGVVHtIGGYMLYVATTFKYVFDFHPED 322
Cdd:cd05969 87 ---------DPEDPTLLHYTSGTTGTPK-------------------------GVLH-VHDAMIFYYFTGKYVLDLHPDD 131
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 323 VFWCTADIGWITGHSYVTYGPLANGATSVLFEGiptYPDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVTKHSRAS 402
Cdd:cd05969 132 IYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEG---RFDAESWYGIIERVKVTVWYTAPTAIRMLMKEGDELARKYDLSS 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 403 LQVLGTVGEPINPEAWLWYHRVVGsqhCPIVDTFWQTETGGHMLTPLPGaTPMKPGSASFPFFGVAPAILNESGEELEGE 482
Cdd:cd05969 209 LRFIHSVGEPLNPEAIRWGMEVFG---VPIHDTWWQTETGSIMIANYPC-MPIKPGSMGKPLPGVKAAVVDENGNELPPG 284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 483 AEGYLVFKQPWPGIMRTIYGNHTRFETtYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEH 562
Cdd:cd05969 285 TKGILALKPGWPSMFRGIWNDEERYKN-SFID--GWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEH 361
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 563 EAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSSTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 642
Cdd:cd05969 362 PAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDELKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLKAKE 441
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
54-546 |
5.39e-104 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 322.72 E-value: 5.39e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 54 LDRNVheKKLGDKVAFywegnEPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALH 133
Cdd:pfam00501 1 LERQA--ARTPDKTAL-----EVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 134 SIVFAGFSAESLCERILDSSCSLLITTDAFYrgeklvnlkelaDESLEKCREKGFPVRCCIVVKHVGRAELGMNDSPSQS 213
Cdd:pfam00501 74 VPLNPRLPAEELAYILEDSGAKVLITDDALK------------LEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 214 PPVkrqcpdvqiswnegvdlwwhelmqeagDEFEPEWCDAEDPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfs 293
Cdd:pfam00501 142 ADV---------------------------PPPPPPPPDPDDLAYIIYTSGTTGKPK----------------------- 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 294 pqGVVHTIgGYMLYVATTFKYV----FDFHPEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTyPDESRLWSIV 369
Cdd:pfam00501 172 --GVMLTH-RNLVANVLSIKRVrprgFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFPA-LDPAALLELI 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 370 DKYKVTKFYTAPTAIRMLMKFGDEPVTKHSraSLQVLGTVGEPINPEAWLWYHRVVGsqhCPIVDTFWQTETGGHMLTPL 449
Cdd:pfam00501 248 ERYKVTVLYGVPTLLNMLLEAGAPKRALLS--SLRLVLSGGAPLPPELARRFRELFG---GALVNGYGLTETTGVVTTPL 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 450 PGATPM-KPGSASFPFFGVAPAILNESGEELEGEAEG-YLVFKQpwPGIMRTIYGNHTRFETTYFKKfpGYYVTGDGCRR 527
Cdd:pfam00501 323 PLDEDLrSLGSVGRPLPGTEVKIVDDETGEPVPPGEPgELCVRG--PGVMKGYLNDPELTAEAFDED--GWYRTGDLGRR 398
|
490
....*....|....*....
gi 1538017002 528 DQDGYYWITGRIDDMLNVS 546
Cdd:pfam00501 399 DEDGYLEIVGRKKDQIKLG 417
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
83-640 |
5.66e-102 |
|
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: 318.13 E-value: 5.66e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 83 TYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLIttda 162
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIV---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 163 fyrgeklvnlkeladeslekcrekgfpvrccivvkhvgraelgmndspsqsppvkrqcpdvqiswnegvdlwwhelmqea 242
Cdd:cd05972 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 243 gdefepewCDAEDPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGVVHTIGgYMLYVATTFKYVFDFHPED 322
Cdd:cd05972 78 --------TDAEDPALIYFTSGTTGLPK-------------------------GVLHTHS-YPLGHIPTAAYWLGLRPDD 123
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 323 VFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTypDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEpvtKHSRAS 402
Cdd:cd05972 124 IHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRF--DAERILELLERYGVTSFCGPPTAYRMLIKQDLS---SYKFSH 198
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 403 LQVLGTVGEPINPEAWLWYHRVVGSqhcPIVDTFWQTETGgHMLTPLPGaTPMKPGSASFPFFGVAPAILNESGEELEGE 482
Cdd:cd05972 199 LRLVVSAGEPLNPEVIEWWRAATGL---PIRDGYGQTETG-LTVGNFPD-MPVKPGSMGRPTPGYDVAIIDDDGRELPPG 273
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 483 AEGYLVFKQPWPGIMRTIYGNHTRFETTYFKkfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEH 562
Cdd:cd05972 274 EEGDIAIKLPPPGLFLGYVGDPEKTEASIRG---DYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEH 350
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1538017002 563 EAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSSTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 640
Cdd:cd05972 351 PAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
255-634 |
1.93e-82 |
|
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: 263.76 E-value: 1.93e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 255 DPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGVVHTIGGYMLYVATTFKYvFDFHPEDVFWCTADIGWIt 334
Cdd:cd04433 1 DPALILYTSGTTGKPK-------------------------GVVLSHRNLLAAAAALAAS-GGLTEGDVFLSTLPLFHI- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 335 GHSYVTYGPLANGATSVLFEGiptyPDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPvtKHSRASLQVLGTVGEPIN 414
Cdd:cd04433 54 GGLFGLLGALLAGGTVVLLPK----FDPEAALELIEREKVTILLGVPTLLARLLKAPESA--GYDLSSLRALVSGGAPLP 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 415 PEAWLWYHRVVGsqhCPIVDTFWQTETGGHMLTPLPGATPMKPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPWP 494
Cdd:cd04433 128 PELLERFEEAPG---IKLVNGYGLTETGGTVATGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSV 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 495 giMRTIYGNhtrFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHP 574
Cdd:cd04433 205 --MKGYWNN---PEATAAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVP 279
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 575 HPVKGECLYCFVTLCDGHTFSStltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIM 634
Cdd:cd04433 280 DPEWGERVVAVVVLRPGADLDA---EELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
2-641 |
2.13e-79 |
|
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: 264.90 E-value: 2.13e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 2 RRRREFWGNIAKefYWKTPCPGPflqYNFDVTKGKIF--TEWMKGATTNICYNVLDRNVHEkklgDKVAFYweGNEPGET 79
Cdd:cd05943 28 DDPGAFWAAVWD--FSGVRGSKP---YDVVVVSGRIMpgARWFPGARLNYAENLLRHADAD----DPAAIY--AAEDGER 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 80 TKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLIT 159
Cdd:cd05943 97 TEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVLDRFGQIEPKVLFA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 160 TDAFYRGEKLVNLkeladesLEKCRE--KGFPVRCCIVVkhvgraelgmndspsqsppVKRQCPDVQISWNEGVD-LWWH 236
Cdd:cd05943 177 VDAYTYNGKRHDV-------REKVAElvKGLPSLLAVVV-------------------VPYTVAAGQPDLSKIAKaLTLE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 237 E-LMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGVVHTIGGYMLYVATTFKYV 315
Cdd:cd05943 231 DfLATGAAGELEFEPLPFDHPLYILYSSGTTGLPK-------------------------CIVHGAGGTLLQHLKEHILH 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 316 FDFHPEDVFWCTADIGWITGHSYVTYgpLANGATSVLFEGIPTYPDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPV 395
Cdd:cd05943 286 CDLRPGDRLFYYTTCGWMMWNWLVSG--LAVGATIVLYDGSPFYPDTNALWDLADEEGITVFGTSAKYLDALEKAGLKPA 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 396 TKHSRASLQVLGTVGEPINPEAWLWYHRVVGSqhcpivDTFWQTETGGhmlTPLPGA-------TPMKPGSASFPFFGVA 468
Cdd:cd05943 364 ETHDLSSLRTILSTGSPLKPESFDYVYDHIKP------DVLLASISGG---TDIISCfvggnplLPVYRGEIQCRGLGMA 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 469 PAILNESGEELEGEAEGyLVFKQPWPGIMRTIYG--NHTRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVS 546
Cdd:cd05943 435 VEAFDEEGKPVWGEKGE-LVCTKPFPSMPVGFWNdpDGSRYRAAYFAKYPGVWAHGDWIEITPRGGVVILGRSDGTLNPG 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 547 GHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSSTLTEELKKQIREKIGPIATPDYIQNAPGLP 626
Cdd:cd05943 514 GVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVELDDELRKRIRSTIRSALSPRHVPAKIIAVPDIP 593
|
650
....*....|....*
gi 1538017002 627 KTRSGKIMRRVLRKI 641
Cdd:cd05943 594 RTLSGKKVEVAVKKI 608
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
53-646 |
2.33e-79 |
|
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: 259.74 E-value: 2.33e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 53 VLDRNVheKKLGDKVAFYWEGnepgetTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGAL 132
Cdd:COG0318 4 LLRRAA--ARHPDRPALVFGG------RRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 133 HSIVFAGFSAESLcERIL-DSSCSLLITtdafyrgeklvnlkeladeslekcrekgfpvrccivvkhvgraelgmndsps 211
Cdd:COG0318 76 VVPLNPRLTAEEL-AYILeDSGARALVT---------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 212 qsppvkrqcpdvqiswnegvdlwwhelmqeagdefepewcdaedpLFILYTSGSTGKPKlcagsicwsvemdtkpqpedp 291
Cdd:COG0318 103 ---------------------------------------------ALILYTSGTTGRPK--------------------- 116
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 292 fspqGVVHTIGGyMLYVATTFKYVFDFHPEDVFWCTADIGWITGHSYVTYGPLANGATSVLfegiPTYPDESRLWSIVDK 371
Cdd:COG0318 117 ----GVMLTHRN-LLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVL----LPRFDPERVLELIER 187
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 372 YKVTKFYTAPTAIRMLMKfgDEPVTKHSRASLQVLGTVGEPINPEAWlwyHRVVGSQHCPIVDTFWQTETGGHMLTPLPG 451
Cdd:COG0318 188 ERVTVLFGVPTMLARLLR--HPEFARYDLSSLRLVVSGGAPLPPELL---ERFEERFGVRIVEGYGLTETSPVVTVNPED 262
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 452 ATPMKPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPWpgIMRTIYGNHTRFEttyfKKFP-GYYVTGDGCRRDQD 530
Cdd:COG0318 263 PGERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPN--VMKGYWNDPEATA----EAFRdGWLRTGDLGRLDED 336
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 531 GYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSstlTEELKKQIREKI 610
Cdd:COG0318 337 GYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELD---AEELRAFLRERL 413
|
570 580 590
....*....|....*....|....*....|....*.
gi 1538017002 611 GPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQNDH 646
Cdd:COG0318 414 ARYKVPRRVEFVDELPRTASGKIDRRALRERYAAGA 449
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
6-640 |
1.35e-74 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 252.36 E-value: 1.35e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 6 EFWGNIAKEF-YWKTpcpgpflQYNFDVTKGKIFTEWMKGATTNICYNVLDRNVHEKKLGDKVAFYWEGNEPGETTKITY 84
Cdd:PTZ00237 23 SFWDEVAKKYvHWDK-------MYDKVYSGDEIYPDWFKGGELNTCYNVLDIHVKNPLKRDQDALIYECPYLKKTIKLTY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 85 RELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITTDAFY 164
Cdd:PTZ00237 96 YQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLIITTNYGI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 165 RGEKLV----NLKELADESLEKcrekgfPvrccivvKHVgrAELGMNDSPSQSPPVKRQcpDVQISWNEgvdLWWHELMQ 240
Cdd:PTZ00237 176 LNDEIItftpNLKEAIELSTFK------P-------SNV--ITLFRNDITSESDLKKIE--TIPTIPNT---LSWYDEIK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 241 EAGD-------EFEPewCDAEDPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGVVHTIGGYMLYVATTFK 313
Cdd:PTZ00237 236 KIKEnnqspfyEYVP--VESSHPLYILYTSGTTGNSK-------------------------AVVRSNGPHLVGLKYYWR 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 314 YVFDFHPEDVFWCTADIGWITGHSYVtYGPLANGATSVLFEGIPTYPD--ESRLWSIVDKYKVTKFYTAPTAIRMLMKFG 391
Cdd:PTZ00237 289 SIIEKDIPTVVFSHSSIGWVSFHGFL-YGSLSLGNTFVMFEGGIIKNKhiEDDLWNTIEKHKVTHTLTLPKTIRYLIKTD 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 392 DEPVTKHSR---ASLQVLGTVGEPINPEAWLWYHRVVGSQhCPIVdtFWQTETGghMLTPLPGATPMKPGSAS-FPFFGV 467
Cdd:PTZ00237 368 PEATIIRSKydlSNLKEIWCGGEVIEESIPEYIENKLKIK-SSRG--YGQTEIG--ITYLYCYGHINIPYNATgVPSIFI 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 468 APAILNESGEELEGEAEGYLVFKQPWP-GIMRTIYGNHTRFETTyFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVS 546
Cdd:PTZ00237 443 KPSILSEDGKELNVNEIGEVAFKLPMPpSFATTFYKNDEKFKQL-FSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKIS 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 547 GHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSSTLTEELKKQIRE----KIGPIATPDYIQNA 622
Cdd:PTZ00237 522 GNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQSNQSIDLNKLKNEINNiitqDIESLAVLRKIIIV 601
|
650
....*....|....*...
gi 1538017002 623 PGLPKTRSGKIMRRVLRK 640
Cdd:PTZ00237 602 NQLPKTKTGKIPRQIISK 619
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
82-640 |
9.48e-74 |
|
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: 244.35 E-value: 9.48e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 82 ITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERiLDSSCSLLITTD 161
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHR-LRTSGARLVVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 162 AFYRgeklvnlkeladeslekcrekgfpvrccivvkhvgraelgmndspsqsppvkrqcpdvqiswnegvdlwwHELmqe 241
Cdd:cd05973 80 AANR----------------------------------------------------------------------HKL--- 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 242 agdefepewcdAEDPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGVVHTIGGYMLYVATtFKYVFDFHPE 321
Cdd:cd05973 87 -----------DSDPFVMMFTSGTTGLPK-------------------------GVPVPLRALAAFGAY-LRDAVDLRPE 129
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 322 DVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDesrLWSIVDKYKVTKFYTAPTAIRMLMKFGdEPVTKHSRA 401
Cdd:cd05973 130 DSFWNAADPGWAYGLYYAITGPLALGHPTILLEGGFSVES---TWRVIERLGVTNLAGSPTAYRLLMAAG-AEVPARPKG 205
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 402 SLQVLGTVGEPINPEAWLWYHRVVGSqhcPIVDTFWQTETGGHMLTPLPGATPMKPGSASFPFFGVAPAILNESGeeleg 481
Cdd:cd05973 206 RLRRVSSAGEPLTPEVIRWFDAALGV---PIHDHYGQTELGMVLANHHALEHPVHAGSAGRAMPGWRVAVLDDDG----- 277
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 482 eaegylvfKQPWPGIMRTI-----------YGNHTRFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLL 550
Cdd:cd05973 278 --------DELGPGEPGRLaidiansplmwFRGYQLPDTPAIDG--GYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRI 347
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 551 STAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSSTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRS 630
Cdd:cd05973 348 GPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPS 427
|
570
....*....|
gi 1538017002 631 GKIMRRVLRK 640
Cdd:cd05973 428 GKIQRFLLRR 437
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
39-662 |
2.62e-67 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 232.76 E-value: 2.62e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 39 TEWMKGATTNICYNVLdRNvhekKLGDKVAFYWEGnEPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILE 118
Cdd:PRK03584 78 ARWFPGARLNYAENLL-RH----RRDDRPAIIFRG-EDGPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 119 LVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITTDAFYRGEKLVN----LKELADE--SLEKcrekgfpvrc 192
Cdd:PRK03584 152 TVVAMLATASLGAIWSSCSPDFGVQGVLDRFGQIEPKVLIAVDGYRYGGKAFDrrakVAELRAAlpSLEH---------- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 193 CIVVKHVGraelgmndspsqSPPVKRQCPDVQIswnegvdlwWHELMQEAGD-EFEPEWCDAEDPLFILYTSGSTGKPKl 271
Cdd:PRK03584 222 VVVVPYLG------------PAAAAAALPGALL---------WEDFLAPAEAaELEFEPVPFDHPLWILYSSGTTGLPK- 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 272 cagsicwsvemdtkpqpedpfspqGVVHTIGGYMLYVATTFKYVFDFHPED-VFWCTAdIGWITGHSYVtyGPLANGATS 350
Cdd:PRK03584 280 ------------------------CIVHGHGGILLEHLKELGLHCDLGPGDrFFWYTT-CGWMMWNWLV--SGLLVGATL 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 351 VLFEGIPTYPDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGSqhc 430
Cdd:PRK03584 333 VLYDGSPFYPDPNVLWDLAAEEGVTVFGTSAKYLDACEKAGLVPGETHDLSALRTIGSTGSPLPPEGFDWVYEHVKA--- 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 431 pivDTFWQTETGG-HMLTPLPGATPMKP---GSASFPFFGVAPAILNESGEELEGEAEGyLVFKQPWPGiMRTIYGNH-- 504
Cdd:PRK03584 410 ---DVWLASISGGtDICSCFVGGNPLLPvyrGEIQCRGLGMAVEAWDEDGRPVVGEVGE-LVCTKPFPS-MPLGFWNDpd 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 505 -TRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLY 583
Cdd:PRK03584 485 gSRYRDAYFDTFPGVWRHGDWIEITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMP 564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 584 CFVTLCDGHTFSSTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIM----RRVLR----KIAQNdhdlgdTSTVA 655
Cdd:PRK03584 565 LFVVLAEGVTLDDALRARIRTTIRTNLSPRHVPDKIIAVPDIPRTLSGKKVelpvKKLLHgrpvKKAVN------RDALA 638
|
....*..
gi 1538017002 656 DPSVINH 662
Cdd:PRK03584 639 NPEALDW 645
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
77-639 |
4.66e-63 |
|
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: 215.76 E-value: 4.66e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 77 GETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSL 156
Cdd:cd05971 2 GTPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 157 LITtdafyrgeklvnlkelaDESlekcrekgfpvrccivvkhvgraelgmndspsqsppvkrqcpdvqiswnegvdlwwh 236
Cdd:cd05971 82 LVT-----------------DGS--------------------------------------------------------- 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 237 elmqeagdefepewcdaEDPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGVVHT-------IGGYMLYva 309
Cdd:cd05971 88 -----------------DDPALIIYTSGTTGPPK-------------------------GALHAhrvllghLPGVQFP-- 123
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 310 ttfkyvFDFHP--EDVFWCTADIGWItghsyvtyGPLANGATSVLFEGIP------TYPDESRLWSIVDKYKVTKFYTAP 381
Cdd:cd05971 124 ------FNLFPrdGDLYWTPADWAWI--------GGLLDVLLPSLYFGVPvlahrmTKFDPKAALDLMSRYGVTTAFLPP 189
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 382 TAIRMlMKFGDEPVtKHSRASLQVLGTVGEPINPEAWLWYHRVVGSqhcPIVDTFWQTEtGGHMLTPLPGATPMKPGSAS 461
Cdd:cd05971 190 TALKM-MRQQGEQL-KHAQVKLRAIATGGESLGEELLGWAREQFGV---EVNEFYGQTE-CNLVIGNCSALFPIKPGSMG 263
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 462 FPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTIYGNHTRFEttyfKKFPG-YYVTGDGCRRDQDGYYWITGRID 540
Cdd:cd05971 264 KPIPGHRVAIVDDNGTPLPPGEVGEIAVELPDPVAFLGYWNNPSATE----KKMAGdWLLTGDLGRKDSDGYFWYVGRDD 339
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 541 DMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSSTLTEELKKQIREKIGPIATPDYIQ 620
Cdd:cd05971 340 DVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDALAREIQELVKTRLAAHEYPREIE 419
|
570
....*....|....*....
gi 1538017002 621 NAPGLPKTRSGKIMRRVLR 639
Cdd:cd05971 420 FVNELPRTATGKIRRRELR 438
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
48-640 |
1.61e-60 |
|
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: 211.56 E-value: 1.61e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 48 NICYNVLDRNVHEKKLGDKV---AFYWEgNEPGETTKITYRELLVQVCQFSNVLRKQ-GIQKGDRVAIYMPMILELVVAM 123
Cdd:cd05928 6 NFASDVLDQWADKEKAGKRPpnpALWWV-NGKGDEVKWSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 124 LACARLGAlhsivfagfsaeslcerILDSSCSLLITTDAFYRgeklvnlkeladesLEKCREKgfpvrcCIVVKHVGRAE 203
Cdd:cd05928 85 VACIRTGL-----------------VFIPGTIQLTAKDILYR--------------LQASKAK------CIVTSDELAPE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 204 LgmnDSpsqsppVKRQCPDVQI-------SWNEGVDLwwHELMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPKLCAgsi 276
Cdd:cd05928 128 V---DS------VASECPSLKTkllvsekSRDGWLNF--KELLNEASTEHHCVETGSQEPMAIYFTSGTTGSPKMAE--- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 277 cwsvemdtkpqpedpfspqgvvHTIGGYMLYVATTFKYVFDFHPEDVFWCTADIGWITGHSYVTYGPLANGATsVLFEGI 356
Cdd:cd05928 194 ----------------------HSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWIQGAC-VFVHHL 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 357 PTYpDESRLWSIVDKYKVTKFYTAPTAIRMLMKfgdEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGSQhcpIVDTF 436
Cdd:cd05928 251 PRF-DPLVILKTLSSYPITTFCGAPTVYRMLVQ---QDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLD---IYEGY 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 437 WQTETGghMLTPLPGATPMKPGS--ASFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTIY-GNHTRFETTYFK 513
Cdd:cd05928 324 GQTETG--LICANFKGMKIKPGSmgKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKPIRPFGLFSGYvDNPEKTAATIRG 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 514 KFpgyYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDghT 593
Cdd:cd05928 402 DF---YLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAP--Q 476
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1538017002 594 FSS----TLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 640
Cdd:cd05928 477 FLShdpeQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| ac_ac_CoA_syn |
TIGR01217 |
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of ... |
41-643 |
3.16e-58 |
|
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: 207.81 E-value: 3.16e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 41 WMKGATTNICYNVLdrnvhEKKLGDKVAFYWegNEPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELV 120
Cdd:TIGR01217 81 WFPGARLNYAENLL-----RAAGTEPALLYV--DETHEPAPVTWAELRRQVASLAAALRALGVRPGDRVSGYLPNIPQAV 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 121 VAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITTDAFYRGEKlvnlKELADESLEKCReKGFP-VRCCIVVKHV 199
Cdd:TIGR01217 154 VAMLATASVGAIWSSCSPDFGARGVLDRFQQIEPKLLFTVDGYRYNGK----EHDRRDKVAEVR-KELPtLRAVVHIPYL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 200 GraelgmnDSPSQSPPVkrqcpdvqiswnEGvDLWWHELMQEAGD-EFEPEWCDAEDPLFILYTSGSTGKPKlcagsicw 278
Cdd:TIGR01217 229 G-------PRETEAPKI------------DG-ALDLEDFTAAAQAaELVFEQLPFDHPLWILFSSGTTGLPK-------- 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 279 svemdtkpqpedpfspqGVVHTIGGYMLYVATTFKYVFDFHPEDVFWCTADIGWITGHSYVTygPLANGATSVLFEGIPT 358
Cdd:TIGR01217 281 -----------------CIVHSAGGTLVQHLKEHGLHCDLGPGDRLFYYTTTGWMMWNWLVS--GLATGATLVLYDGSPG 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 359 YPDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGSqhcpivDTFWQ 438
Cdd:TIGR01217 342 FPATNVLWDIAERTGATLFGTSAKYVMACRKAGVHPARTHDLSALQCVASTGSPLPPDGFRWVYDEIKA------DVWLA 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 439 TETGG-HMLTPLPGATPMKP---GSASFPFFGVAPAILNESGEELEGEAEGyLVFKQPWPGiMRTIYGNH---TRFETTY 511
Cdd:TIGR01217 416 SISGGtDICSCFAGANPTLPvhiGEIQAPGLGTAVQSWDPEGKPVTGEVGE-LVCTNPMPS-MPIRFWNDpdgSKYRDAY 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 512 FKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDG 591
Cdd:TIGR01217 494 FDTYPGVWRHGDWITLTPRGGIVIHGRSDSTLNPQGVRMGSAEIYNAVERLDEVRESLCIGQEQPDGGYRVVLFVHLAPG 573
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1538017002 592 HTFSSTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQ 643
Cdd:TIGR01217 574 ATLDDALLDRIKRTIRAGLSPRHVPDEIIEVPGIPHTLTGKRVEVAVKRVLQ 625
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
51-639 |
6.87e-58 |
|
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: 203.75 E-value: 6.87e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 51 YN---VLDRNVhEKKLGDKVAFYwegnepGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACA 127
Cdd:cd05959 3 YNaatLVDLNL-NEGRGDKTAFI------DDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 128 RLGALHSIVFAGFSAESLCERILDSSCSLLITTDAFYrgeklvnlkELADESLEKCREKgfpVRCCIVVkhvgraelgmN 207
Cdd:cd05959 76 RAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGELA---------PVLAAALTKSEHT---LVVLIVS----------G 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 208 DSPSQSPpvkrqcpdvqiswnegvDLWWHELMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPKlcagsicwsvemdtkpq 287
Cdd:cd05959 134 GAGPEAG-----------------ALLLAELVAAEAEQLKPAATHADDPAFWLYSSGSTGRPK----------------- 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 288 pedpfspqGVVHTIGGyMLYVATTF-KYVFDFHPEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTyPDesRLW 366
Cdd:cd05959 180 --------GVVHLHAD-IYWTAELYaRNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERPT-PA--AVF 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 367 SIVDKYKVTKFYTAPTAIRMLMKfgDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGsqhCPIVDTFWQTETGGHML 446
Cdd:cd05959 248 KRIRRYRPTVFFGVPTLYAAMLA--APNLPSRDLSSLRLCVSAGEALPAEVGERWKARFG---LDILDGIGSTEMLHIFL 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 447 TPLPGAtpMKPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMrtiYGNhtRFETTYfKKFPGYYV-TGDGC 525
Cdd:cd05959 323 SNRPGR--VRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATM---YWN--NRDKTR-DTFQGEWTrTGDKY 394
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 526 RRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSSTLTEELKKQ 605
Cdd:cd05959 395 VRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEALEEELKEF 474
|
570 580 590
....*....|....*....|....*....|....
gi 1538017002 606 IREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 639
Cdd:cd05959 475 VKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
48-645 |
7.70e-57 |
|
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: 201.57 E-value: 7.70e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 48 NICYNVLDRNVHEKKlgDKVAFYWeGNEPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACA 127
Cdd:cd05970 17 NFAYDVVDAMAKEYP--DKLALVW-CDDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 128 RLGAlhsivfagfsaeslcerILDSSCSLLITTDAFYRGEKlvnlkelADESLEKCREKGfpvrccIVVKHV--GRAELG 205
Cdd:cd05970 94 KLGA-----------------IAIPATHQLTAKDIVYRIES-------ADIKMIVAIAED------NIPEEIekAAPECP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 206 mndspsqSPPVKRQC-PDVQISWNEgvdlwWHELMQEAGDEFE-PEWCDA---EDPLFILYTSGSTGKPKLcagsicwsV 280
Cdd:cd05970 144 -------SKPKLVWVgDPVPEGWID-----FRKLIKNASPDFErPTANSYpcgEDILLVYFSSGTTGMPKM--------V 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 281 EMDtkpqpedpfspqgvvHTiggYMLYVATTFKYVFDFHPEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYP 360
Cdd:cd05970 204 EHD---------------FT---YPLGHIVTAKYWQNVREGGLHLTVADTGWGKAVWGKIYGQWIAGAAVFVYDYDKFDP 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 361 DesRLWSIVDKYKVTKFYTAPTAIRMLMKfgdEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGSQhcpIVDTFWQTE 440
Cdd:cd05970 266 K--ALLEKLSKYGVTTFCAPPTIYRFLIR---EDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIK---LMEGFGQTE 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 441 TGGHMLTpLPGATPmKPGSASFPFFGVAPAILNESGEELEGEAEGYLVF----KQPWpGIMRTIYGNHTRFETTYFKkfp 516
Cdd:cd05970 338 TTLTIAT-FPWMEP-KPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIrtskGKPV-GLFGGYYKDAEKTAEVWHD--- 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 517 GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSS 596
Cdd:cd05970 412 GYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSE 491
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1538017002 597 TLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKImRRVlrKIAQND 645
Cdd:cd05970 492 ELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKI-RRV--EIRERD 537
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
51-639 |
2.37e-53 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 191.55 E-value: 2.37e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 51 YNVLDRNVheKKLGDKVAFYWEGnepgetTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLG 130
Cdd:PRK06187 9 GRILRHGA--RKHPDKEAVYFDG------RRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 131 A-LHSI-VFagFSAESLcERIL-DSSCSLLITTDAFyrgEKLV-NLKELADEslekcrekgfpvrccivVKHVgraeLGM 206
Cdd:PRK06187 81 AvLHPInIR--LKPEEI-AYILnDAEDRVVLVDSEF---VPLLaAILPQLPT-----------------VRTV----IVE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 207 NDSPSQSPPVKRQCpdvqiswnegvdlwWHELMQEAGDEFEpeWCDAE--DPLFILYTSGSTGKPKlcagsicwsvemdt 284
Cdd:PRK06187 134 GDGPAAPLAPEVGE--------------YEELLAAASDTFD--FPDIDenDAAAMLYTSGTTGHPK-------------- 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 285 kpqpedpfspqGVVHT---IGGYMLYVATtfkyVFDFHPEDVF-----------WctadiGWitghsyvTYGPLANGATS 350
Cdd:PRK06187 184 -----------GVVLShrnLFLHSLAVCA----WLKLSRDDVYlvivpmfhvhaW-----GL-------PYLALMAGAKQ 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 351 VlfegiptYPDE---SRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVTKHSRASLQVLGtvGEPINPEAWLWYHRVVGs 427
Cdd:PRK06187 237 V-------IPRRfdpENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYG--GAALPPALLREFKEKFG- 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 428 qhCPIVDTFWQTETGG--HMLTPLPGATPM--KPGSASFPFFGVAPAILNESGEELEGEAEGY--LVFKQPWpgIMRTIY 501
Cdd:PRK06187 307 --IDLVQGYGMTETSPvvSVLPPEDQLPGQwtKRRSAGRPLPGVEARIVDDDGDELPPDGGEVgeIIVRGPW--LMQGYW 382
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 502 GNHTRFETTYFKkfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGEC 581
Cdd:PRK06187 383 NRPEATAETIDG---GWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGER 459
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1538017002 582 LYCFVTLCDGHTFSStltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 639
Cdd:PRK06187 460 PVAVVVLKPGATLDA---KELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLR 514
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
64-635 |
2.38e-51 |
|
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: 183.97 E-value: 2.38e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 64 GDKVAFYWEGNEpgettkITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAE 143
Cdd:cd17631 9 PDRTALVFGGRS------LTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 144 SLCERILDSSCSLLIttdafyrgeklvnlkeladeslekcrekgfpvrccivvkhvgraelgmndspsqsppvkrqcpdv 223
Cdd:cd17631 83 EVAYILADSGAKVLF----------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 224 qiswnegvdlwwhelmqeagdefepewcdaEDPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGVVHTIGG 303
Cdd:cd17631 98 ------------------------------DDLALLMYTSGTTGRPK-------------------------GAMLTHRN 122
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 304 yMLYVATTFKYVFDFHPEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGiptyPDESRLWSIVDKYKVTKFYTAPTA 383
Cdd:cd17631 123 -LLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRK----FDPETVLDLIERHRVTSFFLVPTM 197
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 384 IRMLMKFGDEPVTKHSraSLQVLGTVGEPInPEAWLwyhRVVGSQHCPIVDTFWQTETGGHMLTPLPGATPMKPGSASFP 463
Cdd:cd17631 198 IQALLQHPRFATTDLS--SLRAVIYGGAPM-PERLL---RALQARGVKFVQGYGMTETSPGVTFLSPEDHRRKLGSAGRP 271
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 464 FFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRtiyGNHTRFETT--YFKKfpGYYVTGDGCRRDQDGYYWITGRIDD 541
Cdd:cd17631 272 VFFVEVRIVDPDGREVPPGEVGEIVVRGP--HVMA---GYWNRPEATaaAFRD--GWFHTGDLGRLDEDGYLYIVDRKKD 344
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 542 MLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfsSTLTE-ELKKQIREKIGPIATPDYIQ 620
Cdd:cd17631 345 MIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPG----AELDEdELIAHCRERLARYKIPKSVE 420
|
570
....*....|....*
gi 1538017002 621 NAPGLPKTRSGKIMR 635
Cdd:cd17631 421 FVDALPRNATGKILK 435
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
82-639 |
7.89e-51 |
|
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: 182.66 E-value: 7.89e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 82 ITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITtd 161
Cdd:cd05919 11 VTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVT-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 162 afyrgeklvnlkeladeslekcrekgfpvrccivvkhvgraelgmndspsqsppvkrqcpdvqiswnegvdlwwhelmqe 241
Cdd:cd05919 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 242 agdefepewcDAEDPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGVVHTIGGYMLYVATTFKYVFDFHPE 321
Cdd:cd05919 89 ----------SADDIAYLLYSSGTTGPPK-------------------------GVMHAHRDPLLFADAMAREALGLTPG 133
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 322 DVFWCTADI--GWITGHSyvTYGPLANGATSVLFegiPTYPDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPvtKHS 399
Cdd:cd05919 134 DRVFSSAKMffGYGLGNS--LWFPLAVGASAVLN---PGWPTAERVLATLARFRPTVLYGVPTFYANLLDSCAGS--PDA 206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 400 RASLQVLGTVGEPInPEAwLWYhRVVGSQHCPIVDTFWQTETGGHMLTPLPGAtpMKPGSASFPFFGVAPAILNESGEEL 479
Cdd:cd05919 207 LRSLRLCVSAGEAL-PRG-LGE-RWMEHFGGPILDGIGATEVGHIFLSNRPGA--WRLGSTGRPVPGYEIRLVDEEGHTI 281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 480 EGEAEGYLVFKQPWPGIMrtiYGNhtRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESAL 559
Cdd:cd05919 282 PPGEEGDLLVRGPSAAVG---YWN--NPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLI 356
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 560 VEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSSTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 639
Cdd:cd05919 357 IQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
51-639 |
8.81e-51 |
|
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: 183.15 E-value: 8.81e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 51 YNVLDRNVheKKLGDKVAFYWEGnepgetTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLG 130
Cdd:cd05936 2 ADLLEEAA--RRFPDKTALIFMG------RKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 131 AlhsIVFagfsaeslcerildsscsllittdafyrgekLVNLKELADEslekcrekgfpvrccivVKHVgraelgMNDSP 210
Cdd:cd05936 74 A---VVV-------------------------------PLNPLYTPRE-----------------LEHI------LNDSG 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 211 SQsppvkrqcpdVQIswnegVDLWWHELMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPKlcagsicwsvemdtkpqped 290
Cdd:cd05936 97 AK----------ALI-----VAVSFTDLLAAGAPLGERVALTPEDVAVLQYTSGTTGVPK-------------------- 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 291 pfspqGVVHTIGGYMLYVATTFKYVFDFH-PEDVFWCTADIgwitghsYVTYG-------PLANGATSVLfegIPTYPDE 362
Cdd:cd05936 142 -----GAMLTHRNLVANALQIKAWLEDLLeGDDVVLAALPL-------FHVFGltvalllPLALGATIVL---IPRFRPI 206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 363 SRLWSIvDKYKVTKFYTAPTAIRMLMKFGDepVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGsqhCPIVDTFWQTETG 442
Cdd:cd05936 207 GVLKEI-RKHRVTIFPGVPTMYIALLNAPE--FKKRDFSSLRLCISGGAPLPVEVAERFEELTG---VPIVEGYGLTETS 280
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 443 --GHmLTPLPGatPMKPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRtiyGNHTRFETT--YFKKfpGY 518
Cdd:cd05936 281 pvVA-VNPLDG--PRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGP--QVMK---GYWNRPEETaeAFVD--GW 350
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 519 YVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSstl 598
Cdd:cd05936 351 LRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLT--- 427
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1538017002 599 TEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 639
Cdd:cd05936 428 EEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
76-640 |
1.11e-48 |
|
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: 177.89 E-value: 1.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 76 PGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLcERILDSSCS 155
Cdd:cd05926 9 PGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEF-EFYLADLGS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 156 LLITTDAFYRGEKLVNLKELADESLEKCREKGFPVRCCIVVKHVGRAELGMNDSPSQSPpvkrqcpdvqiswnegvdlww 235
Cdd:cd05926 88 KLVLTPKGELGPASRAASKLGLAILELALDVGVLIRAPSAESLSNLLADKKNAKSEGVP--------------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 236 helmqeagdefepewcDAEDPLFILYTSGSTGKPK---LCAGSICWSvemdtkpqpedpfspqgvvhtiggyMLYVATTF 312
Cdd:cd05926 147 ----------------LPDDLALILHTSGTTGRPKgvpLTHRNLAAS-------------------------ATNITNTY 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 313 KYVFD---------FHpedvfwctadigwITGHSYVTYGPLANGATSVlfegIPTYPDESRLWSIVDKYKVTkFYTA-PT 382
Cdd:cd05926 186 KLTPDdrtlvvmplFH-------------VHGLVASLLSTLAAGGSVV----LPPRFSASTFWPDVRDYNAT-WYTAvPT 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 383 AIRMLMKFgDEPVTKHSRASLQVLGTVGEPINPEAwlwYHRVVGSQHCPIVDTFWQTETGGHM-LTPLPgATPMKPGSAS 461
Cdd:cd05926 248 IHQILLNR-PEPNPESPPPKLRFIRSCSASLPPAV---LEALEATFGAPVLEAYGMTEAAHQMtSNPLP-PGPRKPGSVG 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 462 FPFfGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRTIYGNHT-RFEttYFKKFpGYYVTGDGCRRDQDGYYWITGRID 540
Cdd:cd05926 323 KPV-GVEVRILDEDGEILPPGVVGEICLRGP--NVTRGYLNNPEaNAE--AAFKD-GWFRTGDLGYLDADGYLFLTGRIK 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 541 DMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSStltEELKKQIREKIGPIATPDYIQ 620
Cdd:cd05926 397 ELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTE---EELRAFCRKHLAAFKVPKKVY 473
|
570 580
....*....|....*....|
gi 1538017002 621 NAPGLPKTRSGKIMRRVLRK 640
Cdd:cd05926 474 FVDELPKTATGKIQRRKVAE 493
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
82-642 |
8.08e-45 |
|
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: 165.82 E-value: 8.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 82 ITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERIldsscsllittd 161
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRV------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 162 afyrgeklvnlkeladeslekcrEKGFPVRCCIVvkhvgraelgmndspsqsppvkrqcpdvqiswnegvdlwwhelmqe 241
Cdd:cd05974 69 -----------------------DRGGAVYAAVD---------------------------------------------- 79
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 242 agdefepEWCDAEDPLFILYTSGSTGKPKLcagsicwsvemdtkpqpedpfspqgVVHTIGGYMLYVATTFkYVFDFHPE 321
Cdd:cd05974 80 -------ENTHADDPMLLYFTSGTTSKPKL-------------------------VEHTHRSYPVGHLSTM-YWIGLKPG 126
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 322 DVFWCTADIGWiTGHSYVT-YGPLANGATSVLFegipTYP--DESRLWSIVDKYKVTKFYTAPTAIRMLMKfgdEPVTKH 398
Cdd:cd05974 127 DVHWNISSPGW-AKHAWSCfFAPWNAGATVFLF----NYArfDAKRVLAALVRYGVTTLCAPPTVWRMLIQ---QDLASF 198
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 399 SRASLQVLGTvGEPINPEAwlwYHRVVGSQHCPIVDTFWQTETgghmlTPLPGATP---MKPGSASFPFFGVAPAILNES 475
Cdd:cd05974 199 DVKLREVVGA-GEPLNPEV---IEQVRRAWGLTIRDGYGQTET-----TALVGNSPgqpVKAGSMGRPLPGYRVALLDPD 269
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 476 GEELEGEAEGyLVFKQPWP-GIMRTIYGNHTRfetTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAE 554
Cdd:cd05974 270 GAPATEGEVA-LDLGDTRPvGLMKGYAGDPDK---TAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFE 345
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 555 VESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSSTLTEELKKQIREKIGPIATPDYIQNAPgLPKTRSGKIM 634
Cdd:cd05974 346 LESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPETALEIFRFSRERLAPYKRIRRLEFAE-LPKTISGKIR 424
|
....*...
