|
Name |
Accession |
Description |
Interval |
E-value |
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
48-306 |
5.62e-170 |
|
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: 481.97 E-value: 5.62e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 48 VPEYFNFAHDVLDVWSQLEKTGHRPPNPAFWWVNGSGTEVKWTFEELGKQSRKAANVLEGVCGLQPEDRMMLVLPRLPDW 127
Cdd:cd05928 1 VPEYFNFASDVLDQWADKEKAGKRPPNPALWWVNGKGDEVKWSFRELGSLSRKAANVLSGACGLQRGDRVAVILPRVPEW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 128 WLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTSDALAPQVDAISADCPSLQTKLLVSDTSRPGWINFRELLR 207
Cdd:cd05928 81 WLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSVASECPSLKTKLLVSEKSRDGWLNFKELLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 208 AASPEHNCVRTRSGDSVAIYFTSGTTGAPKMVEHSQSSYGLGFVASGRRWMALTESDIFWNTTDTGWVKAAW-TLFSAWS 286
Cdd:cd05928 161 EASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWsSLFEPWI 240
|
250 260
....*....|....*....|
gi 26333877 287 NGACIFVHELPRVDAKTILN 306
Cdd:cd05928 241 QGACVFVHHLPRFDPLVILK 260
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
48-295 |
6.54e-71 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 229.23 E-value: 6.54e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 48 VPEYFNFAHDVLDVWsqLEKTGHRPpnpAFWWVNGSGTEVKWTFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDW 127
Cdd:COG0365 4 VGGRLNIAYNCLDRH--AEGRGDKV---ALIWEGEDGEERTLTYAELRREVNRFANALRAL-GVKKGDRVAIYLPNIPEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 128 WLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTSDA---------LAPQVDAISADCPSLQTKLLV----SDT 194
Cdd:COG0365 78 VIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGglrggkvidLKEKVDEALEELPSLEHVIVVgrtgADV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 195 SRPGWINFRELLRAASPEHNCVRTRSGDSVAIYFTSGTTGAPKMVEHSQSSYGLGFVASGRRWMALTESDIFWNTTDTGW 274
Cdd:COG0365 158 PMEGDLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTADIGW 237
|
250 260
....*....|....*....|..
gi 26333877 275 VKAAW-TLFSAWSNGACIFVHE 295
Cdd:COG0365 238 ATGHSyIVYGPLLNGATVVLYE 259
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
48-310 |
1.66e-63 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 209.27 E-value: 1.66e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 48 VPEYFNFAHDVLDVWSQLEktghrPPNPAFWWVNGSGTEVKWTFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDW 127
Cdd:cd05970 12 VPENFNFAYDVVDAMAKEY-----PDKLALVWCDDAGEERIFTFAELADYSDKTANFFKAM-GIGKGDTVMLTLKRRYEF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 128 WLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVT--SDALAPQVDAISADCPSLQTKLLVSDTSRPGWINFREL 205
Cdd:cd05970 86 WYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAiaEDNIPEEIEKAAPECPSKPKLVWVGDPVPEGWIDFRKL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 206 LRAASPE----HNCVRTRSGDSVAIYFTSGTTGAPKMVEHSQsSYGLGFVASGRRWMALTESDIFWNTTDTGWVKAAW-T 280
Cdd:cd05970 166 IKNASPDferpTANSYPCGEDILLVYFSSGTTGMPKMVEHDF-TYPLGHIVTAKYWQNVREGGLHLTVADTGWGKAVWgK 244
|
250 260 270
....*....|....*....|....*....|
gi 26333877 281 LFSAWSNGACIFVHELPRVDAKTILNVRRK 310
Cdd:cd05970 245 IYGQWIAGAAVFVYDYDKFDPKALLEKLSK 274
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
89-307 |
7.65e-53 |
|
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: 178.68 E-value: 7.65e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 89 WTFEELGKQSRKAANVLEGvCGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTS 168
Cdd:cd05972 1 WSFRELKRESAKAANVLAK-LGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 169 DalapqvdaisadcpslqtkllvSDTSrpgwinfrellraaspehncvrtrsgdsvAIYFTSGTTGAPKMVEHSqSSYGL 248
Cdd:cd05972 80 A----------------------EDPA-----------------------------LIYFTSGTTGLPKGVLHT-HSYPL 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 249 GFVASGRRWMALTESDIFWNTTDTGWVKAAW-TLFSAWSNGACIFVHELPRVDAKTILNV 307
Cdd:cd05972 108 GHIPTAAYWLGLRPDDIHWNIADPGWAKGAWsSFFGPWLLGATVFVYEGPRFDAERILEL 167
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
76-289 |
2.63e-34 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 131.17 E-value: 2.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 76 AFWWVnGSGTEVKWTFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKY 155
Cdd:PRK04319 62 ALRYL-DASRKEKYTYKELKELSNKFANVLKEL-GVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRD 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 156 RLQAARAKSIVTSDALAPQVdaISADCPSLQTKLLVSDTSR--PGWINFRELLRAASPEHNCVRTRSGDSVAIYFTSGTT 233
Cdd:PRK04319 140 RLEDSEAKVLITTPALLERK--PADDLPSLKHVLLVGEDVEegPGTLDFNALMEQASDEFDIEWTDREDGAILHYTSGST 217
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 26333877 234 GAPKMVEHSQSSYgLGFVASGRRWMALTESDIFWNTTDTGWVKA-AWTLFSAWSNGA 289
Cdd:PRK04319 218 GKPKGVLHVHNAM-LQHYQTGKYVLDLHEDDVYWCTADPGWVTGtSYGIFAPWLNGA 273
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
90-305 |
8.03e-34 |
|
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: 128.07 E-value: 8.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 90 TFEELGKQSRKAANVLEGvCGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAksivtsd 169
Cdd:cd05974 2 SFAEMSARSSRVANFLRS-IGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGA------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 170 ALAPQVDAISADCPSLqtkllvsdtsrpgwinfrellraaspehncvrtrsgdsvaIYFTSGTTGAPKMVEHSQSSYGLG 249
Cdd:cd05974 74 VYAAVDENTHADDPML----------------------------------------LYFTSGTTSKPKLVEHTHRSYPVG 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 26333877 250 FVASgRRWMALTESDIFWNTTDTGWVKAAWT-LFSAWSNGACIFVHELPRVDAKTIL 305
Cdd:cd05974 114 HLST-MYWIGLKPGDVHWNISSPGWAKHAWScFFAPWNAGATVFLFNYARFDAKRVL 169
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
65-305 |
5.44e-27 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 109.32 E-value: 5.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 65 LEKTGHRPPN-PAFwwvnGSGTEVKWTFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIP 143
Cdd:pfam00501 1 LERQAARTPDkTAL----EVGEGRRLTYRELDERANRLAAGLRAL-GVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 144 GVSQLTAKDLKYRLQAARAKSIVTSDAL-APQVDAISADCPSLQTKLLVS-DTSRPGWINFRELLRAASPEHNCVRTRSG 221
Cdd:pfam00501 76 LNPRLPAEELAYILEDSGAKVLITDDALkLEELLEALGKLEVVKLVLVLDrDPVLKEEPLPEEAKPADVPPPPPPPPDPD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 222 DSVAIYFTSGTTGAPKMVEHSQSSY---GLGFVASGRRWMALTESDIFWNTT----DTGWVkaaWTLFSAWSNGACI-FV 293
Cdd:pfam00501 156 DLAYIIYTSGTTGKPKGVMLTHRNLvanVLSIKRVRPRGFGLGPDDRVLSTLplfhDFGLS---LGLLGPLLAGATVvLP 232
|
250
....*....|..
gi 26333877 294 HELPRVDAKTIL 305
Cdd:pfam00501 233 PGFPALDPAALL 244
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
47-295 |
1.18e-26 |
|
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: 109.89 E-value: 1.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 47 PVPEYF-----NFAHDVLDVWsqlekTGHRPPNPAFWWVNGSGTEVKWTFEELGKQSRKAANVLEGVcGLQPEDRMMLVL 121
Cdd:cd05968 50 PWAAWFvggrmNIVEQLLDKW-----LADTRTRPALRWEGEDGTSRTLTYGELLYEVKRLANGLRAL-GVGKGDRVGIYL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 122 PRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTSDA---------LAPQVDAISADCPSLQTKLLVS 192
Cdd:cd05968 124 PMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITADGftrrgrevnLKEEADKACAQCPTVEKVVVVR 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 193 DTSRP-GWINFREL---LRAASPEHNCVRTRSGDSVAIYFTSGTTGAPKMVEHSQSSYGLGFVASGRRWMALTESDIFWN 268
Cdd:cd05968 204 HLGNDfTPAKGRDLsydEEKETAGDGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDLLTW 283
|
250 260
....*....|....*....|....*..
gi 26333877 269 TTDTGWVKAAWTLFSAWSNGACIFVHE 295
Cdd:cd05968 284 FTDLGWMMGPWLIFGGLILGATMVLYD 310
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
53-295 |
1.68e-25 |
|
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: 106.51 E-value: 1.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 53 NFAHDVLDvwSQLEKTGHRPpnpAFWWVNGSGTEVK-WTFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLIS 131
Cdd:cd17634 53 NLAANALD--RHLRENGDRT---AIIYEGDDTSQSRtISYRELHREVCRFAGTLLDL-GVKKGDRVAIYMPMIPEAAVAM 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 132 VACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTSDA---------LAPQVD-AISADCPSLQTKLLVSDTSRP---- 197
Cdd:cd17634 127 LACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADGgvragrsvpLKKNVDdALNPNVTSVEHVIVLKRTGSDidwq 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 198 --GWINFRELLRAASPEHNCVRTRSGDSVAIYFTSGTTGAPKMVEHSQSSYGLGFVASGRRWMALTESDIFWNTTDTGWV 275
Cdd:cd17634 207 egRDLWWRDLIAKASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWV 286
|
250 260
....*....|....*....|.