gi 1538017002 635 RRVLRKIA 642
Cdd:cd05974 425 RVELRRRE 432
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
253-639 |
3.09e-44 |
|
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: 164.57 E-value: 3.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 253 AEDPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGVVHTIGGYMLYVATTFKYVFDFHPEDVFWCTADIGW 332
Cdd:cd05958 96 SDDICILAFTSGTTGAPK-------------------------ATMHFHRDPLASADRYAVNVLRLREDDRFVGSPPLAF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 333 ITGHSYVTYGPLANGATSVLFEGipTYPDEsrLWSIVDKYKVTKFYTAPTAIRMLMKFGDEpvTKHSRASLQVLGTVGEP 412
Cdd:cd05958 151 TFGLGGVLLFPFGVGASGVLLEE--ATPDL--LLSAIARYKPTVLFTAPTAYRAMLAHPDA--AGPDLSSLRKCVSAGEA 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 413 INPEAWLWYHRVVGSqhcPIVDTFWQTETGGHMLTPLPGAtpMKPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQP 492
Cdd:cd05958 225 LPAALHRAWKEATGI---PIIDGIGSTEMFHIFISARPGD--ARPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGP 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 493 wpgimrTIY-GNHTRFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVV 571
Cdd:cd05958 300 ------TGCrYLADKRQRTYVQG--GWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVV 371
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1538017002 572 GHPHPVKGECLYCFVTLCDGHTFSSTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 639
Cdd:cd05958 372 GHPDESRGVVVKAFVVLRPGVIPGPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
48-640 |
2.05e-43 |
|
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: 163.47 E-value: 2.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 48 NICYNVLDRNVHEKKlGDKVAFYwegnepGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACA 127
Cdd:TIGR02262 4 NAAEDLLDRNVVEGR-GGKTAFI------DDISSLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 128 RLGALHSIVFAGFSAESLCERILDSSCSLLITTDAFYrgeklvnlkELADESLEKcrekgFPVRCCIVVkhVGRAELGmn 207
Cdd:TIGR02262 77 RAGIVPVALNTLLTADDYAYMLEDSRARVVFVSGALL---------PVIKAALGK-----SPHLEHRVV--VGRPEAG-- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 208 dspsqsppvkrqcpDVQISwnegvdlwwhELMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPKlcagsicwsvemdtkpq 287
Cdd:TIGR02262 139 --------------EVQLA----------ELLATESEQFKPAATQADDPAFWLYSSGSTGMPK----------------- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 288 pedpfspqGVVHTIGGYMLYVATTFKYVFDFHPEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTyPDesRLWS 367
Cdd:TIGR02262 178 --------GVVHTHSNPYWTAELYARNTLGIREDDVCFSAAKLFFAYGLGNALTFPMSVGATTVLMGERPT-PD--AVFD 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 368 IVDKYKVTKFYTAPTAIRMLMkfGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGSQhcpIVDTFWQTETGGHMLT 447
Cdd:TIGR02262 247 RLRRHQPTIFYGVPTLYAAML--ADPNLPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVD---IVDGIGSTEMLHIFLS 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 448 PLPGAtpMKPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMrtIYGNHTRFETTYFKkfpGYYVTGDGCRR 527
Cdd:TIGR02262 322 NLPGD--VRYGTSGKPVPGYRLRLVGDGGQDVADGEPGELLISGPSSATM--YWNNRAKSRDTFQG---EWTRSGDKYVR 394
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 528 DQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHP---VKGEclyCFVTLCDGHTfssTLTEELKK 604
Cdd:TIGR02262 395 NDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEdglIKPK---AFVVLRPGQT---ALETELKE 468
|
570 580 590
....*....|....*....|....*....|....*.
gi 1538017002 605 QIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 640
Cdd:TIGR02262 469 HVKDRLAPYKYPRWIVFVDDLPKTATGKIQRFKLRE 504
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
65-640 |
3.60e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 163.18 E-value: 3.60e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 65 DKVAFYWEGnepgetTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAES 144
Cdd:PRK08316 26 DKTALVFGD------RSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 145 LCeRILDSSCSLLITTDAfyrgeklvNLKELADESLEKCREKGFPVRCcivvkhvgraelgmndSPSQSPPvkrqcPDVQ 224
Cdd:PRK08316 100 LA-YILDHSGARAFLVDP--------ALAPTAEAALALLPVDTLILSL----------------VLGGREA-----PGGW 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 225 ISWNEgvdlwwhelMQEAGDEFEPE-WCDAEDPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGVVHT--- 300
Cdd:PRK08316 150 LDFAD---------WAEAGSVAEPDvELADDDLAQILYTSGTESLPK-------------------------GAMLThra 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 301 -IGGYMLYVATTfkyvfDFHPEDVFWCTADIGwitgHS---YVTYGP-LANGATSVLFEGiptyPDESRLWSIVDKYKVT 375
Cdd:PRK08316 196 lIAEYVSCIVAG-----DMSADDIPLHALPLY----HCaqlDVFLGPyLYVGATNVILDA----PDPELILRTIEAERIT 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 376 KFYTAPTA-IRMLmkfgdepvtKH---SRASLQVL--GTVGEPINPEAWLWYHRvvgsQHCPIVdTFW----QTETGghm 445
Cdd:PRK08316 263 SFFAPPTVwISLL---------RHpdfDTRDLSSLrkGYYGASIMPVEVLKELR----ERLPGL-RFYncygQTEIA--- 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 446 ltplPGATPM-------KPGSASFPFFGVAPAILNESGEELEgeaegylvfkqpwPGIMRTIYGNHTRFETTYFKKfP-- 516
Cdd:PRK08316 326 ----PLATVLgpeehlrRPGSAGRPVLNVETRVVDDDGNDVA-------------PGEVGEIVHRSPQLMLGYWDD-Pek 387
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 517 -------GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLC 589
Cdd:PRK08316 388 taeafrgGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPK 467
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1538017002 590 DGHTFSStltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 640
Cdd:PRK08316 468 AGATVTE---DELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRE 515
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
80-639 |
4.60e-43 |
|
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: 160.53 E-value: 4.60e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 80 TKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALhsivfagfsaeslcerildsscslLIT 159
Cdd:cd05934 2 RRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAV------------------------LVP 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 160 TDAFYRGEKLvnlKELADESlekcrekgfpvRCCIVVKhvgraelgmndspsqsppvkrqcpdvqiswnegvdlwwhelm 239
Cdd:cd05934 58 INTALRGDEL---AYIIDHS-----------GAQLVVV------------------------------------------ 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 240 qeagdefepewcdaeDPLFILYTSGSTGKPKLCagsiCWSvemdtkpqpedpfspqgvvHTiggYMLYVATTFKYVFDFH 319
Cdd:cd05934 82 ---------------DPASILYTSGTTGPPKGV----VIT-------------------HA---NLTFAGYYSARRFGLG 120
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 320 PEDVFWCTADIGWITGHSYVTYGPLANGATSVLfegIPTYpDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVTKHS 399
Cdd:cd05934 121 EDDVYLTVLPLFHINAQAVSVLAALSVGATLVL---LPRF-SASRFWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDRAH 196
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 400 RASLqvlgTVGEPINPEAWLWYHRVVGsqhCPIVDTFWQTETGGHMLTPLPGATPmkPGSASFPFFGVAPAILNESGEEL 479
Cdd:cd05934 197 RLRA----AYGAPNPPELHEEFEERFG---VRLLEGYGMTETIVGVIGPRDEPRR--PGSIGRPAPGYEVRIVDDDGQEL 267
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 480 EGEAEGYLVFK-QPWPGIMRTIYGNhtrfETTYFKKFP-GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVES 557
Cdd:cd05934 268 PAGEPGELVIRgLRGWGFFKGYYNM----PEATAEAMRnGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVER 343
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 558 ALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSStltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRV 637
Cdd:cd05934 344 AILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDP---EELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQ 420
|
..
gi 1538017002 638 LR 639
Cdd:cd05934 421 LR 422
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
78-634 |
7.14e-42 |
|
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: 158.92 E-value: 7.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 78 ETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLL 157
Cdd:cd05911 7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 158 ITTDAFYrgEKLvnlkeladesLEKCREKGFPVRccIVVkhvgraelgMNDSPSQSPPVKrqcpdvqiswnegvDLWWHE 237
Cdd:cd05911 87 FTDPDGL--EKV----------KEAAKELGPKDK--IIV---------LDDKPDGVLSIE--------------DLLSPT 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 238 LMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPKLCAGS---ICWSVEMdtkpqpedpfspqgvvhtiggymlyVATTFKY 314
Cdd:cd05911 130 LGEEDEDLPPPLKDGKDDTAAILYSSGTTGLPKGVCLShrnLIANLSQ-------------------------VQTFLYG 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 315 vfDFHPEDVFWCTADIGWITG-HSYVTYgpLANGATSVLFEGiptyPDESRLWSIVDKYKVTKFYTAPTAIRMLMKfgDE 393
Cdd:cd05911 185 --NDGSNDVILGFLPLYHIYGlFTTLAS--LLNGATVIIMPK----FDSELFLDLIEKYKITFLYLVPPIAAALAK--SP 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 394 PVTKHSRASLQVLGTVGEPINPEAwlwYHRV-VGSQHCPIVDTFWQTETGGhMLTPLPGaTPMKPGSASFPFFGVAPAIL 472
Cdd:cd05911 255 LLDKYDLSSLRVILSGGAPLSKEL---QELLaKRFPNATIKQGYGMTETGG-ILTVNPD-GDDKPGSVGRLLPNVEAKIV 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 473 NESGEELEGEaegylvfKQP---W---PGIMRTIYGNHTRFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVS 546
Cdd:cd05911 330 DDDGKDSLGP-------NEPgeiCvrgPQVMKGYYNNPEATKETFDED--GWLHTGDIGYFDEDGYLYIVDRKKELIKYK 400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 547 GHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfsSTLTE-ELKKQIREKIgpiatPDY------I 619
Cdd:cd05911 401 GFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPG----EKLTEkEVKDYVAKKV-----ASYkqlrggV 471
|
570
....*....|....*
gi 1538017002 620 QNAPGLPKTRSGKIM 634
Cdd:cd05911 472 VFVDEIPKSASGKIL 486
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
113-639 |
2.34e-38 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 148.81 E-value: 2.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 113 MPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITTDAFYRGEKLVnlkELADESLEKCREKgfpvrc 192
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGGRAL---PLYSKVVEAAPAK------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 193 CIVVKHVGRaelgmndspSQSPPVKRQCPdvqiSWNE--GVDLWWHelmQEAGDEFEPEWCDAEDPLFILYTSGSTGKPK 270
Cdd:PLN03051 72 AIVLPAAGE---------PVAVPLREQDL----SWCDflGVAAAQG---SVGGNEYSPVYAPVESVTNILFSSGTTGEPK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 271 lcagSICWsvemdtkpqpeDPFSPQGVVHTIGGYMlyvattfkyvfDFHPEDVFWCTADIGWITGhSYVTYGPLANGATS 350
Cdd:PLN03051 136 ----AIPW-----------THLSPLRCASDGWAHM-----------DIQPGDVVCWPTNLGWMMG-PWLLYSAFLNGATL 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 351 VLFEGIPTYPDesrLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGSQHc 430
Cdd:PLN03051 189 ALYGGAPLGRG---FGKFVQDAGVTVLGLVPSIVKAWRHTGAFAMEGLDWSKLRVFASTGEASAVDDVLWLSSVRGYYK- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 431 PIVDTFWQTETGGHML--TPLpgaTPMKPGSASFPFFGVAPAILNESGEELEGEAEGY--LVFKQPWPGIM-RTIYGNHt 505
Cdd:PLN03051 265 PVIEYCGGTELASGYIssTLL---QPQAPGAFSTASLGTRFVLLNDNGVPYPDDQPCVgeVALAPPMLGASdRLLNADH- 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 506 rfETTYFKKFPGYYVTGDGCRRDQD-------GYYWITGRIDDMLNVSGHLLSTAEVESALVE-HEAVAEAAVVGHPHPV 577
Cdd:PLN03051 341 --DKVYYKGMPMYGSKGMPLRRHGDimkrtpgGYFCVQGRADDTMNLGGIKTSSVEIERACDRaVAGIAETAAVGVAPPD 418
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1538017002 578 KG-ECLYCFVTLCD-GHTFSSTLTEELKKQ----IREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 639
Cdd:PLN03051 419 GGpELLVIFLVLGEeKKGFDQARPEALQKKfqeaIQTNLNPLFKVSRVKIVPELPRNASNKLLRRVLR 486
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
82-658 |
3.86e-38 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 150.11 E-value: 3.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 82 ITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLAcarlGALHSIVFA---GFSAESLCErildsscsLLI 158
Cdd:PRK07529 59 WTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWG----GEAAGIANPinpLLEPEQIAE--------LLR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 159 TTDAfyrgEKLVNLKELADESL-EKCREKgfpVRCCIVVKHVGRAELGMNDSPSQSPPVKRQCPDVQIswneGVDLWWHE 237
Cdd:PRK07529 127 AAGA----KVLVTLGPFPGTDIwQKVAEV---LAALPELRTVVEVDLARYLPGPKRLAVPLIRRKAHA----RILDFDAE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 238 LMQEAGDE-FEPEWCDAEDPLFILYTSGSTGKPKLcagsicwsvemdtkpqpedpfspqgVVHTIGGyMLYVATTFKYVF 316
Cdd:PRK07529 196 LARQPGDRlFSGRPIGPDDVAAYFHTGGTTGMPKL-------------------------AQHTHGN-EVANAWLGALLL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 317 DFHPEDVFWCTADIGWITGhSYVT-YGPLANGAtSVLFEGIPTYPDES---RLWSIVDKYKVTKFYTAPTAIRMLMkfgD 392
Cdd:PRK07529 250 GLGPGDTVFCGLPLFHVNA-LLVTgLAPLARGA-HVVLATPQGYRGPGviaNFWKIVERYRINFLSGVPTVYAALL---Q 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 393 EPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGsqhCPIVDTFWQTE-TGGHMLTPLPGatPMKPGSASFPFFGVAPAI 471
Cdd:PRK07529 325 VPVDGHDISSLRYALCGAAPLPVEVFRRFEAATG---VRIVEGYGLTEaTCVSSVNPPDG--ERRIGSVGLRLPYQRVRV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 472 LNESGEELEGEAEGY-----LVFKQP--WPGIMRTIYGNHTRFEttyfkkfPGYYVTGDGCRRDQDGYYWITGRIDDMLN 544
Cdd:PRK07529 400 VILDDAGRYLRDCAVdevgvLCIAGPnvFSGYLEAAHNKGLWLE-------DGWLNTGDLGRIDADGYFWLTGRAKDLII 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 545 VSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSST-LTEELKKQIREkigPIATPDYIQNAP 623
Cdd:PRK07529 473 RGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATEAeLLAFARDHIAE---RAAVPKHVRILD 549
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1538017002 624 GLPKTRSGKI---------MRRVLRK-IAQNDHDLGDTSTVADPS 658
Cdd:PRK07529 550 ALPKTAVGKIfkpalrrdaIRRVLRAaLRDAGVEAEVVDVVEDGR 594
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
61-640 |
1.83e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 143.51 E-value: 1.83e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 61 KKLGDKVAfYWEGNEpgettKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGF 140
Cdd:PRK07656 16 RRFGDKEA-YVFGDQ-----RLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 141 SAESLCERILDSSCSLLITTDAFyrgeklVNLKELADESLEkcrekgfpvrcciVVKHVGRAElgmndsPSQSPPVKRQC 220
Cdd:PRK07656 90 TADEAAYILARGDAKALFVLGLF------LGVDYSATTRLP-------------ALEHVVICE------TEEDDPHTEKM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 221 pdvqiswnegvdLWWHELMQEA-GDEFEPEwCDAEDPLFILYTSGSTGKPK--LCAGSICWSVEMD----TKPQPED--- 290
Cdd:PRK07656 145 ------------KTFTDFLAAGdPAERAPE-VDPDDVADILFTSGTTGRPKgaMLTHRQLLSNAADwaeyLGLTEGDryl 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 291 ---PFspqgvvhtiggymlyvattfkyvfdFHpedVFWCTAdiGWITghsyvtygPLANGATSVLfegIPTYpDESRLWS 367
Cdd:PRK07656 212 aanPF-------------------------FH---VFGYKA--GVNA--------PLMRGATILP---LPVF-DPDEVFR 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 368 IVDKYKVTKFYTAPTAIRMLMKFGDEpvTKHSRASLQVLGTVGEPInPEAWLwyHRVVGSQHCPIVDT-FWQTETGGHM- 445
Cdd:PRK07656 250 LIETERITVLPGPPTMYNSLLQHPDR--SAEDLSSLRLAVTGAASM-PVALL--ERFESELGVDIVLTgYGLSEASGVTt 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 446 LTPLPGATPMKPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRTIYGNHTrfETTYFKKFPGYYVTGDGC 525
Cdd:PRK07656 325 FNRLDDDRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGP--NVMKGYYDDPE--ATAAAIDADGWLHTGDLG 400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 526 RRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfsSTLTEE-LKK 604
Cdd:PRK07656 401 RLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPG----AELTEEeLIA 476
|
570 580 590
....*....|....*....|....*....|....*.
gi 1538017002 605 QIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 640
Cdd:PRK07656 477 YCREHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
78-638 |
2.94e-36 |
|
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: 141.90 E-value: 2.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 78 ETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGAlhsiVFAGFSAESLCERIL----DSS 153
Cdd:cd05930 9 GDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGA----AYVPLDPSYPAERLAyileDSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 154 CSLLITtdafyrgeklvnlkeladeslekcrekgfpvrccivvkhvgraelgmndspsqsppvkrqcpdvqiswnegvdl 233
Cdd:cd05930 85 AKLVLT-------------------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 234 wwhelmqeagdefepewcDAEDPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGVVHTIGGYMLYVATtFK 313
Cdd:cd05930 91 ------------------DPDDLAYVIYTSGSTGKPK-------------------------GVMVEHRGLVNLLLW-MQ 126
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 314 YVFDFHPEDVFWCTADIGWItGHSYVTYGPLANGATSVLfegIP--TYPDESRLWSIVDKYKVTKFYTAPTAIRMLMKFG 391
Cdd:cd05930 127 EAYPLTPGDRVLQFTSFSFD-VSVWEIFGALLAGATLVV---LPeeVRKDPEALADLLAEEGITVLHLTPSLLRLLLQEL 202
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 392 DEPVtkhsRASLQVLGTVGEPINPEAW------LWYHRVV---GSQHCPIVDTFWQTETGGHMLTPLP-GAtpmkpgsas 461
Cdd:cd05930 203 ELAA----LPSLRLVLVGGEALPPDLVrrwrelLPGARLVnlyGPTEATVDATYYRVPPDDEEDGRVPiGR--------- 269
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 462 fPFFGVAPAILNESGeelegeaegylvfkQPWP-GIMRTIY--------GNHTRFETTYFK-----KFPG--YYVTGDGC 525
Cdd:cd05930 270 -PIPNTRVYVLDENL--------------RPVPpGVPGELYiggaglarGYLNRPELTAERfvpnpFGPGerMYRTGDLV 334
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 526 RRDQDG--YYwiTGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSstlTEELK 603
Cdd:cd05930 335 RWLPDGnlEF--LGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELD---EEELR 409
|
570 580 590
....*....|....*....|....*....|....*
gi 1538017002 604 KQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 638
Cdd:cd05930 410 AHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
82-643 |
1.70e-35 |
|
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: 141.05 E-value: 1.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 82 ITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHsiVFAGFS-----AESLCERildSSCSL 156
Cdd:COG1021 51 LSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIP--VFALPAhrraeISHFAEQ---SEAVA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 157 LITTDAfYRGeklVNLKELADESLEKCREkgfpVRCCIVVkhvGRAElgmndspsqsppvkrqcpdvqiswnEGVDLwwH 236
Cdd:COG1021 126 YIIPDR-HRG---FDYRALARELQAEVPS----LRHVLVV---GDAG-------------------------EFTSL--D 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 237 ELMQEAGDEFEPEwCDAEDPLFILYTSGSTGKPKLcagsIcwsvemdtkPQPEDPFspqgvvhtiggymLYVATTFKYVF 316
Cdd:COG1021 168 ALLAAPADLSEPR-PDPDDVAFFQLSGGTTGLPKL----I---------PRTHDDY-------------LYSVRASAEIC 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 317 DFHPEDVFWCTADIGwitgHSY-----VTYGPLANGATSVLFEGipTYPDEsrLWSIVDKYKVTkfYTA--PTAIRMLMK 389
Cdd:COG1021 221 GLDADTVYLAALPAA----HNFplsspGVLGVLYAGGTVVLAPD--PSPDT--AFPLIERERVT--VTAlvPPLALLWLD 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 390 FGDEpvTKHSRASLQVLGTVGEPINPEA----------WLW-----------Y-------HRVVGSQHCP--------IV 433
Cdd:COG1021 291 AAER--SRYDLSSLRVLQVGGAKLSPELarrvrpalgcTLQqvfgmaeglvnYtrlddpeEVILTTQGRPispddevrIV 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 434 DtfwqtETGghmlTPLPgatpmkPGSAsfpffGVapailnesgeelegeaegyLVFKQPWpgimrTIYGnhtrfettYFK 513
Cdd:COG1021 369 D-----EDG----NPVP------PGEV-----GE-------------------LLTRGPY-----TIRG--------YYR 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 514 KfP----------GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGE--C 581
Cdd:COG1021 397 A-PehnaraftpdGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGErsC 475
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1538017002 582 LycFVTLcDGHTFSstlTEELKKQIREKiGpIAT---PDYIQNAPGLPKTRSGKIMRRVLRKIAQ 643
Cdd:COG1021 476 A--FVVP-RGEPLT---LAELRRFLRER-G-LAAfklPDRLEFVDALPLTAVGKIDKKALRAALA 532
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
40-640 |
6.47e-35 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 141.37 E-value: 6.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 40 EWMKGATTNICYNVLDRNVHEKklGDKVAFYW--EGNEPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMIL 117
Cdd:PLN03052 167 QWLPGAVLNVAECCLTPKPSKT--DDSIAIIWrdEGSDDLPVNRMTLSELRSQVSRVANALDALGFEKGDAIAIDMPMNV 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 118 ELVVAMLAcarlgalhsIVFAG---------FSAESLCERILDSSCSLLITTDAFYRGEKLVNLKEladeslekcrekgf 188
Cdd:PLN03052 245 HAVIIYLA---------IILAGcvvvsiadsFAPSEIATRLKISKAKAIFTQDVIVRGGKSIPLYS-------------- 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 189 pvRcciVVKhvgraelgmndspSQSP-----PVKRQCPDVQIswNEGvDLWWHELMQEA-----GDEFEPEWCDAEDPLF 258
Cdd:PLN03052 302 --R---VVE-------------AKAPkaivlPADGKSVRVKL--REG-DMSWDDFLARAnglrrPDEYKAVEQPVEAFTN 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 259 ILYTSGSTGKPKlcagSICWsvemdTKPQPedpfspqgvvhtiggyMLYVATTFKYVfDFHPEDVF-WCTaDIGWITGHs 337
Cdd:PLN03052 361 ILFSSGTTGEPK----AIPW-----TQLTP----------------LRAAADAWAHL-DIRKGDIVcWPT-NLGWMMGP- 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 338 YVTYGPLANGATSVLFEGIPTYPDESRLwsiVDKYKVTKFYTAPTAIRMLMKFGdePVTKHSRASLQVLGTVGEPINPEA 417
Cdd:PLN03052 413 WLVYASLLNGATLALYNGSPLGRGFAKF---VQDAKVTMLGTVPSIVKTWKNTN--CMAGLDWSSIRCFGSTGEASSVDD 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 418 WLWYhrVVGSQHCPIVDTFWQTETGGHMLTplpgATPMKP---GSASFPFFGVAPAILNESGeelegeaegylvfkQPWP 494
Cdd:PLN03052 488 YLWL--MSRAGYKPIIEYCGGTELGGGFVT----GSLLQPqafAAFSTPAMGCKLFILDDSG--------------NPYP 547
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 495 ---------GIMRTIYGNHTRF-----ETTYFKKFPGYYVT-----GDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEV 555
Cdd:PLN03052 548 ddapctgelALFPLMFGASSTLlnadhYKVYFKGMPVFNGKilrrhGDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEI 627
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 556 E----SAlveHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSSTLTEELKK----QIREKIGPIATPDYIQNAPGLPK 627
Cdd:PLN03052 628 ErvcnAA---DESVLETAAIGVPPPGGGPEQLVIAAVLKDPPGSNPDLNELKKifnsAIQKKLNPLFKVSAVVIVPSFPR 704
|
650
....*....|...
gi 1538017002 628 TRSGKIMRRVLRK 640
Cdd:PLN03052 705 TASNKVMRRVLRQ 717
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
47-638 |
2.84e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 134.70 E-value: 2.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 47 TNICYNVldrNVHEKKLGDKVAFYWEGNEpgettkITYRELLVQVCQFSNVL-RKQGIQKGDRVAIYMPMILELVVAMLA 125
Cdd:PRK08314 10 TSLFHNL---EVSARRYPDKTAIVFYGRA------ISYRELLEEAERLAGYLqQECGVRKGDRVLLYMQNSPQFVIAYYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 126 CARLGALHSIVFAGFSAESLCERILDSSCSLLITTDAFY-RGEKLVNLKELAdeslekcrekgfpvrcCIVVKHVGRAel 204
Cdd:PRK08314 81 ILRANAVVVPVNPMNREEELAHYVTDSGARVAIVGSELApKVAPAVGNLRLR----------------HVIVAQYSDY-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 205 gMNDSPSQSPPVK-RQCPDVQISWNEGVDLWwhELMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPKLCagsicwsveMD 283
Cdd:PRK08314 143 -LPAEPEIAVPAWlRAEPPLQALAPGGVVAW--KEALAAGLAPPPHTAGPDDLAVLPYTSGTTGVPKGC---------MH 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 284 TKpqpedpfspQGVVHTIGGYMLYvattfkyvFDFHPEDVFWCTADIGWITGHSYVTYGPLANGATSVLfegIPTYpDES 363
Cdd:PRK08314 211 TH---------RTVMANAVGSVLW--------SNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVL---MPRW-DRE 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 364 RLWSIVDKYKVTkFYTAPTAirMLMKFGDEP-VTKHSRASLQVLGTVGEPInPEAwlwyhrvVGS---QHC--PIVDTFW 437
Cdd:PRK08314 270 AAARLIERYRVT-HWTNIPT--MVVDFLASPgLAERDLSSLRYIGGGGAAM-PEA-------VAErlkELTglDYVEGYG 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 438 QTETGGHMLTPLPGATpmKPGSASFPFFGVAPAILNESGEELEGEAEG--YLVFKqpwPGIMRTIYGNHTRFETTyFKKF 515
Cdd:PRK08314 339 LTETMAQTHSNPPDRP--KLQCLGIPTFGVDARVIDPETLEELPPGEVgeIVVHG---PQVFKGYWNRPEATAEA-FIEI 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 516 PG--YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHT 593
Cdd:PRK08314 413 DGkrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEAR 492
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1538017002 594 fSSTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 638
Cdd:PRK08314 493 -GKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQL 536
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
78-638 |
3.03e-31 |
|
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: 127.42 E-value: 3.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 78 ETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLL 157
Cdd:cd17643 9 EDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILADSGPSLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 158 ITtdafyrgeklvnlkeladeslekcrekgfpvrccivvkhvgraelgmndspsqsppvkrqcpdvqiswnegvdlwwhe 237
Cdd:cd17643 89 LT------------------------------------------------------------------------------ 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 238 lmqeagdefepewcDAEDPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGVVHTIGGYM-LYVATTfkYVF 316
Cdd:cd17643 91 --------------DPDDLAYVIYTSGSTGRPK-------------------------GVVVSHANVLaLFAATQ--RWF 129
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 317 DFHPEDVfwctadigWITGHSYV-------TYGPLANGATSVlfegIPTYP---DESRLWSIVDKYKVTKFYTAPTAIRM 386
Cdd:cd17643 130 GFNEDDV--------WTLFHSYAfdfsvweIWGALLHGGRLV----VVPYEvarSPEDFARLLRDEGVTVLNQTPSAFYQ 197
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 387 LMKFGDEPVTKHSRASLQVLGtvGEPINPeAWL--WYHRVvGSQHCPIVDTFWQTETGGHM----LTP--LPGATpMKPG 458
Cdd:cd17643 198 LVEAADRDGRDPLALRYVIFG--GEALEA-AMLrpWAGRF-GLDRPQLVNMYGITETTVHVtfrpLDAadLPAAA-ASPI 272
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 459 SASFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTIYGNHTRFETTYFKKfPG--YYVTGDGCRRDQDGYYWIT 536
Cdd:cd17643 273 GRPLPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGG-PGsrMYRTGDLARRLPDGELEYL 351
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 537 GRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFsstLTEELKKQIREKIgpiatP 616
Cdd:cd17643 352 GRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAA---DIAELRALLKELL-----P 423
|
570 580
....*....|....*....|....*..