gi 26333877 276 KA-AWTLFSAWSNGACIFVHE 295
Cdd:cd17634 287 TGhSYLLYGPLACGATTLLYE 307
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
89-295 |
7.03e-25 |
|
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: 103.74 E-value: 7.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 89 WTFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTS 168
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSL-GVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 169 DalapqvdaisadcpslqtkllvsdtsrpgwinfrELLRAASPEhncvrtrsgDSVAIYFTSGTTGAPKMVEHSQSSYGL 248
Cdd:cd05969 80 E----------------------------------ELYERTDPE---------DPTLLHYTSGTTGTPKGVLHVHDAMIF 116
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 26333877 249 GFVaSGRRWMALTESDIFWNTTDTGWVK-AAWTLFSAWSNGACIFVHE 295
Cdd:cd05969 117 YYF-TGKYVLDLHPDDIYWCTADPGWVTgTVYGIWAPWLNGVTNVVYE 163
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
50-292 |
9.28e-25 |
|
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: 103.99 E-value: 9.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 50 EYFNFAHDVLDvwsQLEKTghRPPNPAFWWVNGSgtevkWTFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWL 129
Cdd:cd05959 1 EKYNAATLVDL---NLNEG--RGDKTAFIDDAGS-----LTYAELEAEARRVAGALRAL-GVKREERVLLIMLDTVDFPT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 130 ISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTSDALAPQV-DAISADCPSLQTkLLVSDTSRP--GWINFRELL 206
Cdd:cd05959 70 AFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLaAALTKSEHTLVV-LIVSGGAGPeaGALLLAELV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 207 RAASPEHNCVRTRSGDSVAIYFTSGTTGAPKMVEHSQSSYGLGFVASGRRWMALTESDIFWNTTdtgwvkaawTLFSAWS 286
Cdd:cd05959 149 AAEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVLGIREDDVCFSAA---------KLFFAYG 219
|
....*..
gi 26333877 287 NG-ACIF 292
Cdd:cd05959 220 LGnSLTF 226
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
53-275 |
1.64e-22 |
|
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: 97.63 E-value: 1.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 53 NFAHDVLDVWsqLEKTGHRPpnpAFWWV-NGSGTEVKWTFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLIS 131
Cdd:cd05966 53 NISYNCLDRH--LKERGDKV---AIIWEgDEPDQSRTITYRELLREVCRFANVLKSL-GVKKGDRVAIYMPMIPELVIAM 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 132 VACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTSDA---------LAPQVDAISADCPSLQTKLLVSDTSRPGWIN- 201
Cdd:cd05966 127 LACARIGAVHSVVFAGFSAESLADRINDAQCKLVITADGgyrggkvipLKEIVDEALEKCPSVEKVLVVKRTGGEVPMTe 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 202 -----FRELLRAASPEHNCVRTRSGDSVAIYFTSGTTGAPKMVEHSQSSYGLGfVASGRRWM-ALTESDIFWNTTDTGWV 275
Cdd:cd05966 207 grdlwWHDLMAKQSPECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTGGYLLY-AATTFKYVfDYHPDDIYWCTADIGWI 285
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
70-266 |
6.65e-22 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 95.94 E-value: 6.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 70 HRPPNPAFWWVNGsGTEVKWTFEELGKQSRKAANVLEGvCGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLT 149
Cdd:COG1022 23 RFPDRVALREKED-GIWQSLTWAEFAERVRALAAGLLA-LGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIYPTSS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 150 AKDLKYRLQAARAKSIVTSD-ALAPQVDAISADCPSLQtKLLVSD----TSRPGWINFRELLRAASPEHN------CVRT 218
Cdd:COG1022 101 AEEVAYILNDSGAKVLFVEDqEQLDKLLEVRDELPSLR-HIVVLDprglRDDPRLLSLDELLALGREVADpaeleaRRAA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 26333877 219 RSGDSVA-IYFTSGTTGAPKMVEHSQSSYgLGFVASGRRWMALTESDIF 266
Cdd:COG1022 180 VKPDDLAtIIYTSGTTGRPKGVMLTHRNL-LSNARALLERLPLGPGDRT 227
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
86-245 |
4.54e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 90.38 E-value: 4.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 86 EVKWTFEELGKQSRKAANVLEGVcGLQPEDRMMLvLPRLPDWWLIS-VACMRTGVVMIPGVSQLTAKDLKYRLQAARAKS 164
Cdd:PRK08316 34 DRSWTYAELDAAVNRVAAALLDL-GLKKGDRVAA-LGHNSDAYALLwLACARAGAVHVPVNFMLTGEELAYILDHSGARA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 165 IVTSDALAPQVDAISADCPSLQTKLLVSDTSRP---GWINFRELLRAASPEHNCVRTRSGDSVAIYFTSGTTGAPKMVEH 241
Cdd:PRK08316 112 FLVDPALAPTAEAALALLPVDTLILSLVLGGREapgGWLDFADWAEAGSVAEPDVELADDDLAQILYTSGTESLPKGAML 191
|
....
gi 26333877 242 SQSS 245
Cdd:PRK08316 192 THRA 195
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
85-266 |
6.56e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 89.86 E-value: 6.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 85 TEVKWTFEELGKQSRKAANVLEGvCGLQPEDRMMLVlprlpDW----WLISV-ACMRTGVVMIPGVSQLTAKDLKYRLQA 159
Cdd:PRK06187 28 DGRRTTYAELDERVNRLANALRA-LGVKKGDRVAVF-----DWnsheYLEAYfAVPKIGAVLHPINIRLKPEEIAYILND 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 160 ARAKSIVTSDALAPQVDAISADCPSLQTKLLVSDTSRPG----WINFRELLRAASPEHNCVRTRSGDSVAIYFTSGTTGA 235
Cdd:PRK06187 102 AEDRVVLVDSEFVPLLAAILPQLPTVRTVIVEGDGPAAPlapeVGEYEELLAAASDTFDFPDIDENDAAAMLYTSGTTGH 181
|
170 180 190
....*....|....*....|....*....|.
gi 26333877 236 PKMVEHSQSSYGLGfVASGRRWMALTESDIF 266
Cdd:PRK06187 182 PKGVVLSHRNLFLH-SLAVCAWLKLSRDDVY 211
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
84-295 |
1.04e-19 |
|
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: 89.23 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 84 GTEVKWTFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLISVACMRTGV---VMIPGVSqltAKDLKYRLQAA 160
Cdd:TIGR02188 84 GEVRKITYRELHREVCRFANVLKSL-GVKKGDRVAIYMPMIPEAAIAMLACARIGAihsVVFGGFS---AEALADRINDA 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 161 RAKSIVTSD---------ALAPQVDAISADCPSLQTKLLV---SDTSRPGWIN-----FRELLRAASPEHNCVRTRSGDS 223
Cdd:TIGR02188 160 GAKLVITADeglrggkviPLKAIVDEALEKCPVSVEHVLVvrrTGNPVVPWVEgrdvwWHDLMAKASAYCEPEPMDSEDP 239
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26333877 224 VAIYFTSGTTGAPKMVEHSQSSYGLGFVASGRRWMALTESDIFWNTTDTGWVKA-AWTLFSAWSNGACIFVHE 295
Cdd:TIGR02188 240 LFILYTSGSTGKPKGVLHTTGGYLLYAAMTMKYVFDIKDGDIFWCTADVGWITGhSYIVYGPLANGATTVMFE 312
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
90-244 |
2.15e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 85.34 E-value: 2.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 90 TFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTSD 169
Cdd:PRK07656 32 TYAELNARVRRAAAALAAL-GIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFVLG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 170 ALAPQVDAISADCPSLQTKLLVSDT----SRPGWINFRELLRAASPEHNcVRTRSGDSVA-IYFTSGTTGAPK--MVEHS 242
Cdd:PRK07656 111 LFLGVDYSATTRLPALEHVVICETEeddpHTEKMKTFTDFLAAGDPAER-APEVDPDDVAdILFTSGTTGRPKgaMLTHR 189
|
..
gi 26333877 243 QS 244
Cdd:PRK07656 190 QL 191
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
53-275 |
9.63e-18 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 83.65 E-value: 9.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 53 NFAHDVLDVwsQLEKTGHRPpnpAFWWVNGSGTEV-KWTFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLIS 131
Cdd:PRK00174 67 NVSYNCLDR--HLKTRGDKV---AIIWEGDDPGDSrKITYRELHREVCRFANALKSL-GVKKGDRVAIYMPMIPEAAVAM 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 132 VACMRTGV---VMIPGVSqltAKDLKYRLQAARAKSIVTSD---------ALAPQVDAISADCPSLQTKLLVSDTSRP-G 198
Cdd:PRK00174 141 LACARIGAvhsVVFGGFS---AEALADRIIDAGAKLVITADegvrggkpiPLKANVDEALANCPSVEKVIVVRRTGGDvD 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 199 WINFR-----ELLRAASPEHNCVRTRSGDSVAIYFTSGTTGAPKMVEHSQSSYGLgfvasgrrWMALT--------ESDI 265
Cdd:PRK00174 218 WVEGRdlwwhELVAGASDECEPEPMDAEDPLFILYTSGSTGKPKGVLHTTGGYLV--------YAAMTmkyvfdykDGDV 289
|
250
....*....|
gi 26333877 266 FWNTTDTGWV 275
Cdd:PRK00174 290 YWCTADVGWV 299
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
43-243 |
5.44e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 81.24 E-value: 5.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 43 LGRQPVPEYfnfahdvLDVWSQLektghRPPNPAFWWVngsGTEVkwTFEELGKQSRKAANVLEGVcGLQPEDRMMLVLP 122
Cdd:PRK06178 30 HGERPLTEY-------LRAWARE-----RPQRPAIIFY---GHVI--TYAELDELSDRFAALLRQR-GVGAGDRVAVFLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 123 RLPDWWLISVACMRTGVVMIPgVSQLT-AKDLKYRLQAARAKSIVTSDALAPQVDAISADC-----------------PS 184
Cdd:PRK06178 92 NCPQFHIVFFGILKLGAVHVP-VSPLFrEHELSYELNDAGAEVLLALDQLAPVVEQVRAETslrhvivtsladvlpaePT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26333877 185 LQTKLLVSDTSR--PGWINFRELLRAASPEHNCVRTRSGDSVAIYFTSGTTGAPKMVEHSQ 243
Cdd:PRK06178 171 LPLPDSLRAPRLaaAGAIDLLPALRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQ 231
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
47-275 |
2.88e-16 |
|
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: 79.28 E-value: 2.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 47 PVPEYF-----NFAHDVLDVWSQlektGHRPPNPAFWWVNGS-GTEVKWTFEELGKQSRKAANVLEGVcGLQPEDRMMLV 120
Cdd:cd05967 39 PFTRWFvggrlNTCYNALDRHVE----AGRGDQIALIYDSPVtGTERTYTYAELLDEVSRLAGVLRKL-GVVKGDRVIIY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 121 LPRLPDWWLISVACMRTGV---VMIPGVSqltAKDLKYRLQAARAKSIVTSDA---------LAPQVD-AIS------AD 181
Cdd:cd05967 114 MPMIPEAAIAMLACARIGAihsVVFGGFA---AKELASRIDDAKPKLIVTASCgiepgkvvpYKPLLDkALElsghkpHH 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 182 CPSLQTKLLVSDTSRPG-WINFRELLRAASPeHNCVRTRSGDSVAIYFTSGTTGAPKMVEHSQSSYGLGFVASGRRWMAL 260
Cdd:cd05967 191 VLVLNRPQVPADLTKPGrDLDWSELLAKAEP-VDCVPVAATDPLYILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYGI 269
|
250
....*....|....*
gi 26333877 261 TESDIFWNTTDTGWV 275
Cdd:cd05967 270 KPGDVWWAASDVGWV 284
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
61-310 |
5.71e-16 |
|
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: 77.99 E-value: 5.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 61 VWSQLEKT-GHRPPNPAFWWvngsgTEVKWTFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLISVACMRTGV 139
Cdd:cd05936 1 LADLLEEAaRRFPDKTALIF-----MGRKLTYRELDALAEAFAAGLQNL-GVQPGDRVALMLPNCPQFPIAYFGALKAGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 140 VMIPGVSQLTAKDLKYRLQaaraksivtsdalapqvdaisaDCpslQTKLLVSDTSrpgwinFRELLRAASPEHNCVRTR 219
Cdd:cd05936 75 VVVPLNPLYTPRELEHILN----------------------DS---GAKALIVAVS------FTDLLAAGAPLGERVALT 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 220 SGDSVAIYFTSGTTGAPKMVEHSQSSYgLGFVASGRRWM--ALTESDIFwnttdtgwVKA-------AWT--LFSAWSNG 288
Cdd:cd05936 124 PEDVAVLQYTSGTTGVPKGAMLTHRNL-VANALQIKAWLedLLEGDDVV--------LAAlplfhvfGLTvaLLLPLALG 194
|
250 260
....*....|....*....|..
gi 26333877 289 ACIFVheLPRVDAKTILNVRRK 310
Cdd:cd05936 195 ATIVL--IPRFRPIGVLKEIRK 214
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
56-305 |
1.46e-15 |
|
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: 76.77 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 56 HDVLDVWSQlektgHRPPNPAFwwVNGSGTevkWTFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLISVACM 135
Cdd:COG0318 2 ADLLRRAAA-----RHPDRPAL--VFGGRR---LTYAELDARARRLAAALRAL-GVGPGDRVALLLPNSPEFVVAFLAAL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 136 RTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTsdalapqvdaisadcpslqtkllvsdtsrpgwinfrellraaspehnc 215
Cdd:COG0318 71 RAGAVVVPLNPRLTAEELAYILEDSGARALVT------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 216 vrtrsgdsVAIYFTSGTTGAPKMVEHSQSSYgLGFVASGRRWMALTESDIFWNTT----DTGWVkaaWTLFSAWSNGACI 291
Cdd:COG0318 103 --------ALILYTSGTTGRPKGVMLTHRNL-LANAAAIAAALGLTPGDVVLVALplfhVFGLT---VGLLAPLLAGATL 170
|
250
....*....|....
gi 26333877 292 FVheLPRVDAKTIL 305
Cdd:COG0318 171 VL--LPRFDPERVL 182
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
82-239 |
2.42e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 76.10 E-value: 2.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 82 GSGTEvkWTFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAAR 161
Cdd:PRK08276 7 PSGEV--VTYGELEARSNRLAHGLRAL-GLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSG 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26333877 162 AKSIVTSDALAPQVDAISADCPSLQTKLLVSDTSRPGWINFRELLRAASPEHNCVRTRSGDsvaIYFTSGTTGAPKMV 239
Cdd:PRK08276 84 AKVLIVSAALADTAAELAAELPAGVPLLLVVAGPVPGFRSYEEALAAQPDTPIADETAGAD---MLYSSGTTGRPKGI 158
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
60-266 |
3.06e-15 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 75.87 E-value: 3.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 60 DVWSQL-EKTGHrppNPAFWWVNGSGTEVKWTFEELGKQSRKAANVLEGvCGLQPEDRMMLVLPRLPDWWLISVACMRTG 138
Cdd:PRK08008 11 QMWDDLaDVYGH---KTALIFESSGGVVRRYSYLELNEEINRTANLFYS-LGIRKGDKVALHLDNCPEFIFCWFGLAKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 139 VVMIPGVSQLTAKDLKYRLQAARAKSIVTSDALAPQVDAISADCPSLQTKLLVSDTSRP---GWINFRELLRAASPEHNC 215
Cdd:PRK08008 87 AIMVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDATPLRHICLTRVALPaddGVSSFTQLKAQQPATLCY 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 26333877 216 VRTRSGDSVA-IYFTSGTTGAPKMVEHSQssYGLGFVASGRRWM-ALTESDIF 266
Cdd:PRK08008 167 APPLSTDDTAeILFTSGTTSRPKGVVITH--YNLRFAGYYSAWQcALRDDDVY 217
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
61-266 |
6.13e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 75.00 E-value: 6.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 61 VWSQLEKTGHRPPN-PAFWWVngsGTEVkwTFEELGKQSRKAANVLEGVCGLQPEDRMMLVLPRLPDWWLISVACMRTGV 139
Cdd:PRK08314 12 LFHNLEVSARRYPDkTAIVFY---GRAI--SYRELLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 140 VMIPGVSQLTAKDLKYRLQAARAKSIVTSDALAPQV------------------DAISADCP-----SLQTKLLVSDTSR 196
Cdd:PRK08314 87 VVVPVNPMNREEELAHYVTDSGARVAIVGSELAPKVapavgnlrlrhvivaqysDYLPAEPEiavpaWLRAEPPLQALAP 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26333877 197 PGWINFRELLRA--ASPEHNcvrTRSGDSVAIYFTSGTTGAPKMVEHSQSSYgLGFVASGRRWMALTESDIF 266
Cdd:PRK08314 167 GGVVAWKEALAAglAPPPHT---AGPDDLAVLPYTSGTTGVPKGCMHTHRTV-MANAVGSVLWSNSTPESVV 234
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
71-237 |
7.12e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 74.81 E-value: 7.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 71 RPPNPAFWWVnGSGTevkwTFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTA 150
Cdd:PRK07786 30 QPDAPALRFL-GNTT----TWRELDDRVAALAGALSRR-GVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 151 KDLKYRLQAARAKSIVTSDALAPQVDAISADCPSLQTKLLVSDTSRPGWINFRELLRAASPEHNCVRTRSGDSVAIYFTS 230
Cdd:PRK07786 104 PEIAFLVSDCGAHVVVTEAALAPVATAVRDIVPLLSTVVVAGGSSDDSVLGYEDLLAEAGPAHAPVDIPNDSPALIMYTS 183
|
....*..
gi 26333877 231 GTTGAPK 237
Cdd:PRK07786 184 GTTGRPK 190
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
121-295 |
1.51e-14 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 73.70 E-value: 1.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 121 LPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTSDALA------PQVDAISADCPSLQTKLLVSDT 194
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLrggralPLYSKVVEAAPAKAIVLPAAGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 195 S-----RPGWINFRELLRAASP-------EHNCVRTRSGDSVAIYFTSGTTGAPKMVEHSQSSyGLGFVASGRRWMALTE 262
Cdd:PLN03051 81 PvavplREQDLSWCDFLGVAAAqgsvggnEYSPVYAPVESVTNILFSSGTTGEPKAIPWTHLS-PLRCASDGWAHMDIQP 159
|
170 180 190
....*....|....*....|....*....|...
gi 26333877 263 SDIFWNTTDTGWVKAAWTLFSAWSNGACIFVHE 295
Cdd:PLN03051 160 GDVVCWPTNLGWMMGPWLLYSAFLNGATLALYG 192
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
90-284 |
1.87e-13 |
|
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: 70.24 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 90 TFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTSd 169
Cdd:cd05973 2 TFGELRALSARFANALQEL-GVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 170 alAPQVDAISADcpslqtkLLVsdtsrpgwinfrellraaspehncvrtrsgdsvaIYFTSGTTGAPKMVEHSQSsYGLG 249
Cdd:cd05973 80 --AANRHKLDSD-------PFV----------------------------------MMFTSGTTGLPKGVPVPLR-ALAA 115
|
170 180 190
....*....|....*....|....*....|....*
gi 26333877 250 FVASGRRWMALTESDIFWNTTDTGWvkaAWTLFSA 284
Cdd:cd05973 116 FGAYLRDAVDLRPEDSFWNAADPGW---AYGLYYA 147
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
86-264 |
2.53e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 70.19 E-value: 2.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 86 EVKWTFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSI 165
Cdd:PRK12583 43 ALRYTWRQLADAVDRLARGLLAL-GVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 166 VTSDA------------LAPQV------DAISADCPSLQTKLLVSDTSRPGWINFRELLRAA---SPEHNCVRT---RSG 221
Cdd:PRK12583 122 ICADAfktsdyhamlqeLLPGLaegqpgALACERLPELRGVVSLAPAPPPGFLAWHELQARGetvSREALAERQaslDRD 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 26333877 222 DSVAIYFTSGTTGAPK--MVEHSQSSYGLGFVAsgrRWMALTESD 264
Cdd:PRK12583 202 DPINIQYTSGTTGFPKgaTLSHHNILNNGYFVA---ESLGLTEHD 243
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
90-250 |
2.87e-13 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 70.01 E-value: 2.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 90 TFEELGKQSRKAANVLEGVCGLQPEDRMMLVLPRLPDW---WL------ISVACMRTgvvmipgvsQLTAKDLKYRLQAA 160
Cdd:cd05938 7 TYRDVDRRSNQAARALLAHAGLRPGDTVALLLGNEPAFlwiWLglaklgCPVAFLNT---------NIRSKSLLHCFRCC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 161 RAKSIVTSDALapqVDAISADCPSLQTK-----LLVSDTSRPGWINFRELLRAASPEHNCVRTRSG---DSVAIY-FTSG 231
Cdd:cd05938 78 GAKVLVVAPEL---QEAVEEVLPALRADgvsvwYLSHTSNTEGVISLLDKVDAASDEPVPASLRAHvtiKSPALYiYTSG 154
|
170 180
....*....|....*....|.