gi 1538017002 617 DYIQNA-----PGLPKTRSGKIMRRVL 638
Cdd:cd17643 424 DYMVPAryvplDALPLTVNGKLDRAAL 450
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
65-639 |
3.56e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 122.02 E-value: 3.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 65 DKVAFYWEGnepgetTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLG----ALHSIVfagf 140
Cdd:PRK06188 27 DRPALVLGD------TRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGlrrtALHPLG---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 141 SAESLCERILDSSCSLLITTDAFYRgeklvnlkELADESLEKCREkgfpvrccivVKHVgraeLGMNDSPsqsppvkrqc 220
Cdd:PRK06188 97 SLDDHAYVLEDAGISTLIVDPAPFV--------ERALALLARVPS----------LKHV----LTLGPVP---------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 221 pdvqiswnEGVDLWwhelmqEAGDEFEPE----WCDAEDPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqG 296
Cdd:PRK06188 145 --------DGVDLL------AAAAKFGPAplvaAALPPDIAGLAYTGGTTGKPK-------------------------G 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 297 VVHT---IGGYMLYVATTFKYvfdfhPEDV-FWCTADIGWITGHSYVtygP-LANGATSVLFEGIptypDESRLWSIVDK 371
Cdd:PRK06188 186 VMGThrsIATMAQIQLAEWEW-----PADPrFLMCTPLSHAGGAFFL---PtLLRGGTVIVLAKF----DPAEVLRAIEE 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 372 YKVTKFYTAPTAIRMLMKFGDepVTKHSRASLQVLGTVGEPINP----EAwlwyHRVVGsqhcPI-VDTFWQTETGgHML 446
Cdd:PRK06188 254 QRITATFLVPTMIYALLDHPD--LRTRDLSSLETVYYGASPMSPvrlaEA----IERFG----PIfAQYYGQTEAP-MVI 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 447 TPLP-----GATPMKPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRtiyGNHTRFETT--YFKKfpGYY 519
Cdd:PRK06188 323 TYLRkrdhdPDDPKRLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGP--LVMD---GYWNRPEETaeAFRD--GWL 395
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 520 VTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSstlT 599
Cdd:PRK06188 396 HTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVD---A 472
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1538017002 600 EELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 639
Cdd:PRK06188 473 AELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALR 512
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
554-632 |
5.53e-29 |
|
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: 109.94 E-value: 5.53e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1538017002 554 EVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfSSTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGK 632
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPG---VELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
83-570 |
7.75e-29 |
|
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: 119.29 E-value: 7.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 83 TYRELLVQVCQFSNVLRKQ-GIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLcERIL-DSSCSLLITT 160
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERL-AFILeDAGARLLLTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 161 DAFyrgeklvnlkeladesLEKCREKGFPVRCCivvkhVGRAELGMNDSPSQSPPVKRQCPDvqiswnegvdlwwhelmq 240
Cdd:TIGR01733 80 SAL----------------ASRLAGLVLPVILL-----DPLELAALDDAPAPPPPDAPSGPD------------------ 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 241 eagdefepewcdaeDPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGVVHTIGGyMLYVATTFKYVFDFHP 320
Cdd:TIGR01733 121 --------------DLAYVIYTSGSTGRPK-------------------------GVVVTHRS-LVNLLAWLARRYGLDP 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 321 EDVfwctadigWITGHSYV-------TYGPLANGATSVLFEGIPTYPDESRLWSIVDKYKVTKFYTAPTAIRMLMkfgDE 393
Cdd:TIGR01733 161 DDR--------VLQFASLSfdasveeIFGALLAGATLVVPPEDEERDDAALLAALIAEHPVTVLNLTPSLLALLA---AA 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 394 PVTkhSRASLQVLGTVGEPINPEAWLWYHRVVGSqhCPIVDTFWQTETG---GHMLTPLPGATPMKPGSASFPFFGVAPA 470
Cdd:TIGR01733 230 LPP--ALASLRLVILGGEALTPALVDRWRARGPG--ARLINLYGPTETTvwsTATLVDPDDAPRESPVPIGRPLANTRLY 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 471 ILNESGeelegeaegylvfkQPWP-GIMRTIY--------GNHTRFETT--YFKKFPGY-------YVTGDGCRRDQDGY 532
Cdd:TIGR01733 306 VLDDDL--------------RPVPvGVVGELYiggpgvarGYLNRPELTaeRFVPDPFAggdgarlYRTGDLVRYLPDGN 371
|
490 500 510
....*....|....*....|....*....|....*...
gi 1538017002 533 YWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAV 570
Cdd:TIGR01733 372 LEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
82-638 |
8.60e-29 |
|
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: 120.80 E-value: 8.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 82 ITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITTD 161
Cdd:cd05904 33 LTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 162 AFYrgeklvnlkeladeslEKCREKGFPVRCC-IVVKHVGRAELGMNDSPSQSPPVkrqcpdVQISwnegvdlwwhelmq 240
Cdd:cd05904 113 ELA----------------EKLASLALPVVLLdSAEFDSLSFSDLLFEADEAEPPV------VVIK-------------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 241 eagdefepewcdAEDPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGVVHTIGGYmlyVATTFKYVFDF-- 318
Cdd:cd05904 157 ------------QDDVAALLYSSGTTGRSK-------------------------GVMLTHRNL---IAMVAQFVAGEgs 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 319 --HPEDVFWCTADIGWITGHSYVTYGPLANGATSVLfegIPTYpDESRLWSIVDKYKVTKFYTAPTAIRMLMKfgDEPVT 396
Cdd:cd05904 197 nsDSEDVFLCVLPMFHIYGLSSFALGLLRLGATVVV---MPRF-DLEELLAAIERYKVTHLPVVPPIVLALVK--SPIVD 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 397 KHSRASLQVLGTVGEPINPEAWLWYHRVVGsqHCPIVDTFWQTETGG--HMlTPLPGATPMKPGSASFPFFGVAPAILNE 474
Cdd:cd05904 271 KYDLSSLRQIMSGAAPLGKELIEAFRAKFP--NVDLGQGYGMTESTGvvAM-CFAPEKDRAKYGSVGRLVPNVEAKIVDP 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 475 SGEELegeaegyLVFKQP---W---PGIMRTIYGNHTRFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGH 548
Cdd:cd05904 348 ETGES-------LPPNQTgelWirgPSIMKGYLNNPEATAATIDKE--GWLHTGDLCYIDEDGYLFIVDRLKELIKYKGF 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 549 LLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfsSTLTE-ELKKQIREKIGP------IATPDYIqn 621
Cdd:cd05904 419 QVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPG----SSLTEdEIMDFVAKQVAPykkvrkVAFVDAI-- 492
|
570
....*....|....*..
gi 1538017002 622 apglPKTRSGKIMRRVL 638
Cdd:cd05904 493 ----PKSPSGKILRKEL 505
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
261-642 |
1.03e-28 |
|
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: 117.97 E-value: 1.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 261 YTSGSTGKPKLCAgsicwsvemdtkpqpedpfspqgvvHTIGGyMLYVATTFKYVFDFHPEDVFWCTADIGWITGhSYVT 340
Cdd:cd05944 9 HTGGTTGTPKLAQ-------------------------HTHSN-EVYNAWMLALNSLFDPDDVLLCGLPLFHVNG-SVVT 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 341 YG-PLANGAtSVLFEGIPTYPDES---RLWSIVDKYKVTKFYTAPTAIRMLMKfgdEPVTKhSRASLQVLGTVGEPINPE 416
Cdd:cd05944 62 LLtPLASGA-HVVLAGPAGYRNPGlfdNFWKLVERYRITSLSTVPTVYAALLQ---VPVNA-DISSLRFAMSGAAPLPVE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 417 AwlwYHRVVGSQHCPIVDTFWQTE-TGGHMLTPlPGaTPMKPGSAS--FPFFGVAPAILNESGEELEGEAEGylvfkQPW 493
Cdd:cd05944 137 L---RARFEDATGLPVVEGYGLTEaTCLVAVNP-PD-GPKRPGSVGlrLPYARVRIKVLDGVGRLLRDCAPD-----EVG 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 494 PGIM--RTIYGNHTRFETTYFKKF-PGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAV 570
Cdd:cd05944 207 EICVagPGVFGGYLYTEGNKNAFVaDGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGA 286
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1538017002 571 VGHPHPVKGECLYCFVTLCDGHTFSstlTEELKKQIREKIGP-IATPDYIQNAPGLPKTRSGKIMRRVLRKIA 642
Cdd:cd05944 287 VGQPDAHAGELPVAYVQLKPGAVVE---EEELLAWARDHVPErAAVPKHIEVLEELPVTAVGKVFKPALRADA 356
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
64-640 |
2.04e-28 |
|
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: 119.66 E-value: 2.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 64 GDKVAFYWEGnePGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGA-LHSI---VFAg 139
Cdd:cd12119 10 GDREIVSRTH--EGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAvLHTInprLFP- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 140 fsaeslcERILdsscslLITTDAfyrGEKLVnlkeLADESLEKCREKGFPVrcCIVVKHVGRAELGmNDSPSQSPPvkrq 219
Cdd:cd12119 87 -------EQIA------YIINHA---EDRVV----FVDRDFLPLLEAIAPR--LPTVEHVVVMTDD-AAMPEPAGV---- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 220 cpdvqiswneGVDLWWHELMQEAGDEFEPEWcDAEDPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGVV- 298
Cdd:cd12119 140 ----------GVLAYEELLAAESPEYDWPDF-DENTAAAICYTSGTTGNPK-------------------------GVVy 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 299 -------HTIGGYMlyvattfKYVFDFHPEDVF-----------WCTADIGWITGHSYVTYGPLANGATsvlfegiptyp 360
Cdd:cd12119 184 shrslvlHAMAALL-------TDGLGLSESDVVlpvvpmfhvnaWGLPYAAAMVGAKLVLPGPYLDPAS----------- 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 361 desrLWSIVDKYKVTKFYTAPTAIRMLMKFGDEpvTKHSRASLQVLgtvgepinpeawlwyhrVVGSQHCP--------- 431
Cdd:cd12119 246 ----LAELIEREGVTFAAGVPTVWQGLLDHLEA--NGRDLSSLRRV-----------------VIGGSAVPrslieafee 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 432 -IVDTF--W-QTETG--GHMLTPLPGATP----------MKPGsasFPFFGVAPAILNESGEELEGEAEGY--LVFKQPW 493
Cdd:cd12119 303 rGVRVIhaWgMTETSplGTVARPPSEHSNlsedeqlalrAKQG---RPVPGVELRIVDDDGRELPWDGKAVgeLQVRGPW 379
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 494 pgIMRTIYGNHtrfETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGH 573
Cdd:cd12119 380 --VTKSYYKND---EESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGV 454
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1538017002 574 PHPVKGECLYCFVTLCDGHTFSStltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 640
Cdd:cd12119 455 PHPKWGERPLAVVVLKEGATVTA---EELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
61-640 |
8.44e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 117.83 E-value: 8.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 61 KKLGDKVAFYWegnepGETTkITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALhsIVFAGF 140
Cdd:PRK07470 18 RRFPDRIALVW-----GDRS-WTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAV--WVPTNF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 141 S---------AESlcerildSSCSLLITTDAFyrgeklvnlkelaDESLEKCREKGFPVRCCIVVkhvGRAELGmndsps 211
Cdd:PRK07470 90 RqtpdevaylAEA-------SGARAMICHADF-------------PEHAAAVRAASPDLTHVVAI---GGARAG------ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 212 qsppvkrqcPDVQiswnegvdlwwHELMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedp 291
Cdd:PRK07470 141 ---------LDYE-----------ALVARHLGARVANAAVDHDDPCWFFFTSGTTGRPK--------------------- 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 292 fspqGVVHTiGGYMLYVATTfkyvfdfHPEDVFWCTadigwiTGH--SYVTyGPL------------ANGATSVLFEGIP 357
Cdd:PRK07470 180 ----AAVLT-HGQMAFVITN-------HLADLMPGT------TEQdaSLVV-APLshgagihqlcqvARGAATVLLPSER 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 358 TYPDEsrLWSIVDKYKVTKFYTAPTAIRMLMKfgDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGSQhcpIVDTFW 437
Cdd:PRK07470 241 FDPAE--VWALVERHRVTNLFTVPTILKMLVE--HPAVDRYDHSSLRYVIYAGAPMYRADQKRALAKLGKV---LVQYFG 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 438 QTETGGHMlTPLPGA------TPM-KPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQP--WPGIMRTIYGNHTRFE 508
Cdd:PRK07470 314 LGEVTGNI-TVLPPAlhdaedGPDaRIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPavFAGYYNNPEANAKAFR 392
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 509 TTYFKkfpgyyvTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTL 588
Cdd:PRK07470 393 DGWFR-------TGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVA 465
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1538017002 589 CDGHTFSStltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 640
Cdd:PRK07470 466 RDGAPVDE---AELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVRE 514
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
83-640 |
1.76e-27 |
|
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: 115.94 E-value: 1.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 83 TYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALhsivfagfsaeslcerildsSCSLLittdA 162
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAV--------------------TNPIL----P 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 163 FYRGEKLVNLkeladesLEKCREKGFPVrccivvkhvgraelgmndspsqsPPVKRQcpdvqiswnegvdlwwhelmqea 242
Cdd:cd05903 59 FFREHELAFI-------LRRAKAKVFVV-----------------------PERFRQ----------------------- 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 243 gdeFEPEwCDAEDPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGVVHTiGGYMLYVATTFKYVFDFHPED 322
Cdd:cd05903 86 ---FDPA-AMPDAVALLLFTSGTTGEPK-------------------------GVMHS-HNTLSASIRQYAERLGLGPGD 135
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 323 VFWCTADIGWITGHSYVTYGPLANGATSVLFEGIptypDESRLWSIVDKYKVTKFYTAPTAIRMLMK---FGDEPVtkhs 399
Cdd:cd05903 136 VFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIW----DPDKALALMREHGVTFMMGATPFLTDLLNaveEAGEPL---- 207
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 400 rASLQVLGTVGEPINP----EAWlwyhRVVGSQHCPIvdtFWQTETGGHMLTPLPGATPMKPGSASFPFFGVAPAILNES 475
Cdd:cd05903 208 -SRLRTFVCGGATVPRslarRAA----ELLGAKVCSA---YGSTECPGAVTSITPAPEDRRLYTDGRPLPGVEIKVVDDT 279
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 476 GEELEGEAEGYLVFKQPwpgimRTIYGNHTRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEV 555
Cdd:cd05903 280 GATLAPGVEGELLSRGP-----SVFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEV 354
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 556 ESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFS-STLTEELKKQ--IREKIgpiatPDYIQNAPGLPKTRSGK 632
Cdd:cd05903 355 EDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTfDELVAYLDRQgvAKQYW-----PERLVHVDDLPRTPSGK 429
|
....*...
gi 1538017002 633 IMRRVLRK 640
Cdd:cd05903 430 VQKFRLRE 437
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
77-639 |
3.50e-27 |
|
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: 115.52 E-value: 3.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 77 GETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLcERILDSSCSL 156
Cdd:cd17651 16 AEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERL-AFMLADAGPV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 157 LITTDAFYRGEklvnlkeladeslekcrekgFPVRccivvkhvgraelgmndspsqsppvkrqcpdvqiswnEGVDLWWH 236
Cdd:cd17651 95 LVLTHPALAGE--------------------LAVE-------------------------------------LVAVTLLD 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 237 ELMQEAGDEFEPEW-CDAEDPLFILYTSGSTGKPKlcagsicwSVEMdtkpqpedpfsPQGVV------HTIGGYMLYVA 309
Cdd:cd17651 118 QPGAAAGADAEPDPaLDADDLAYVIYTSGSTGRPK--------GVVM-----------PHRSLanlvawQARASSLGPGA 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 310 TTFKYV---FDFHPEDVFwctadigwitghsyvtyGPLANGATSVLfegIPTY--PDESRLWSIVDKYKVTKFYTAPTAI 384
Cdd:cd17651 179 RTLQFAglgFDVSVQEIF-----------------STLCAGATLVL---PPEEvrTDPPALAAWLDEQRISRVFLPTVAL 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 385 RMLMKFGDEPVTKHsrASLQVLGTVGEPINPE-------AWLWYHRVVgsqhcpivDTFWQTET---GGHMLTPLPGATP 454
Cdd:cd17651 239 RALAEHGRPLGVRL--AALRYLLTGGEQLVLTedlrefcAGLPGLRLH--------NHYGPTEThvvTALSLPGDPAAWP 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 455 MKPgSASFPFFGVAPAILNEsgeelegeaegylvFKQPWP------------GIMRtiyGNHTRFETTYfKKF------P 516
Cdd:cd17651 309 APP-PIGRPIDNTRVYVLDA--------------ALRPVPpgvpgelyiggaGLAR---GYLNRPELTA-ERFvpdpfvP 369
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 517 G--YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTlcdGHTF 594
Cdd:cd17651 370 GarMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVV---GDPE 446
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1538017002 595 SSTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 639
Cdd:cd17651 447 APVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
83-639 |
9.57e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 114.52 E-value: 9.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 83 TYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITTDA 162
Cdd:PRK09088 24 TYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLGDDA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 163 fyrgeklvnlkeLADeslekcrekgfpvrccivvkhvGRAElgmndspsqsppvkrqcpdvqiswneGVDLwwhELMQEA 242
Cdd:PRK09088 104 ------------VAA----------------------GRTD--------------------------VEDL---AAFIAS 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 243 GDEFEP---EWCDAEDPLFILYTSGSTGKPKlcaGSIcwsvemdtkpqpedpFSPQGVVHTiggymlyvATTFKYVFDFH 319
Cdd:PRK09088 121 ADALEPadtPSIPPERVSLILFTSGTSGQPK---GVM---------------LSERNLQQT--------AHNFGVLGRVD 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 320 PEDVFWCTAD----IGWITGHSYVtygpLANGATSVLFEGIPtyPDESRLWSIVDKYKVTKFYTAPtaiRMLMKFGDEPV 395
Cdd:PRK09088 175 AHSSFLCDAPmfhiIGLITSVRPV----LAVGGSILVSNGFE--PKRTLGRLGDPALGITHYFCVP---QMAQAFRAQPG 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 396 TKHSR-ASLQVLGTVGEPiNPE----AWLwyhrvvgSQHCPIVDTFWQTETGGHMLTPL-PGATPMKPGSASFPFFGVAP 469
Cdd:PRK09088 246 FDAAAlRHLTALFTGGAP-HAAedilGWL-------DDGIPMVDGFGMSEAGTVFGMSVdCDVIRAKAGAAGIPTPTVQT 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 470 AILNESGEELEGEAEGYLVFKQP--WPGIMRTIYGNHTRFETTyfkkfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSG 547
Cdd:PRK09088 318 RVVDDQGNDCPAGVPGELLLRGPnlSPGYWRRPQATARAFTGD------GWFRTGDIARRDADGFFWVVDRKKDMFISGG 391
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 548 HLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfSSTLTEELKKQIREKIGPIATPDYIQNAPGLPK 627
Cdd:PRK09088 392 ENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADG---APLDLERIRSHLSTRLAKYKVPKHLRLVDALPR 468
|
570
....*....|..
gi 1538017002 628 TRSGKIMRRVLR 639
Cdd:PRK09088 469 TASGKLQKARLR 480
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
83-638 |
2.47e-26 |
|
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: 112.77 E-value: 2.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 83 TYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLcERIL-DSSCSLLITTD 161
Cdd:cd12116 14 SYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRL-RYILeDAEPALVLTDD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 162 AfyrgeklvnlkeLADeslekcrekgfPVRCCIVVKHVGRAELGMNDSPSQSPPVkrqcPDvqiswnegvdlwwhelmqe 241
Cdd:cd12116 93 A------------LPD-----------RLPAGLPVLLLALAAAAAAPAAPRTPVS----PD------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 242 agdefepewcdaeDPLFILYTSGSTGKPKLCA----GSICWSVEMDTKPQ--PEDpfspqgvvhtiggYMLYVATtfkYV 315
Cdd:cd12116 127 -------------DLAYVIYTSGSTGRPKGVVvshrNLVNFLHSMRERLGlgPGD-------------RLLAVTT---YA 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 316 FDFHPEDVFWctadigwitghsyvtygPLANGATSVLFEGIPTYpDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPv 395
Cdd:cd12116 178 FDISLLELLL-----------------PLLAGARVVIAPRETQR-DPEALARLIEAHSITVMQATPATWRMLLDAGWQG- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 396 tkhsRASLQVL-GtvGEPINPEawlwyhrvVGSQHCPIVDTFWQ----TETgghmlTPLPGATPMKPGSASFPffgVAPA 470
Cdd:cd12116 239 ----RAGLTALcG--GEALPPD--------LAARLLSRVGSLWNlygpTET-----TIWSTAARVTAAAGPIP---IGRP 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 471 ILNESGeelegeaegYLV--FKQPWP-GIMRTIY--------GNHTRFETTyFKKF-------PG--YYVTGDGCRRDQD 530
Cdd:cd12116 297 LANTQV---------YVLdaALRPVPpGVPGELYiggdgvaqGYLGRPALT-AERFvpdpfagPGsrLYRTGDLVRRRAD 366
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 531 GYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGEcLYCFVTLCDGHTFSstlTEELKKQIREKI 610
Cdd:cd12116 367 GRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRR-LVAYVVLKAGAAPD---AAALRAHLRATL 442
|
570 580
....*....|....*....|....*...
gi 1538017002 611 GPIATPDYIQNAPGLPKTRSGKIMRRVL 638
Cdd:cd12116 443 PAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
58-639 |
4.96e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 112.48 E-value: 4.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 58 VHEKKLGDKVAFYWegnePGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVF 137
Cdd:PRK13391 5 IHAQTTPDKPAVIM----ASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 138 AGFSAESLCERILDSSCSLLITTDAFYrgeklvnlkELADESLEKCrekgfP-VRCCIVVKHVGRAElGMNDSPsqspPV 216
Cdd:PRK13391 81 SHLTPAEAAYIVDDSGARALITSAAKL---------DVARALLKQC-----PgVRHRLVLDGDGELE-GFVGYA----EA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 217 KRQCPDVQI-SWNEGVDLwwhelmqeagdefepewcdaedplfiLYTSGSTGKPKLCAGSIcwsvemdTKPQPEDPFSPQ 295
Cdd:PRK13391 142 VAGLPATPIaDESLGTDM--------------------------LYSSGTTGRPKGIKRPL-------PEQPPDTPLPLT 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 296 GVVHTIGGY---MLYVATTFKYvfdfHPEDVFWCTADIgwitghsyvtygplANGATSVLFEGIptypDESRLWSIVDKY 372
Cdd:PRK13391 189 AFLQRLWGFrsdMVYLSPAPLY----HSAPQRAVMLVI--------------RLGGTVIVMEHF----DAEQYLALIEEY 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 373 KVTKFYTAPTA-IRMLmKFGDEPVTKHSRASLQVLGTVGEPINPE------AWlWyhrvvgsqhCPIVDTFWQTETGGhm 445
Cdd:PRK13391 247 GVTHTQLVPTMfSRML-KLPEEVRDKYDLSSLEVAIHAAAPCPPQvkeqmiDW-W---------GPIIHEYYAATEGL-- 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 446 ltplpGATPM-------KPGSASFPFFGVaPAILNESGeelegeaegylvfkQPWP-GIMRTIYgnhtrFET-TYFKKF- 515
Cdd:PRK13391 314 -----GFTACdseewlaHPGTVGRAMFGD-LHILDDDG--------------AELPpGEPGTIW-----FEGgRPFEYLn 368
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 516 ------------PGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLY 583
Cdd:PRK13391 369 dpaktaearhpdGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVK 448
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1538017002 584 CFVTLCDGHTFSSTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 639
Cdd:PRK13391 449 AVVQPVDGVDPGPALAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLR 504
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
65-641 |
9.24e-26 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 111.21 E-value: 9.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 65 DKVAFYWEGnepgetTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGAlhSIVFAG--FSA 142
Cdd:PRK03640 17 DRTAIEFEE------KKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGA--VAVLLNtrLSR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 143 ESLCERILDSSCSLLITTDAFyrgeklvnlkeladeslekcrekgfpvrccivvkhvgraelgmndspsqsppVKRQCPD 222
Cdd:PRK03640 89 EELLWQLDDAEVKCLITDDDF----------------------------------------------------EAKLIPG 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 223 VQISWNEgvdlwwheLMQEAGDEFEP-EWCDAEDPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGVVHTI 301
Cdd:PRK03640 117 ISVKFAE--------LMNGPKEEAEIqEEFDLDEVATIMYTSGTTGKPK-------------------------GVIQTY 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 302 GGYmLYVATTFKYVFDFHPEDVFWCTADIGWITGHSYVTygplangaTSVLFeGIPTYP----DESRLWSIVDKYKVTKF 377
Cdd:PRK03640 164 GNH-WWSAVGSALNLGLTEDDCWLAAVPIFHISGLSILM--------RSVIY-GMRVVLvekfDAEKINKLLQTGGVTII 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 378 YTAPTAI-RMLMKFGDEPVTKHSRASLqvLGtvGEPInPEAWLwyhrvvgsQHC-----PIVDTFWQTETGGHMLTPLPG 451
Cdd:PRK03640 234 SVVSTMLqRLLERLGEGTYPSSFRCML--LG--GGPA-PKPLL--------EQCkekgiPVYQSYGMTETASQIVTLSPE 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 452 ATPMKPGSASFPFFGVAPAILNESGEELEGEAEGYLVfKQP--WPGIMRTIYGNHTRFETTYFKkfpgyyvTGDGCRRDQ 529
Cdd:PRK03640 301 DALTKLGSAGKPLFPCELKIEKDGVVVPPFEEGEIVV-KGPnvTKGYLNREDATRETFQDGWFK-------TGDIGYLDE 372
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 530 DGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLcdGHTFSStltEELKKQIREK 609
Cdd:PRK03640 373 EGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK--SGEVTE---EELRHFCEEK 447
|
570 580 590
....*....|....*....|....*....|..
gi 1538017002 610 IGPIATPDYIQNAPGLPKTRSGKIMRRVLRKI 641
Cdd:PRK03640 448 LAKYKVPKRFYFVEELPRNASGKLLRHELKQL 479
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
91-639 |
1.41e-25 |
|
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: 110.22 E-value: 1.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 91 VCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAEslcerILDSSCSLLITtdafYRGEKLV 170
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFVPLNPT-----LKESVLRYLVA----DAGGRIV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 171 nlkeLADESLekcrekgfpvrccivvkhVGRAELGMNDSPSqsppvkrqcPDVQISwnegVDLWWHELMQEAGDEFEPEw 250
Cdd:cd05922 74 ----LADAGA------------------ADRLRDALPASPD---------PGTVLD----ADGIRAARASAPAHEVSHE- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 251 cdaeDPLFILYTSGSTGKPKLCAGSicwsvemdtkpqpedpfspqgvvHTiggYMLYVATTFKYVFDFHPEDVFWCTADI 330
Cdd:cd05922 118 ----DLALLLYTSGSTGSPKLVRLS-----------------------HQ---NLLANARSIAEYLGITADDRALTVLPL 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 331 GWITGHSYVTYGpLANGATSVLFEGipTYPDESrLWSIVDKYKVTKFYTAPTAIRML--MKFGDEPVtkhsrASLQVLGT 408
Cdd:cd05922 168 SYDYGLSVLNTH-LLRGATLVLTND--GVLDDA-FWEDLREHGATGLAGVPSTYAMLtrLGFDPAKL-----PSLRYLTQ 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 409 VGEPInPEAWLWYHR--VVGSQhcpIVDTFWQTETGGHMLTPLPGATPMKPGSASFPFFGVAPAILNESGEELEGEAEGY 486
Cdd:cd05922 239 AGGRL-PQETIARLRelLPGAQ---VYVMYGQTEATRRMTYLPPERILEKPGSIGLAIPGGEFEILDDDGTPTPPGEPGE 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 487 LVFKQPWpgIMRTiYGNHTRFETTYfKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVA 566
Cdd:cd05922 315 IVHRGPN--VMKG-YWNDPPYRRKE-GRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLII 390
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1538017002 567 EAAVVGHPHPVkGECLYCFVTLCDGHTFSstlteELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 639
Cdd:cd05922 391 EAAAVGLPDPL-GEKLALFVTAPDKIDPK-----DVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
65-638 |
2.88e-25 |
|
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: 109.26 E-value: 2.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 65 DKVAFYWEGnepgetTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAES 144
Cdd:cd05945 6 DRPAVVEGG------RTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 145 LcERILD-SSCSLLITtdafyrgeklvnlkeladeslekcrekgfpvrccivvkhvgraelgmndspsqsppvkrqcpdv 223
Cdd:cd05945 80 I-REILDaAKPALLIA---------------------------------------------------------------- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 224 qiswnegvdlwwhelmqeAGDefepewcdaeDPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGVVHTIGG 303
Cdd:cd05945 95 ------------------DGD----------DNAYIIFTSGSTGRPK-------------------------GVQISHDN 121
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 304 YMLYVATTFKYvFDFHPEDVFWCTA---------DIgwitghsyvtYGPLANGATSV------------LFEGIPTYPde 362
Cdd:cd05945 122 LVSFTNWMLSD-FPLGPGDVFLNQApfsfdlsvmDL----------YPALASGATLVpvprdatadpkqLFRFLAEHG-- 188
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 363 srlwsivdkykVTKFYTAPTAIRMLMkfGDEPVTKHSRASL-QVLgTVGEPI-NPEAWLWYHRVvgsQHCPIVDTFWQTE 440
Cdd:cd05945 189 -----------ITVWVSTPSFAAMCL--LSPTFTPESLPSLrHFL-FCGEVLpHKTARALQQRF---PDARIYNTYGPTE 251
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 441 T----GGHMLTPLPGATpMKPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQP--WPGIMRTiYGNHTRFettyFKK 514
Cdd:cd05945 252 AtvavTYIEVTPEVLDG-YDRLPIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPsvSKGYLNN-PEKTAAA----FFP 325
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 515 FPGY--YVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGH 592
Cdd:cd05945 326 DEGQraYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGA 405
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1538017002 593 TFSstLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 638
Cdd:cd05945 406 EAG--LTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
65-643 |
7.63e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 109.36 E-value: 7.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 65 DKVAFYWEGNEpgettkITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAES 144
Cdd:PRK06178 48 QRPAIIFYGHV------ITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 145 LCERILDSSCSLLITTDAFYrgeKLVNlkeladeslekcrekgfPVRCCIVVKHVGRAELG--MNDSPSQSPPVKRQCPD 222
Cdd:PRK06178 122 LSYELNDAGAEVLLALDQLA---PVVE-----------------QVRAETSLRHVIVTSLAdvLPAEPTLPLPDSLRAPR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 223 VQISWnegvdlwWHELMQ--EAGDEFEPEWCDAEDPLFIL-YTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGVVH 299
Cdd:PRK06178 182 LAAAG-------AIDLLPalRACTAPVPLPPPALDALAALnYTGGTTGMPK-------------------------GCEH 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 300 TiGGYMLYVATTFKYVFDFHPED-VFWCTADIGWITGHSYVTYGPLANGATSVLFegipTYPDESRLWSIVDKYKVTK-F 377
Cdd:PRK06178 230 T-QRDMVYTAAAAYAVAVVGGEDsVFLSFLPEFWIAGENFGLLFPLFSGATLVLL----ARWDAVAFMAAVERYRVTRtV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 378 YTAPTAIRMLmkfgDEP-VTKHSRASLQVLGTVG--EPINPEAWLWYHRVVGSQhcpIVDTFW-QTET------------ 441
Cdd:PRK06178 305 MLVDNAVELM----DHPrFAEYDLSSLRQVRVVSfvKKLNPDYRQRWRALTGSV---LAEAAWgMTEThtcdtftagfqd 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 442 GGHMLT--------PLPGA----TPMKPGsASFPFfGV-------APAILnesgeelegeaegylvfkqpwpgimrTIYG 502
Cdd:PRK06178 378 DDFDLLsqpvfvglPVPGTefkiCDFETG-ELLPL-GAegeivvrTPSLL--------------------------KGYW 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 503 NHTRFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECL 582
Cdd:PRK06178 430 NKPEATAEALRD--GWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVP 507
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1538017002 583 YCFVTLCDGHTFSStltEELKKQIREKIGPIATPD-YIQNApgLPKTRSGKIMRRVLRKIAQ 643
Cdd:PRK06178 508 VAFVQLKPGADLTA---AALQAWCRENMAVYKVPEiRIVDA--LPMTATGKVRKQDLQALAE 564
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
82-638 |
2.65e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 107.43 E-value: 2.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 82 ITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITTD 161
Cdd:PRK06710 50 ITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 162 AFYrgEKLVNLKELAD-ESLEKCREKGF-PVRCCIVVKHVGRaelgmndspsqsppvKRQCPDVQISWNEGVDLWwHELM 239
Cdd:PRK06710 130 LVF--PRVTNVQSATKiEHVIVTRIADFlPFPKNLLYPFVQK---------------KQSNLVVKVSESETIHLW-NSVE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 240 QEAGDEFEPEwCDAEDPLFIL-YTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGVVHTIGGYMLYVATTFKYVFD- 317
Cdd:PRK06710 192 KEVNTGVEVP-CDPENDLALLqYTGGTTGFPK-------------------------GVMLTHKNLVSNTLMGVQWLYNc 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 318 FHPEDVFWCTADIGWITGHSYVTYGPLANGATSVLfegIPTYpDESRLWSIVDKYKVTKFYTAPTAIRMLMkfgDEPVTK 397
Cdd:PRK06710 246 KEGEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVL---IPKF-DMKMVFEAIKKHKVTLFPGAPTIYIALL---NSPLLK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 398 -HSRASLQVLGTVGEPINPEAWLWYHRVVGSQhcpIVDTFWQTETgghmlTPLPGATPM----KPGSASFPFFGVAPAIL 472
Cdd:PRK06710 319 eYDISSIRACISGSAPLPVEVQEKFETVTGGK---LVEGYGLTES-----SPVTHSNFLwekrVPGSIGVPWPDTEAMIM 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 473 NESGEELEGEAEG-YLVFKQPwpGIMRtiyGNHTRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLS 551
Cdd:PRK06710 391 SLETGEALPPGEIgEIVVKGP--QIMK---GYWNKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVY 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 552 TAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSStltEELKKQIREKIGPIATPDYIQNAPGLPKTRSG 631
Cdd:PRK06710 466 PREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSE---EELNQFARKYLAAYKVPKVYEFRDELPKTTVG 542
|
....*..