gi 26333877 232 TTGAPK--MVEHSQSSYGLGF 250
Cdd:cd05938 155 TTGLPKaaRISHLRVLQCSGF 175
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
71-239 |
5.14e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 69.33 E-value: 5.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 71 RPPNPAFWwVNGSGTEVkwTFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTA 150
Cdd:PRK13391 10 TPDKPAVI-MASTGEVV--TYRELDERSNRLAHLFRSL-GLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 151 KDLKYRLQAARAKSIVTSDALAPQVDAISADCPSLQTKLLV-SDTSRPGWINFRELLrAASPEHNCVRTRSGDsvAIYFT 229
Cdd:PRK13391 86 AEAAYIVDDSGARALITSAAKLDVARALLKQCPGVRHRLVLdGDGELEGFVGYAEAV-AGLPATPIADESLGT--DMLYS 162
|
170
....*....|
gi 26333877 230 SGTTGAPKMV 239
Cdd:PRK13391 163 SGTTGRPKGI 172
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
89-267 |
5.46e-13 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 69.01 E-value: 5.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 89 WTFEELG-KQSRKAANVLEgvCGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVT 167
Cdd:PRK06087 50 YTYSALDhAASRLANWLLA--KGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 168 SDALA-----PQVDAISADCPSLQTKLLVsDTSRPGW--INFRELLRAASPEHNCVRTRSGDSVAIYFTSGTTGAPK--M 238
Cdd:PRK06087 128 PTLFKqtrpvDLILPLQNQLPQLQQIVGV-DKLAPATssLSLSQIIADYEPLTTAITTHGDELAAVLFTSGTEGLPKgvM 206
|
170 180 190
....*....|....*....|....*....|..
gi 26333877 239 VEHSQssyglgFVASGRRWMA---LTESDIFW 267
Cdd:PRK06087 207 LTHNN------ILASERAYCArlnLTWQDVFM 232
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
86-239 |
9.72e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 68.37 E-value: 9.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 86 EVKWTFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSI 165
Cdd:PRK07798 26 DRRLTYAELEERANRLAHYLIAQ-GLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVAL 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26333877 166 VTSDALAPQVDAISADCPSLQTKLLVSDTS----RPGWINFRELLRAASPEHNcVRTRSGDSVAIYFTSGTTGAPKMV 239
Cdd:PRK07798 105 VYEREFAPRVAEVLPRLPKLRTLVVVEDGSgndlLPGAVDYEDALAAGSPERD-FGERSPDDLYLLYTGGTTGMPKGV 181
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
90-291 |
1.22e-12 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 68.18 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 90 TFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTSD 169
Cdd:PLN03052 210 TLSELRSQVSRVANALDAL-GFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSIADSFAPSEIATRLKISKAKAIFTQD 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 170 -----------------ALAPQVDAISADCPSLQTKLLVSDTSrpgWINFRELL--RAASPEHNCVRtRSGDSVA-IYFT 229
Cdd:PLN03052 289 vivrggksiplysrvveAKAPKAIVLPADGKSVRVKLREGDMS---WDDFLARAngLRRPDEYKAVE-QPVEAFTnILFS 364
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26333877 230 SGTTGAPKMVEHSQSSyglGFVASGRRW--MALTESDIFWNTTDTGWVKAAWTLFSAWSNGACI 291
Cdd:PLN03052 365 SGTTGEPKAIPWTQLT---PLRAAADAWahLDIRKGDIVCWPTNLGWMMGPWLVYASLLNGATL 425
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
85-294 |
2.54e-12 |
|
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: 66.85 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 85 TEVKWTFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKS 164
Cdd:cd05911 7 TGKELTYAQLRTLSRRLAAGLRKL-GLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 165 IVTSDALAPQVDAISADCPSlQTKLLVSDTSRPGWINFRELLRAAS--PEHN---CVRTRSGDSVAIYFTSGTTGAPK-- 237
Cdd:cd05911 86 IFTDPDGLEKVKEAAKELGP-KDKIIVLDDKPDGVLSIEDLLSPTLgeEDEDlppPLKDGKDDTAAILYSSGTTGLPKgv 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26333877 238 ---------MVEHSQSSYGLGFVASGRRWMALTesdIFWNTTDTgwvkaaWTLFSAWsNGACIFVH 294
Cdd:cd05911 165 clshrnliaNLSQVQTFLYGNDGSNDVILGFLP---LYHIYGLF------TTLASLL-NGATVIIM 220
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
222-306 |
8.04e-12 |
|
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: 65.00 E-value: 8.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 222 DSVAIYFTSGTTGAPKMVEHSQSSYgLGFVASGRRWMALTESDIFWNTTDTGWVKAAWTLFSAWSNGACIFVHelPRVDA 301
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNL-LAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLL--PKFDP 77
|
....*
gi 26333877 302 KTILN 306
Cdd:cd04433 78 EAALE 82
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
90-306 |
1.46e-11 |
|
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: 64.59 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 90 TFEELGKQSRKAANVLEGVCGLQPEDRMMLVLPRLPdwWLI--SVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVT 167
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGDRVAVLLERSA--ELVvaILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 168 SDALAPQVD--AISADCPSLQTKLLVSDtsrpgwinfrellrAASPEHNCVRTRSGDSVAIYFTSGTTGAPK--MVEHSQ 243
Cdd:TIGR01733 79 DSALASRLAglVLPVILLDPLELAALDD--------------APAPPPPDAPSGPDDLAYVIYTSGSTGRPKgvVVTHRS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26333877 244 SSYglgFVASGRRWMALTESDIFWNTTDTGWVKAAWTLFSAWSNGACIFVheLPRVDAKTILN 306
Cdd:TIGR01733 145 LVN---LLAWLARRYGLDPDDRVLQFASLSFDASVEEIFGALLAGATLVV--PPEDEERDDAA 202
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
86-295 |
1.94e-11 |
|
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: 64.14 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 86 EVKWTFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDwwliSVACM----RTGVVMIPGVSQLTAKDLKYRLQAAR 161
Cdd:cd12117 20 DRSLTYAELNERANRLARRLRAA-GVGPGDVVGVLAERSPE----LVVALlavlKAGAAYVPLDPELPAERLAFMLADAG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 162 AKSIVTSDALAPQVDAisadcpsLQTKLLVSDTSRPGwinfrellraasPEHNCVRTRSGDSVA-IYFTSGTTGAPK--M 238
Cdd:cd12117 95 AKVLLTDRSLAGRAGG-------LEVAVVIDEALDAG------------PAGNPAVPVSPDDLAyVMYTSGSTGRPKgvA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 26333877 239 VEHsqssYGLGFVASGRRWMALTESDIFWNTTDTGWVKAAWTLFSAWSNGACIFVHE 295
Cdd:cd12117 156 VTH----RGVVRLVKNTNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAP 208
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
89-241 |
2.21e-11 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 64.13 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 89 WTFEELGKQSRKAANVLEGvCGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTS 168
Cdd:PRK07514 29 YTYGDLDAASARLANLLVA-LGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCD 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26333877 169 DALAPQVDAISADCPSLQTKLLvsDTSRPGwiNFRELLRAASPEHNCVRTRSGDSVAIYFTSGTTGAPK--MVEH 241
Cdd:PRK07514 108 PANFAWLSKIAAAAGAPHVETL--DADGTG--SLLEAAAAAPDDFETVPRGADDLAAILYTSGTTGRSKgaMLSH 178
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
86-293 |
2.69e-11 |
|
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: 64.49 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 86 EVKWTFEELGKQSRKAANVLEGvCGLQPEDRMMLVLPRLPDWwLISV-ACMRTGVVMIPGVSQLTAKDLKYRLQAARAKS 164
Cdd:COG1020 499 DQSLTYAELNARANRLAHHLRA-LGVGPGDLVGVCLERSLEM-VVALlAVLKAGAAYVPLDPAYPAERLAYMLEDAGARL 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 165 IVTSDALAPQVdaisadcPSLQTKLLVSDtsrpgwinfrELLRAASPEHNCVRTRSGDSVA-IYFTSGTTGAPK--MVEH 241
Cdd:COG1020 577 VLTQSALAARL-------PELGVPVLALD----------ALALAAEPATNPPVPVTPDDLAyVIYTSGSTGRPKgvMVEH 639
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 26333877 242 SqssyGLG-FVASGRRWMALTESDIFWNTTDTGWVKAAWTLFSAWSNGACIFV 293
Cdd:COG1020 640 R----ALVnLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVL 688
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
65-241 |
6.79e-11 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 62.69 E-value: 6.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 65 LEKTGHRPPNPAFwwVNGSGTEVkWTFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPG 144
Cdd:PLN02246 30 FERLSEFSDRPCL--IDGATGRV-YTYADVELLSRRVAAGLHKL-GIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 145 VSQLTAKDLKYRLQAARAKSIVTSDALAPQVDAISADCPslqTKLLVSDTSRPGWINFRELLRAASPEHNCVRTRSGDSV 224
Cdd:PLN02246 106 NPFYTPAEIAKQAKASGAKLIITQSCYVDKLKGLAEDDG---VTVVTIDDPPEGCLHFSELTQADENELPEVEISPDDVV 182
|
170
....*....|....*....
gi 26333877 225 AIYFTSGTTGAPK--MVEH 241
Cdd:PLN02246 183 ALPYSSGTTGLPKgvMLTH 201
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
61-258 |
8.32e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 62.71 E-value: 8.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 61 VWSQLEKTGHRPpnpAFWWVnGSGTevkwTFEELGKQSRKAANVLEgVCGLQPEDRMMLVLPRLPDWWLISVACMRTGVV 140
Cdd:PRK05605 38 YDNAVARFGDRP---ALDFF-GATT----TYAELGKQVRRAAAGLR-ALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 141 MIPGVSQLTAKDLKYRLQAARAKSIVTSDALAPQVDAISADCPsLQTKLLVSDTSR------------------------ 196
Cdd:PRK05605 109 VVEHNPLYTAHELEHPFEDHGARVAIVWDKVAPTVERLRRTTP-LETIVSVNMIAAmpllqrlalrlpipalrkaraalt 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26333877 197 ---PGWINFRELLRAASPEH----NCVRTRSGDSVAIYFTSGTTGAPK--MVEHSQSSYGLgfvASGRRWM 258
Cdd:PRK05605 188 gpaPGTVPWETLVDAAIGGDgsdvSHPRPTPDDVALILYTSGTTGKPKgaQLTHRNLFANA---AQGKAWV 255
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
56-266 |
1.15e-10 |
|
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: 62.09 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 56 HDVLDVWSQlektgHRPPNPAFwwVNGsgtEVKWTFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLISVACM 135
Cdd:COG1021 28 GDLLRRRAE-----RHPDRIAV--VDG---ERRLSYAELDRRADRLAAGLLAL-GLRPGDRVVVQLPNVAEFVIVFFALF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 136 RTGVvmIPgVSQLTA---KDLKYRLQAARAKSIVTSD-----ALAPQVDAISADCPSLQTKLLVSDTSrpGWINFRELLr 207
Cdd:COG1021 97 RAGA--IP-VFALPAhrrAEISHFAEQSEAVAYIIPDrhrgfDYRALARELQAEVPSLRHVLVVGDAG--EFTSLDALL- 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 208 aASPEHNCVRTRSGDSVAIYFTS-GTTGAPKMVEHSQSSYGLGFVASGRRWmALTESDIF 266
Cdd:COG1021 171 -AAPADLSEPRPDPDDVAFFQLSgGTTGLPKLIPRTHDDYLYSVRASAEIC-GLDADTVY 228
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
90-245 |
2.95e-10 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 60.95 E-value: 2.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 90 TFEELGKQSRKAANVLEGVCGLQPEDRMMLVLPRLPDWW--LISVACMrtGVVMIPGVSQLTAKDLKYRLQAARAKSIVT 167
Cdd:PRK05620 40 TFAAIGARAAALAHALHDELGITGDQRVGSMMYNCAEHLevLFAVACM--GAVFNPLNKQLMNDQIVHIINHAEDEVIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 168 SDALAPQVDAISADCPSLQTKLLVSD-------TSRPGWI---NFRELLRAASPEHNCVRTRSGDSVAIYFTSGTTGAPK 237
Cdd:PRK05620 118 DPRLAEQLGEILKECPCVRAVVFIGPsdadsaaAHMPEGIkvySYEALLDGRSTVYDWPELDETTAAAICYSTGTTGAPK 197
|
....*...
gi 26333877 238 MVEHSQSS 245
Cdd:PRK05620 198 GVVYSHRS 205
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
84-307 |
4.73e-10 |
|
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: 60.14 E-value: 4.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 84 GTEVKWTFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAK 163
Cdd:cd05971 2 GTPEKVTFKELKTASNRFANVLKEI-GLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 164 SIVTsDAlapqvdaisADCPSLqtkllvsdtsrpgwinfrellraaspehncvrtrsgdsvaIYFTSGTTGAPKMVEHSQ 243
Cdd:cd05971 81 ALVT-DG---------SDDPAL----------------------------------------IIYTSGTTGPPKGALHAH 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26333877 244 SSYgLGF--VASGRRWMALTESDIFWNTTDTGWVKAAW-TLFSAWSNGACIFVHELPRVDAKTILNV 307
Cdd:cd05971 111 RVL-LGHlpGVQFPFNLFPRDGDLYWTPADWAWIGGLLdVLLPSLYFGVPVLAHRMTKFDPKAALDL 176
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
84-246 |
5.59e-10 |
|
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: 59.92 E-value: 5.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 84 GTEVKWTFEELGKQSRKAANVLEGvCGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAK 163
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIA-LGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 164 SIVTSDAlapqvdaisadcpslqtkllvsdtsrpgwinfrellraaspehncvrtrsgDSVA-IYFTSGTTGAPKMVEHS 242
Cdd:cd05907 80 ALFVEDP---------------------------------------------------DDLAtIIYTSGTTGRPKGVMLS 108
|
....
gi 26333877 243 QSSY 246
Cdd:cd05907 109 HRNI 112
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
86-301 |
1.02e-09 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 59.00 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 86 EVKWTFEELGKQSRKAANVLEgVCGLQPEDRMMLVL---PRLPDWWLisvACMRTGVVMIPGVSQLTAKDLKYRLQAARA 162
Cdd:PRK06155 44 GTRWTYAEAARAAAAAAHALA-AAGVKRGDRVALMCgnrIEFLDVFL---GCAWLGAIAVPINTALRGPQLEHILRNSGA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 163 KSIVTSDALAPQVDAISADCPSLQTKLLV----SDTSRPGWiNFRELLRAASPEhNCVRTRSGDSVAIYFTSGTTGAPKM 238
Cdd:PRK06155 120 RLLVVEAALLAALEAADPGDLPLPAVWLLdapaSVSVPAGW-STAPLPPLDAPA-PAAAVQPGDTAAILYTSGTTGPSKG 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26333877 239 V--EHSQsSYGLGFVASgrRWMALTESDIFWNTTDTGWVKAAWTLFSAWSNGACIFVheLPRVDA 301
Cdd:PRK06155 198 VccPHAQ-FYWWGRNSA--EDLEIGADDVLYTTLPLFHTNALNAFFQALLAGATYVL--EPRFSA 257
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
89-269 |
1.05e-09 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 59.12 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 89 WTFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLISVACMRTGVV--MIPgvSQLTAKDLKYRLQAARAKSIV 166
Cdd:PRK08279 63 ISYAELNARANRYAHWAAAR-GVGKGDVVALLMENRPEYLAAWLGLAKLGAVvaLLN--TQQRGAVLAHSLNLVDAKHLI 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 167 TSDALAPQVDAISADcPSLQTKLLVSD----TSRPGWINFRELLRAAsPEHNCVRTRS--GDSVAIY-FTSGTTGAPKMV 239
Cdd:PRK08279 140 VGEELVEAFEEARAD-LARPPRLWVAGgdtlDDPEGYEDLAAAAAGA-PTTNPASRSGvtAKDTAFYiYTSGTTGLPKAA 217
|
170 180 190
....*....|....*....|....*....|...