gi 1538017002 632 KIMRRVL 638
Cdd:PRK06710 543 KILRRVL 549
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
65-645 |
1.42e-23 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 105.14 E-value: 1.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 65 DKVAFYWEGNEPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAES 144
Cdd:PRK13295 39 DKTAVTAVRLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 145 LCERILDSSCSLLITTDAFyrgeklvnlkeladeslekcreKGFpvrccivvkhvgraelgmnDSPSQSPPVKRQCPDVQ 224
Cdd:PRK13295 119 LSFMLKHAESKVLVVPKTF----------------------RGF-------------------DHAAMARRLRPELPALR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 225 ---ISWNEGVDLW--------WhELMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfs 293
Cdd:PRK13295 158 hvvVVGGDGADSFeallitpaW-EQEPDAPAILARLRPGPDDVTQLIYTSGTTGEPK----------------------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 294 pqGVVHT----IGGYMLYVATtfkyvFDFHPEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEgiptYPDESRLWSIV 369
Cdd:PRK13295 214 --GVMHTantlMANIVPYAER-----LGLGADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQD----IWDPARAAELI 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 370 DKYKVTkFYTAPTAirMLMKFGDepVTKHSR---ASLQVLGTVGEPINP----EAWlwyhRVVGSQhcpIVDTFWQTETG 442
Cdd:PRK13295 283 RTEGVT-FTMASTP--FLTDLTR--AVKESGrpvSSLRTFLCAGAPIPGalveRAR----AALGAK---IVSAWGMTENG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 443 GHMLTpLPGATPMKPG-SASFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpgimrTIYGNHTRFETTYFKKFPGYYVT 521
Cdd:PRK13295 351 AVTLT-KLDDPDERAStTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGC------SNFGGYLKRPQLNGTDADGWFDT 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 522 GDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFS-STLTE 600
Cdd:PRK13295 424 GDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDfEEMVE 503
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1538017002 601 ELKKQireKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQND 645
Cdd:PRK13295 504 FLKAQ---KVAKQYIPERLVVRDALPRTPSGKIQKFRLREMLRGE 545
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
82-638 |
1.48e-23 |
|
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: 104.10 E-value: 1.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 82 ITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITTd 161
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 162 afyrgeklvnlkeladeslekcrekgfpvrccivvkhvgrAELgmndspsqsppvkrqcpdvqiswnegvdlwwhelmqe 241
Cdd:cd05935 81 ----------------------------------------SEL------------------------------------- 83
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 242 agdefepewcdaEDPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGVVHTiGGYMLYVATTFKYVFDFHPE 321
Cdd:cd05935 84 ------------DDLALIPYTSGTTGLPK-------------------------GCMHT-HFSAAANALQSAVWTGLTPS 125
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 322 DVFWCTADIGWITGHSYVTYGPLANGATSVLFegipTYPDESRLWSIVDKYKVTKFYTAPTAIRMLMkfGDEPVTKHSRA 401
Cdd:cd05935 126 DVILACLPLFHVTGFVGSLNTAVYVGGTYVLM----ARWDRETALELIEKYKVTFWTNIPTMLVDLL--ATPEFKTRDLS 199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 402 SLQVLGTVGEPInPEAWLwyHRVVGSQHCPIVDTFWQTETGGHMLTPLPGAtpMKPGSASFPFFGVAPAILNESGEELEG 481
Cdd:cd05935 200 SLKVLTGGGAPM-PPAVA--EKLLKLTGLRFVEGYGLTETMSQTHTNPPLR--PKLQCLGIP*FGVDARVIDIETGRELP 274
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 482 EAEG-YLVFKQPwpGIMRTiYGNHTRFETTYFKKFPG--YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESA 558
Cdd:cd05935 275 PNEVgEIVVRGP--QIFKG-YWNRPEETEESFIEIKGrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAK 351
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 559 LVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtFSSTLTEE-LKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRV 637
Cdd:cd05935 352 LYKHPAI*EVCVISVPDERVGEEVKAFIVLRPE--YRGKVTEEdIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRL 429
|
.
gi 1538017002 638 L 638
Cdd:cd05935 430 L 430
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
61-638 |
1.75e-23 |
|
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: 104.21 E-value: 1.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 61 KKLGDKVAFYWEGnepgetTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGF 140
Cdd:cd12117 8 ARTPDAVAVVYGD------RSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 141 SAESLCERILDSSCSLLITtdafyrgeklvnlkelaDESLEKcrekGFPVRCCIVVKHVGRAElgmndSPSQSPPVKrqc 220
Cdd:cd12117 82 PAERLAFMLADAGAKVLLT-----------------DRSLAG----RAGGLEVAVVIDEALDA-----GPAGNPAVP--- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 221 pdvqiswnegvdlwwhelmqeagdefepewCDAEDPLFILYTSGSTGKPKlcaGSICwsvemdtkpqpedpfSPQGVVHT 300
Cdd:cd12117 133 ------------------------------VSPDDLAYVMYTSGSTGRPK---GVAV---------------THRGVVRL 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 301 I--GGYMlyvattfkyvfDFHPEDVFWCTADIGWiTGHSYVTYGPLANGATSVLfegIPTYP--DESRLWSIVDKYKVTK 376
Cdd:cd12117 165 VknTNYV-----------TLGPDDRVLQTSPLAF-DASTFEIWGALLNGARLVL---APKGTllDPDALGALIAEEGVTV 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 377 -FYTAP-------TAIRMLmkfgdepvtkhsrASLQVLGTVGEPINPEawlWYHRVVgsQHCP---IVDTFWQTETGG-- 443
Cdd:cd12117 230 lWLTAAlfnqladEDPECF-------------AGLRELLTGGEVVSPP---HVRRVL--AACPglrLVNGYGPTENTTft 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 444 --HMLTPL-PGATPMKPGSasfPFFGVAPAILNesgeelegeaegylVFKQPWP-GIMRTIY--------GNHTRFETTY 511
Cdd:cd12117 292 tsHVVTELdEVAGSIPIGR---PIANTRVYVLD--------------EDGRPVPpGVPGELYvggdglalGYLNRPALTA 354
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 512 fKKF------PG--YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLY 583
Cdd:cd12117 355 -ERFvadpfgPGerLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLV 433
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1538017002 584 CFVTLCDGHTfsstlTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 638
Cdd:cd12117 434 AYVVAEGALD-----AAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
65-639 |
4.89e-23 |
|
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: 102.45 E-value: 4.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 65 DKVAFYWEGNEpgettkITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAES 144
Cdd:cd17649 2 DAVALVFGDQS------LSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 145 LCERILDSSCSLLITtdafyrgeklvnlkeladeslekcrekgfpvrccivvkhvgraelgmndspsQSPpvkrqcpdvq 224
Cdd:cd17649 76 LRYMLEDSGAGLLLT----------------------------------------------------HHP---------- 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 225 iswnegvdlwwhelmqeagdefepewcdaEDPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGVVHTIGGY 304
Cdd:cd17649 94 -----------------------------RQLAYVIYTSGSTGTPK-------------------------GVAVSHGPL 119
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 305 MLYVATTFKYvFDFHPEDVFWCTADIGWITGHSYVtYGPLANGAtSVLFEGIPTYPDESRLWSIVDKYKVTKFYTAPTAI 384
Cdd:cd17649 120 AAHCQATAER-YGLTPGDRELQFASFNFDGAHEQL-LPPLICGA-CVVLRPDELWASADELAEMVRELGVTVLDLPPAYL 196
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 385 RMLMKFGDEpVTKHSRASLQVLGTVGEPINPE-AWLWyhrvvGSQHCPIVDTFWQTETgghMLTPL--PGATPMKPGSAS 461
Cdd:cd17649 197 QQLAEEADR-TGDGRPPSLRLYIFGGEALSPElLRRW-----LKAPVRLFNAYGPTEA---TVTPLvwKCEAGAARAGAS 267
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 462 FP----FFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRtiyGNHTRFETTYfKKF-------PG--YYVTGDGCRRD 528
Cdd:cd17649 268 MPigrpLGGRSAYILDADLNPVPVGVTGELYIGGE--GLAR---GYLGRPELTA-ERFvpdpfgaPGsrLYRTGDLARWR 341
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 529 QDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVkGECLYCFVTLCDGHTFSSTLtEELKKQIRE 608
Cdd:cd17649 342 DDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAG-GKQLVAYVVLRAAAAQPELR-AQLRTALRA 419
|
570 580 590
....*....|....*....|....*....|.
gi 1538017002 609 KIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 639
Cdd:cd17649 420 SLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
64-638 |
6.63e-23 |
|
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: 102.74 E-value: 6.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 64 GDKVAFYWEGnepgetTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAE 143
Cdd:cd17646 12 PDAPAVVDEG------RTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 144 SLCERILDSSCSLLITT-DAFYRGEKLVNLKELADESLekcrekgfpvrccivvkhvgraelgmnDSPSQSPPVKRQCPD 222
Cdd:cd17646 86 RLAYMLADAGPAVVLTTaDLAARLPAGGDVALLGDEAL---------------------------AAPPATPPLVPPRPD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 223 vqiswnegvdlwwhelmqeagdefepewcdaeDPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGVV---H 299
Cdd:cd17646 139 --------------------------------NLAYVIYTSGSTGRPK-------------------------GVMvthA 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 300 TIGGYMLYvattFKYVFDFHPEDVFWCTADIG-----WitghsyVTYGPLANGATSVLFE----GIPTYpdesrLWSIVD 370
Cdd:cd17646 162 GIVNRLLW----MQDEYPLGPGDRVLQKTPLSfdvsvW------ELFWPLVAGARLVVARpgghRDPAY-----LAALIR 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 371 KYKVTKFYTAPTairMLMKFGDEPvTKHSRASLQVLGTVGEPINPEAWLWYHRVVgsqHCPIVDTFWQTET--------- 441
Cdd:cd17646 227 EHGVTTCHFVPS---MLRVFLAEP-AAGSCASLRRVFCSGEALPPELAARFLALP---GAELHNLYGPTEAaidvthwpv 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 442 -GGHMLTPLPGATPMkPGSASFpffgVAPAILNEsgeelegeaegylvfkQPwPGIMRTIY--------GNHTRFETTYf 512
Cdd:cd17646 300 rGPAETPSVPIGRPV-PNTRLY----VLDDALRP----------------VP-VGVPGELYlggvqlarGYLGRPALTA- 356
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 513 KKF------PG--YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYC 584
Cdd:cd17646 357 ERFvpdpfgPGsrMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVG 436
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1538017002 585 FVTLCDGHTfsSTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 638
Cdd:cd17646 437 YVVPAAGAA--GPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
76-638 |
9.26e-23 |
|
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: 102.20 E-value: 9.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 76 PGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERI-LDSSC 154
Cdd:cd05923 23 PARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIeRGEMT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 155 SLLITTDAfyrgeklvnlkELADESlekcreKGFPVRCCIVVKHVGraeLGMNDSpsqsppvkrqcpdvqiswnegvdlw 234
Cdd:cd05923 103 AAVIAVDA-----------QVMDAI------FQSGVRVLALSDLVG---LGEPES------------------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 235 whelmqeAGDEFEPEWCDAEDPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfsPQGVVH-TIGGYMLYVATTFK 313
Cdd:cd05923 138 -------AGPLIEDPPREPEQPAFVFYTSGTTGLPK-----------------------GAVIPQrAAESRVLFMSTQAG 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 314 YVFDFHpeDVFWCTADIGWITGHSYVTYGPLANGATSVLfegiPTYPDESRLWSIVDKYKVTKFYTAPTAIRMLMkfGDE 393
Cdd:cd05923 188 LRHGRH--NVVLGLMPLYHVIGFFAVLVAALALDGTYVV----VEEFDPADALKLIEQERVTSLFATPTHLDALA--AAA 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 394 PVTKHSRASLQVLGTVGEPInPEAWLwyHRVVGSQHCPIVDTFWQTETGGHMLTPLPGA-TPMKPGsasfpFFG---VAP 469
Cdd:cd05923 260 EFAGLKLSSLRHVTFAGATM-PDAVL--ERVNQHLPGEKVNIYGTTEAMNSLYMRDARTgTEMRPG-----FFSevrIVR 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 470 aILNESGEELEGEAEGYLVFKQP----WPGIMRtiygnhtRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNV 545
Cdd:cd05923 332 -IGGSPDEALANGEEGELIVAAAadaaFTGYLN-------QPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIIS 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 546 SGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfssTLTEELKKQ--IREKIGPIATPDYIQNAP 623
Cdd:cd05923 404 GGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREG-----TLSADELDQfcRASELADFKRPRRYFFLD 478
|
570
....*....|....*
gi 1538017002 624 GLPKTRSGKIMRRVL 638
Cdd:cd05923 479 ELPKNAMNKVLRRQL 493
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
77-639 |
1.29e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 101.90 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 77 GETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSL 156
Cdd:PRK08276 7 PSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 157 LITTDAFyrgekLVNLKELADESlekcrEKGFPVRccivvkHVGRAELgmndspsqsppvkrqcpdvqiswnEGVDLWWH 236
Cdd:PRK08276 87 LIVSAAL-----ADTAAELAAEL-----PAGVPLL------LVVAGPV------------------------PGFRSYEE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 237 ELMQEAGDEFEPEWCDAEdplfILYTSGSTGKPKlcaGSIcwsvemdtKPQPE-DPFSPQGVVHTIGGYMlyvattfkyv 315
Cdd:PRK08276 127 ALAAQPDTPIADETAGAD----MLYSSGTTGRPK---GIK--------RPLPGlDPDEAPGMMLALLGFG---------- 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 316 FDFHPEDVFWCTADIGwitgHSYVT-YG--PLANGATSVLFEGIptypDESRLWSIVDKYKVTKFYTAPTA-IRMLmKFG 391
Cdd:PRK08276 182 MYGGPDSVYLSPAPLY----HTAPLrFGmsALALGGTVVVMEKF----DAEEALALIERYRVTHSQLVPTMfVRML-KLP 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 392 DEPVTKHSRASLQVLGTVGEPINPE------AWlWyhrvvGsqhcPIVD-TFWQTETGGHMLtplpgATP----MKPGSA 460
Cdd:PRK08276 253 EEVRARYDVSSLRVAIHAAAPCPVEvkramiDW-W-----G----PIIHeYYASSEGGGVTV-----ITSedwlAHPGSV 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 461 SFPFFGVApAILNESGEELEGEAEGYLVFKQPWPGImrTIYGNHTRFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRID 540
Cdd:PRK08276 318 GKAVLGEV-RILDEDGNELPPGEIGTVYFEMDGYPF--EYHNDPEKTAAARNPH--GWVTVGDVGYLDEDGYLYLTDRKS 392
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 541 DMLnVSGHL-LSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSSTLTEELKKQIREKIGPIATPDYI 619
Cdd:PRK08276 393 DMI-ISGGVnIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAGDALAAELIAWLRGRLAHYKCPRSI 471
|
570 580
....*....|....*....|
gi 1538017002 620 QNAPGLPKTRSGKIMRRVLR 639
Cdd:PRK08276 472 DFEDELPRTPTGKLYKRRLR 491
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
65-640 |
3.02e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 101.01 E-value: 3.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 65 DKVAFYWEGNEpgettkITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAES 144
Cdd:PRK07786 32 DAPALRFLGNT------TTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 145 LCERILDSSCSLLITTDAfyrgekLVNLKELADESLekcrekgfPVRCCIVVkhVGRAelgmndspsqsppvkrqcpdvq 224
Cdd:PRK07786 106 IAFLVSDCGAHVVVTEAA------LAPVATAVRDIV--------PLLSTVVV--AGGS---------------------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 225 iswNEGVDLWWHELMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPKlcaGSIcwsvemdtkpqpedpfspqgVVHT-IGG 303
Cdd:PRK07786 148 ---SDDSVLGYEDLLAEAGPAHAPVDIPNDSPALIMYTSGTTGRPK---GAV--------------------LTHAnLTG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 304 YMLYVATTFKYvfdFHPEDVFWCTADIGWITGhsyvtygpLANGATSVLFeGIPT--YP----DESRLWSIVDKYKVTKF 377
Cdd:PRK07786 202 QAMTCLRTNGA---DINSDVGFVGVPLFHIAG--------IGSMLPGLLL-GAPTviYPlgafDPGQLLDVLEAEKVTGI 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 378 YTAPTAIRMLMkfgDEPVTKHSRASLQVLGTVGEPiNPEAWL--WYHRVVGSQhcpIVDTFWQTEtgghmLTPLpgaTPM 455
Cdd:PRK07786 270 FLVPAQWQAVC---AEQQARPRDLALRVLSWGAAP-ASDTLLrqMAATFPEAQ---ILAAFGQTE-----MSPV---TCM 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 456 --------KPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpgIMRTIYGNHTRFETTYFKKfpGYYVTGDGCRR 527
Cdd:PRK07786 335 llgedairKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAP---TLMSGYWNNPEATAEAFAG--GWFHSGDLVRQ 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 528 DQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfSSTLT-EELKKQI 606
Cdd:PRK07786 410 DEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRND---DAALTlEDLAEFL 486
|
570 580 590
....*....|....*....|....*....|....
gi 1538017002 607 REKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 640
Cdd:PRK07786 487 TDRLARYKHPKALEIVDALPRNPAGKVLKTELRE 520
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
78-576 |
3.09e-22 |
|
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: 102.24 E-value: 3.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 78 ETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGAlhsivfA------GFSAESLcERIL- 150
Cdd:COG1020 498 GDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGA------AyvpldpAYPAERL-AYMLe 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 151 DSSCSLLITTDAFyrgeklvnLKELADESLEkcrekgfpvrcCIVVkhvgrAELGMNDSPSQSPPVKRqcpdvqiswneg 230
Cdd:COG1020 571 DAGARLVLTQSAL--------AARLPELGVP-----------VLAL-----DALALAAEPATNPPVPV------------ 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 231 vdlwwhelmqeagdefepewcDAEDPLFILYTSGSTGKPKlcaGsicwsVEMdtkpqpedpfSPQGVVHTIGGY------ 304
Cdd:COG1020 615 ---------------------TPDDLAYVIYTSGSTGRPK---G-----VMV----------EHRALVNLLAWMqrrygl 655
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 305 -----MLYVATtfkYVFDFHPEDVFWctadigwitghsyvtygPLANGATSVLfegiptYPDESR-----LWSIVDKYKV 374
Cdd:COG1020 656 gpgdrVLQFAS---LSFDASVWEIFG-----------------ALLSGATLVL------APPEARrdpaaLAELLARHRV 709
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 375 TKFYTAPTAIRMLMKFGDEPVtkhsrASLQVLGTVGEPINPEAWLWYHRVVGsqHCPIVDTFWQTETG----GHMLTPLP 450
Cdd:COG1020 710 TVLNLTPSLLRALLDAAPEAL-----PSLRLVLVGGEALPPELVRRWRARLP--GARLVNLYGPTETTvdstYYEVTPPD 782
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 451 GATPMKP-GSasfPFFGVAPAILNEsgeelegeaegylvFKQPWP-GIMRTIY--------GNHTRFETT--YF----KK 514
Cdd:COG1020 783 ADGGSVPiGR---PIANTRVYVLDA--------------HLQPVPvGVPGELYiggaglarGYLNRPELTaeRFvadpFG 845
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1538017002 515 FPG--YYVTGDGCRRDQDG---YywiTGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHP 576
Cdd:COG1020 846 FPGarLYRTGDLARWLPDGnleF---LGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDA 909
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
259-640 |
3.15e-22 |
|
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: 99.73 E-value: 3.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 259 ILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGVVHTIGGYmLYVATTFKYVFDFHPEDVFWCTADIGWITGHSY 338
Cdd:cd05912 82 IMYTSGTTGKPK-------------------------GVQQTFGNH-WWSAIGSALNLGLTEDDNWLCALPLFHISGLSI 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 339 VTYGpLANGATSVLFEGIptypDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVTKHSRASLqvLGtvGEPInPEAW 418
Cdd:cd05912 136 LMRS-VIYGMTVYLVDKF----DAEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYPNNLRCIL--LG--GGPA-PKPL 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 419 LwyhrvvgsQHC-----PIVDTFWQTETGGHMLTPLPGATPMKPGSASFPFFGVAPAILNESGEELEGEAegyLVFKQPw 493
Cdd:cd05912 206 L--------EQCkekgiPVYQSYGMTETCSQIVTLSPEDALNKIGSAGKPLFPVELKIEDDGQPPYEVGE---ILLKGP- 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 494 pGIMRTIYG----NHTRFETTYFKkfpgyyvTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAA 569
Cdd:cd05912 274 -NVTKGYLNrpdaTEESFENGWFK-------TGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAG 345
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1538017002 570 VVGHPHPVKGECLYCFVTLcdghtfSSTLT-EELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 640
Cdd:cd05912 346 VVGIPDDKWGQVPVAFVVS------ERPISeEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
81-642 |
4.19e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 100.62 E-value: 4.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 81 KITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITT 160
Cdd:PRK12583 45 RYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 161 DAFyRGEKLVN-----LKELADESLEKCREKGFPVRCCIVVkhvgraeLGMNDSPSQsppvkrqcpdvqiswnegvdLWW 235
Cdd:PRK12583 125 DAF-KTSDYHAmlqelLPGLAEGQPGALACERLPELRGVVS-------LAPAPPPGF--------------------LAW 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 236 HELmQEAGDEFEPE-------WCDAEDPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGVV---HTI--GG 303
Cdd:PRK12583 177 HEL-QARGETVSREalaerqaSLDRDDPINIQYTSGTTGFPK-------------------------GATlshHNIlnNG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 304 YMLYVAttfkyvFDFHPEDVFWCTADIGWITGHSYVTYGPLANGATsVLFEGIPTYPDESrlWSIVDKYKVTKFYTAPTa 383
Cdd:PRK12583 231 YFVAES------LGLTEHDRLCVPVPLYHCFGMVLANLGCMTVGAC-LVYPNEAFDPLAT--LQAVEEERCTALYGVPT- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 384 irMLMKFGDEPvtKHSRASLQVLGT---VGEPINPEAwlwYHRVVGSQHCP-IVDTFWQTETGGhmLTPLPGAT-PMKPG 458
Cdd:PRK12583 301 --MFIAELDHP--QRGNFDLSSLRTgimAGAPCPIEV---MRRVMDEMHMAeVQIAYGMTETSP--VSLQTTAAdDLERR 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 459 SASF----PFFGVApaILNESGEELEGEAEGYLVFKqpwpG--IMRTIYGNHTRFETTYFKKfpGYYVTGDGCRRDQDGY 532
Cdd:PRK12583 372 VETVgrtqPHLEVK--VVDPDGATVPRGEIGELCTR----GysVMKGYWNNPEATAESIDED--GWMHTGDLATMDEQGY 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 533 YWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSStltEELKKQIREKIGP 612
Cdd:PRK12583 444 VRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASE---EELREFCKARIAH 520
|
570 580 590
....*....|....*....|....*....|
gi 1538017002 613 IATPDYIQNAPGLPKTRSGKIMRRVLRKIA 642
Cdd:PRK12583 521 FKVPRYFRFVDEFPMTVTGKVQKFRMREIS 550
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
77-643 |
5.86e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 100.20 E-value: 5.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 77 GETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSL 156
Cdd:PRK06164 31 DEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARW 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 157 LITTDAFyRGEKLVN-LKELADESLEkcrekgfPVRCCIVVkhvgraELGMNDSPSQSPPVKRQCPDVqiswnegvdlww 235
Cdd:PRK06164 111 LVVWPGF-KGIDFAAiLAAVPPDALP-------PLRAIAVV------DDAADATPAPAPGARVQLFAL------------ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 236 hELMQEAGDEFEPEwcDAEDPLFILY-TSGSTGKPKLcagsicwsvemdtkpqpedpfspqgVVHTIGGyMLYVATTFKY 314
Cdd:PRK06164 165 -PDPAPPAAAGERA--ADPDAGALLFtTSGTTSGPKL-------------------------VLHRQAT-LLRHARAIAR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 315 VFDFHPEDVFWCTADIGWITGHSYVTyGPLANGATSVLfegIPTYpDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEP 394
Cdd:PRK06164 216 AYGYDPGAVLLAALPFCGVFGFSTLL-GALAGGAPLVC---EPVF-DAARTARALRRHRVTHTFGNDEMLRRILDTAGER 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 395 vtkHSRASLQVLGTVGepINPeAWLWYHRVVGSQHCPIVDTFWQTE-----TGGHMLTP-----LPGATPMKPGSASFPF 464
Cdd:PRK06164 291 ---ADFPSARLFGFAS--FAP-ALGELAALARARGVPLTGLYGSSEvqalvALQPATDPvsvriEGGGRPASPEARVRAR 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 465 FGVAPAILNESGEELEGEAEgylvfkqpwPGIMRTIYGN--HTRFETTYfkkfPGYYVTGDGCRRDQDGYYWITGRIDDM 542
Cdd:PRK06164 365 DPQDGALLPDGESGEIEIRA---------PSLMRGYLDNpdATARALTD----DGYFRTGDLGYTRGDGQFVYQTRMGDS 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 543 LNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGEClYCFVTLCDGhtfSSTLTEELKKQIREKIGPIATPDYIQNA 622
Cdd:PRK06164 432 LRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGKTVP-VAFVIPTDG---ASPDEAGLMAACREALAGFKVPARVQVV 507
|
570 580
....*....|....*....|....
gi 1538017002 623 PGLPKTRSG---KIMRRVLRKIAQ 643
Cdd:PRK06164 508 EAFPVTESAngaKIQKHRLREMAQ 531
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
80-638 |
8.51e-22 |
|
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: 99.32 E-value: 8.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 80 TKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALhsIVFAGFSaeslcerildsscsllit 159
Cdd:cd05920 39 RRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAV--PVLALPS------------------ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 160 tdafYRGEKLVNLKELADeslekcrekgfpvrcciVVKHVGRAELGMNDSPSQSPPVKRQCPDVQiswnegvdlwwhelm 239
Cdd:cd05920 99 ----HRRSELSAFCAHAE-----------------AVAYIVPDRHAGFDHRALARELAESIPEVA--------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 240 qeagdefepewcdaedplFILYTSGSTGKPKLCagsicwsvemdtkPQPEDPFSpqgvvhtiggymlYVATTFKYVFDFH 319
Cdd:cd05920 143 ------------------LFLLSGGTTGTPKLI-------------PRTHNDYA-------------YNVRASAEVCGLD 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 320 PEDVFWCTADIGwitgHSYVTYGP-----LANGATSVLfegiPTYPDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEP 394
Cdd:cd05920 179 QDTVYLAVLPAA----HNFPLACPgvlgtLLAGGRVVL----APDPSPDAAFPLIEREGVTVTALVPALVSLWLDAAASR 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 395 vtKHSRASLQVLGTVGEPINPEAWLWYHRVVGsqhCPIVDTFWQTE-----------------TGGHMLTPL-------P 450
Cdd:cd05920 251 --RADLSSLRLLQVGGARLSPALARRVPPVLG---CTLQQVFGMAEgllnytrlddpdeviihTQGRPMSPDdeirvvdE 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 451 GATPMKPGSASfpffgvapailnesgeelegeaegYLVFKQPWpgimrTIYG-------NHTRFETTyfkkfpGYYVTGD 523
Cdd:cd05920 326 EGNPVPPGEEG------------------------ELLTRGPY-----TIRGyyrapehNARAFTPD------GFYRTGD 370
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 524 GCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDghtfSSTLTEELK 603
Cdd:cd05920 371 LVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRD----PPPSAAQLR 446
|
570 580 590
....*....|....*....|....*....|....*...
gi 1538017002 604 KQIREKigPIAT---PDYIQNAPGLPKTRSGKIMRRVL 638
Cdd:cd05920 447 RFLRER--GLAAyklPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
77-641 |
1.81e-21 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 98.39 E-value: 1.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 77 GETTKITYRELLVQVCQFSNVLRKQ-GIQKGDRVAIYMPMILELVVAMLACARLGALhSIVFagfsaeslcerildsscs 155
Cdd:PRK06839 23 TEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECI-AVPL------------------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 156 llittdafyrgeklvNLKELADESLEKCREKGFPVRCCivVKHVGRAELGMNDSPSQSPPVkrqcpdvqisWNEGVDlww 235
Cdd:PRK06839 84 ---------------NIRLTENELIFQLKDSGTTVLFV--EKTFQNMALSMQKVSYVQRVI----------SITSLK--- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 236 hELMQEAGDEFEPEwcDAEDPLFILYTSGSTGKPKlcaGSICWSVEMdtkpqpedpfspqgvvhtiggymLYVATTFKYV 315
Cdd:PRK06839 134 -EIEDRKIDNFVEK--NESASFIICYTSGTTGKPK---GAVLTQENM-----------------------FWNALNNTFA 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 316 FDFHPEDVFWCTADIGWITGHSYVTYGPLANGATSVlfegIPTYPDESRLWSIVDKYKVTKFYTAPT---AIRMLMKFgd 392
Cdd:PRK06839 185 IDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVII----VPRKFEPTKALSMIEKHKVTVVMGVPTihqALINCSKF-- 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 393 epvTKHSRASLQVLGTVGEPInPEAWLwyhRVVGSQHCPIVDTFWQTETGGHMLTPLPGATPMKPGSASFPFFGVAPAIL 472
Cdd:PRK06839 259 ---ETTNLQSVRWFYNGGAPC-PEELM---REFIDRGFLFGQGFGMTETSPTVFMLSEEDARRKVGSIGKPVLFCDYELI 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 473 NESGEELEGEAEGYLVFKQPwpGIMRTIYGNHTRFETTYFKkfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLST 552
Cdd:PRK06839 332 DENKNKVEVGEVGELLIRGP--NVMKEYWNRPDATEETIQD---GWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYP 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 553 AEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfSSTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGK 632
Cdd:PRK06839 407 LEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSS---SVLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGK 483
|
....*....
gi 1538017002 633 IMRRVLRKI 641
Cdd:PRK06839 484 IQKAQLVNQ 492
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
234-640 |
2.56e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 98.21 E-value: 2.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 234 WWHELMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPKLCagsICwsvemdtkpqpedpfsPQGVVhTIGGYMLyvATTFk 313
Cdd:PRK07867 132 WADELAAHRDAEPPFRVADPDDLFMLIFTSGTSGDPKAV---RC----------------THRKV-ASAGVML--AQRF- 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 314 yvfDFHPEDVFWCTADI--------GWITGhsyvtygpLANGATSVL---FEGiptypdeSRLWSIVDKYKVTKFYTAPT 382
Cdd:PRK07867 189 ---GLGPDDVCYVSMPLfhsnavmaGWAVA--------LAAGASIALrrkFSA-------SGFLPDVRRYGATYANYVGK 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 383 AIRMLMKFGDEPVTKHSraSLQVL-GTVGEPINPEAwlwYHRVVGsqhCPIVDTFWQTEtGGHMLTPLPGaTPmkPGSAS 461
Cdd:PRK07867 251 PLSYVLATPERPDDADN--PLRIVyGNEGAPGDIAR---FARRFG---CVVVDGFGSTE-GGVAITRTPD-TP--PGALG 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 462 FPFFGVA-----------PAILNESGEELEGEAEGYLVFKQPwPGIMRTIYGNHtrfETTYFKKFPGYYVTGDGCRRDQD 530
Cdd:PRK07867 319 PLPPGVAivdpdtgtecpPAEDADGRLLNADEAIGELVNTAG-PGGFEGYYNDP---EADAERMRGGVYWSGDLAYRDAD 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 531 GYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTF-SSTLTEELKKQirEK 609
Cdd:PRK07867 395 GYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKFdPDAFAEFLAAQ--PD 472
|
410 420 430
....*....|....*....|....*....|.
gi 1538017002 610 IGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 640
Cdd:PRK07867 473 LGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
517-640 |
2.77e-21 |
|
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: 96.98 E-value: 2.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 517 GYYVTGDGCRRDQDGYYWITGRI-DDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTfs 595
Cdd:cd05941 320 GWFKTGDLGVVDEDGYYWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAA-- 397
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1538017002 596 sTLT-EELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 640
Cdd:cd05941 398 -ALSlEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
235-639 |
2.90e-21 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 97.79 E-value: 2.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 235 WHELMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPKlcagsicwSVEMdtkpqpedpfsPQGVVHTIGgymlyVATTFKY 314
Cdd:PRK13388 131 YAELVAAAGALTPHREVDAMDPFMLIFTSGTTGAPK--------AVRC-----------SHGRLAFAG-----RALTERF 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 315 vfDFHPEDVFWCTADIGwitgHS---YVTYGP-LANGATSVLfegiPTYPDESRLWSIVDKYKVTKFYTAPTAIRMLMKF 390
Cdd:PRK13388 187 --GLTRDDVCYVSMPLF----HSnavMAGWAPaVASGAAVAL----PAKFSASGFLDDVRRYGATYFNYVGKPLAYILAT 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 391 GDEPvtKHSRASLQV-LGTVGEPINPEAwlwYHRVVGsqhCPIVDTFWQTETGGhMLTPLPGaTPmkPGSASFPFFGVAp 469
Cdd:PRK13388 257 PERP--DDADNPLRVaFGNEASPRDIAE---FSRRFG---CQVEDGYGSSEGAV-IVVREPG-TP--PGSIGRGAPGVA- 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 470 aILNESGEelegeaegylvfkQPWPgimRTIYGNHTRF-----------ETTYFKKFPGYYV---------------TGD 523
Cdd:PRK13388 324 -IYNPETL-------------TECA---VARFDAHGALlnadeaigelvNTAGAGFFEGYYNnpeataermrhgmywSGD 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 524 GCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFS-STLTEEL 602
Cdd:PRK13388 387 LAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATFDpDAFAAFL 466
|
410 420 430
....*....|....*....|....*....|....*..
gi 1538017002 603 KKQirEKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 639
Cdd:PRK13388 467 AAQ--PDLGTKAWPRYVRIAADLPSTATNKVLKRELI 501
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
53-573 |
3.50e-21 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 97.86 E-value: 3.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 53 VLDRNVheKKLGDKVAFYWEGNepGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGAL 132
Cdd:COG1022 16 LLRRRA--ARFPDRVALREKED--GIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 133 HSIVFAGFSAESLcERIL-DSSCSLLITTDAfyrgEKLVNLKELADE--SLEKcrekgfpvrccIVVkhvgraelgMNds 209
Cdd:COG1022 92 TVPIYPTSSAEEV-AYILnDSGAKVLFVEDQ----EQLDKLLEVRDElpSLRH-----------IVV---------LD-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 210 psqsPPVKRQCPDVqiswnegvdLWWHELMQEAGDEFEPEW-------CDAEDPLFILYTSGSTGKPKlcagsicwsvem 282
Cdd:COG1022 145 ----PRGLRDDPRL---------LSLDELLALGREVADPAElearraaVKPDDLATIIYTSGTTGRPK------------ 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 283 dtkpqpedpfspqGVVHTIGGyMLYVATTFKYVFDFHPEDVF-----WCtadigWITGHSyVTYGPLANGATSVLFEGI- 356
Cdd:COG1022 200 -------------GVMLTHRN-LLSNARALLERLPLGPGDRTlsflpLA-----HVFERT-VSYYALAAGATVAFAESPd 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 357 ----------PTY----PdesRLW-SIVDKYkVTKFYTAPTAIRML----MKFGdepvTKHSRASLQvlgtvGEPINPEA 417
Cdd:COG1022 260 tlaedlrevkPTFmlavP---RVWeKVYAGI-QAKAEEAGGLKRKLfrwaLAVG----RRYARARLA-----GKSPSLLL 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 418 WLWY---HRVVGSQhcpivdtfWQTETGGHMLTPLPGATPMKPGSASFpFFGV--------------APAILNESGEele 480
Cdd:COG1022 327 RLKHalaDKLVFSK--------LREALGGRLRFAVSGGAALGPELARF-FRALgipvlegygltetsPVITVNRPGD--- 394
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 481 geaegylvFK-----QPWPG-----------------IMRtiyGnhtrfettYFKKfP----------GYYVTGD-GcRR 527
Cdd:COG1022 395 --------NRigtvgPPLPGvevkiaedgeilvrgpnVMK---G--------YYKN-PeataeafdadGWLHTGDiG-EL 453
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1538017002 528 DQDGYYWITGRIDDMLNVS-GHLLSTAEVESALVEHEAVAEAAVVGH 573
Cdd:COG1022 454 DEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVVVGD 500
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
78-638 |
3.75e-21 |
|
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: 97.00 E-value: 3.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 78 ETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLL 157
Cdd:cd12115 21 GDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 158 ITtdafyrgeklvnlkeladeslekcrekgfpvrccivvkhvgraelgmndspsqsppvkrqcpdvqiswnegvdlwwhe 237
Cdd:cd12115 101 LT------------------------------------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 238 lmqeagdefepewcDAEDPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGVVHTIGGymlyvATTFkyvfd 317
Cdd:cd12115 103 --------------DPDDLAYVIYTSGSTGRPK-------------------------GVAIEHRN-----AAAF----- 133
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 318 fhpedVFWCTADIG--WITGHSYVT-----------YGPLANGATSVLFEGIPTYPDESRLwsivdkYKVTKFYTAPTAI 384
Cdd:cd12115 134 -----LQWAAAAFSaeELAGVLASTsicfdlsvfelFGPLATGGKVVLADNVLALPDLPAA------AEVTLINTVPSAA 202
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 385 RMLMKFGDEPvtkhsrASLQVLGTVGEPINPEAwlwYHRVVGSQHC--------PIVDTFWQTetgGHMLTPLPGATPmk 456
Cdd:cd12115 203 AELLRHDALP------ASVRVVNLAGEPLPRDL---VQRLYARLQVervvnlygPSEDTTYST---VAPVPPGASGEV-- 268
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 457 pgSASFPFFGVAPAILNEsgeelegeaegylvFKQPWP-GIMRTIY-GNHT--------------RFETTYFkkFPG--Y 518
Cdd:cd12115 269 --SIGRPLANTQAYVLDR--------------ALQPVPlGVPGELYiGGAGvargylgrpgltaeRFLPDPF--GPGarL 330
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 519 YVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfSSTL 598
Cdd:cd12115 331 YRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPG---AAGL 407
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1538017002 599 TEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 638
Cdd:cd12115 408 VEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
237-640 |
3.76e-21 |
|
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: 97.37 E-value: 3.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 237 ELMQEAGDEFEPEWCDAE-DPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGVVHTIGGYMLyVATTFKYV 315
Cdd:cd12118 115 DLLAEGDPDFEWIPPADEwDPIALNYTSGTTGRPK-------------------------GVVYHHRGAYL-NALANILE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 316 FDFHPEDVFWCTADI----GWItghsyVTYGPLANGATSVLFEGIptypDESRLWSIVDKYKVTKFYTAPTAIRMLMKfG 391
Cdd:cd12118 169 WEMKQHPVYLWTLPMfhcnGWC-----FPWTVAAVGGTNVCLRKV----DAKAIYDLIEKHKVTHFCGAPTVLNMLAN-A 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 392 DEPVTKHSRASLQVLgTVGEPiNPEAWLWYHRVVGSQhcpIVDTFWQTETGGhmltplPGAT-PMKPGSASFPffGVAPA 470
Cdd:cd12118 239 PPSDARPLPHRVHVM-TAGAP-PPAAVLAKMEELGFD---VTHVYGLTETYG------PATVcAWKPEWDELP--TEERA 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 471 ILNESGEELEGEAEGYLVFKQ------PWPG------------IMRTIYGNHtrfETTYfKKFP-GYYVTGDGCRRDQDG 531
Cdd:cd12118 306 RLKARQGVRYVGLEEVDVLDPetmkpvPRDGktigeivfrgniVMKGYLKNP---EATA-EAFRgGWFHSGDLAVIHPDG 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 532 YYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfSSTLTEELKKQIREKIG 611
Cdd:cd12118 382 YIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEG---AKVTEEEIIAFCREHLA 458
|
410 420
....*....|....*....|....*....