gi 26333877 240 EHSQS---SYGLGFVASgrrwMALTESDIFWNT 269
Cdd:PRK08279 218 VMSHMrwlKAMGGFGGL----LRLTPDDVLYCC 246
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
80-243 |
1.32e-09 |
|
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: 58.83 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 80 VNGSGTEVKWTFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPR----LPDWWlisvACMRTGVVMIPgvsqlTAKDLKY 155
Cdd:cd05906 31 IDADGSEEFQSYQDLLEDARRLAAGLRQL-GLRPGDSVILQFDDnedfIPAFW----ACVLAGFVPAP-----LTVPPTY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 156 RLQAARAKS------------IVTSDALAPQVDAISADCPSLQTKLLVSdtsrpgwinfrELLRAASPEHNCVRTRSGDS 223
Cdd:cd05906 101 DEPNARLRKlrhiwqllgspvVLTDAELVAEFAGLETLSGLPGIRVLSI-----------EELLDTAADHDLPQSRPDDL 169
|
170 180
....*....|....*....|
gi 26333877 224 VAIYFTSGTTGAPKMVEHSQ 243
Cdd:cd05906 170 ALLMLTSGSTGFPKAVPLTH 189
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
70-265 |
1.36e-09 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 58.91 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 70 HRPPNPAFWWVN-GSGTEVKWTFEELGKQSRKAANVLEGVcGLQPEDrmmLVLPRLPDWWLISV---ACMRTGVVMIPGV 145
Cdd:PRK13295 36 SCPDKTAVTAVRlGTGAPRRFTYRELAALVDRVAVGLARL-GVGRGD---VVSCQLPNWWEFTVlylACSRIGAVLNPLM 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 146 SQLTAKDLKYRLQAARAKSIVtsdalAPQ----------VDAISADCPSLQTKLLV---SDTS------RPGWinfrELL 206
Cdd:PRK13295 112 PIFRERELSFMLKHAESKVLV-----VPKtfrgfdhaamARRLRPELPALRHVVVVggdGADSfealliTPAW----EQE 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 26333877 207 RAASPEHNCVRTRSGDSVAIYFTSGTTGAPKMVEHSQSSYGLGFVASGRRwMALTESDI 265
Cdd:PRK13295 183 PDAPAILARLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAER-LGLGADDV 240
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
81-266 |
1.95e-09 |
|
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: 58.41 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 81 NGSGTEVKWTFEELGKQSRKAANVLEGVcGLQPEDRmmlvlprlpdwwlISVACMRT--------GVVMIPGV-----SQ 147
Cdd:cd12119 18 THEGEVHRYTYAEVAERARRLANALRRL-GVKPGDR-------------VATLAWNThrhlelyyAVPGMGAVlhtinPR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 148 LTAKDLKYRLQAARAKSIVTSDALAPQVDAISADCPSLQTKLLVSD------TSRPGWINFRELLRAASPEHNCVRTRSG 221
Cdd:cd12119 84 LFPEQIAYIINHAEDRVVFVDRDFLPLLEAIAPRLPTVEHVVVMTDdaampePAGVGVLAYEELLAAESPEYDWPDFDEN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 26333877 222 DSVAIYFTSGTTGAPKMVEHSQSS---YGLGFVASGRrwMALTESDIF 266
Cdd:cd12119 164 TAAAICYTSGTTGNPKGVVYSHRSlvlHAMAALLTDG--LGLSESDVV 209
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
87-259 |
2.36e-09 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 58.04 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 87 VKWTFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMiPGVSQLTAKDLKYRLQAARAKSIV 166
Cdd:PRK07529 57 ETWTYAELLADVTRTANLLHSL-GVGPGDVVAFLLPNLPETHFALWGGEAAGIAN-PINPLLEPEQIAELLRAAGAKVLV 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 167 TsdaLAPQ--------VDAISADCPSLQTKLLVsDTSR--PGW----------------INF-RELLRAASPEHNCVRTR 219
Cdd:PRK07529 135 T---LGPFpgtdiwqkVAEVLAALPELRTVVEV-DLARylPGPkrlavplirrkahariLDFdAELARQPGDRLFSGRPI 210
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 26333877 220 SGDSVAIYF-TSGTTGAPKMVEHSQSsyglGFVASGrrWMA 259
Cdd:PRK07529 211 GPDDVAAYFhTGGTTGMPKLAQHTHG----NEVANA--WLG 245
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
88-293 |
2.51e-09 |
|
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: 57.92 E-value: 2.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 88 KWTFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWwLISV-ACMRTGVVMIPgvsqLtakDLKYrlQAARAKSIV 166
Cdd:cd05930 12 SLTYAELDARANRLARYLRER-GVGPGDLVAVLLERSLEM-VVAIlAVLKAGAAYVP----L---DPSY--PAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 167 tSDAlapqvdaisadcpslQTKLLVSDtsrpgwinfrellraaspehncvrtrsGDSVA-IYFTSGTTGAPK--MVEHSQ 243
Cdd:cd05930 81 -EDS---------------GAKLVLTD---------------------------PDDLAyVIYTSGSTGKPKgvMVEHRG 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 26333877 244 ssyglgfVASGRRWMA----LTESDIFWNTTDTGWVKAAWTLFSAWSNGACIFV 293
Cdd:cd05930 118 -------LVNLLLWMQeaypLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVV 164
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
53-275 |
3.88e-09 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 57.65 E-value: 3.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 53 NFAHDVLDVWsqLEKtghRPPNPAFWWVNG-SGTEVKWTFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLIS 131
Cdd:PRK10524 53 NLCHNAVDRH--LAK---RPEQLALIAVSTeTDEERTYTFRQLHDEVNRMAAMLRSL-GVQRGDRVLIYMPMIAEAAFAM 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 132 VACMRTGV---VMIPGvsqLTAKDLKYRLQAARAKSIVTSDALA---------PQVDAISADCPSLQTKLLVSD------ 193
Cdd:PRK10524 127 LACARIGAihsVVFGG---FASHSLAARIDDAKPVLIVSADAGSrggkvvpykPLLDEAIALAQHKPRHVLLVDrglapm 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 194 TSRPGwinfREL----LRAASPEHN--CVRTRSGDSVAIYFTSGTTGAPKMVEHSQSSYGLGFVASGRRWMALTESDIFW 267
Cdd:PRK10524 204 ARVAG----RDVdyatLRAQHLGARvpVEWLESNEPSYILYTSGTTGKPKGVQRDTGGYAVALATSMDTIFGGKAGETFF 279
|
....*...
gi 26333877 268 NTTDTGWV 275
Cdd:PRK10524 280 CASDIGWV 287
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
89-264 |
8.36e-09 |
|
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: 56.15 E-value: 8.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 89 WTFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTS 168
Cdd:cd12116 13 LSYAELDERANRLAARLRAR-GVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLTD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 169 DALApqvDAISADCPSLQtkllvsdtsrpgwinfRELLRAASPEHNCVRTRSGDSVA-IYFTSGTTGAPKMVEHSQSSYg 247
Cdd:cd12116 92 DALP---DRLPAGLPVLL----------------LALAAAAAAPAAPRTPVSPDDLAyVIYTSGSTGRPKGVVVSHRNL- 151
|
170
....*....|....*..
gi 26333877 248 LGFVASGRRWMALTESD 264
Cdd:cd12116 152 VNFLHSMRERLGLGPGD 168
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
86-305 |
9.90e-09 |
|
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: 55.95 E-value: 9.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 86 EVKWTFEELGKQSRKAANVLEGVCGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSI 165
Cdd:cd05958 8 EREWTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 166 VTSDALapqvdaisadcpslqtkllvsdtsrpgwinfrellraaspehncvrTRSGDSVAIYFTSGTTGAPKMVEHSQSS 245
Cdd:cd05958 88 LCAHAL----------------------------------------------TASDDICILAFTSGTTGAPKATMHFHRD 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26333877 246 YGLGFVASGRRWMALTESDIFwnttdTGWVKAAWT------LFSAWSNGACIFVheLPRVDAKTIL 305
Cdd:cd05958 122 PLASADRYAVNVLRLREDDRF-----VGSPPLAFTfglggvLLFPFGVGASGVL--LEEATPDLLL 180
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
77-295 |
1.05e-08 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 56.06 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 77 FWWVNGSGTEVKWTFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYR 156
Cdd:PLN02654 109 YWEGNEPGFDASLTYSELLDRVCQLANYLKDV-GVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQR 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 157 LQAARAKSIVTSDA---------LAPQVDA---------ISAD-CPSLQTKLLVSDTSRPgWINFREL----LRAASPEH 213
Cdd:PLN02654 188 IVDCKPKVVITCNAvkrgpktinLKDIVDAaldesakngVSVGiCLTYENQLAMKREDTK-WQEGRDVwwqdVVPNYPTK 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 214 NCVR-TRSGDSVAIYFTSGTTGAPKMVEHSQSSYGLGFVASGRRWMALTESDIFWNTTDTGWVKA-AWTLFSAWSNGACI 291
Cdd:PLN02654 267 CEVEwVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTDVYWCTADCGWITGhSYVTYGPMLNGATV 346
|
....
gi 26333877 292 FVHE 295
Cdd:PLN02654 347 LVFE 350
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
86-293 |
1.30e-08 |
|
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: 55.81 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 86 EVKWTFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSI 165
Cdd:cd17651 18 GRRLTYAELDRRANRLAHRLRAR-GVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVLV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 166 VTSDALAPQVDAISAdcpslqtkllvsdtsrPGWINFRELLRAASPEHNCVRTRSGDSVAIYFTSGTTGAPKMVEHSQSS 245
Cdd:cd17651 97 LTHPALAGELAVELV----------------AVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHRS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 26333877 246 YgLGFVASGRRWMALTESDIFWNTTDTGWVKAAWTLFSAWSNGACIFV 293
Cdd:cd17651 161 L-ANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVL 207
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
90-269 |
2.15e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 55.01 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 90 TFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTSD 169
Cdd:PRK13390 26 SYRQLDDDSAALARVLYDA-GLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVLVASA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 170 ALAPQVDAISADCPslqtkLLVSDTSR-PGWINFRELLRAASP---EHNCvrtrsgdSVAIYFTSGTTGAPKMV-----E 240
Cdd:PRK13390 105 ALDGLAAKVGADLP-----LRLSFGGEiDGFGSFEAALAGAGPrltEQPC-------GAVMLYSSGTTGFPKGIqpdlpG 172
|
170 180
....*....|....*....|....*....
gi 26333877 241 HSQSSYGLGFVASGRRWMALTESDIFWNT 269
Cdd:PRK13390 173 RDVDAPGDPIVAIARAFYDISESDIYYSS 201
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
86-266 |
2.23e-08 |
|
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: 55.03 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 86 EVKWTFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSI 165
Cdd:cd05920 38 DRRLTYRELDRRADRLAAGLRGL-GIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPSHRRSELSAFCAHAEAVAY 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 166 VTSDALAPqvdaisADCPSLqtkllvsdtsrpgwinFRELLRaaspehncvrtrSGDSVAIYFTS-GTTGAPKMVEHSQS 244
Cdd:cd05920 117 IVPDRHAG------FDHRAL----------------ARELAE------------SIPEVALFLLSgGTTGTPKLIPRTHN 162
|
170 180
....*....|....*....|..
gi 26333877 245 SYGLGFVASGrRWMALTESDIF 266
Cdd:cd05920 163 DYAYNVRASA-EVCGLDQDTVY 183
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
90-267 |
2.30e-08 |
|
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: 54.69 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 90 TFEELGKQSRKAANVLEGVcGLQPEDRmmlVLPRLPDWW---LISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIV 166
Cdd:cd05903 3 TYSELDTRADRLAAGLAAL-GVGPGDV---VAFQLPNWWefaVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 167 TSDAlapqvdaisadcpslqtkllvsdtsrpgwinFRELLRAASPehncvrtrsGDSVAIYFTSGTTGAPKMVEHSQSSY 246
Cdd:cd05903 79 VPER-------------------------------FRQFDPAAMP---------DAVALLLFTSGTTGEPKGVMHSHNTL 118
|
170 180
....*....|....*....|.