gi 1538017002 612 PIATPDYIQNAPgLPKTRSGKIMRRVLRK 640
Cdd:cd12118 459 GFMVPKTVVFGE-LPKTSTGKIQKFVLRD 486
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
77-572 |
4.86e-21 |
|
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: 96.51 E-value: 4.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 77 GETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESlCERIL-DSSCS 155
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQ-IAYILnDSEAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 156 LLITTDAfyrgeklvnlkeladeslekcrekgfpvrccivvkhvgraelgmndspsqsppvkrqcpdvqiswnegvdlww 235
Cdd:cd05907 80 ALFVEDP------------------------------------------------------------------------- 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 236 helmqeagdefepewcdaEDPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGVVHTIGGYMLYVATTFKYV 315
Cdd:cd05907 87 ------------------DDLATIIYTSGTTGRPK-------------------------GVMLSHRNILSNALALAERL 123
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 316 fDFHPEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDESRlwsivdKYKVTKFYTAP-------------- 381
Cdd:cd05907 124 -PATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSAETLLDDLS------EVRPTVFLAVPrvwekvyaaikvka 196
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 382 -TAIRMLMkfgdepVTKHSRASLQVLGTVGEPINPEAWLWYHRvVGsqhCPIVDTFWQTETGGHMLTPLPGATpmKPGSA 460
Cdd:cd05907 197 vPGLKRKL------FDLAVGGRLRFAASGGAPLPAELLHFFRA-LG---IPVYEGYGLTETSAVVTLNPPGDN--RIGTV 264
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 461 SFPFFGVAPAILNESGeelegeaegyLVFKQpwPGIMRTIYGN--HTRFETTYfkkfPGYYVTGDGCRRDQDGYYWITGR 538
Cdd:cd05907 265 GKPLPGVEVRIADDGE----------ILVRG--PNVMLGYYKNpeATAEALDA----DGWLHTGDLGEIDEDGFLHITGR 328
|
490 500 510
....*....|....*....|....*....|....*
gi 1538017002 539 IDDML-NVSGHLLSTAEVESALVEHEAVAEAAVVG 572
Cdd:cd05907 329 KKDLIiTSGGKNISPEPIENALKASPLISQAVVIG 363
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
53-640 |
9.65e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 96.61 E-value: 9.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 53 VLDRNVHEkkLGDKVAFYWEGNEpgettkITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGA- 131
Cdd:PRK05605 37 LYDNAVAR--FGDRPALDFFGAT------TTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAv 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 132 --LHSIVFAGFSAESLCE----RIL---DSSCSLLITTDAFYRGEKLVN---------LKELADE-SLEKCREKgfpvrc 192
Cdd:PRK05605 109 vvEHNPLYTAHELEHPFEdhgaRVAivwDKVAPTVERLRRTTPLETIVSvnmiaamplLQRLALRlPIPALRKA------ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 193 civvkhvgRAELgmndspsqSPPVkrqcPDVqISWNEGVDlwwhELMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPK-- 270
Cdd:PRK05605 183 --------RAAL--------TGPA----PGT-VPWETLVD----AAIGGDGSDVSHPRPTPDDVALILYTSGTTGKPKga 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 271 -LCAGSICWSVEMDTKPQPEDPFSPQGVvhtiggymlYVATTFkyvfdFHPEDVFWCtadigwitghsyVTYGPLAnGAT 349
Cdd:PRK05605 238 qLTHRNLFANAAQGKAWVPGLGDGPERV---------LAALPM-----FHAYGLTLC------------LTLAVSI-GGE 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 350 SVLFegiPTyPDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEP-VTKHS-RASLQvlGTVGEPInpeawlwyhrvvgs 427
Cdd:PRK05605 291 LVLL---PA-PDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERgVDLSGvRNAFS--GAMALPV-------------- 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 428 qhcPIVDTfWQTETGGHM-----LT---PLPGATPM----KPGSASFPFFGVAPAILNESGEELEGEAEGY--LVFKQPw 493
Cdd:PRK05605 351 ---STVEL-WEKLTGGLLvegygLTetsPIIVGNPMsddrRPGYVGVPFPDTEVRIVDPEDPDETMPDGEEgeLLVRGP- 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 494 pgimRTIYGNHTRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGH 573
Cdd:PRK05605 426 ----QVFKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGL 501
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1538017002 574 PHPVKGECLYCFVTLCDGHTFSStltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 640
Cdd:PRK05605 502 PREDGSEEVVAAVVLEPGAALDP---EGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVRE 565
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
82-641 |
4.16e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 94.22 E-value: 4.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 82 ITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITTD 161
Cdd:PRK07788 75 LTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKALVYDD 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 162 AFyrgeklVNLKELADESLEKCRekgfpvrccivvkhvgraelGMNDSPSQSPPVKRQCPDVQiswnegvdlwwhELMQE 241
Cdd:PRK07788 155 EF------TDLLSALPPDLGRLR--------------------AWGGNPDDDEPSGSTDETLD------------DLIAG 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 242 AGDEFEPEWcdAEDPLFILYTSGSTGKPKlcaGSicwsvemdtkPQPEdPFSPQgvvhTIGGYMLYVAttfkyvfdFHPE 321
Cdd:PRK07788 197 SSTAPLPKP--PKPGGIVILTSGTTGTPK---GA----------PRPE-PSPLA----PLAGLLSRVP--------FRAG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 322 DVFWCTADIGWITGHSYVTYGpLANGATSVL---FegiptypDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVTKH 398
Cdd:PRK07788 249 ETTLLPAPMFHATGWAHLTLA-MALGSTVVLrrrF-------DPEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 399 SRASLQVLGTVGEPINPEAWLWYHRVVGsqhcPIVDTFW-QTETGGHMLtplpgATP----MKPGSASFPFFGVAPAILN 473
Cdd:PRK07788 321 DTSSLKIIFVSGSALSPELATRALEAFG----PVLYNLYgSTEVAFATI-----ATPedlaEAPGTVGRPPKGVTVKILD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 474 ESGeelegeaegylvfkQPWP-GIMRTIY-GNHTRFETtYF-----KKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVS 546
Cdd:PRK07788 392 ENG--------------NEVPrGVVGRIFvGNGFPFEG-YTdgrdkQIIDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSG 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 547 GHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfsSTLTEE-LKKQIREKIGPIATPDYIQNAPGL 625
Cdd:PRK07788 457 GENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPG----AALDEDaIKDYVRDNLARYKVPRDVVFLDEL 532
|
570
....*....|....*.
gi 1538017002 626 PKTRSGKIMRRVLRKI 641
Cdd:PRK07788 533 PRNPTGKVLKRELREM 548
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
77-638 |
1.33e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 94.25 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 77 GETTkITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSL 156
Cdd:PRK12316 533 GEET-LDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQL 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 157 LITTDAFyrGEKLvnlkeladeslekcrekgfPVrccivvkhvgraelgmndspsqSPPVKRQCPDVQISWNEGvdlWWH 236
Cdd:PRK12316 612 LLSQSHL--GRKL-------------------PL----------------------AAGVQVLDLDRPAAWLEG---YSE 645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 237 ElmqeagdefEPEWC-DAEDPLFILYTSGSTGKPKLCAGS-------ICWSVEMDTKPqpedpfspqgvvhtIGGYMLYV 308
Cdd:PRK12316 646 E---------NPGTElNPENLAYVIYTSGSTGKPKGAGNRhralsnrLCWMQQAYGLG--------------VGDTVLQK 702
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 309 aTTFKyvFDFHPEDVFWctadigwitghsyvtygPLANGATSVLF-EGIPTYPDesRLWSIVDKYKVTKFYTAPTAIRML 387
Cdd:PRK12316 703 -TPFS--FDVSVWEFFW-----------------PLMSGARLVVAaPGDHRDPA--KLVELINREGVDTLHFVPSMLQAF 760
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 388 MKFGDEPvtkhSRASLQVLGTVGEPINPEAWLwyhRVVGSQ-HCPIVDTFWQTETGghmlTPLPGATPMKPGSASF---- 462
Cdd:PRK12316 761 LQDEDVA----SCTSLRRIVCSGEALPADAQE---QVFAKLpQAGLYNLYGPTEAA----IDVTHWTCVEEGGDSVpigr 829
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 463 PFFGVAPAILNESGeelegeaegylvfkQPWP-GIMRTIY--------GNHTRFETTYFKKFPGYYV-------TGDGCR 526
Cdd:PRK12316 830 PIANLACYILDANL--------------EPVPvGVLGELYlagrglarGYHGRPGLTAERFVPSPFVagermyrTGDLAR 895
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 527 RDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGhphpVKGECLYCFVTLCDGhtfSSTLTEELKKQI 606
Cdd:PRK12316 896 YRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDGKQLVGYVVLESE---GGDWREALKAHL 968
|
570 580 590
....*....|....*....|....*....|..
gi 1538017002 607 REKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 638
Cdd:PRK12316 969 AASLPEYMVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
62-639 |
4.14e-19 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 90.90 E-value: 4.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 62 KLGDKVAFYWEgNEPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFS 141
Cdd:PRK08008 19 VYGHKTALIFE-SSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 142 AESlCERILDSS-CSLLITTDAFYrgeklvnlkELADESLekcREKGFPVRCCIVVKHVGRAELGMND---SPSQSPPVK 217
Cdd:PRK08008 98 REE-SAWILQNSqASLLVTSAQFY---------PMYRQIQ---QEDATPLRHICLTRVALPADDGVSSftqLKAQQPATL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 218 RQCPDVQiswnegvdlwwhelmqeagdefepewcdAEDPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGV 297
Cdd:PRK08008 165 CYAPPLS----------------------------TDDTAEILFTSGTTSRPK-------------------------GV 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 298 VHT-----IGGYmlY----VATTFKYVF-----DFHPEdvFWCTADIGWITGhsyvtygplanGATSVLFEgipTYpDES 363
Cdd:PRK08008 192 VIThynlrFAGY--YsawqCALRDDDVYltvmpAFHID--CQCTAAMAAFSA-----------GATFVLLE---KY-SAR 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 364 RLWSIVDKYKVTKFYTAPTAIRMLMKfgdEPVTKHSRaslqvlgtvgepinpeawlwyhrvvgsQHC--------PIVD- 434
Cdd:PRK08008 253 AFWGQVCKYRATITECIPMMIRTLMV---QPPSANDR---------------------------QHClrevmfylNLSDq 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 435 ---------------TFWQTETGGHMLTPLPGATPMKPgSASFPFFGVAPAILNESGEELEGEAEGYLVFK-QPWPGIMR 498
Cdd:PRK08008 303 ekdafeerfgvrlltSYGMTETIVGIIGDRPGDKRRWP-SIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKgVPGKTIFK 381
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 499 TIYGNHTrfETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVK 578
Cdd:PRK08008 382 EYYLDPK--ATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIR 459
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1538017002 579 GECLYCFVTLCDGHTFSstlTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 639
Cdd:PRK08008 460 DEAIKAFVVLNEGETLS---EEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
82-639 |
1.11e-18 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 89.82 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 82 ITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITTD 161
Cdd:PRK13382 69 LTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYDE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 162 AFyrgeklvnlKELADESLEKCrekgfpvrccivvkhvgraelgmndspsqsPPVKRQcpdvqISWNEGVDLWWHELMQE 241
Cdd:PRK13382 149 EF---------SATVDRALADC------------------------------PQATRI-----VAWTDEDHDLTVEVLIA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 242 AGDEFEPEWCDAEDPLfILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGVVHT-IGGYMlyvatTFKYVFDFHP 320
Cdd:PRK13382 185 AHAGQRPEPTGRKGRV-ILLTSGTTGTPK-------------------------GARRSgPGGIG-----TLKAILDRTP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 321 edvfwctadigWITGHSYVTYGPL--ANGATSVLFEGIPTYP-------DESRLWSIVDKYKVTKFYTAPTAIRMLMKFG 391
Cdd:PRK13382 234 -----------WRAEEPTVIVAPMfhAWGFSQLVLAASLACTivtrrrfDPEATLDLIDRHRATGLAVVPVMFDRIMDLP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 392 DEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGSQhcpIVDTFWQTETGghMLTPlpgATP----MKPGSASFPFFGV 467
Cdd:PRK13382 303 AEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDV---IYNNYNATEAG--MIAT---ATPadlrAAPDTAGRPAEGT 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 468 APAILNESgeelegeaegylvFKQPWPGIMRTIY-GNHTRFE-----TTyfKKF-PGYYVTGDGCRRDQDGYYWITGRID 540
Cdd:PRK13382 375 EIRILDQD-------------FREVPTGEVGTIFvRNDTQFDgytsgST--KDFhDGFMASGDVGYLDENGRLFVVGRDD 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 541 DMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfSSTLTEELKKQIREKIGPIATPDYIQ 620
Cdd:PRK13382 440 EMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPG---ASATPETLKQHVRDNLANYKVPRDIV 516
|
570
....*....|....*....
gi 1538017002 621 NAPGLPKTRSGKIMRRVLR 639
Cdd:PRK13382 517 VLDELPRGATGKILRRELQ 535
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
78-636 |
2.25e-18 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 88.79 E-value: 2.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 78 ETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGAlhsIVFAgfsaeslceriLDSScslL 157
Cdd:PRK05852 40 DRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADL---VVVP-----------LDPA---L 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 158 ITTDAFYRGEKLVNLKELADeSLEKCREKGFPVRCCIVVKHVGRAELGMNDSPSQSPPVKRQcPDVQISWNEGVdlwwhe 237
Cdd:PRK05852 103 PIAEQRVRSQAAGARVVLID-ADGPHDRAEPTTRWWPLTVNVGGDSGPSGGTLSVHLDAATE-PTPATSTPEGL------ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 238 lmqeagdefepewcdAEDPLFILYTSGSTGKPKLCagsicwsvemdtkpqPEDPFSPQGVVHTI-GGYMLyvattfkyvf 316
Cdd:PRK05852 175 ---------------RPDDAMIMFTGGTTGLPKMV---------------PWTHANIASSVRAIiTGYRL---------- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 317 dfHPEDVfwCTADIGWITGHSYVT--YGPLANGATSVLfegiptyPDESRL-----WSIVDKYKVTKFYTAPTAIRMLMK 389
Cdd:PRK05852 215 --SPRDA--TVAVMPLYHGHGLIAalLATLASGGAVLL-------PARGRFsahtfWDDIKAVGATWYTAVPTIHQILLE 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 390 FGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGSqhcPIVDTFWQTET---------GGHMLTPLPGATPMKPGSA 460
Cdd:PRK05852 284 RAATEPSGRKPAALRFIRSCSAPLTAETAQALQTEFAA---PVVCAFGMTEAthqvtttqiEGIGQTENPVVSTGLVGRS 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 461 SFPFFGVA--------PAILNesgeelegeaegylvfkQPW---PGIMRTIYGNHtrfETTYFKKFPGYYVTGDGCRRDQ 529
Cdd:PRK05852 361 TGAQIRIVgsdglplpAGAVG-----------------EVWlrgTTVVRGYLGDP---TITAANFTDGWLRTGDLGSLSA 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 530 DGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSStltEELKKQIREK 609
Cdd:PRK05852 421 AGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTA---EELVQFCRER 497
|
570 580
....*....|....*....|....*..
gi 1538017002 610 IGPIATPDYIQNAPGLPKTRSGKIMRR 636
Cdd:PRK05852 498 LAAFEIPASFQEASGLPHTAKGSLDRR 524
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
517-639 |
9.37e-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: 9.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 517 GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSS 596
Cdd:cd05917 230 GWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTE 309
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1538017002 597 tltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 639
Cdd:cd05917 310 ---EDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
61-638 |
1.16e-17 |
|
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: 86.23 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 61 KKLGDKVAFYWEGNepgettKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGF 140
Cdd:cd17655 8 EKTPDHTAVVFEDQ------TLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 141 SAESLcERIL-DSSCSLLITTDAFYRGEKlvnlkeladeslekcrekgfpvrccivvkHVGRAELgMNDSPSQSppvkrq 219
Cdd:cd17655 82 PEERI-QYILeDSGADILLTQSHLQPPIA-----------------------------FIGLIDL-LDEDTIYH------ 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 220 cpdvqiswnegvdlwwhelmqEAGDEFEPEwCDAEDPLFILYTSGSTGKPKlcagsicwSVEMDTkpqpedpfspQGVVH 299
Cdd:cd17655 125 ---------------------EESENLEPV-SKSDDLAYVIYTSGSTGKPK--------GVMIEH----------RGVVN 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 300 TIGGY--------MLYVATTFKYVFDFHPEDVFwctadigwitghsyvtyGPLANGATSVLfegiptYPDESR-----LW 366
Cdd:cd17655 165 LVEWAnkviyqgeHLRVALFASISFDASVTEIF-----------------ASLLSGNTLYI------VRKETVldgqaLT 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 367 SIVDKYKVTKFYTAPTAIRMLMKFGDEPvtkhsRASLQVLGTVGEPINPE-AWLWYHRVVGSqhCPIVDTFWQTETG-GH 444
Cdd:cd17655 222 QYIRQNRITIIDLTPAHLKLLDAADDSE-----GLSLKHLIVGGEALSTElAKKIIELFGTN--PTITNAYGPTETTvDA 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 445 MLTPLpgaTPMKPGSASFPffgVAPAILNESGeelegeaegYLVFK--QPWP-GIMRTIY--------GNHTRFETTYfK 513
Cdd:cd17655 295 SIYQY---EPETDQQVSVP---IGKPLGNTRI---------YILDQygRPQPvGVAGELYiggegvarGYLNRPELTA-E 358
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 514 KF------PG--YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCF 585
Cdd:cd17655 359 KFvddpfvPGerMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAY 438
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 1538017002 586 VTlCDGHTFSSTLTEELKKQIREKIgpiaTPDYIQNAPGLPKTRSGKIMRRVL 638
Cdd:cd17655 439 IV-SEKELPVAQLREFLARELPDYM----IPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
80-642 |
1.30e-17 |
|
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: 86.23 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 80 TKITYRELLVQVCQFSNVLRKQGIQkGDRVAIYMPMILELVVAMLACARLGALhsIVFAGFSAEslcERILDSSCSL--- 156
Cdd:cd05909 6 TSLTYRKLLTGAIALARKLAKMTKE-GENVGVMLPPSAGGALANFALALSGKV--PVMLNYTAG---LRELRACIKLagi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 157 --LITTDAFYRGEKLVNLKELADE----SLEKCREK-GFPVRCcivvkhvgRAELGMNDSPSqsppvkrqcpdvqiswne 229
Cdd:cd05909 80 ktVLTSKQFIEKLKLHHLFDVEYDarivYLEDLRAKiSKADKC--------KAFLAGKFPPK------------------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 230 gvdlWWHELMQEAGDefepewcDAEDPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGVVHTIGGYMLYVA 309
Cdd:cd05909 134 ----WLLRIFGVAPV-------QPDDPAVILFTSGSEGLPK-------------------------GVVLSHKNLLANVE 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 310 TTFKyVFDFHPEDVFWCTADIGWITGHSYVTYGPLANGAtSVLFEGIPTYPDesRLWSIVDKYKVTKFYTAPTAIRMLMK 389
Cdd:cd05909 178 QITA-IFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGI-KVVFHPNPLDYK--KIPELIYDKKATILLGTPTFLRGYAR 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 390 FgdepVTKHSRASLQVLGTVGEPINPEAW-LWYHRvvgsQHCPIVDTFWQTETGGHMLTPLPgATPMKPGSASFPFFGVA 468
Cdd:cd05909 254 A----AHPEDFSSLRLVVAGAEKLKDTLRqEFQEK----FGIRILEGYGTTECSPVISVNTP-QSPNKEGTVGRPLPGME 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 469 PAILNESGEELEGEAEGYLVFKQPwPGIMRTIYGNHtrfETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGH 548
Cdd:cd05909 325 VKIVSVETHEEVPIGEGGLLLVRG-PNVMLGYLNEP---ELTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGE 400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 549 LLSTAEVESALVEHEAV-AEAAVVGHPHPVKGECLYCFVTLcdghtfSSTLTEELKKQIRE-KIGPIATPDYIQNAPGLP 626
Cdd:cd05909 401 MVSLEAIEDILSEILPEdNEVAVVSVPDGRKGEKIVLLTTT------TDTDPSSLNDILKNaGISNLAKPSYIHQVEEIP 474
|
570
....*....|....*.
gi 1538017002 627 KTRSGKIMRRVLRKIA 642
Cdd:cd05909 475 LLGTGKPDYVTLKALA 490
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
517-639 |
2.14e-17 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 85.88 E-value: 2.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 517 GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDghtfsS 596
Cdd:PRK08974 432 GWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKD-----P 506
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1538017002 597 TLT-EELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 639
Cdd:PRK08974 507 SLTeEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
78-644 |
3.01e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 85.22 E-value: 3.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 78 ETTKITYRELLVQVCQFSNVLRKQGiQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLL 157
Cdd:PRK07638 23 NDRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 158 ITtDAFYrgeklvnlkeladeslekcrekgfpvrccivvkhvgraelgMNDSPSQSPPVkrqcpdvqISWNEgvdlwWHE 237
Cdd:PRK07638 102 VT-ERYK-----------------------------------------LNDLPDEEGRV--------IEIDE-----WKR 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 238 LMQEAGDEFEPEwCDAE-DPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedPF--SPQGVVHTIggymlyvaTTFKY 314
Cdd:PRK07638 127 MIEKYLPTYAPI-ENVQnAPFYMGFTSGSTGKPK--------------------AFlrAQQSWLHSF--------DCNVH 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 315 VFDFHPEDVFWctadigwITG---HSYVTYGplangATSVLFEG-----IPTY-PDESRLWsiVDKYKVTKFYTAPTAIR 385
Cdd:PRK07638 178 DFHMKREDSVL-------IAGtlvHSLFLYG-----AISTLYVGqtvhlMRKFiPNQVLDK--LETENISVMYTVPTMLE 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 386 MLMK---FGDEPVT------KHSRASLQVLGTvgepINPEAWLWyhrvvgsqhcpivdTFWQTETGGHMLTPLPGATPMK 456
Cdd:PRK07638 244 SLYKenrVIENKMKiissgaKWEAEAKEKIKN----IFPYAKLY--------------EFYGASELSFVTALVDEESERR 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 457 PGSASFPFFGVAPAILNESGeelegeaegylvfKQPWPGIMRTIYGNHTRFettyfkkFPGYYVTGDGCRR--------- 527
Cdd:PRK07638 306 PNSVGRPFHNVQVRICNEAG-------------EEVQKGEIGTVYVKSPQF-------FMGYIIGGVLARElnadgwmtv 365
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 528 ------DQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLycfVTLCDGHTFSstltEE 601
Cdd:PRK07638 366 rdvgyeDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKP---VAIIKGSATK----QQ 438
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1538017002 602 LKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQN 644
Cdd:PRK07638 439 LKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWIEN 481
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
63-641 |
4.58e-17 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 84.81 E-value: 4.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 63 LGDKVAFYWEGnepgetTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSA 142
Cdd:PRK06155 34 YPDRPLLVFGG------TRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 143 ESLcERILDSSCSLLITTDAfyrgeKLVNLKELADESLEKCREKGFpvrccIVVKHVGRAELGMNDSPSqsPPVKRQCPD 222
Cdd:PRK06155 108 PQL-EHILRNSGARLLVVEA-----ALLAALEAADPGDLPLPAVWL-----LDAPASVSVPAGWSTAPL--PPLDAPAPA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 223 VQISwnegvdlwwhelmqeagdefepewcdAEDPLFILYTSGSTGKPKlcaGSICwsvemdtkpqpedpfsPQGVVHTIG 302
Cdd:PRK06155 175 AAVQ--------------------------PGDTAAILYTSGTTGPSK---GVCC----------------PHAQFYWWG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 303 GYMlyvattfkyvfdfhpedvfwcTADIGWITGHSYVTYGPL-------------ANGATSVLFEGIPTypdeSRLWSIV 369
Cdd:PRK06155 210 RNS---------------------AEDLEIGADDVLYTTLPLfhtnalnaffqalLAGATYVLEPRFSA----SGFWPAV 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 370 DKYKVTKFYTAPTAIRMLMKfgdEPVTKHSRAS-LQV-LGTVGEPINPEAWLWYHRVvgsqhcPIVDTFWQTETGGHMLT 447
Cdd:PRK06155 265 RRHGATVTYLLGAMVSILLS---QPARESDRAHrVRVaLGPGVPAALHAAFRERFGV------DLLDGYGSTETNFVIAV 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 448 PLPGAtpmKPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTIYGNHTRFETTYFKKFpgYYVTGDGCRR 527
Cdd:PRK06155 336 THGSQ---RPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRADEPFAFATGYFGMPEKTVEAWRNL--WFHTGDRVVR 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 528 DQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSStltEELKKQIR 607
Cdd:PRK06155 411 DADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEP---VALVRHCE 487
|
570 580 590
....*....|....*....|....*....|....
gi 1538017002 608 EKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKI 641
Cdd:PRK06155 488 PRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQ 521
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
259-639 |
9.03e-17 |
|
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: 83.58 E-value: 9.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 259 ILYTSGSTGKPKLCagsicwsvemdtkpQPEDPFSPQGVVHTIGgymlyvattFKYVFDFHPEDVFWCTADIGWITGHSy 338
Cdd:cd05929 130 MLYSGGTTGRPKGI--------------KRGLPGGPPDNDTLMA---------AALGFGPGADSVYLSPAPLYHAAPFR- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 339 VTYGPLANGATSVLFEGIptypDESRLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVTKHSRASLQVLGTVGEPINP--- 415
Cdd:cd05929 186 WSMTALFMGGTLVLMEKF----DPEEFLRLIERYRVTFAQFVPTMFVRLLKLPEAVRNAYDLSSLKRVIHAAAPCPPwvk 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 416 EAWL-WYHrvvgsqhcPIVDTFWQ-TETGGhmLTPLPGATPMK-PGSASFPFFGVApAILNESGEelegeaegylvfKQP 492
Cdd:cd05929 262 EQWIdWGG--------PIIWEYYGgTEGQG--LTIINGEEWLThPGSVGRAVLGKV-HILDEDGN------------EVP 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 493 wPGIMRTIY--GNHTRFETTYFKKFP------GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEA 564
Cdd:cd05929 319 -PGEIGEVYfaNGPGFEYTNDPEKTAaarnegGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPK 397
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1538017002 565 VAEAAVVGHPHPVKGECLYCFVTLCDGHTFSSTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 639
Cdd:cd05929 398 VLDAAVVGVPDEELGQRVHAVVQPAPGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
255-642 |
9.56e-17 |
|
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: 81.99 E-value: 9.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 255 DPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGVVHTIGGyMLYVATTFKYVFDFHPEDVFWCTADIGWIT 334
Cdd:cd17630 1 RLATVILTSGSTGTPK-------------------------AVVHTAAN-LLASAAGLHSRLGFGGGDSWLLSLPLYHVG 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 335 GHSYVTYGPLANGATSVLFEGIPTYPDESRlwsivdkYKVTKFYTAPTAIRMLMkfgDEPVTKHSRASLQVLGTVGEPIN 414
Cdd:cd17630 55 GLAILVRSLLAGAELVLLERNQALAEDLAP-------PGVTHVSLVPTQLQRLL---DSGQGPAALKSLRAVLLGGAPIP 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 415 PEAwlwyHRVVGSQHCPIVDTFWQTETGGHMLTPLPGATpmKPGSASFPFFGVAPAILNESGEelegeaegylvfkqpWP 494
Cdd:cd17630 125 PEL----LERAADRGIPLYTTYGMTETASQVATKRPDGF--GRGGVGVLLPGRELRIVEDGEI---------------WV 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 495 GIMRTIYGNHTRFETTYFKKfPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHP 574
Cdd:cd17630 184 GGASLAMGYLRGQLVPEFNE-DGWFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVP 262
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1538017002 575 HPVKGECLYCFVTLCDGHTfsstlTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 642
Cdd:cd17630 263 DEELGQRPVAVIVGRGPAD-----PAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
79-638 |
1.09e-16 |
|
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: 82.90 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 79 TTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLI 158
Cdd:cd17650 10 TRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 159 Ttdafyrgeklvnlkeladeslekcrekgfpvrccivvkhvgraelgmndspsqsppvkrqcpdvqiswnegvdlwwhel 238
Cdd:cd17650 90 T------------------------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 239 mqeagdefepewcDAEDPLFILYTSGSTGKPK--------LCAGSICWSVEMDTkpqpeDPFSPQgvvhtiggyMLYVAT 310
Cdd:cd17650 91 -------------QPEDLAYVIYTSGTTGKPKgvmvehrnVAHAAHAWRREYEL-----DSFPVR---------LLQMAS 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 311 tfkyvFDFhpeDVFwcTADIGWitghsyvtygPLANGATSVLfegIP--TYPDESRLWSIVDKYKVTKFYTAPTAIRMLM 388
Cdd:cd17650 144 -----FSF---DVF--AGDFAR----------SLLNGGTLVI---CPdeVKLDPAALYDLILKSRITLMESTPALIRPVM 200
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 389 KFGDEPVTKHSRASLQVLGTVGEPINPEAWLwYHRVvgSQHCPIVDTFWQTET--------GGhmLTPLPGATPMKPGSa 460
Cdd:cd17650 201 AYVYRNGLDLSAMRLLIVGSDGCKAQDFKTL-AARF--GQGMRIINSYGVTEAtidstyyeEG--RDPLGDSANVPIGR- 274
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 461 sfPFFGVAPAILNESGeelegeaegylvfkQPWP-GIMRTIY--------GNHTRFETTYfKKF------PG--YYVTGD 523
Cdd:cd17650 275 --PLPNTAMYVLDERL--------------QPQPvGVAGELYiggagvarGYLNRPELTA-ERFvenpfaPGerMYRTGD 337
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 524 GCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHpHPVKGE---CLYCFVTlcdghtfSSTLTE 600
Cdd:cd17650 338 LARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVR-EDKGGEarlCAYVVAA-------ATLNTA 409
|
570 580 590
....*....|....*....|....*....|....*...
gi 1538017002 601 ELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 638
Cdd:cd17650 410 ELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
35-641 |
1.96e-16 |
|
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: 82.96 E-value: 1.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 35 GKIFTEWMKGATTNICYNVLDRnvhEKKLGDKVAFYWEGNEpgetTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMP 114
Cdd:cd17642 5 PGPFYPLEDGTAGEQLHKAMKR---YASVPGTIAFTDAHTG----VNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 115 MILELVVAMLACARLGalhsiVFAGFSAESLCERILDSSCSLLITTDAFYRGEKLvnlkeladESLEKCREKGFPVRCCI 194
Cdd:cd17642 78 NSLQFFLPVIAGLFIG-----VGVAPTNDIYNERELDHSLNISKPTIVFCSKKGL--------QKVLNVQKKLKIIKTII 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 195 VVKhvGRAELGmndspsqsppvKRQCPDVQISWNEGVDLWWHELMQEAGDEfepewcdAEDPLFILYTSGSTGKPK---L 271
Cdd:cd17642 145 ILD--SKEDYK-----------GYQCLYTFITQNLPPGFNEYDFKPPSFDR-------DEQVALIMNSSGSTGLPKgvqL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 272 CAGSICwsVEMDTKPQPedpfspqgvvhtIGGYMLYVATTFKYVFDFHpeDVFWCTADIGWITGhsyvtygplanGATSV 351
Cdd:cd17642 205 THKNIV--ARFSHARDP------------IFGNQIIPDTAILTVIPFH--HGFGMFTTLGYLIC-----------GFRVV 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 352 LfegIPTYPDESRLWSIVDkYKVTKFYTAPTAIRMLMKfgDEPVTKHSRASLQVLGTVGEPINPEawlwyhrvVGSQ--- 428
Cdd:cd17642 258 L---MYKFEEELFLRSLQD-YKVQSALLVPTLFAFFAK--STLVDKYDLSNLHEIASGGAPLSKE--------VGEAvak 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 429 --HCPIV-DTFWQTETGGHML-TPlpgATPMKPGSAS--FPFFGvAPAILNESGEELEGEAEGYLVFKQPwpGIMRTIYG 502
Cdd:cd17642 324 rfKLPGIrQGYGLTETTSAILiTP---EGDDKPGAVGkvVPFFY-AKVVDLDTGKTLGPNERGELCVKGP--MIMKGYVN 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 503 NHTRFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECL 582
Cdd:cd17642 398 NPEATKALIDKD--GWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELP 475
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1538017002 583 YCFVTLCDGhtfsSTLTEelkKQIREKIGPIATPDY-----IQNAPGLPKTRSGKIMRRVLRKI 641
Cdd:cd17642 476 AAVVVLEAG----KTMTE---KEVMDYVASQVSTAKrlrggVKFVDEVPKGLTGKIDRRKIREI 532
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
255-635 |
2.56e-16 |
|
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: 80.53 E-value: 2.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 255 DPLFILYTSGSTGKPKLCAGSI-CWsveMDTKPQPEDPFSpqgvvhtiggymlyvattfkyvfdFHPEDvfwctadigwi 333
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSErSW---IESFVCNEDLFN------------------------ISGED----------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 334 tghSYVTYGPLA-----NGATSVLFEG----IPTYPDESRLWSIVDKYKVTKFYTAPTAIRMLMKFgDEPVTKhsrasLQ 404
Cdd:cd17633 43 ---AILAPGPLShslflYGAISALYLGgtfiGQRKFNPKSWIRKINQYNATVIYLVPTMLQALART-LEPESK-----IK 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 405 VLGTVGEPINPEAwlwyHRVV--GSQHCPIVDTFWQTETGghMLTPLPGATPMKPGSASFPFFGVAPAILNESGeelege 482
Cdd:cd17633 114 SIFSSGQKLFEST----KKKLknIFPKANLIEFYGTSELS--FITYNFNQESRPPNSVGRPFPNVEIEIRNADG------ 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 483 aegylvfkqpwpGIMRTIYGNHTRFETTY----FKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESA 558
Cdd:cd17633 182 ------------GEIGKIFVKSEMVFSGYvrggFSNPDGWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESV 249
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1538017002 559 LVEHEAVAEAAVVGHPHPVKGEcLYCFVTLCDGHTFSSTLTEELKKQIREKIgpiatPDYIQNAPGLPKTRSGKIMR 635
Cdd:cd17633 250 LKAIPGIEEAIVVGIPDARFGE-IAVALYSGDKLTYKQLKRFLKQKLSRYEI-----PKKIIFVDSLPYTSSGKIAR 320
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
517-645 |
3.81e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 81.92 E-value: 3.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 517 GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSs 596
Cdd:PRK08162 416 GWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGASAT- 494
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1538017002 597 tlTEELKKQIREKIGPIATPDYIQNAPgLPKTRSGKIMRRVLRKIAQND 645
Cdd:PRK08162 495 --EEEIIAHCREHLAGFKVPKAVVFGE-LPKTSTGKIQKFVLREQAKSL 540
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
75-639 |
1.24e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 80.05 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 75 EPGETtkITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSC 154
Cdd:PRK13390 20 ETGEQ--VSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 155 SLLITTDAfyrgeklvnLKELAdeslekcrekgfpvrccivvkhvgrAELGmNDSPsqsppvkrqcpdVQISWNEGVDLW 234
Cdd:PRK13390 98 RVLVASAA---------LDGLA-------------------------AKVG-ADLP------------LRLSFGGEIDGF 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 235 --WHELMQEAGDEFEPEWCDAedplFILYTSGSTGKPKlcagSICWSVEMDTKPQPEDPfspqgVVHTIGGYmlyvattf 312
Cdd:PRK13390 131 gsFEAALAGAGPRLTEQPCGA----VMLYSSGTTGFPK----GIQPDLPGRDVDAPGDP-----IVAIARAF-------- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 313 kyvFDFHPEDVFWCTADIGwitgHSyvtyGPL-------ANGATSVLFEGIptypDESRLWSIVDKYKVTKFYTAPTAIR 385
Cdd:PRK13390 190 ---YDISESDIYYSSAPIY----HA----APLrwcsmvhALGGTVVLAKRF----DAQATLGHVERYRITVTQMVPTMFV 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 386 MLMKFGDEPVTKHSRASLQVLGTVGEPINPEA------WLWyhrvvgsqhcPIVDTFWQTeTGGHMLTPL-PGATPMKPG 458
Cdd:PRK13390 255 RLLKLDADVRTRYDVSSLRAVIHAAAPCPVDVkhamidWLG----------PIVYEYYSS-TEAHGMTFIdSPDWLAHPG 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 459 SASFPFFGVApAILNESGEELEGEAEGYLVFKQPwpgimRTIYGNHTRFETTYFKKFPG---YYVTGDGCRRDQDGYYWI 535
Cdd:PRK13390 324 SVGRSVLGDL-HICDDDGNELPAGRIGTVYFERD-----RLPFRYLNDPEKTAAAQHPAhpfWTTVGDLGSVDEDGYLYL 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 536 TGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSSTLTEELKKQIREKIGPIAT 615
Cdd:PRK13390 398 ADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDELARELIDYTRSRIAHYKA 477
|
570 580
....*....|....*....|....
gi 1538017002 616 PDYIQNAPGLPKTRSGKIMRRVLR 639
Cdd:PRK13390 478 PRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
65-655 |
3.25e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 80.00 E-value: 3.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 65 DKVAFYWEGNEpgettkITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAES 144
Cdd:PRK12316 3072 DAVALAFGEQR------LSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEER 3145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 145 LCERILDSSCSLLITTDAFyrgeklvnlkeladeslekcrekgfpvrccivvkhvgraelgmndSPSQSPPVKRQCPDVQ 224
Cdd:PRK12316 3146 LAYMLEDSGAQLLLSQSHL---------------------------------------------RLPLAQGVQVLDLDRG 3180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 225 iswnegvdlwwhelMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPKlCAGSICWSVEMDTkpqpedpfspQGVVHTIG-G 303
Cdd:PRK12316 3181 --------------DENYAEANPAIRTMPENLAYVIYTSGSTGKPK-GVGIRHSALSNHL----------CWMQQAYGlG 3235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 304 YMLYVATTFKYVFDFHPEDVFWctadigwitghsyvtygPLANGATSVLfEGIPTYPDESRLWSIVDKYKVTKFYTAPTA 383
Cdd:PRK12316 3236 VGDRVLQFTTFSFDVFVEELFW-----------------PLMSGARVVL-AGPEDWRDPALLVELINSEGVDVLHAYPSM 3297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 384 IRMLMkfgdEPVTKHSRASLQVLGTVGEPINPEAwlwYHRVVGSQhcPIVDTFWQTETgghmlTPLPGATPMKPGSASFP 463
Cdd:PRK12316 3298 LQAFL----EEEDAHRCTSLKRIVCGGEALPADL---QQQVFAGL--PLYNLYGPTEA-----TITVTHWQCVEEGKDAV 3363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 464 FFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTIYGNHTR-------FETTYFKKFPGYYVTGDGCRRDQDGYYWIT 536
Cdd:PRK12316 3364 PIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRpgltaerFVPDPFVPGERLYRTGDLARYRADGVIEYI 3443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 537 GRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGhphpVKGECLYCFVTLCDGhtfSSTLTEELKKQIREKIgpiatP 616
Cdd:PRK12316 3444 GRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLA----VDGRQLVAYVVPEDE---AGDLREALKAHLKASL-----P 3511
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1538017002 617 DYIQNA-----PGLPKTRSGKIMRRVLRKIaqnDHDLGDTSTVA 655
Cdd:PRK12316 3512 EYMVPAhllflERMPLTPNGKLDRKALPRP---DAALLQQDYVA 3552
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
508-639 |
4.28e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 78.39 E-value: 4.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 508 ETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVT 587
Cdd:PRK06145 364 EKTAEAFYGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVV 443
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1538017002 588 LCDGHTFSstlTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 639
Cdd:PRK06145 444 LNPGATLT---LEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLR 492
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
82-638 |
4.79e-15 |
|
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: 78.08 E-value: 4.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 82 ITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLcERIL-DSSCSLLITt 160
Cdd:cd12114 13 LTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARR-EAILaDAGARLVLT- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 161 dafyrgeklvnlkeladeslekcrekgfpvrccivvkhvgraelgmndspsQSPPVKrQCPDVQISWNEGVDLwwhelmQ 240
Cdd:cd12114 91 ---------------------------------------------------DGPDAQ-LDVAVFDVLILDLDA------L 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 241 EAGDEFEPEWCDAEDPLFILYTSGSTGKPKlcagsicwSVEMdtkpqpedpfSPQGVVHTIGgymlyvATTFKYVFDfhP 320
Cdd:cd12114 113 AAPAPPPPVDVAPDDLAYVIFTSGSTGTPK--------GVMI----------SHRAALNTIL------DINRRFAVG--P 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 321 EDVFWCTA---------DIgwitghsyvtYGPLANGATSVLfegiptyPDESRL-----W-SIVDKYKVTKFYTAPTAIR 385
Cdd:cd12114 167 DDRVLALSslsfdlsvyDI----------FGALSAGATLVL-------PDEARRrdpahWaELIERHGVTLWNSVPALLE 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 386 MLMKF-GDEPVTKHSRAsLQVLGtvGEPINPEawlwyhrvvgsqhcpIVDTFWQTETGGHmLTPLPGAT----------- 453
Cdd:cd12114 230 MLLDVlEAAQALLPSLR-LVLLS--GDWIPLD---------------LPARLRALAPDAR-LISLGGATeasiwsiyhpi 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 454 -PMKPGSASFPFfGVAPA-----ILNESgeelegeaegylvfKQPWP------------GIMRTIYGNHTRFETTYFKKF 515
Cdd:cd12114 291 dEVPPDWRSIPY-GRPLAnqryrVLDPR--------------GRDCPdwvpgelwiggrGVALGYLGDPELTAARFVTHP 355
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 516 PG--YYVTGD-GCRRDqDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPvKGECLYCFVTLCDGH 592
Cdd:cd12114 356 DGerLYRTGDlGRYRP-DGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDP-GGKRLAAFVVPDNDG 433
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1538017002 593 TfsSTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 638
Cdd:cd12114 434 T--PIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
82-639 |
5.74e-15 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 78.14 E-value: 5.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 82 ITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITTD 161
Cdd:PRK07059 49 ITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVVLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 162 AFYRGEKLV----NLKELADESL-EKCREKGFPVRccIVVKHVGRAelgmndSPSQSPPVKRQCPDVqiswnegvdlwwh 236
Cdd:PRK07059 129 NFATTVQQVlaktAVKHVVVASMgDLLGFKGHIVN--FVVRRVKKM------VPAWSLPGHVRFNDA------------- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 237 eLMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPK---LCAGSICWSVE---------MDTKPQPEDPFspqgvvhTIGGY 304
Cdd:PRK07059 188 -LAEGARQTFKPVKLGPDDVAFLQYTGGTTGVSKgatLLHRNIVANVLqmeawlqpaFEKKPRPDQLN-------FVCAL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 305 MLYvattfkyvfdfHpedVFWCTADiGWITghsyvtygpLANGATSVLfegIPTYPDESRLWSIVDKYKVTKFYTAPTAI 384
Cdd:PRK07059 260 PLY-----------H---IFALTVC-GLLG---------MRTGGRNIL---IPNPRDIPGFIKELKKYQVHIFPAVNTLY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 385 RMLMKFGDEPVTKHSRASLQVLG--TVGEPInpeAWLWYHRVvgsqHCPIVDTFWQTETGGhMLTPLPGATPMKPGSASF 462
Cdd:PRK07059 313 NALLNNPDFDKLDFSKLIVANGGgmAVQRPV---AERWLEMT----GCPITEGYGLSETSP-VATCNPVDATEFSGTIGL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 463 PFFGVAPAILNESGEElegeaegyLVFKQPW------PGIMRtiyGNHTRFETTYFKKFP-GYYVTGDGCRRDQDGYYWI 535
Cdd:PRK07059 385 PLPSTEVSIRDDDGND--------LPLGEPGeicirgPQVMA---GYWNRPDETAKVMTAdGFFRTGDVGVMDERGYTKI 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 536 TGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDghtfsSTLTEE-LKKQIREKIGPIA 614
Cdd:PRK07059 454 VDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVVKKD-----PALTEEdVKAFCKERLTNYK 528
|
570 580
....*....|....*....|....*
gi 1538017002 615 TPDYIQNAPGLPKTRSGKIMRRVLR 639
Cdd:PRK07059 529 RPKFVEFRTELPKTNVGKILRRELR 553
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
61-639 |
1.36e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 77.11 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 61 KKLGDKVAFywegNEPGETtkITYRELLVQVCQFSNVLRKQ-GIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAG 139
Cdd:PRK05677 35 QRFADKPAF----SNLGKT--LTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 140 FSAESLCERILDSSCSLLITtdafyrgekLVNLKELADESLEKCRekgfpvrccivVKHVGRAELGmndspSQSPPVKRQ 219
Cdd:PRK05677 109 YTAREMEHQFNDSGAKALVC---------LANMAHLAEKVLPKTG-----------VKHVIVTEVA-----DMLPPLKRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 220 CPDVQISWNEGVDLWWH---------ELMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPK------------------LC 272
Cdd:PRK05677 164 LINAVVKHVKKMVPAYHlpqavkfndALAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKgamlthrnlvanmlqcraLM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 273 AGSICWSVEMDTKPQPedpfspqgvvhtiggymLYvattFKYVFDFHpedvfwCTAdigwitghsyvtygPLANGATSVL 352
Cdd:PRK05677 244 GSNLNEGCEILIAPLP-----------------LY----HIYAFTFH------CMA--------------MMLIGNHNIL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 353 fegIPTYPDESRLWSIVDKYKVTKFYTAPTAIRMLMKfgDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGsqhCPI 432
Cdd:PRK05677 283 ---ISNPRDLPAMVKELGKWKFSGFVGLNTLFVALCN--NEAFRKLDFSALKLTLSGGMALQLATAERWKEVTG---CAI 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 433 VDTFWQTETgghmlTPLPGATPMK---PGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRTIYGNHTrfET 509
Cdd:PRK05677 355 CEGYGMTET-----SPVVSVNPSQaiqVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVKGP--QVMKGYWQRPE--AT 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 510 TYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLC 589
Cdd:PRK05677 426 DEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVK 505
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1538017002 590 DGhtfsSTLTEE-LKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 639
Cdd:PRK05677 506 PG----ETLTKEqVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELR 552
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
517-640 |
2.55e-14 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 75.94 E-value: 2.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 517 GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSS 596
Cdd:PRK06018 410 GFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATR 489
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1538017002 597 tltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 640
Cdd:PRK06018 490 ---EEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALRE 530
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
81-640 |
2.68e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 77.30 E-value: 2.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 81 KITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITT 160
Cdd:PRK12316 4576 KLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQ 4655
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 161 DAFYrgEKLVNLKELADESLEKCRE-KGFPvrccivvkhvgraelgmndspSQSPPVKrqcpdvqiswnegvdlwwhelm 239
Cdd:PRK12316 4656 SHLL--QRLPIPDGLASLALDRDEDwEGFP---------------------AHDPAVR---------------------- 4690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 240 qeagdefepewCDAEDPLFILYTSGSTGKPKLCAGS-------ICWSVEmdtKPQ--PED---PFSPqgvvhtiggymly 307
Cdd:PRK12316 4691 -----------LHPDNLAYVIYTSGSTGRPKGVAVShgslvnhLHATGE---RYEltPDDrvlQFMS------------- 4743
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 308 vattfkYVFDFHPEdvfwctadiGWitghsyvtYGPLANGAtSVLFEGiPTYPDESRLWSIVDKYKVTKFYTAPTAIRML 387
Cdd:PRK12316 4744 ------FSFDGSHE---------GL--------YHPLINGA-SVVIRD-DSLWDPERLYAEIHEHRVTVLVFPPVYLQQL 4798
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 388 MKfGDEPVTKHSRASLQVLGtvGEPINPEAW-LWY--------HRVVGSQHCPIVDTFWQTETGghmltPLPGATPMKPG 458
Cdd:PRK12316 4799 AE-HAERDGEPPSLRVYCFG--GEAVAQASYdLAWralkpvylFNGYGPTETTVTVLLWKARDG-----DACGAAYMPIG 4870
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 459 SasfPFFGVAPAILNESGeelegeaegylvfkQPWP-GIMRTIY--------GNH-------TRFETTYFKKfPG--YYV 520
Cdd:PRK12316 4871 T---PLGNRSGYVLDGQL--------------NPLPvGVAGELYlggegvarGYLerpaltaERFVPDPFGA-PGgrLYR 4932
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 521 TGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVkGECLYCFVTLCDGHTFSSTLTE 600
Cdd:PRK12316 4933 TGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAV-GKQLVGYVVPQDPALADADEAQ 5011
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1538017002 601 -ELKKQIREKIGPiATPDYIQNA-----PGLPKTRSGKIMRRVLRK 640
Cdd:PRK12316 5012 aELRDELKAALRE-RLPEYMVPAhlvflARMPLTPNGKLDRKALPQ 5056
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
81-641 |
3.94e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 76.74 E-value: 3.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 81 KITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITT 160
Cdd:PRK12467 3120 QLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQ 3199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 161 DAFyrgeklvnlkeladesLEKcrekgfpvrccIVVKHVGRAELGMNDSPSQSPPvkrQCPDVQIswnegvdlwwhelmq 240
Cdd:PRK12467 3200 AHL----------------LEQ-----------LPAPAGDTALTLDRLDLNGYSE---NNPSTRV--------------- 3234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 241 eagdefepewcDAEDPLFILYTSGSTGKPKLCAGSI-------CWSVEMdtkpqpedpfspqgvvhtiggYMLYVATT-- 311
Cdd:PRK12467 3235 -----------MGENLAYVIYTSGSTGKPKGVGVRHgalanhlCWIAEA---------------------YELDANDRvl 3282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 312 --FKYVFDFHPEDVFWctadigwitghsyvtygPLANGATSVLFEGIPTYPDEsrLWSIVDKYKVTKFYTAPTAIRMLMK 389
Cdd:PRK12467 3283 lfMSFSFDGAQERFLW-----------------TLICGGCLVVRDNDLWDPEE--LWQAIHAHRISIACFPPAYLQQFAE 3343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 390 FGDepvtKHSRASLQVLGTVGEPINPEAWLWYHRVV---------GSQHCPIVDTFWQTETGGhmlTPLPGATPMkpgsa 460
Cdd:PRK12467 3344 DAG----GADCASLDIYVFGGEAVPPAAFEQVKRKLkprgltngyGPTEAVVTVTLWKCGGDA---VCEAPYAPI----- 3411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 461 SFPFFGVAPAILNESGeelegeaegylvfkQPWP-GIMRTIY--------GNH-------TRFETTYFKKFPG-YYVTGD 523
Cdd:PRK12467 3412 GRPVAGRSIYVLDGQL--------------NPVPvGVAGELYiggvglarGYHqrpsltaERFVADPFSGSGGrLYRTGD 3477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 524 GCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPhPVKGECLYCFVTLcdgHTFSSTLTEELK 603
Cdd:PRK12467 3478 LARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARD-GAGGKQLVAYVVP---ADPQGDWRETLR 3553
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1538017002 604 KQIREKIgpiatPDYIQNA-----PGLPKTRSGKIMRRVLRKI 641
Cdd:PRK12467 3554 DHLAASL-----PDYMVPAqllvlAAMPLGPNGKVDRKALPDP 3591
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
517-635 |
4.12e-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: 4.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 517 GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfsS 596
Cdd:cd17638 215 GWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPG----V 290
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1538017002 597 TLTEE-LKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMR 635
Cdd:cd17638 291 TLTEEdVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
517-644 |
4.70e-14 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 75.41 E-value: 4.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 517 GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGE--CLYCFVTlcdghtf 594
Cdd:PRK10946 409 GFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEksCAFLVVK------- 481
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1538017002 595 SSTLTEELKKQIREK-IGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQN 644
Cdd:PRK10946 482 EPLKAVQLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQWLAS 532
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
252-643 |
4.73e-14 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 75.44 E-value: 4.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 252 DAEDPLFILYTSGSTGKPK----------LCAGSICWSVEMDTKPqpedpfspqgvvhtiggymLYVATTfkyvfdfhpe 321
Cdd:PLN03102 184 DEHDPISLNYTSGTTADPKgvvishrgayLSTLSAIIGWEMGTCP-------------------VYLWTL---------- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 322 DVFWCTadiGWItghsyVTYGPLANGATSVLFEGIpTYPDesrLWSIVDKYKVTKFYTAPTAIRMLMKfGDEPVTKHSRA 401
Cdd:PLN03102 235 PMFHCN---GWT-----FTWGTAARGGTSVCMRHV-TAPE---IYKNIEMHNVTHMCCVPTVFNILLK-GNSLDLSPRSG 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 402 SLQVLgTVGEPiNPEAWLWYHRVVGSQhcpIVDTFWQTETGGHML--------TPLPGATPMK-PGSASFPFFGVAPAIL 472
Cdd:PLN03102 302 PVHVL-TGGSP-PPAALVKKVQRLGFQ---VMHAYGLTEATGPVLfcewqdewNRLPENQQMElKARQGVSILGLADVDV 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 473 NESGEELEG----EAEGYLVFKQPwpGIMRTiYGNHTRFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGH 548
Cdd:PLN03102 377 KNKETQESVprdgKTMGEIVIKGS--SIMKG-YLKNPKATSEAFKH--GWLNTGDVGVIHPDGHVEIKDRSKDIIISGGE 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 549 LLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSS-------TLTEELKKQIREKIGPIATPDYIQN 621
Cdd:PLN03102 452 NISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETTKEdrvdklvTRERDLIEYCRENLPHFMCPRKVVF 531
|
410 420
....*....|....*....|..
gi 1538017002 622 APGLPKTRSGKIMRRVLRKIAQ 643
Cdd:PLN03102 532 LQELPKNGNGKILKPKLRDIAK 553
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
83-640 |
5.16e-14 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 75.17 E-value: 5.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 83 TYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITTDA 162
Cdd:PRK06087 51 TYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 163 FYRGEKLVNLKELADEslekcrekgfpvrccivVKHVGRAELGMNDSPSQSPPVKRQCpdvqISWNEGVDlwwhelmqea 242
Cdd:PRK06087 131 FKQTRPVDLILPLQNQ-----------------LPQLQQIVGVDKLAPATSSLSLSQI----IADYEPLT---------- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 243 gdefEPEWCDAEDPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGVVHTIGGyMLYVATTFKYVFDFHPED 322
Cdd:PRK06087 180 ----TAITTHGDELAAVLFTSGTEGLPK-------------------------GVMLTHNN-ILASERAYCARLNLTWQD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 323 VFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPtyPDESrlWSIVDKYKVTKFYTAPTAIRMLMKFGDEPVTKHSraS 402
Cdd:PRK06087 230 VFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFT--PDAC--LALLEQQRCTCMLGATPFIYDLLNLLEKQPADLS--A 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 403 LQVLGTVGEPInPEawlwyhRVVgsQHC-----PIVDTFWQTETGGHMLTPLPGATPMKPGSASFPFFGVAPAILNESge 477
Cdd:PRK06087 304 LRFFLCGGTTI-PK------KVA--RECqqrgiKLLSVYGSTESSPHAVVNLDDPLSRFMHTDGYAAAGVEIKVVDEA-- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 478 elegeaegylvfKQPWPgimrtiYGNHTRFETTYFKKFPGY----------------YVTGDGCRRDQDGYYWITGRIDD 541
Cdd:PRK06087 373 ------------RKTLP------PGCEGEEASRGPNVFMGYldepeltaraldeegwYYSGDLCRMDEAGYIKITGRKKD 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 542 MLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLcDGHTFSSTLTEELKKQIREKIGPIATPDYIQN 621
Cdd:PRK06087 435 IIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVL-KAPHHSLTLEEVVAFFSRKRVAKYKYPEHIVV 513
|
570
....*....|....*....
gi 1538017002 622 APGLPKTRSGKIMRRVLRK 640
Cdd:PRK06087 514 IDKLPRTASGKIQKFLLRK 532
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
53-639 |
5.33e-14 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 75.45 E-value: 5.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 53 VLDRNVHEKKLGDKVAFYwegnepgETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGAL 132
Cdd:PRK06060 9 LLAEQASEAGWYDRPAFY-------AADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 133 HSIVFAGFSAESLCERILDSSCSLLITTDAF---YRGEKLVNLKELADESlekcrekgfpvrccivvkhvGRAElgmnds 209
Cdd:PRK06060 82 AFLANPELHRDDHALAARNTEPALVVTSDALrdrFQPSRVAEAAELMSEA--------------------ARVA------ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 210 PSQSPPVkrqcpdvqiswnegvdlwwhelmqeAGDEFEpewcdaedplFILYTSGSTGKPKLCAGSICwsvemdtkpqpe 289
Cdd:PRK06060 136 PGGYEPM-------------------------GGDALA----------YATYTSGTTGPPKAAIHRHA------------ 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 290 DPFSpqgvvhtiggymlYVATTFKYVFDFHPEDVFWCTADIGWITGHSYVTYGPLANGATSVLfEGIPTYPDESRLWSIv 369
Cdd:PRK06060 169 DPLT-------------FVDAMCRKALRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVI-NSAPVTPEAAAILSA- 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 370 dKYKVTKFYTAPTAIRMLMkfgdEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGSqhCPIVDTFWQTETGGHMLTPl 449
Cdd:PRK06060 234 -RFGPSVLYGVPNFFARVI----DSCSPDSFRSLRCVVSAGEALELGLAERLMEFFGG--IPILDGIGSTEVGQTFVSN- 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 450 pGATPMKPGSAS--FPFFG---VAPAilnesgeelegeaegylvFKQPWPGIMRTIYGNHTRFETTYFKKfP-------G 517
Cdd:PRK06060 306 -RVDEWRLGTLGrvLPPYEirvVAPD------------------GTTAGPGVEGDLWVRGPAIAKGYWNR-PdspvaneG 365
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 518 YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSST 597
Cdd:PRK06060 366 WLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGS 445
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1538017002 598 LTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 639
Cdd:PRK06060 446 VMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
61-642 |
6.64e-14 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 74.91 E-value: 6.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 61 KKLGDKVAFYWEGnepgetTKITYRELLVQVCQF-SNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAG 139
Cdd:PRK08751 36 AKFADRPAYHSFG------KTITYREADQLVEQFaAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 140 FSAESLCERILDSSCSLLITTDAFYRGEKLVnlkeLADESLEKCREK------GFPVRCCI--VVKHVgraelgmndsps 211
Cdd:PRK08751 110 YTPRELKHQLIDSGASVLVVIDNFGTTVQQV----IADTPVKQVITTglgdmlGFPKAALVnfVVKYV------------ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 212 qsppvKRQCPDVQISwneGVDLWWHELMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedp 291
Cdd:PRK08751 174 -----KKLVPEYRIN---GAIRFREALALGRKHSMPTLQIEPDDIAFLQYTGGTTGVAK--------------------- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 292 fspqgvvhtigGYMLyvatTFKYVFDFHPEDVFWCTADIGWITGHSYV-TYGPL-------ANGATSVLFEGIPTYPDES 363
Cdd:PRK08751 225 -----------GAML----THRNLVANMQQAHQWLAGTGKLEEGCEVViTALPLyhifaltANGLVFMKIGGCNHLISNP 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 364 R-LWSIVDKYKVTKFyTAPTAIRMLM-KFGDEP-VTKHSRASLQVLGTVGEPINPEAWLWYHRVVGsqhCPIVDTFWQTE 440
Cdd:PRK08751 290 RdMPGFVKELKKTRF-TAFTGVNTLFnGLLNTPgFDQIDFSSLKMTLGGGMAVQRSVAERWKQVTG---LTLVEAYGLTE 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 441 TgghmlTPLPGATPMK----PGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRTIYGNHTrfETTYFKKFP 516
Cdd:PRK08751 366 T-----SPAACINPLTlkeyNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGP--QVMKGYWKRPE--ETAKVMDAD 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 517 GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDghtfsS 596
Cdd:PRK08751 437 GWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVKKD-----P 511
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1538017002 597 TLT-EELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 642
Cdd:PRK08751 512 ALTaEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRDAA 558
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
63-632 |
7.43e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 74.54 E-value: 7.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 63 LGDKVAFYWeGNEpgettKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSA 142
Cdd:PRK07798 16 VPDRVALVC-GDR-----RLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 143 ESLCERILDSSCSLLITTDAFyrGEKLVNLKEladeSLEKcrekgfpVRCCIVVkhvgraelgmNDSPSQSPPVkrqcpd 222
Cdd:PRK07798 90 DELRYLLDDSDAVALVYEREF--APRVAEVLP----RLPK-------LRTLVVV----------EDGSGNDLLP------ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 223 vqiswnEGVDlwWHELMQEAGDE--FEPEwcdAEDPLFILYTSGSTGKPK--LCAGSICWSVEMD-----TKPQPEDPFS 293
Cdd:PRK07798 141 ------GAVD--YEDALAAGSPErdFGER---SPDDLYLLYTGGTTGMPKgvMWRQEDIFRVLLGgrdfaTGEPIEDEEE 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 294 PQGVVHTIGGYMLYVATTFkyvfdfhpedvfwctadigwITGHS-YVTYGPLANGATSVLfegiptYPDES----RLWSI 368
Cdd:PRK07798 210 LAKRAAAGPGMRRFPAPPL--------------------MHGAGqWAAFAALFSGQTVVL------LPDVRfdadEVWRT 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 369 VDKYKVTkfytaptaiRMLMkFGD---EPVTKHSRA-------SLQVLGTVGEPINP---EAWLwyhrvvgsQHCP---I 432
Cdd:PRK07798 264 IEREKVN---------VITI-VGDamaRPLLDALEArgpydlsSLFAIASGGALFSPsvkEALL--------ELLPnvvL 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 433 VDTFWQTETGGHMLtplpGATPMKPGSASFPFFGVAPAILnesgeelegeaegylVFK------QPWPGiMRTIYGNHTR 506
Cdd:PRK07798 326 TDSIGSSETGFGGS----GTVAKGAVHTGGPRFTIGPRTV---------------VLDedgnpvEPGSG-EIGWIARRGH 385
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 507 FETTYFKK-------FP---G--YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHP 574
Cdd:PRK07798 386 IPLGYYKDpektaetFPtidGvrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVP 465
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1538017002 575 HPVKGECLYCFVTLCDGHTFSStltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGK 632
Cdd:PRK07798 466 DERWGQEVVAVVQLREGARPDL---AELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
235-640 |
8.51e-14 |
|
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: 74.39 E-value: 8.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 235 WHELMQEAGDEFEP-EWCDAEDPLFILYTSGSTGKPKlCAgsicwsvemdtkpqpedpfspqgVVHTIGGYMLYVATTFK 313
Cdd:cd05915 133 GYLAYEEALGEEADpVRVPERAACGMAYTTGTTGLPK-GV-----------------------VYSHRALVLHSLAASLV 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 314 YVFDFHPEDVFWCTADIGWITGHSYVtYGPLANGATSVLFEGIPTypDESRLWSIVdKYKVTKFYTAPTAIRMLMKFGDE 393
Cdd:cd05915 189 DGTALSEKDVVLPVVPMFHVNAWCLP-YAATLVGAKQVLPGPRLD--PASLVELFD-GEGVTFTAGVPTVWLALADYLES 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 394 pVTKHSRASLQVLGTVGEPinPEAWL-----WYHRVVGSQHCPIV-----DTFWQTEtgghmLTPLPGATPMK-PGSASF 462
Cdd:cd05915 265 -TGHRLKTLRRLVVGGSAA--PRSLIarferMGVEVRQGYGLTETspvvvQNFVKSH-----LESLSEEEKLTlKAKTGL 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 463 PFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTIYGNHTRFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDM 542
Cdd:cd05915 337 PIPLVRLRVADEEGRPVPKDGKALGEVQLKGPWITGGYYGNEEATRSALTPD--GFFRTGDIAVWDEEGYVEIKDRLKDL 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 543 LNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDghtfSSTLTEELKKQIREKIGPIAT-PDYIQN 621
Cdd:cd05915 415 IKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRG----EKPTPEELNEHLLKAGFAKWQlPDAYVF 490
|
410
....*....|....*....
gi 1538017002 622 APGLPKTRSGKIMRRVLRK 640
Cdd:cd05915 491 AEEIPRTSAGKFLKRALRE 509
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
517-643 |
1.23e-13 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 74.11 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 517 GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFS- 595
Cdd:PLN02479 430 GWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSd 509
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1538017002 596 -STLTEELKKQIREKIGPIATPDYIQNAPgLPKTRSGKIMRRVLRKIAQ 643
Cdd:PLN02479 510 eAALAEDIMKFCRERLPAYWVPKSVVFGP-LPKTATGKIQKHVLRAKAK 557
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
517-642 |
2.84e-13 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 72.93 E-value: 2.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 517 GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfsS 596
Cdd:PRK12492 441 GWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDP----G 516
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1538017002 597 TLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 642
Cdd:PRK12492 517 LSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDIA 562
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
82-640 |
4.39e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 73.07 E-value: 4.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 82 ITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITTD 161
Cdd:PRK12316 2029 LSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQR 2108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 162 AFYrgEKLVNLKELADESLEkcrekgfpvrccivvkhvgrAELGMNDSPSQSPPVKrqcpdvqiswnegvdlwwhelmqe 241
Cdd:PRK12316 2109 HLL--ERLPLPAGVARLPLD--------------------RDAEWADYPDTAPAVQ------------------------ 2142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 242 agdefepewCDAEDPLFILYTSGSTGKPKLCAGS------ICWSVEMDTKPQPEDpfspqgvvhtiggYMLYVATtfkYV 315
Cdd:PRK12316 2143 ---------LAGENLAYVIYTSGSTGLPKGVAVShgalvaHCQAAGERYELSPAD-------------CELQFMS---FS 2197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 316 FDFHPEDVFWctadigwitghsyvtygPLANGATSVLFEGipTYPDESRLWSIVDKYKVTKFYTAPTairMLMKFGDEPV 395
Cdd:PRK12316 2198 FDGAHEQWFH-----------------PLLNGARVLIRDD--ELWDPEQLYDEMERHGVTILDFPPV---YLQQLAEHAE 2255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 396 TKHSRASLQVLGTVGEPINPEAWLWYHRVVGSQHcpIVDTFWQTETgghMLTPLP-GATPMKPGSASFPFFGVAPA---- 470
Cdd:PRK12316 2256 RDGRPPAVRVYCFGGEAVPAASLRLAWEALRPVY--LFNGYGPTEA---VVTPLLwKCRPQDPCGAAYVPIGRALGnrra 2330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 471 -ILNESGEELEgeaegylvfkqpwPGIMRTIYGNHTRFETTYFKKfPG-----------------YYVTGDGCRRDQDGY 532
Cdd:PRK12316 2331 yILDADLNLLA-------------PGMAGELYLGGEGLARGYLNR-PGltaerfvpdpfsasgerLYRTGDLARYRADGV 2396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 533 YWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPvKGECLYCFVTLCDGHTfssTLTEELKKQIREKIGP 612
Cdd:PRK12316 2397 VEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGA-SGKQLVAYVVPDDAAE---DLLAELRAWLAARLPA 2472
|
570 580
....*....|....*....|....*...