gi 26333877 247 GLGFVASGRRWMaLTESDIFW 267
Cdd:cd05903 119 SASIRQYAERLG-LGPGDVFL 138
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
87-264 |
3.16e-08 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 54.43 E-value: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 87 VKWTFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMipgVSQLTA---KDLKYRLQAARAK 163
Cdd:PRK08315 42 LRWTYREFNEEVDALAKGLLAL-GIEKGDRVGIWAPNVPEWVLTQFATAKIGAIL---VTINPAyrlSELEYALNQSGCK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 164 SIVTSDA------------LAPQVDAI------SADCPSLQTKLLVSDTSRPGWINFRELL-RAASPEHNCVRTRSG--- 221
Cdd:PRK08315 118 ALIAADGfkdsdyvamlyeLAPELATCepgqlqSARLPELRRVIFLGDEKHPGMLNFDELLaLGRAVDDAELAARQAtld 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 26333877 222 --DSVAIYFTSGTTGAPK--MVEHsqssYGLG----FVAsgrRWMALTESD 264
Cdd:PRK08315 198 pdDPINIQYTSGTTGFPKgaTLTH----RNILnngyFIG---EAMKLTEED 241
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
71-298 |
3.58e-08 |
|
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: 54.18 E-value: 3.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 71 RPPNPAFWWvngsgTEVKWTFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPgvsqlta 150
Cdd:cd05945 4 NPDRPAVVE-----GGRTLTYRELKERADALAAALASL-GLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVP------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 151 kdlkyrlqaaraksivtsdalapqVDAISAdcpslqtkllvsdTSRpgwinFRELLRAASPEhnCVRTRSGDSVAIYFTS 230
Cdd:cd05945 71 ------------------------LDASSP-------------AER-----IREILDAAKPA--LLIADGDDNAYIIFTS 106
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26333877 231 GTTGAPKMVEHSQSSyglgfVASGRRWM----ALTESDIFWNTTDTGWVKAAWTLFSAWSNGACIFVheLPR 298
Cdd:cd05945 107 GSTGRPKGVQISHDN-----LVSFTNWMlsdfPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVP--VPR 171
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
83-239 |
3.85e-08 |
|
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: 54.24 E-value: 3.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 83 SGTEVKWTFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARA 162
Cdd:cd05926 9 PGSTPALTYADLAELVDDLARQLAAL-GIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 163 KSIVT-SDALAPQVDAISADCPSLQTklLVSDTSRPGWINFRELLRAASPEHNCVRT----RSGDSVAIYFTSGTTGAPK 237
Cdd:cd05926 88 KLVLTpKGELGPASRAASKLGLAILE--LALDVGVLIRAPSAESLSNLLADKKNAKSegvpLPDDLALILHTSGTTGRPK 165
|
..
gi 26333877 238 MV 239
Cdd:cd05926 166 GV 167
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
89-241 |
4.78e-08 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 54.21 E-value: 4.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 89 WTFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTS 168
Cdd:PLN02330 56 VTYGEVVRDTRRFAKALRSL-GLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTN 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 169 DALAPQVDAISADCpslqtkLLVSDTSRPGWINFRELLRAASpehncvrtRSGDSV-----------AIYFTSGTTGAPK 237
Cdd:PLN02330 135 DTNYGKVKGLGLPV------IVLGEEKIEGAVNWKELLEAAD--------RAGDTSdneeilqtdlcALPFSSGTTGISK 200
|
....*.
gi 26333877 238 --MVEH 241
Cdd:PLN02330 201 gvMLTH 206
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
84-293 |
5.79e-08 |
|
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: 53.82 E-value: 5.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 84 GTEVKWTFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAK 163
Cdd:cd17646 19 DEGRTLTYRELDERANRLAHLLRAR-GVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 164 SIVTSDALAPQVDAISADCPSLQTKLLVSDTSRPGwinfrellraaspehncVRTRSGDSVAIYFTSGTTGAPK--MVEH 241
Cdd:cd17646 98 VVLTTADLAARLPAGGDVALLGDEALAAPPATPPL-----------------VPPRPDNLAYVIYTSGSTGRPKgvMVTH 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 26333877 242 SQssyglgfVASGRRWM----ALTESDIFWNTTDTGWVKAAWTLFSAWSNGACIFV 293
Cdd:cd17646 161 AG-------IVNRLLWMqdeyPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVV 209
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
65-251 |
6.86e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 53.51 E-value: 6.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 65 LEKTGHRPPN-PAFWWvngsGTEVkWTFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIP 143
Cdd:PRK07470 13 LRQAARRFPDrIALVW----GDRS-WTWREIDARVDALAAALAAR-GVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 144 GVSQLTAKDLKYRLQAARAKSIVTSDALAPQVDAISADCPSLqtKLLVSDTSRPGWINFRELLRA-ASPEHNCVRTRSGD 222
Cdd:PRK07470 87 TNFRQTPDEVAYLAEASGARAMICHADFPEHAAAVRAASPDL--THVVAIGGARAGLDYEALVARhLGARVANAAVDHDD 164
|
170 180 190
....*....|....*....|....*....|.
gi 26333877 223 SVAIYFTSGTTGAPK--MVEHSQssygLGFV 251
Cdd:PRK07470 165 PCWFFFTSGTTGRPKaaVLTHGQ----MAFV 191
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
69-241 |
1.35e-07 |
|
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: 52.63 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 69 GHRPPNPAFWWVN-GSGTEVKWTFEELGKQSRKAANVLEGVCGlqPEDRMMLVLPRLPDWWLISVACMRTGVVMIPgVSQ 147
Cdd:cd05931 4 AARPDRPAYTFLDdEGGREETLTYAELDRRARAIAARLQAVGK--PGDRVLLLAPPGLDFVAAFLGCLYAGAIAVP-LPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 148 LTAKDLKYRLQA----ARAKSIVTSDALAPQVDAISADCPSLQTkllvsdtsrpGWINFRELLRAASPEHNCVRTRSGDS 223
Cdd:cd05931 81 PTPGRHAERLAAiladAGPRVVLTTAAALAAVRAFAASRPAAGT----------PRLLVVDLLPDTSAADWPPPSPDPDD 150
|
170 180
....*....|....*....|.
gi 26333877 224 VA-IYFTSGTTGAPK--MVEH 241
Cdd:cd05931 151 IAyLQYTSGSTGTPKgvVVTH 171
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
88-310 |
1.50e-07 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 52.29 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 88 KWTFEELGKQSRKAANVLEGvCGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVT 167
Cdd:cd05934 3 RWTYAELLRESARIAAALAA-LGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 168 sdalapqvdaisadcpslqtkllvsdtsrpgwinfrellraaspehncvrtrsgDSVAIYFTSGTTGAPKMVEHSQSSYg 247
Cdd:cd05934 82 ------------------------------------------------------DPASILYTSGTTGPPKGVVITHANL- 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26333877 248 LGFVASGRRWMALTESDIFWNTTDTGWVKA-AWTLFSAWSNGACIFVheLPRVDAKTILNVRRK 310
Cdd:cd05934 107 TFAGYYSARRFGLGEDDVYLTVLPLFHINAqAVSVLAALSVGATLVL--LPRFSASRFWSDVRR 168
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
90-249 |
1.51e-07 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 52.74 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 90 TFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTSD 169
Cdd:PRK10252 485 SYREMREQVVALANLLRER-GVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTA 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 170 ALAPQVDAISADCPSLQTKLLVSDTSRPgwinfrelLRAASPEHncvrtrsgdSVAIYFTSGTTGAPK--MVEHS----- 242
Cdd:PRK10252 564 DQLPRFADVPDLTSLCYNAPLAPQGAAP--------LQLSQPHH---------TAYIIFTSGSTGRPKgvMVGQTaivnr 626
|
170
....*....|.
gi 26333877 243 ----QSSYGLG 249
Cdd:PRK10252 627 llwmQNHYPLT 637
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
84-247 |
1.69e-07 |
|
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: 52.47 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 84 GTEVKWTFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAK 163
Cdd:cd05932 2 GQVVEFTWGEVADKARRLAAALRAL-GLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 164 SIVTS-----DALAPQVDAisadcpSLQTKLLVSDTSRPGWINFRELLRAASPEHNCVRTRSGDSVAIYFTSGTTGAPKM 238
Cdd:cd05932 81 ALFVGklddwKAMAPGVPE------GLISISLPPPSAANCQYQWDDLIAQHPPLEERPTRFPEQLATLIYTSGTTGQPKG 154
|
....*....
gi 26333877 239 VEHSQSSYG 247
Cdd:cd05932 155 VMLTFGSFA 163
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
80-262 |
1.89e-07 |
|
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: 52.27 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 80 VNGSGTevkWTFEELGKQSRKAANVLEGvCGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQA 159
Cdd:cd12114 7 ICGDGT---LTYGELAERARRVAGALKA-AGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILAD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 160 ARAKSIVTSDALAPQVDAISADCPSLQTKLlvsdtsrpgwinfrellrAASPEHNCVRTRSGDSVAIYFTSGTTGAPK-- 237
Cdd:cd12114 83 AGARLVLTDGPDAQLDVAVFDVLILDLDAL------------------AAPAPPPPVDVAPDDLAYVIFTSGSTGTPKgv 144
|
170 180 190
....*....|....*....|....*....|....
gi 26333877 238 MVEHSQSS---------YGLGfvaSGRRWMALTE 262
Cdd:cd12114 145 MISHRAALntildinrrFAVG---PDDRVLALSS 175
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
90-266 |
2.29e-07 |
|
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: 51.71 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 90 TFEELGKQSRKAANVLEGvCGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTSD 169
Cdd:cd05935 3 TYLELLEVVKKLASFLSN-KGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 170 ALapqvdaisadcpslqtkllvsdtsrpgwinfrellraaspehncvrtrsgDSVA-IYFTSGTTGAPKMVEHSQSSYgL 248
Cdd:cd05935 82 EL--------------------------------------------------DDLAlIPYTSGTTGLPKGCMHTHFSA-A 110
|
170
....*....|....*...
gi 26333877 249 GFVASGRRWMALTESDIF 266
Cdd:cd05935 111 ANALQSAVWTGLTPSDVI 128
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
84-269 |
3.06e-07 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 51.40 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 84 GTEVKWTFEELGKQSRKAANVLEGVCGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAK 163
Cdd:PRK06839 23 TEEEEMTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 164 SIVTSDALAPQVDAISAdcpslqtkllVSDTSRPGWINFRELLRAASPEhNCVRTRSGDSVAIYFTSGTTGAPKmvehsq 243
Cdd:PRK06839 103 VLFVEKTFQNMALSMQK----------VSYVQRVISITSLKEIEDRKID-NFVEKNESASFIICYTSGTTGKPK------ 165
|
170 180
....*....|....*....|....*.