gi 1538017002 613 IATPDYIQNAPGLPKTRSGKIMRRVLRK 640
Cdd:PRK12316 2473 YMVPAHWVVLERLPLNPNGKLDRKALPK 2500
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
83-638 |
6.78e-13 |
|
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: 71.13 E-value: 6.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 83 TYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITTda 162
Cdd:cd17652 14 TYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLLTT-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 163 fyrgeklvnlkeladeslekcrekgfpvrccivvkhvgraelgmndspsqsppvkrqcpdvqiswnegvdlwwhelmqea 242
Cdd:cd17652 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 243 gdefepewcdAEDPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGVVHTIGGYMLYVATTFKYvFDFHPED 322
Cdd:cd17652 92 ----------PDNLAYVIYTSGSTGRPK-------------------------GVVVTHRGLANLAAAQIAA-FDVGPGS 135
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 323 VFWCTADIGWITGHSYVTYGPLAnGATSVLFEGIPTYPDESrLWSIVDKYKVTkFYTAPTAIRMLMKFGDEPvtkhsraS 402
Cdd:cd17652 136 RVLQFASPSFDASVWELLMALLA-GATLVLAPAEELLPGEP-LADLLREHRIT-HVTLPPAALAALPPDDLP-------D 205
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 403 LQVLGTVGEPINPE-AWLWyhrvvgSQHCPIVDTFWQTET--GGHMLTPLPGATPMKPGSasfPFFGVAPAILNESGeel 479
Cdd:cd17652 206 LRTLVVAGEACPAElVDRW------APGRRMINAYGPTETtvCATMAGPLPGGGVPPIGR---PVPGTRVYVLDARL--- 273
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 480 egeaegylvfkQPWP-GIMRTIY--------GNHTRFETTYfKKF-------PG--YYVTGDGCRRDQDGYYWITGRIDD 541
Cdd:cd17652 274 -----------RPVPpGVPGELYiagaglarGYLNRPGLTA-ERFvadpfgaPGsrMYRTGDLARWRADGQLEFLGRADD 341
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 542 MLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfSSTLTEELKKQIREKIGPIATPDYIQN 621
Cdd:cd17652 342 QVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPG---AAPTAAELRAHLAERLPGYMVPAAFVV 418
|
570
....*....|....*..
gi 1538017002 622 APGLPKTRSGKIMRRVL 638
Cdd:cd17652 419 LDALPLTPNGKLDRRAL 435
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
254-635 |
7.40e-13 |
|
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: 70.37 E-value: 7.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 254 EDPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqgvvhtigGYMLYVATTFKYVFDFHPEDVFWCTADIGWI 333
Cdd:cd17635 1 EDPLAVIFTSGTTGEPK--------------------------------AVLLANKTFFAVPDILQKEGLNWVVGDVTYL 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 334 TGHSYVTYGpLANGATSVLFEG-IPTYPDESRLWS---IVDKYKVTKFYTAPTAIRMLMKfgdepVTKHSRA---SLQVL 406
Cdd:cd17635 49 PLPATHIGG-LWWILTCLIHGGlCVTGGENTTYKSlfkILTTNAVTTTCLVPTLLSKLVS-----ELKSANAtvpSLRLI 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 407 GTVGE-PINPEA--WLWYHRVVGSQHcpivdtFWQTETGGHMLTPLpGATPMKPGSASFPFFGVAPAILNESGEELEGEA 483
Cdd:cd17635 123 GYGGSrAIAADVrfIEATGLTNTAQV------YGLSETGTALCLPT-DDDSIEINAVGRPYPGVDVYLAATDGIAGPSAS 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 484 EGYLVFKQPWpgIMRTIYGNHTRFETTYFKkfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHE 563
Cdd:cd17635 196 FGTIWIKSPA--NMLGYWNNPERTAEVLID---GWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVS 270
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1538017002 564 AVAEAAVVGHPHPVKGEcLYCFVTLCDGHTFSSTLTeELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMR 635
Cdd:cd17635 271 GVQECACYEISDEEFGE-LVGLAVVASAELDENAIR-ALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
86-639 |
1.63e-12 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 70.11 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 86 ELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLIT-TDAFy 164
Cdd:PRK12406 16 ELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAhADLL- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 165 rgeklvnlkeladESLEKCREKGFPVRCCIVVKHVgRAELGMndspsqsPPVKRQCPDVQISWNEgvdlwWheLMQEAGD 244
Cdd:PRK12406 95 -------------HGLASALPAGVTVLSVPTPPEI-AAAYRI-------SPALLTPPAGAIDWEG-----W--LAQQEPY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 245 EFEPewcdAEDPLFILYTSGSTGKPKlcagsicwSVEMDTkPQPEDPFSPQGVVHTIGGYMLYVATTfkyvfdfhpedvf 324
Cdd:PRK12406 147 DGPP----VPQPQSMIYTSGTTGHPK--------GVRRAA-PTPEQAAAAEQMRALIYGLKPGIRAL------------- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 325 wctadigwITGHSYVT----YGPLAN--GATSVL---FEgiptyPDEsrLWSIVDKYKVTKFYTAPTAIRMLMKFGDEPV 395
Cdd:PRK12406 201 --------LTGPLYHSapnaYGLRAGrlGGVLVLqprFD-----PEE--LLQLIERHRITHMHMVPTMFIRLLKLPEEVR 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 396 TKHSRASLQVLGTVGEPINPE------AWlWyhrvvgsqhCPIVDTFW-QTETGGhmltpLPGATP----MKPGSASFPF 464
Cdd:PRK12406 266 AKYDVSSLRHVIHAAAPCPADvkramiEW-W---------GPVIYEYYgSTESGA-----VTFATSedalSHPGTVGKAA 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 465 FGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRTIYGNHTRFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLN 544
Cdd:PRK12406 331 PGAELRFVDEDGRPLPQGEIGEIYSRIA--GNPDFTYHNKPEKRAEIDRG--GFITSGDVGYLDADGYLFLCDRKRDMVI 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 545 VSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSstlTEELKKQIREKIGPIATPDYIQNAPG 624
Cdd:PRK12406 407 SGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLD---EADIRAQLKARLAGYKVPKHIEIMAE 483
|
570
....*....|....*
gi 1538017002 625 LPKTRSGKIMRRVLR 639
Cdd:PRK12406 484 LPREDSGKIFKRRLR 498
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
517-639 |
1.93e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 70.02 E-value: 1.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 517 GYYVTGDGCRRDQDGYYWITGRID-DMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTfs 595
Cdd:PRK07787 350 GWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVA-- 427
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1538017002 596 stlTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 639
Cdd:PRK07787 428 ---ADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
53-270 |
2.25e-12 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 69.90 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 53 VLDRNVHekKLGDKVAFYWEGnepgetTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGAL 132
Cdd:PRK08279 42 VFEEAAA--RHPDRPALLFED------QSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 133 HSIVFAGFSAESL--CERILDSscSLLITtdafyrGEKLVNLKELADESLEKcrekgfPVRCCIVVKHVGRAELGMNDSP 210
Cdd:PRK08279 114 VALLNTQQRGAVLahSLNLVDA--KHLIV------GEELVEAFEEARADLAR------PPRLWVAGGDTLDDPEGYEDLA 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 211 SQSppvkRQCPDVQISWNEGVdlwwhelmqeagdefepewcDAEDPLFILYTSGSTGKPK 270
Cdd:PRK08279 180 AAA----AGAPTTNPASRSGV--------------------TAKDTAFYIYTSGTTGLPK 215
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
75-639 |
2.66e-12 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 69.52 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 75 EPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGAlhsiVF-----AGFSAEsLCERI 149
Cdd:PRK07514 22 ETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGA----VFlplntAYTLAE-LDYFI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 150 LDSSCSLLITTDAfyrgeklvnlkelADESLEKCREK-GfpvrccivVKHVgrAELGMNDSPSQSppvkrqcpdvqiswn 228
Cdd:PRK07514 97 GDAEPALVVCDPA-------------NFAWLSKIAAAaG--------APHV--ETLDADGTGSLL--------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 229 egvdlwwhELMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPK--------LCAGSI----CWSvemdtkpqpedpFSPQG 296
Cdd:PRK07514 139 --------EAAAAAPDDFETVPRGADDLAAILYTSGTTGRSKgamlshgnLLSNALtlvdYWR------------FTPDD 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 297 VV-------HTIGgymLYVATTF------KYVF--DFHPEDVfwctadigwitghsyvtygpLANGATSVLFEGIPTypd 361
Cdd:PRK07514 199 VLihalpifHTHG---LFVATNVallagaSMIFlpKFDPDAV--------------------LALMPRATVMMGVPT--- 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 362 esrlwsivdkykvtkFYTaptaiRMLmkfgDEP-----VTKHSRasLQVLGTVgePINPEAWL-WYHRvvgSQHcPIVDT 435
Cdd:PRK07514 253 ---------------FYT-----RLL----QEPrltreAAAHMR--LFISGSA--PLLAETHReFQER---TGH-AILER 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 436 FWQTETGghMLTPLPGATPMKPGSASFPFFGVAPAILNESGEELEGEAEGYL-------VFKQPW--PGimrtiygnHTR 506
Cdd:PRK07514 301 YGMTETN--MNTSNPYDGERRAGTVGFPLPGVSLRVTDPETGAELPPGEIGMievkgpnVFKGYWrmPE--------KTA 370
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 507 FETTYfkkfPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFV 586
Cdd:PRK07514 371 EEFRA----DGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVV 446
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1538017002 587 TLCDGHTFS-STLTEELKKQI-REKIgpiatPDYIQNAPGLPKTRSGKIMRRVLR 639
Cdd:PRK07514 447 VPKPGAALDeAAILAALKGRLaRFKQ-----PKRVFFVDELPRNTMGKVQKNLLR 496
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
82-641 |
2.85e-12 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 69.49 E-value: 2.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 82 ITYRELLVQVCQFSNVLRKQ-GIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITt 160
Cdd:PLN02574 67 ISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFT- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 161 dafyrgeklvnlkelADESLEKCREKGFPVrccivvkhVGRAELGMNDSPSQSPPVkrqcpdvqiswnegvdlwWHELMQ 240
Cdd:PLN02574 146 ---------------SPENVEKLSPLGVPV--------IGVPENYDFDSKRIEFPK------------------FYELIK 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 241 EAGDEFEPEWCDAEDPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGVVHTIGGYMLYVATTFKYVFDFHP 320
Cdd:PLN02574 185 EDFDFVPKPVIKQDDVAAIMYSSGTTGASK-------------------------GVVLTHRNLIAMVELFVRFEASQYE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 321 ----EDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIptypDESRLWSIVDKYKVTKFYTAPTAIRMLMKfGDEPVT 396
Cdd:PLN02574 240 ypgsDNVYLAALPMFHIYGLSLFVVGLLSLGSTIVVMRRF----DASDMVKVIDRFKVTHFPVVPPILMALTK-KAKGVC 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 397 KHSRASLQVLGTVGEPINPEAWLWYHRVVgsQHCPIVDTFWQTETGGHMLTPLPGATPMKPGSASFpffgVAPAILNESG 476
Cdd:PLN02574 315 GEVLKSLKQVSCGAAPLSGKFIQDFVQTL--PHVDFIQGYGMTESTAVGTRGFNTEKLSKYSSVGL----LAPNMQAKVV 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 477 EELEGEAEGYLVFKQPW---PGIMRTIYGNHTRFETTYFKKfpGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTA 553
Cdd:PLN02574 389 DWSTGCLLPPGNCGELWiqgPGVMKGYLNNPKATQSTIDKD--GWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPA 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 554 EVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfsSTLTEE-LKKQIREKIGPIATPDYIQNAPGLPKTRSGK 632
Cdd:PLN02574 467 DLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQG----STLSQEaVINYVAKQVAPYKKVRKVVFVQSIPKSPAGK 542
|
....*....
gi 1538017002 633 IMRRVLRKI 641
Cdd:PLN02574 543 ILRRELKRS 551
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
77-644 |
4.62e-12 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 68.85 E-value: 4.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 77 GETTKI-TYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCS 155
Cdd:PLN02246 45 GATGRVyTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 156 LLITTDAFYrgEKLVNLKEladeslekcrEKGFPVRCCivvkhvgraelgmnDSPsqsppvkrqcPDVQISWNEgvdlww 235
Cdd:PLN02246 125 LIITQSCYV--DKLKGLAE----------DDGVTVVTI--------------DDP----------PEGCLHFSE------ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 236 heLMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGVVHTIGGYMLYVAttfKYV 315
Cdd:PLN02246 163 --LTQADENELPEVEISPDDVVALPYSSGTTGLPK-------------------------GVMLTHKGLVTSVA---QQV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 316 ------FDFHPEDVFWCTADIGWITGHSYVTYGPLANGATSVLfegIPTYpDESRLWSIVDKYKVTkfyTAPTAIRMLMK 389
Cdd:PLN02246 213 dgenpnLYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILI---MPKF-EIGALLELIQRHKVT---IAPFVPPIVLA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 390 FGDEP-VTKHSRASLQVLGTVGEPINPEawlwyhrvvgsqhcpIVDTFW-------------QTETGGHMLTPLPGA--- 452
Cdd:PLN02246 286 IAKSPvVEKYDLSSIRMVLSGAAPLGKE---------------LEDAFRaklpnavlgqgygMTEAGPVLAMCLAFAkep 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 453 TPMKPGSAsfpffgvAPAILNESGEELEGEAEGYLVFKQPW------PGIMRTIYGNHTRFETTYFKKfpGYYVTGDGCR 526
Cdd:PLN02246 351 FPVKSGSC-------GTVVRNAELKIVDPETGASLPRNQPGeicirgPQIMKGYLNDPEATANTIDKD--GWLHTGDIGY 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 527 RDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfsSTLTE-ELK-- 603
Cdd:PLN02246 422 IDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNG----SEITEdEIKqf 497
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1538017002 604 --KQI--REKIGPIATPDYIqnapglPKTRSGKIMRRVLR-KIAQN 644
Cdd:PLN02246 498 vaKQVvfYKRIHKVFFVDSI------PKAPSGKILRKDLRaKLAAG 537
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
361-635 |
5.21e-12 |
|
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: 67.68 E-value: 5.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 361 DESRLWSIVDKYKVTKFYTAPTAIRMLMkfgdEPVTKHSR--ASLQVLGTVGEPINPEAWlwyHRVVGSqhcpivdTFW- 437
Cdd:cd17637 76 DPAEALELIEEEKVTLMGSFPPILSNLL----DAAEKSGVdlSSLRHVLGLDAPETIQRF---EETTGA-------TFWs 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 438 ---QTETGGhMLTPLPGATpmKPGSASFPFFGVAPAILNESGEELEGEAEGY------LVFKQPWPGIMRTiygNHTrfe 508
Cdd:cd17637 142 lygQTETSG-LVTLSPYRE--RPGSAGRPGPLVRVRIVDDNDRPVPAGETGEivvrgpLVFQGYWNLPELT---AYT--- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 509 ttyFKKfpGYYVTGDGCRRDQDGYYWITGRI--DDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFV 586
Cdd:cd17637 213 ---FRN--GWHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVC 287
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1538017002 587 TLCDGHTFSStltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMR 635
Cdd:cd17637 288 VLKPGATLTA---DELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
81-638 |
6.45e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 69.42 E-value: 6.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 81 KITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITT 160
Cdd:PRK12467 1599 ELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQ 1678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 161 dafyrgeklvnlKELADEslekcrekgFPVrccivvkhvgraelgmndspsqspPVKRQCPDVqiswnEGVDLWWhelmq 240
Cdd:PRK12467 1679 ------------SHLQAR---------LPL------------------------PDGLRSLVL-----DQEDDWL----- 1703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 241 EAGDEFEPEWCDAEDPL-FILYTSGSTGKPK---LCAGS----ICWSvemdtkpQPEDPFSPQGVVhtiggymlyvatTF 312
Cdd:PRK12467 1704 EGYSDSNPAVNLAPQNLaYVIYTSGSTGRPKgagNRHGAlvnrLCAT-------QEAYQLSAADVV------------LQ 1764
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 313 K--YVFDFHPEDVFWctadigwitghsyvtygPLANGAtSVLFEGIPTYPDESRLWSIVDKYKVTKFYTAPTAIRMLMKF 390
Cdd:PRK12467 1765 FtsFAFDVSVWELFW-----------------PLINGA-RLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQM 1826
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 391 gDEPVTKHSraSLQVLGTVGEPINPEAW-LWYHRVVGSQhcpIVDTFWQTETGGHmLTPLPGATPMKPGSASFPFfGVAP 469
Cdd:PRK12467 1827 -DEQVEHPL--SLRRVVCGGEALEVEALrPWLERLPDTG---LFNLYGPTETAVD-VTHWTCRRKDLEGRDSVPI-GQPI 1898
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 470 AILNEsgeelegeaegYLVFKQ--PWP-GIMRTIY--------GNH-------TRFETTYFKKFPG-YYVTGDGCRRDQD 530
Cdd:PRK12467 1899 ANLST-----------YILDASlnPVPiGVAGELYlggvglarGYLnrpaltaERFVADPFGTVGSrLYRTGDLARYRAD 1967
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 531 GYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPvKGECLYCFVT-----LCDGHTFSSTLTEELKKQ 605
Cdd:PRK12467 1968 GVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQDGA-NGKQLVAYVVptdpgLVDDDEAQVALRAILKNH 2046
|
570 580 590
....*....|....*....|....*....|....*...
gi 1538017002 606 IREKIgpiatPDYIQNA-----PGLPKTRSGKIMRRVL 638
Cdd:PRK12467 2047 LKASL-----PEYMVPAhlvflARMPLTPNGKLDRKAL 2079
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
82-640 |
1.22e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 68.65 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 82 ITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLITtd 161
Cdd:PRK12467 538 LSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLT-- 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 162 afyRGEKLVNLKELADESLEKCREKGFPVRccivvkhvGRAELgmNDSPSQSPpvkrqcpdvqiswnegvdlwwhelmqe 241
Cdd:PRK12467 616 ---QSHLLAQLPVPAGLRSLCLDEPADLLC--------GYSGH--NPEVALDP--------------------------- 655
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 242 agdefepewcdaEDPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGVVHTIGGYMLYVATTFKYvFDFHPE 321
Cdd:PRK12467 656 ------------DNLAYVIYTSGSTGQPK-------------------------GVAISHGALANYVCVIAER-LQLAAD 697
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 322 DVFWCTADIGWITGHsYVTYGPLANGATsVLFEGIPTYPDESRLWSIVDKYKVTKFYTAPTAIRMLMKfgDEPVTKHSRA 401
Cdd:PRK12467 698 DSMLMVSTFAFDLGV-TELFGALASGAT-LHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQ--ASRVALPRPQ 773
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 402 SLQVLGtvGEpINPEAWLWYHRVVGSQhCPIVDTFWQTETGGHMLT-PLPGATpmKPGSASF---PFFGVAPAILNEsge 477
Cdd:PRK12467 774 RALVCG--GE-ALQVDLLARVRALGPG-ARLINHYGPTETTVGVSTyELSDEE--RDFGNVPigqPLANLGLYILDH--- 844
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 478 elegeaegYLvfkQPWP-GIMRTIY--------GNHTR--FETTYFKKFPG------YYVTGDGCRRDQDGYYWITGRID 540
Cdd:PRK12467 845 --------YL---NPVPvGVVGELYiggaglarGYHRRpaLTAERFVPDPFgadggrLYRTGDLARYRADGVIEYLGRMD 913
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 541 DMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECL-YCFVTLCDGHTFSSTLTEELKKQIREKIGPIATPDYI 619
Cdd:PRK12467 914 HQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLVaYLVPAAVADGAEHQATRDELKAQLRQVLPDYMVPAHL 993
|
570 580
....*....|....*....|.
gi 1538017002 620 QNAPGLPKTRSGKIMRRVLRK 640
Cdd:PRK12467 994 LLLDSLPLTPNGKLDRKALPK 1014
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
77-640 |
1.74e-11 |
|
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: 66.56 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 77 GETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLcERILDSS-CS 155
Cdd:cd17653 18 SLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARI-QAILRTSgAT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 156 LLITTDAfyrgeklvnlkeladeslekcrekgfpvrccivvkhvgraelgmndspsqsppvkrqcpdvqiswnegvdlww 235
Cdd:cd17653 97 LLLTTDS------------------------------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 236 helmqeagdefepewcdAEDPLFILYTSGSTGKPKLCagsicwsvemdtkpqpedPFSPQGVVHTI--GGYMLY------ 307
Cdd:cd17653 104 -----------------PDDLAYIIFTSGSTGIPKGV------------------MVPHRGVLNYVsqPPARLDvgpgsr 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 308 VATTFKYVFDFhpedvfwCTADIgwitghsyvtYGPLANGATSVLFEGIPTYPDESRlwsivdkyKVTKFYTAPTAIRML 387
Cdd:cd17653 149 VAQVLSIAFDA-------CIGEI----------FSTLCNGGTLVLADPSDPFAHVAR--------TVDALMSTPSILSTL 203
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 388 mkfgdepvtkhSRASLQVLGTV---GEPINP---EAWlWYHRVV----GSQHCPIVDTFWQTETGghmlTPLPGATPMkP 457
Cdd:cd17653 204 -----------SPQDFPNLKTIflgGEAVPPsllDRW-SPGRRLynayGPTECTISSTMTELLPG----QPVTIGKPI-P 266
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 458 GSASFpffgvapaILNESgeelegeaegylvfKQPWP------------GIMRTIYGNH----TRFETTYFKKFPGYYVT 521
Cdd:cd17653 267 NSTCY--------ILDAD--------------LQPVPegvvgeicisgvQVARGYLGNPaltaSKFVPDPFWPGSRMYRT 324
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 522 GDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVES-ALVEHEAVAEAAVVGHphpvkGECLYCFVTLcdghtfSSTLTE 600
Cdd:cd17653 325 GDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEvVLQSQPEVTQAAAIVV-----NGRLVAFVTP------ETVDVD 393
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1538017002 601 ELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 640
Cdd:cd17653 394 GLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
521-642 |
2.04e-11 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 66.76 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 521 TGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSStltE 600
Cdd:PRK08315 431 TGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTE---E 507
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1538017002 601 ELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 642
Cdd:PRK08315 508 DVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREMM 549
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
491-646 |
2.99e-11 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 66.17 E-value: 2.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 491 QPWPGIMRTIYGNHTRFETT--------YFKKF---PGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESAL 559
Cdd:PRK07445 287 QVLPHAQITIPANQTGNITIqaqslalgYYPQIldsQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAI 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 560 VEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfsSTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 639
Cdd:PRK07445 367 LATGLVQDVCVLGLPDPHWGEVVTAIYVPKDP----SISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQ 442
|
....*..
gi 1538017002 640 KIAQNDH 646
Cdd:PRK07445 443 QIAVQRL 449
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
80-638 |
9.92e-11 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 65.45 E-value: 9.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 80 TKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLcERIL-DSSCSLLI 158
Cdd:PRK10252 482 YQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRL-KMMLeDARPSLLI 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 159 TTDAFyrGEKLVNLKELADESLekcrekgfpvrccivvkhvgRAELgmndSPSQSPPVKRQCPDvqiswnegvdlwwhel 238
Cdd:PRK10252 561 TTADQ--LPRFADVPDLTSLCY--------------------NAPL----APQGAAPLQLSQPH---------------- 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 239 mqeagdefepewcdaeDPLFILYTSGSTGKPKlcaGSIcwsVE----------MdtkpQPEDPFSPQGVvhtiggymlyV 308
Cdd:PRK10252 599 ----------------HTAYIIFTSGSTGRPK---GVM---VGqtaivnrllwM----QNHYPLTADDV----------V 642
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 309 ATTFKYVFDFHPEDVFWctadigwitghsyvtygPLANGATSVLFEgiptyPDESR----LWSIVDKYKVTKFYTAPTai 384
Cdd:PRK10252 643 LQKTPCSFDVSVWEFFW-----------------PFIAGAKLVMAE-----PEAHRdplaMQQFFAEYGVTTTHFVPS-- 698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 385 rMLMKFGDEPVTKHSRASLQVLGTV---GEPINPEAWLWYHRVVGSqhcPIVDTFWQTE---------TGGHMLTPLPGA 452
Cdd:PRK10252 699 -MLAAFVASLTPEGARQSCASLRQVfcsGEALPADLCREWQQLTGA---PLHNLYGPTEaavdvswypAFGEELAAVRGS 774
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 453 T-PMkpgsaSFPFFGVAPAILNESGeelegeaegylvfkQPWP-GIMRTIY--------GNHTRFETTYfKKF------P 516
Cdd:PRK10252 775 SvPI-----GYPVWNTGLRILDARM--------------RPVPpGVAGDLYltgiqlaqGYLGRPDLTA-SRFiadpfaP 834
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 517 G--YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEH----EAVAEAAVVGHPHPVKGEC--LYCFVTL 588
Cdd:PRK10252 835 GerMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALpdveQAVTHACVINQAAATGGDArqLVGYLVS 914
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1538017002 589 CDGHTFSStltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 638
Cdd:PRK10252 915 QSGLPLDT---SALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
61-270 |
2.43e-10 |
|
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: 63.41 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 61 KKLGDKVAFYWEGNEPGETTKITYRELLVQVCQFSNVLRKQGiQKGDRVAIYMPMILELVVAMLACARLGALHSIVFA-- 138
Cdd:cd05931 4 AARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPpt 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 139 -GFSAESLCERILDSSCSLLITTDAFyrgeklvnlkeladeslekcrekgfpvrccivvkhvgRAELgmndspsqsPPVK 217
Cdd:cd05931 83 pGRHAERLAAILADAGPRVVLTTAAA-------------------------------------LAAV---------RAFA 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1538017002 218 RQCPDVQISWNEGVDLwwheLMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPK 270
Cdd:cd05931 117 ASRPAAGTPRLLVVDL----LPDTSAADWPPPSPDPDDIAYLQYTSGSTGTPK 165
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
65-640 |
3.13e-10 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 63.07 E-value: 3.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 65 DKVAFYwegnEPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGAlhsiVFAGFSAES 144
Cdd:PLN02330 43 DKVAFV----EAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGG----VFSGANPTA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 145 LCERILD----SSCSLLITTDAFYrgeklvnlkeladeslEKCREKGFPVrccIVVKHVgraelgmndspsqsppvkrqC 220
Cdd:PLN02330 115 LESEIKKqaeaAGAKLIVTNDTNY----------------GKVKGLGLPV---IVLGEE--------------------K 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 221 PDVQISWNEGVDLwwhelMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPK--------LCAgSICWSVemdtkpqpedpF 292
Cdd:PLN02330 156 IEGAVNWKELLEA-----ADRAGDTSDNEEILQTDLCALPFSSGTTGISKgvmlthrnLVA-NLCSSL-----------F 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 293 SpqgvvhtIGGYMLYVATTFKYVFDFHpedvfwctadIGWITGHSYVTygpLANGATSVLfegIPTYPDESRLWSIVDKy 372
Cdd:PLN02330 219 S-------VGPEMIGQVVTLGLIPFFH----------IYGITGICCAT---LRNKGKVVV---MSRFELRTFLNALITQ- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 373 KVTKFYTAPTAIRMLMKfgdEPVTKH---SRASLQVLGTVGEPINPEAWLWYH-RVVGSQhcpIVDTFWQTETGGHMLT- 447
Cdd:PLN02330 275 EVSFAPIVPPIILNLVK---NPIVEEfdlSKLKLQAIMTAAAPLAPELLTAFEaKFPGVQ---VQEAYGLTEHSCITLTh 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 448 --PLPGATPMKPGSASFPFFGVAPAILNESGEelegeaegyLVFKQPWPG--------IMRTIYGNHTRFETTYFKKfpG 517
Cdd:PLN02330 349 gdPEKGHGIAKKNSVGFILPNLEVKFIDPDTG---------RSLPKNTPGelcvrsqcVMQGYYNNKEETDRTIDED--G 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 518 YYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSSt 597
Cdd:PLN02330 418 WLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESE- 496
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1538017002 598 ltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 640
Cdd:PLN02330 497 --EDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKE 537
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
491-648 |
3.37e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 62.80 E-value: 3.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 491 QPWPGIMrtiYGN-HTR---FETTYFKK-----FPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVE 561
Cdd:PRK07008 377 LPWDGKA---FGDlQVRgpwVIDRYFRGdasplVDGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVA 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 562 HEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSStltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKI 641
Cdd:PRK07008 454 HPAVAEAACIACAHPKWDERPLLVVVKRPGAEVTR---EELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQ 530
|
....*..
gi 1538017002 642 AQnDHDL 648
Cdd:PRK07008 531 FR-DYVL 536
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
517-638 |
4.54e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 62.71 E-value: 4.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 517 GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLcdgHTFSS 596
Cdd:PRK13383 396 GMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVL---HPGSG 472
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1538017002 597 TLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 638
Cdd:PRK13383 473 VDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
521-638 |
7.37e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 61.59 E-value: 7.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 521 TGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGE--CLycfvTLCDGHTFSstl 598
Cdd:PRK08308 295 TKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGErvKA----KVISHEEID--- 367
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1538017002 599 TEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 638
Cdd:PRK08308 368 PVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
235-577 |
7.44e-10 |
|
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: 61.72 E-value: 7.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 235 WHELMQEAGDEFEPEWCDAEDPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGVVHTIGGYMlYVATTFKY 314
Cdd:cd05932 118 WDDLIAQHPPLEERPTRFPEQLATLIYTSGTTGQPK-------------------------GVMLTFGSFA-WAAQAGIE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 315 VFDFHPEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDE------------SRLWS-----IVDKYKVTKf 377
Cdd:cd05932 172 HIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESLDTFVEDvqrarptlffsvPRLWTkfqqgVQDKIPQQK- 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 378 ytaptaIRMLMK--FGDEPVTKHSRASL-----QVLGTVGEPINPEAWLWYHRVvgsqHCPIVDTFWQTETGGHMLTPLP 450
Cdd:cd05932 251 ------LNLLLKipVVNSLVKRKVLKGLgldqcRLAGCGSAPVPPALLEWYRSL----GLNILEAYGMTENFAYSHLNYP 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 451 GATpmKPGSASFPFFGVAPAIlnesgeelegEAEGYLVFKQPwpGIMRTIYGNHTRFETTYFKKfpGYYVTGDGCRRDQD 530
Cdd:cd05932 321 GRD--KIGTVGNAGPGVEVRI----------SEDGEILVRSP--ALMMGYYKDPEATAEAFTAD--GFLRTGDKGELDAD 384
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1538017002 531 GYYWITGRIDDMLNVS-GHLLSTAEVESALVEHEAVAEAAVVGH--PHPV 577
Cdd:cd05932 385 GNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIGSglPAPL 434
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
254-638 |
9.21e-10 |
|
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: 61.30 E-value: 9.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 254 EDPLFILYTSGSTGKPKlcaGSIcwsvemdtkpqpedpFSPQGVV-HTIGGYMLYVATTFKYV-------FDFHPEDVFw 325
Cdd:cd17644 106 ENLAYVIYTSGSTGKPK---GVM---------------IEHQSLVnLSHGLIKEYGITSSDRVlqfasiaFDVAAEEIY- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 326 ctadIGWITGHSYVTygplangatsVLFEGIPTYPDesrLWSIVDKYKVTKFYTAPTAIRMLMKFGdEPVTKHSRASLQV 405
Cdd:cd17644 167 ----VTLLSGATLVL----------RPEEMRSSLED---FVQYIQQWQLTVLSLPPAYWHLLVLEL-LLSTIDLPSSLRL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 406 LGTVGEPINPEAW-LW---------YHRVVGSQHCPIVDTFwqtetggHMLTPLPGATPMKPGSASfPFFGVAPAILNEs 475
Cdd:cd17644 229 VIVGGEAVQPELVrQWqknvgnfiqLINVYGPTEATIAATV-------CRLTQLTERNITSVPIGR-PIANTQVYILDE- 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 476 geelegeaegylvFKQPWP-GIMRTIYGNHTRFETTYF-------KKF--------PG--YYVTGDGCRRDQDGYYWITG 537
Cdd:cd17644 300 -------------NLQPVPvGVPGELHIGGVGLARGYLnrpeltaEKFishpfnssESerLYKTGDLARYLPDGNIEYLG 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 538 RIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTlcdGHTFSSTLTEELKKQIREKIGPIATPD 617
Cdd:cd17644 367 RIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIV---PHYEESPSTVELRQFLKAKLPDYMIPS 443
|
410 420
....*....|....*....|.
gi 1538017002 618 YIQNAPGLPKTRSGKIMRRVL 638
Cdd:cd17644 444 AFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
83-270 |
9.28e-10 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 61.75 E-value: 9.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 83 TYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGA-LHSIVFAGFSAEslCERILDSS-CSLLITT 160
Cdd:PRK08315 45 TYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAiLVTINPAYRLSE--LEYALNQSgCKALIAA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 161 DAF----YRG--EKLVnlKELADESLEKCREKGFPvrcciVVKHVGRaeLGMNDSPSQSPpvkrqcpdvqiswnegvdlw 234
Cdd:PRK08315 123 DGFkdsdYVAmlYELA--PELATCEPGQLQSARLP-----ELRRVIF--LGDEKHPGMLN-------------------- 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1538017002 235 WHELMqEAGDEFEPEWCDA-------EDPLFILYTSGSTGKPK 270
Cdd:PRK08315 174 FDELL-ALGRAVDDAELAArqatldpDDPINIQYTSGTTGFPK 215
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
516-640 |
1.09e-09 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 60.83 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 516 PGYYVTGDGCRRDqDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLycfVTLCDGHTFS 595
Cdd:PRK07824 233 PGWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRV---VAAVVGDGGP 308
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1538017002 596 STLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 640
Cdd:PRK07824 309 APTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVR 353
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
517-640 |
1.20e-09 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 61.34 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 517 GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSS 596
Cdd:PRK05620 430 GWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTR 509
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1538017002 597 TLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 640
Cdd:PRK05620 510 ETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQ 553
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
78-638 |
2.52e-09 |
|
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: 60.18 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 78 ETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLL 157
Cdd:cd17656 10 ENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 158 ITtdafyrgeklvnlkeladeslekCREkgfpvrccivvkhvgraelgMNDSPSQSPPVkrqcpdVQISWnegvDLWWHE 237
Cdd:cd17656 90 LT-----------------------QRH--------------------LKSKLSFNKST------ILLED----PSISQE 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 238 LMQEAGDEFEpewcdAEDPLFILYTSGSTGKPKLCAgsicwsVEMDTKPQPEDPFSPQGVVHTIGGYMLYVATTFkyvfd 317
Cdd:cd17656 117 DTSNIDYINN-----SDDLLYIIYTSGTTGKPKGVQ------LEHKNMVNLLHFEREKTNINFSDKVLQFATCSF----- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 318 fhpeDVfwCTADIgwitghsyvtYGPLANGATSVLFEGiPTYPDESRLWSIVDKYKVTKFYTAPTAIRMLmkFGDEPVTK 397
Cdd:cd17656 181 ----DV--CYQEI----------FSTLLSGGTLYIIRE-ETKRDVEQLFDLVKRHNIEVVFLPVAFLKFI--FSEREFIN 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 398 HSRASLQVLGTVGEPI---NPeawlwYHRVVGSQHCPIVDTFWQTETggHMLT--------PLPGATPM-KPGSASFPFf 465
Cdd:cd17656 242 RFPTCVKHIITAGEQLvitNE-----FKEMLHEHNVHLHNHYGPSET--HVVTtytinpeaEIPELPPIgKPISNTWIY- 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 466 gvapaILNESgeelegeaegylvfKQPWP-GIMRTIY--------GNHTRFETTYFKKFPG-------YYVTGDGCRRDQ 529
Cdd:cd17656 314 -----ILDQE--------------QQLQPqGIVGELYisgasvarGYLNRQELTAEKFFPDpfdpnerMYRTGDLARYLP 374
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 530 DGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVtlCDGHTFSstlTEELKKQIREK 609
Cdd:cd17656 375 DGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYF--VMEQELN---ISQLREYLAKQ 449
|
570 580
....*....|....*....|....*....
gi 1538017002 610 IGPIATPDYIQNAPGLPKTRSGKIMRRVL 638
Cdd:cd17656 450 LPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
252-644 |
3.21e-09 |
|
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: 59.86 E-value: 3.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 252 DAEDPLFILYTSGSTGKPK--------LCAGSICWSVEMdtkpqpedPFSPQGVVhtiggymLYVATtfkYVFDFHPEDV 323
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKgvviehraLSTSALAHGRAL--------GLTSESRV-------LQFAS---YTFDVSILEI 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 324 FwctadigwitghsyvtyGPLANGATSVlfegIPtyPDESRLWSIVD---KYKVTkfyTA---PTAIRMLmkfGDEPVTk 397
Cdd:cd05918 166 F-----------------TTLAAGGCLC----IP--SEEDRLNDLAGfinRLRVT---WAfltPSVARLL---DPEDVP- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 398 hsraSLQVLGTVGEPINPEAW-LWYHRV------------VGSQHCPIVD-------------TFWQTETGGH-MLTPLp 450
Cdd:cd05918 216 ----SLRTLVLGGEALTQSDVdTWADRVrlinaygpaectIAATVSPVVPstdprnigrplgaTCWVVDPDNHdRLVPI- 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 451 GAT-------PMkpgsasfpffgVAPAILNESGEELEgeaegylVFKQPWPGIMRTIYGNHTRFettyfkkfpgyYVTGD 523
Cdd:cd05918 291 GAVgelliegPI-----------LARGYLNDPEKTAA-------AFIEDPAWLKQEGSGRGRRL-----------YRTGD 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 524 GCRRDQDG--YYwiTGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGEC---LYCFVTLcDGHTFSSTL 598
Cdd:cd05918 342 LVRYNPDGslEY--VGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVVKPKDGSSspqLVAFVVL-DGSSSGSGD 418
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1538017002 599 TEELKKQIREKIGPIAT----------PDY-IQNA----PGLPKTRSGKIMRRVLRKIAQN 644
Cdd:cd05918 419 GDSLFLEPSDEFRALVAelrsklrqrlPSYmVPSVflplSHLPLTASGKIDRRALRELAES 479
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
519-638 |
3.22e-09 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 60.57 E-value: 3.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 519 YVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAvVGHPHPVKGECLYCFVTLCDGHTFSSTL 598
Cdd:PRK05691 4104 YRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAA-VAVQEGVNGKHLVGYLVPHQTVLAQGAL 4182
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1538017002 599 TEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 638
Cdd:PRK05691 4183 LERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
79-638 |
4.23e-09 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 59.64 E-value: 4.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 79 TTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESL---CErILDSSCS 155
Cdd:PRK05857 39 TSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIerfCQ-ITDPAAA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 156 LLIttdafyRGEKLvnlkelADESLEKCREKGFPVRCCIVVKHVGRAELGMNDSPSQSPpvkrqcpdvqiswNEGVDlww 235
Cdd:PRK05857 118 LVA------PGSKM------ASSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAGNA-------------DQGSE--- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 236 helmqeagdefepewcdaeDPLFILYTSGSTGKPKLcagsicwsvemdtkpqpedpfspqgvvhtiggyMLYVATTFKYV 315
Cdd:PRK05857 170 -------------------DPLAMIFTSGTTGEPKA---------------------------------VLLANRTFFAV 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 316 FD-FHPEDVFWctadIGWITGHSyvTYGPLAngATSV---------LFEG---IPTYPDESRLWSIVDKYKVTKFYTAPT 382
Cdd:PRK05857 198 PDiLQKEGLNW----VTWVVGET--TYSPLP--ATHIgglwwiltcLMHGglcVTGGENTTSLLEILTTNAVATTCLVPT 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 383 AIRML---MKFGDEPVtkhsrASLQVLGTVG-EPINPEAwlwyhRVVGSQHCPIVDTFWQTETGGHMLTpLP----GATP 454
Cdd:PRK05857 270 LLSKLvseLKSANATV-----PSLRLVGYGGsRAIAADV-----RFIEATGVRTAQVYGLSETGCTALC-LPtddgSIVK 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 455 MKPGSASFPFFGV----APAILNESGEELEGEAEGYLVFKQPWPGIMRTIYGNHTRFETTYFKkfpGYYVTGDGCRRDQD 530
Cdd:PRK05857 339 IEAGAVGRPYPGVdvylAATDGIGPTAPGAGPSASFGTLWIKSPANMLGYWNNPERTAEVLID---GWVNTGDLLERRED 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 531 GYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFV---TLCDGHTfsstlTEELKKQI- 606
Cdd:PRK05857 416 GFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVvasAELDESA-----ARALKHTIa 490
|
570 580 590
....*....|....*....|....*....|....*
gi 1538017002 607 ---REKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 638
Cdd:PRK05857 491 arfRRESEPMARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
254-632 |
4.50e-09 |
|
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: 58.93 E-value: 4.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 254 EDPLFILYTSGSTGKPKlcagSICWSvemdtkpqPEDPFSpqgvvhTIGGYMLYVATTFKYVFDFHPEDVfwCTADIGW- 332
Cdd:cd05924 3 ADDLYILYTGGTTGMPK----GVMWR--------QEDIFR------MLMGGADFGTGEFTPSEDAHKAAA--AAAGTVMf 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 333 -----ITGHSYVTYGPLANGATSVLFEGIPTYPDEsrLWSIVDKYKVTKF------YTAPTaIRMLMKFGDEPVTkhsra 401
Cdd:cd05924 63 papplMHGTGSWTAFGGLLGGQTVVLPDDRFDPEE--VWRTIEKHKVTSMtivgdaMARPL-IDALRDAGPYDLS----- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 402 SLQVLGTVGEPINPEawlwyHRVVGSQHCP---IVDTFWQTETGGHMLTPlpgATPMKPGSASFPFFGVAPAILNESgee 478
Cdd:cd05924 135 SLFAISSGGALLSPE-----VKQGLLELVPnitLVDAFGSSETGFTGSGH---SAGSGPETGPFTRANPDTVVLDDD--- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 479 legeaegyLVFKQPWPGIMRTI----------YGNHTRFETTyFKKFPG--YYVTGDGCRRDQDGYYWITGRIDDMLNVS 546
Cdd:cd05924 204 --------GRVVPPGSGGVGWIarrghiplgyYGDEAKTAET-FPEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTG 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 547 GHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSStltEELKKQIREKIGPIATPDYIQNAPGLP 626
Cdd:cd05924 275 GEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQLREGAGVDL---EELREHCRTRIARYKLPKQVVFVDEIE 351
|
....*.
gi 1538017002 627 KTRSGK 632
Cdd:cd05924 352 RSPAGK 357
|
|
| ACAS_N |
pfam16177 |
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many ... |
6-53 |
5.61e-09 |
|
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: 52.47 E-value: 5.61e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1538017002 6 EFWGNIAKEFYWKTPCpgpflQYNFDVTKGkIFTEWMKGATTNICYNV 53
Cdd:pfam16177 14 GFWGEVAKELDWFKPF-----DKVLDGSNG-PFAKWFVGGKLNVCYNC 55
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
77-638 |
6.62e-09 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 59.41 E-value: 6.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 77 GETtkITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSL 156
Cdd:PRK05691 2211 GQT--LSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGL 2288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 157 LITTDAFYRGeklvnLKELADESLEKCREKGFPVRccivvkhvgraelgmnDSPSQSPPVKRQCPDVQIswnegvdlwwh 236
Cdd:PRK05691 2289 LLSDRALFEA-----LGELPAGVARWCLEDDAAAL----------------AAYSDAPLPFLSLPQHQA----------- 2336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 237 elmqeagdefepewcdaedplFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGVVHTIGGYMLYVATTFKyVF 316
Cdd:PRK05691 2337 ---------------------YLIYTSGSTGKPK-------------------------GVVVSHGEIAMHCQAVIE-RF 2369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 317 DFHPEDvfwCTADIGWIT--GHSYVTYGPLANGATSVL-FEGiptYPDESRLWSIVDKYKVTKFYTAPTAIRMLMKFgde 393
Cdd:PRK05691 2370 GMRADD---CELHFYSINfdAASERLLVPLLCGARVVLrAQG---QWGAEEICQLIREQQVSILGFTPSYGSQLAQW--- 2440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 394 PVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGSQHcpIVDTFWQTETgghMLTPLPGATP--MKPGSASFPFFGVAPA- 470
Cdd:PRK05691 2441 LAGQGEQLPVRMCITGGEALTGEHLQRIRQAFAPQL--FFNAYGPTET---VVMPLACLAPeqLEEGAASVPIGRVVGAr 2515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 471 ---ILNESGEELEGEAEGYLvfkqpWPGIMRTIYGNH-------TRFETTYFKKFPG-YYVTGDGCRRDQDGYYWITGRI 539
Cdd:PRK05691 2516 vayILDADLALVPQGATGEL-----YVGGAGLAQGYHdrpgltaERFVADPFAADGGrLYRTGDLVRLRADGLVEYVGRI 2590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 540 DDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPvKGECLYCFV---TLCDGHTFSSTLTEELKKQIREKIgpiatP 616
Cdd:PRK05691 2591 DHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTP-SGKQLAGYLvsaVAGQDDEAQAALREALKAHLKQQL-----P 2664
|
570 580
....*....|....*....|....*..
gi 1538017002 617 DYIQNA-----PGLPKTRSGKIMRRVL 638
Cdd:PRK05691 2665 DYMVPAhlillDSLPLTANGKLDRRAL 2691
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
79-640 |
7.46e-09 |
|
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: 58.59 E-value: 7.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 79 TTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLLI 158
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 159 TtdafyrgeklvNLKELADESLEKcrekgfpvrccivvkhvgraelgmndspsqSPPVkrqCPDVqiswnegvdlwwhel 238
Cdd:cd05939 81 F-----------NLLDPLLTQSST------------------------------EPPS---QDDV--------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 239 mqeagdefepewcDAEDPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfsPQGVVHTiggYMLYVATTFKYVFDF 318
Cdd:cd05939 102 -------------NFRDKLFYIYTSGTTGLPK-----------------------AAVIVHS---RYYRIAAGAYYAFGM 142
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 319 HPEDVFWCTADIgWITGHSYVTYGP-LANGATSVLFEGIPTypdeSRLWSIVDKYKVTKF-YTAPTAIRMLMKFGDEPVT 396
Cdd:cd05939 143 RPEDVVYDCLPL-YHSAGGIMGVGQaLLHGSTVVIRKKFSA----SNFWDDCVKYNCTIVqYIGEICRYLLAQPPSEEEQ 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 397 KHsraslQVLGTVGEPINPEAWlwyHRVVGSQHCPIVDTFWQTETGGHMLTPLPGatpmKPGSASF-PFFG--VAPAIL- 472
Cdd:cd05939 218 KH-----NVRLAVGNGLRPQIW---EQFVRRFGIPQIGEFYGATEGNSSLVNIDN----HVGACGFnSRILpsVYPIRLi 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 473 --NESGEELEGEAEGYLVFKQPW-PGIM--RTIYGNHTRFETTY--------------FKKFPGYYVTGDGCRRDQDGYY 533
Cdd:cd05939 286 kvDEDTGELIRDSDGLCIPCQPGePGLLvgKIIQNDPLRRFDGYvnegatnkkiardvFKKGDSAFLSGDVLVMDELGYL 365
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 534 WITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHP-VKGEC----LYCFVTLCDGHTFSSTLTEELKkqire 608
Cdd:cd05939 366 YFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVEVPgVEGRAgmaaIVDPERKVDLDRFSAVLAKSLP----- 440
|
570 580 590
....*....|....*....|....*....|..
gi 1538017002 609 kigPIATPDYIQNAPGLPKTRSGKIMRRVLRK 640
Cdd:cd05939 441 ---PYARPQFIRLLPEVDKTGTFKLQKTDLQK 469
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
77-270 |
1.29e-08 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 58.20 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 77 GETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSL 156
Cdd:PLN02387 102 GEYEWITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTT 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 157 LITtdafyrGEKlvNLKELAD--ESLEkcrekgfpvrcciVVKHVgraeLGMNDSPSQSPPVKRQCPDVQISWNEGVDlw 234
Cdd:PLN02387 182 VIC------DSK--QLKKLIDisSQLE-------------TVKRV----IYMDDEGVDSDSSLSGSSNWTVSSFSEVE-- 234
|
170 180 190
....*....|....*....|....*....|....*.
gi 1538017002 235 whELMQEAgdEFEPEWCDAEDPLFILYTSGSTGKPK 270
Cdd:PLN02387 235 --KLGKEN--PVDPDLPSPNDIAVIMYTSGSTGLPK 266
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
83-640 |
1.62e-08 |
|
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: 57.44 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 83 TYRELLVQVCQFSNVLRKQ-GIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESL--CERIldSSCSLLIT 159
Cdd:cd05937 7 TYSETYDLVLRYAHWLHDDlGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLihCLKL--SGSRFVIV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 160 TDafyrgeklvnlkeladeslekcrekgfpvrccivvkhvgraelgmndspsqsppvkrqcpdvqiswnegvdlwwhelm 239
Cdd:cd05937 85 DP------------------------------------------------------------------------------ 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 240 qeagdefepewcdaEDPLFILYTSGSTGKPKLCAGSI------CWSVEMDTKPQPEDP-FSPQGVVHTIGG-----YMLY 307
Cdd:cd05937 87 --------------DDPAILIYTSGTTGLPKAAAISWrrtlvtSNLLSHDLNLKNGDRtYTCMPLYHGTAAflgacNCLM 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 308 VATTFKYVFDFHPEDvFWctADIgwitghsyvtygpLANGATSVLFEG--------IPTYPDESR--------------L 365
Cdd:cd05937 153 SGGTLALSRKFSASQ-FW--KDV-------------RDSGATIIQYVGelcryllsTPPSPYDRDhkvrvawgnglrpdI 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 366 WsivDKYK-------VTKFYTAPTAIRMLMKFGDEPVTkhsraslqvLGTVGEpinpEAWLWyHRVVGSQHCPI-VDTfw 437
Cdd:cd05937 217 W---ERFRerfnvpeIGEFYAATEGVFALTNHNVGDFG---------AGAIGH----HGLIR-RWKFENQVVLVkMDP-- 277
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 438 qtETGGHMLTPLPGatpmkpgsasfpFFGVAPailnesgeELEGEAEGYLVFKQP---WPGIMRTIYGNHTRFETTYFKK 514
Cdd:cd05937 278 --ETDDPIRDPKTG------------FCVRAP--------VGEPGEMLGRVPFKNreaFQGYLHNEDATESKLVRDVFRK 335
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 515 FPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVG---HPHPVKGECLYCfvTLCDG 591
Cdd:cd05937 336 GDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGvkvPGHDGRAGCAAI--TLEES 413
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1538017002 592 HTFSSTLT-EELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 640
Cdd:cd05937 414 SAVPTEFTkSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRD 463
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
78-353 |
1.88e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 57.68 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 78 ETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSLL 157
Cdd:PTZ00216 118 ETRYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAI 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 158 ITTdafyrGEKLVNLkeladesLEKCREKGFPvRCCIVvkHVGraelgmndspSQSPPVKRQCPDVqISWNEGVDLWWHE 237
Cdd:PTZ00216 198 VCN-----GKNVPNL-------LRLMKSGGMP-NTTII--YLD----------SLPASVDTEGCRL-VAWTDVVAKGHSA 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 238 LMQEAGDefEPEWCDAEdpLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGVVHTIGGYMLYVATTFKYVFD 317
Cdd:PTZ00216 252 GSHHPLN--IPENNDDL--ALIMYTSGTTGDPK-------------------------GVMHTHGSLTAGILALEDRLND 302
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1538017002 318 F--HPEDvfwctadigwitGHSYVTYGPLAN----GATSVLF 353
Cdd:PTZ00216 303 LigPPEE------------DETYCSYLPLAHimefGVTNIFL 332
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
517-643 |
1.04e-07 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 55.32 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 517 GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALveHEAVAEA----AVVGHPHPVKGECLycfVTLcdgH 592
Cdd:PRK08633 1019 GWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEEL--AKALGGEevvfAVTAVPDEKKGEKL---VVL---H 1090
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1538017002 593 TFSSTLTEELKKQIRE-KIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQ 643
Cdd:PRK08633 1091 TCGAEDVEELKRAIKEsGLPNLWKPSRYFKVEALPLLGSGKLDLKGLKELAL 1142
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
237-640 |
1.31e-07 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 54.80 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 237 ELMQEAGDEFEPEWCDA-EDPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGVvhTIGGYMLYVATTFKYV 315
Cdd:PLN02860 154 MLKQRALGTTELDYAWApDDAVLICFTSGTTGRPK-------------------------GV--TISHSALIVQSLAKIA 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 316 F-DFHPEDVFWCTADIGWITGHSYVtygpLAN---GATSVLfegIPTYpDESRLWSIVDKYKVTKFYTAPTAIRMLMKFG 391
Cdd:PLN02860 207 IvGYGEDDVYLHTAPLCHIGGLSSA----LAMlmvGACHVL---LPKF-DAKAALQAIKQHNVTSMITVPAMMADLISLT 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 392 DEPVTKHSRASLQVL----GTVGEPINPEAWLWYHRVvgsqhcPIVDTFWQTETGGHM-LTPLPGATPMKPGSASFPFFG 466
Cdd:PLN02860 279 RKSMTWKVFPSVRKIlnggGSLSSRLLPDAKKLFPNA------KLFSAYGMTEACSSLtFMTLHDPTLESPKQTLQTVNQ 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 467 VAPAILNESGEELEGEAEGYLVFKQPWPGIMRT----IYGNHT--RF-----ETTYFKKFPGYYVTGDGCRRDQDGYYWI 535
Cdd:PLN02860 353 TKSSSVHQPQGVCVGKPAPHVELKIGLDESSRVgrilTRGPHVmlGYwgqnsETASVLSNDGWLDTGDIGWIDKAGNLWL 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 536 TGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSSTLT-----------EELKK 604
Cdd:PLN02860 433 IGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDGWIWSDNEKenakknltlssETLRH 512
|
410 420 430
....*....|....*....|....*....|....*...
gi 1538017002 605 QIREK-IGPIATPD-YIQNAPGLPKTRSGKIMRRVLRK 640
Cdd:PLN02860 513 HCREKnLSRFKIPKlFVQWRKPFPLTTTGKIRRDEVRR 550
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
64-270 |
1.70e-07 |
|
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: 54.38 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 64 GDKVAFYWEGNEP------GETT--------KITYRELLVQVCQFSNVLR-KQGIQKGDRVAIYMPMILELVVAMLACAR 128
Cdd:cd17632 36 ADRPALGQRATELvtdpatGRTTlrllprfeTITYAELWERVGAVAAAHDpEQPVRPGDFVAVLGFTSPDYATVDLALTR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 129 LGALHSIVFAGFSAESLCErILDSSCSLLITTDAfyrgeklvnlkELADESLEKCREKGFPVRcciVVKHVGRAELGMND 208
Cdd:cd17632 116 LGAVSVPLQAGASAAQLAP-ILAETEPRLLAVSA-----------EHLDLAVEAVLEGGTPPR---LVVFDHRPEVDAHR 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1538017002 209 SPSQSppVKRQCPDVQISWNEGVDLWWHELMQEAGDEFEPEwcDAEDPL-FILYTSGSTGKPK 270
Cdd:cd17632 181 AALES--ARERLAAVGIPVTTLTLIAVRGRDLPPAPLFRPE--PDDDPLaLLIYTSGSTGTPK 239
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
252-638 |
1.72e-07 |
|
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: 54.33 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 252 DAEDPLFILYTSGSTGKPKlcagsicwSVemdtkpqpedPFSPQGVVHTI----GGYML------YVATTFKYVFDFHPE 321
Cdd:cd17648 92 NSTDLAYAIYTSGTTGKPK--------GV----------LVEHGSVVNLRtslsERYFGrdngdeAVLFFSNYVFDFFVE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 322 DVFwctadIGWITGHSYVTYGPlangatSVLFegiptypDESRLWSIVDKYKVTKFYTAPTAIRMLmKFGdepvtkhSRA 401
Cdd:cd17648 154 QMT-----LALLNGQKLVVPPD------EMRF-------DPDRFYAYINREKVTYLSGTPSVLQQY-DLA-------RLP 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 402 SLQVLGTVGEPINPEAwlwYHRVVGSQHCPIVDTFWQTETGGHML-TPLPGATPmKPGSASFPFFGVAPAILNESGeele 480
Cdd:cd17648 208 HLKRVDAAGEEFTAPV---FEKLRSRFAGLIINAYGPTETTVTNHkRFFPGDQR-FDKSLGRPVRNTKCYVLNDAM---- 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 481 geaegylvfkQPWP-GIMRTIY--------GNHTRFETTYFK---------------KFPGYYVTGDGCRRDQDGYYWIT 536
Cdd:cd17648 280 ----------KRVPvGAVGELYlggdgvarGYLNRPELTAERflpnpfqteqerargRNARLYKTGDLVRWLPSGELEYL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 537 GRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGEC-----LYCFVTLCDGHtfsstLTE-ELKKQIREKI 610
Cdd:cd17648 350 GRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQSriqkyLVGYYLPEPGH-----VPEsDLLSFLRAKL 424
|
410 420
....*....|....*....|....*...
gi 1538017002 611 GPIATPDYIQNAPGLPKTRSGKIMRRVL 638
Cdd:cd17648 425 PRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
517-631 |
2.02e-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: 53.46 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 517 GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSS 596
Cdd:cd17636 217 GWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTE 296
|
90 100 110
....*....|....*....|....*....|....*
gi 1538017002 597 tltEELKKQIREKIGPIATPDYIQNAPGLPKTRSG 631
Cdd:cd17636 297 ---AELIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
81-164 |
2.08e-07 |
|
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: 53.90 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 81 KITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESL--CERIldSSCSLLI 158
Cdd:cd05940 3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLahCLNV--SSAKHLV 80
|
....*.
gi 1538017002 159 TTDAFY 164
Cdd:cd05940 81 VDAALY 86
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
54-269 |
3.23e-06 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 50.51 E-value: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 54 LDRNVHEkkLGDKVAFYW---EGNEPGETTKITYRELLVQVCQFSNVLrKQGIQKGDRVAIYMPMILELVVAMLACARLG 130
Cdd:PRK12476 40 IERNIAN--VGDTVAYRYldhSHSAAGCAVELTWTQLGVRLRAVGARL-QQVAGPGDRVAILAPQGIDYVAGFFAAIKAG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 131 ALHSIVFA----GfSAESLCERILDSSCSLLITTDAfyrgeklvnlkelADESLEKCREKgfpvrccivVKHVGRAELGM 206
Cdd:PRK12476 117 TIAVPLFApelpG-HAERLDTALRDAEPTVVLTTTA-------------AAEAVEGFLRN---------LPRLRRPRVIA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1538017002 207 NDspsqsppvkrQCPDvqiswnegvdlwwhelmqEAGDEFEPEWCDAEDPLFILYTSGSTGKP 269
Cdd:PRK12476 174 ID----------AIPD------------------SAGESFVPVELDTDDVSHLQYTSGSTRPP 208
|
|
| PRK09188 |
PRK09188 |
serine/threonine protein kinase; Provisional |
558-650 |
7.10e-06 |
|
serine/threonine protein kinase; Provisional
Pssm-ID: 236400 [Multi-domain] Cd Length: 365 Bit Score: 48.61 E-value: 7.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 558 ALVEHEAVAEAAVVGHPHPVKGECLYCFVtlcdgHTFSSTLTEELKKQIREKIGPIAtPDYIQNAPGLPKTRSGKIMRRV 637
Cdd:PRK09188 248 ALKSDPAVSDVAIALFSLPAKGVGLYAFV-----EAELPADEKSLRARLAGAKPPKP-PEHIQPVAALPRDADGTVRDDI 321
|
90
....*....|...
gi 1538017002 638 LRKIAQNDHDLGD 650
Cdd:PRK09188 322 LRLIAMNQIDELD 334
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
77-635 |
7.88e-06 |
|
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: 48.98 E-value: 7.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 77 GETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSL 156
Cdd:cd05914 3 YGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 157 LITTdafyrgeklvnlkeladeslekcrekgfpvrccivvkhvgraelgmndspsqsppvkrqcpdvqiswnegvdlwwh 236
Cdd:cd05914 83 IFVS---------------------------------------------------------------------------- 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 237 elmqeagdefepewcDAEDPLFILYTSGSTGKPK---LCAGSICWSV----EMDtKPQPEDpfspqgvvHTIGgyMLYVA 309
Cdd:cd05914 87 ---------------DEDDVALINYTSGTTGNSKgvmLTYRNIVSNVdgvkEVV-LLGKGD--------KILS--ILPLH 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 310 TTFKYVFDFhpedvfwctadigwitghsyVTygPLANGATSVLFEGIPTYPDE-------------SRLWSIVDKYKVTK 376
Cdd:cd05914 141 HIYPLTFTL--------------------LL--PLLNGAHVVFLDKIPSAKIIalafaqvtptlgvPVPLVIEKIFKMDI 198
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 377 FYTAPTAI---RMLMKFGDEPVTKHSRASLQ----------VLGtvGEPINPEAwLWYHRVVGsqhCPIVDTFWQTETGg 443
Cdd:cd05914 199 IPKLTLKKfkfKLAKKINNRKIRKLAFKKVHeafggnikefVIG--GAKINPDV-EEFLRTIG---FPYTIGYGMTETA- 271
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 444 hmltPLPGATP---MKPGSASFPFFGVAPAIlnesGEELEGEAEGYLVFKQpwPGIMRTIYGNHtrfETTYFKKFP-GYY 519
Cdd:cd05914 272 ----PIISYSPpnrIRLGSAGKVIDGVEVRI----DSPDPATGEGEIIVRG--PNVMKGYYKNP---EATAEAFDKdGWF 338
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 520 VTGDGCRRDQDGYYWITGRIDDM-LNVSGHLLSTAEVESALVEHEAVAEAAVV---------GHPHP----VKGECLycf 585
Cdd:cd05914 339 HTGDLGKIDAEGYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVLESLVVvqekklvalAYIDPdfldVKALKQ--- 415
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1538017002 586 VTLCDghtfssTLTEELKKQIREKigpiaTPDY-------IQNAPgLPKTRSGKIMR 635
Cdd:cd05914 416 RNIID------AIKWEVRDKVNQK-----VPNYkkiskvkIVKEE-FEKTPKGKIKR 460
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
519-638 |
9.87e-06 |
|
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: 48.32 E-value: 9.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 519 YVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTlcdghTFSSTL 598
Cdd:cd17645 325 YRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVT-----APEEIP 399
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1538017002 599 TEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 638
Cdd:cd17645 400 HEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
516-644 |
1.05e-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: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 516 PGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTlcdghtfS 595
Cdd:PRK08043 590 RGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASKGEALVLFTT-------D 662
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1538017002 596 STLT-EELKKQIREKIGP-IATPDYIQNAPGLPKTRSGKIMRRVLRKIAQN 644
Cdd:PRK08043 663 SELTrEKLQQYAREHGVPeLAVPRDIRYLKQLPLLGSGKPDFVTLKSMVDE 713
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
65-638 |
2.51e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 47.86 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 65 DKVAFYWEGNEpgettkITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAES 144
Cdd:PRK05691 1146 ERIALVWDGGS------LDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAER 1219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 145 LCERILDSSCSLLITTDAFyrgekLVNLKELADeslekcrekgfpvrccivVKHVGRAELGMNDSPSQSPpvkrqcpdvq 224
Cdd:PRK05691 1220 LAYMLADSGVELLLTQSHL-----LERLPQAEG------------------VSAIALDSLHLDSWPSQAP---------- 1266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 225 iswneGVDLWWHELMqeagdefepewcdaedplFILYTSGSTGKPKLCagsicwsvemdtkpqpedpfspqGVVH-TIGG 303
Cdd:PRK05691 1267 -----GLHLHGDNLA------------------YVIYTSGSTGQPKGV-----------------------GNTHaALAE 1300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 304 YMLYVATTfkYVFDfhPEDVFWCTADIGWITGhSYVTYGPLANGATSVLfEGIPTYPDESRLWSIVDKYKVTKFYTAPTa 383
Cdd:PRK05691 1301 RLQWMQAT--YALD--DSDVLMQKAPISFDVS-VWECFWPLITGCRLVL-AGPGEHRDPQRIAELVQQYGVTTLHFVPP- 1373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 384 irMLMKFGDEPVTKHSRaSLQVLGTVGEPINPE---------AWLWYHRVVGSQHCPIVDTFWQTETGGHMLTPLpgatp 454
Cdd:PRK05691 1374 --LLQLFIDEPLAAACT-SLRRLFSGGEALPAElrnrvlqrlPQVQLHNRYGPTETAINVTHWQCQAEDGERSPI----- 1445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 455 mkpgsaSFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRTIYG----NHTRFETTYFKKfPG--YYVTGDGCRRD 528
Cdd:PRK05691 1446 ------GRPLGNVLCRVLDAELNLLPPGVAGELCIGGA--GLARGYLGrpalTAERFVPDPLGE-DGarLYRTGDRARWN 1516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 529 QDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHpHPVKGECLYCFVTLCDGHtfsSTLTEELKKQIRE 608
Cdd:PRK05691 1517 ADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVR-EGAAGAQLVGYYTGEAGQ---EAEAERLKAALAA 1592
|
570 580 590
....*....|....*....|....*....|....*
gi 1538017002 609 KIgpiatPDYIQNA-----PGLPKTRSGKIMRRVL 638
Cdd:PRK05691 1593 EL-----PEYMVPAqlirlDQMPLGPSGKLDRRAL 1622
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
61-159 |
6.05e-05 |
|
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: 46.01 E-value: 6.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 61 KKLGDKVAFYWEGNepgettKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGF 140
Cdd:cd17645 9 ERTPDHVAVVDRGQ------SLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDY 82
|
90
....*....|....*....
gi 1538017002 141 SAESLCERILDSSCSLLIT 159
Cdd:cd17645 83 PGERIAYMLADSSAKILLT 101
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
77-159 |
1.00e-04 |
|
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: 45.28 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 77 GETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCSL 156
Cdd:cd17639 1 GEYKYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSA 80
|
...
gi 1538017002 157 LIT 159
Cdd:cd17639 81 IFT 83
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
75-633 |
1.11e-04 |
|
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: 45.16 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 75 EPGETTKITYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACARLGAlhsiVFAGFSAESLCERILdssc 154
Cdd:cd17654 10 QTTSDTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGA----AYAPIDPASPEQRSL---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 155 SLLITTDAFYrgeKLVNlkeladeslekcrekgfpvrccivvKHVGRAelgmndsPSQSPPVKRqcpdvqiswnegvdlw 234
Cdd:cd17654 82 TVMKKCHVSY---LLQN-------------------------KELDNA-------PLSFTPEHR---------------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 235 wHELMQEAGdefepewCDAedplFILYTSGSTGKPKlcagsicwSVEMdtkpqPEDPFSPQgVVHtiggymlyvattFKY 314
Cdd:cd17654 111 -HFNIRTDE-------CLA----YVIHTSGTTGTPK--------IVAV-----PHKCILPN-IQH------------FRS 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 315 VFDFHPEDVFWCTadigwitghSYVTYGP--------LANGATSVlfegipTYPDE-----SRLWSIVDK-YKVTKFYTA 380
Cdd:cd17654 153 LFNITSEDILFLT---------SPLTFDPsvveiflsLSSGATLL------IVPTSvkvlpSKLADILFKrHRITVLQAT 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 381 PTAIRMLMK--FGDEPVTKHSraSLQVLGTVGE--PINPEAWLWYHRVVGSQHCPIVDTfwqTETGGHMLT--------P 448
Cdd:cd17654 218 PTLFRRFGSqsIKSTVLSATS--SLRVLALGGEpfPSLVILSSWRGKGNRTRIFNIYGI---TEVSCWALAykvpeedsP 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 449 LPGATPMkpgsasfpffgVAPAILNESGEELEGEAEGYLvfkqpwPGIMRTIY--GNHTRFETTYfkkfpgyYVTGDGCR 526
Cdd:cd17654 293 VQLGSPL-----------LGTVIEVRDQNGSEGTGQVFL------GGLNRVCIldDEVTVPKGTM-------RATGDFVT 348
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 527 RdQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHphpvKGECLYCFVTlcdGHTFSSTLTEELKKQI 606
Cdd:cd17654 349 V-KDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLS----DQQRLIAFIV---GESSSSRIHKELQLTL 420
|
570 580
....*....|....*....|....*..
gi 1538017002 607 REkigPIATPDYIQNAPGLPKTRSGKI 633
Cdd:cd17654 421 LS---SHAIPDTFVQIDKLPLTSHGKV 444
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
242-418 |
3.40e-04 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 43.73 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 242 AGDEFEPEWCDAEDPLFILYTSGSTGKPKlcagsicwsvemdtkpqpedpfspqGVVHTIGgymLYVA--TTFKYVFDFH 319
Cdd:PRK09274 162 AAAPFPMADLAPDDMAAILFTSGSTGTPK-------------------------GVVYTHG---MFEAqiEALREDYGIE 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 320 PEDVFWCTADIgwitghsYVTYGPlANGATSVLFEGIPTYP---DESRLWSIVDKYKVTKFYTAPTAIrmlmkfgdEPVT 396
Cdd:PRK09274 214 PGEIDLPTFPL-------FALFGP-ALGMTSVIPDMDPTRPatvDPAKLFAAIERYGVTNLFGSPALL--------ERLG 277
|
170 180
....*....|....*....|....*...
gi 1538017002 397 KHSRASLQVLGTV------GEPINPEAW 418
Cdd:PRK09274 278 RYGEANGIKLPSLrrvisaGAPVPIAVI 305
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
517-644 |
7.55e-04 |
|
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: 42.65 E-value: 7.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 517 GYYVTGD-GCRRDqdGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAE--AAVVGHPHPVKGECLYC--FVTLCDG 591
Cdd:cd05906 409 GWFRTGDlGFLDN--GNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsfTAAFAVRDPGAETEELAifFVPEYDL 486
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1538017002 592 HTFSSTLTEELKKQIREKIGpiATPDYI----QNApgLPKTRSGKIMRRVLRKIAQN 644
Cdd:cd05906 487 QDALSETLRAIRSVVSREVG--VSPAYLiplpKEE--IPKTSLGKIQRSKLKAAFEA 539
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
517-643 |
1.57e-03 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 41.87 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538017002 517 GYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTlcdghtfSS 596
Cdd:PRK06814 1010 GWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDARKGERIILLTT-------AS 1082
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1538017002 597 TLT-EELKKQIREK-IGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQ 643
Cdd:PRK06814 1083 DATrAAFLAHAKAAgASELMVPAEIITIDEIPLLGTGKIDYVAVTKLAE 1131
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
83-127 |
2.34e-03 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 40.95 E-value: 2.34e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1538017002 83 TYRELLVQVCQFSNVLRKQGIQKGDRVAIYMPMILELVVAMLACA 127
Cdd:PLN02430 78 TYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACA 122
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
78-136 |
4.83e-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: 4.83e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1538017002 78 ETTKITYRellvQVCQFSNV----LRKQGIQKGDRVAIYMPMILELVVAMLACARLGALHSIV 136
Cdd:TIGR03443 267 KTRSFTYK----QINEASNIlahyLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVI 325
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
78-132 |
4.84e-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: 4.84e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1538017002 78 ETTKITYRELLVQVCQFSNVLR-KQGIQKGDRVAIYMPMILELVVAMLACARLGAL 132
Cdd:cd05905 11 EATTLTWGKLLSRAEKIAAVLQkKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVV 66
|
|
| |