gi 26333877 244 ssyglGFVasgrrwmaLTESDIFWNT 269
Cdd:PRK06839 166 -----GAV--------LTQENMFWNA 178
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
81-243 |
5.05e-07 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 51.03 E-value: 5.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 81 NGSGTEVKWTFEELGKQSRKAANVLEGvCGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPgVS---QLTAKD---LK 154
Cdd:PRK08180 62 GADGGWRRLTYAEALERVRAIAQALLD-RGLSAERPLMILSGNSIEHALLALAAMYAGVPYAP-VSpaySLVSQDfgkLR 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 155 YRLQAARAKSIVTSDAlAPQVDAISADCPsLQTKLLVSDTSRPG--WINFRELL-----RAASPEHNCVRtrsGDSVAIY 227
Cdd:PRK08180 140 HVLELLTPGLVFADDG-AAFARALAAVVP-ADVEVVAVRGAVPGraATPFAALLatpptAAVDAAHAAVG---PDTIAKF 214
|
170
....*....|....*..
gi 26333877 228 -FTSGTTGAPKMVEHSQ 243
Cdd:PRK08180 215 lFTSGSTGLPKAVINTH 231
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
90-310 |
5.73e-07 |
|
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: 50.54 E-value: 5.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 90 TFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTSD 169
Cdd:cd05919 12 TYGQLHDGANRLGSALRNL-GVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 170 alapqvdaisADCPSLQtkllvsdtsrpgwinfrellraaspehncvrtrsgdsvaiyFTSGTTGAPKMVEHSQSSYgLG 249
Cdd:cd05919 91 ----------DDIAYLL-----------------------------------------YSSGTTGPPKGVMHAHRDP-LL 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26333877 250 FV-ASGRRWMALTESDIFWNTTDTGWvkaAW----TLFSAWSNGA-CIFVHELPRVDAKTILNVRRK 310
Cdd:cd05919 119 FAdAMAREALGLTPGDRVFSSAKMFF---GYglgnSLWFPLAVGAsAVLNPGWPTAERVLATLARFR 182
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
110-265 |
6.22e-07 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 50.80 E-value: 6.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 110 GLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTS----DALAPQVDAISADcpsl 185
Cdd:PRK06060 51 GLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSdalrDRFQPSRVAEAAE---- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 186 qtklLVSDTSRPGWINFRELlraaspehncvrtrSGDSVAI-YFTSGTTGAPKMVEHSQSSYgLGFV-ASGRRWMALTES 263
Cdd:PRK06060 127 ----LMSEAARVAPGGYEPM--------------GGDALAYaTYTSGTTGPPKAAIHRHADP-LTFVdAMCRKALRLTPE 187
|
..
gi 26333877 264 DI 265
Cdd:PRK06060 188 DT 189
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
88-247 |
8.08e-07 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 50.35 E-value: 8.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 88 KWTFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVT 167
Cdd:PRK03640 27 KVTFMELHEAVVSVAGKLAAL-GVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLIT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 168 SDALApqvDAISADCPSLQTKLLVSDTSRPGWINFRELLRAASpehncvrtrsgdsvaIYFTSGTTGAPKMVehsQSSYG 247
Cdd:PRK03640 106 DDDFE---AKLIPGISVKFAELMNGPKEEAEIQEEFDLDEVAT---------------IMYTSGTTGKPKGV---IQTYG 164
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
41-291 |
1.10e-06 |
|
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: 49.96 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 41 ISLGRQPVPEYF-----NFAHDVLdvwsqlekTGHRPPNPAFWWVNGSGTEVKWTFEELGKQSRKAANVLEGvCGLQPED 115
Cdd:cd05943 54 VSGRIMPGARWFpgarlNYAENLL--------RHADADDPAAIYAAEDGERTEVTWAELRRRVARLAAALRA-LGVKPGD 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 116 RMMLVLPRLPDwwlISVACMRT--------------GVvmiPGVSQltakdlkyRLQAARAKSIVTSDA---------LA 172
Cdd:cd05943 125 RVAGYLPNIPE---AVVAMLATasigaiwsscspdfGV---PGVLD--------RFGQIEPKVLFAVDAytyngkrhdVR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 173 PQVDAISADCPSLQTKLLVSDTSRPGWINFRE----------LLRAASPEHNCVRTRSGDSVAIYFTSGTTGAPKMVEHS 242
Cdd:cd05943 191 EKVAELVKGLPSLLAVVVVPYTVAAGQPDLSKiakaltledfLATGAAGELEFEPLPFDHPLYILYSSGTTGLPKCIVHG 270
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 26333877 243 QSSYGLGFVASGRRWMALTESD-IFWNTTdTGWVKAAWtLFSAWSNGACI 291
Cdd:cd05943 271 AGGTLLQHLKEHILHCDLRPGDrLFYYTT-CGWMMWNW-LVSGLAVGATI 318
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
75-241 |
1.24e-06 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 49.82 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 75 PAFwwvngSGTEVKWTFEELGKQSRKAANVLEGVCGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLK 154
Cdd:PRK12492 41 PAF-----SNLGVTLSYAELERHSAAFAAYLQQHTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 155 YRLQAARAKSIVTSDALAPQVDAISADC--------------PSLQ----------TKLLVSDTSRPGWINFRELLRAAS 210
Cdd:PRK12492 116 HQFKDSGARALVYLNMFGKLVQEVLPDTgieylieakmgdllPAAKgwlvntvvdkVKKMVPAYHLPQAVPFKQALRQGR 195
|
170 180 190
....*....|....*....|....*....|....
gi 26333877 211 PEHNCVRTRSGDSVAIY-FTSGTTGAPK--MVEH 241
Cdd:PRK12492 196 GLSLKPVPVGLDDIAVLqYTGGTTGLAKgaMLTH 229
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
90-252 |
1.33e-06 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 49.51 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 90 TFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMI---PGVSQltaKDLKYRLQAARAksiv 166
Cdd:PRK09274 43 SFAELDARSDAIAHGLNAA-GIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVlvdPGMGI---KNLKQCLAEAQP---- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 167 tsDALAPQVDAISADC------PSLQTKLLVSDTSRPGWINFRELLRAASP-EHNCVRTRSGDSVAIYFTSGTTGAPKMV 239
Cdd:PRK09274 115 --DAFIGIPKAHLARRlfgwgkPSVRRLVTVGGRLLWGGTTLATLLRDGAAaPFPMADLAPDDMAAILFTSGSTGTPKGV 192
|
170
....*....|...
gi 26333877 240 EHSQSSyglgFVA 252
Cdd:PRK09274 193 VYTHGM----FEA 201
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
86-241 |
1.50e-06 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 49.28 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 86 EVKWTFEELGKQSRKAANVLEgVCGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSI 165
Cdd:cd17640 3 PKRITYKDLYQEILDFAAGLR-SLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVAL 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26333877 166 VtsdalapqvdaisadcpslqtkllvsdtsrpgwinfrellraaspehncVRTRSGDSVAIYFTSGTTGAPK--MVEH 241
Cdd:cd17640 82 V-------------------------------------------------VENDSDDLATIIYTSGTTGNPKgvMLTH 110
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
110-308 |
5.81e-06 |
|
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: 47.43 E-value: 5.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 110 GLQPEDRMMLVLPRLPDW-WL---ISVACMRTGVVMIPGVSQLTAKDLKYrLQAARAKSIVTSDA-LAPQVDAISADCPS 184
Cdd:cd05922 14 GGVRGERVVLILPNRFTYiELsfaVAYAGGRLGLVFVPLNPTLKESVLRY-LVADAGGRIVLADAgAADRLRDALPASPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 185 LQTKLLVSdtsrpGWINFRELLRAASPEHNcvrtrsgDSVAIYFTSGTTGAPK--MVEHSQSSYGLGFVASgrrWMALTE 262
Cdd:cd05922 93 PGTVLDAD-----GIRAARASAPAHEVSHE-------DLALLLYTSGSTGSPKlvRLSHQNLLANARSIAE---YLGITA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 26333877 263 SDIFWNTTDTGWVKAAWTLFSAWSNGACIFVHELPRVDAKTILNVR 308
Cdd:cd05922 158 DDRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVLDDAFWEDLR 203
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
110-239 |
7.47e-06 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 47.19 E-value: 7.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 110 GLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKsIVTSDALAP-QVDAISADCPSLQTK 188
Cdd:PRK05852 64 GLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGAR-VVLIDADGPhDRAEPTTRWWPLTVN 142
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 26333877 189 LLVSDTSRPGWINFRelLRAASPEHNCVRTRSG---DSVAIYFTSGTTGAPKMV 239
Cdd:PRK05852 143 VGGDSGPSGGTLSVH--LDAATEPTPATSTPEGlrpDDAMIMFTGGTTGLPKMV 194
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
75-241 |
9.24e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 47.07 E-value: 9.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 75 PAFwwvngSGTEVKWTFEELGKQSRKAANVLEGVCGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLK 154
Cdd:PRK05677 41 PAF-----SNLGKTLTYGELYKLSGAFAAWLQQHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREME 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 155 YRLQAARAKSIVTSDALAPQVDAI-------------SADCPSLQTKLLVSDTSR-----------PGWINFRELL-RAA 209
Cdd:PRK05677 116 HQFNDSGAKALVCLANMAHLAEKVlpktgvkhvivteVADMLPPLKRLLINAVVKhvkkmvpayhlPQAVKFNDALaKGA 195
|
170 180 190
....*....|....*....|....*....|....
gi 26333877 210 SPEHNCVRTRSGDSVAIYFTSGTTGAPK--MVEH 241
Cdd:PRK05677 196 GQPVTEANPQADDVAVLQYTGGTTGVAKgaMLTH 229
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
86-293 |
1.49e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 46.87 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 86 EVKWTFEELGKQSRKAANVL--EGVcglQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAK 163
Cdd:PRK12316 4574 EEKLTYAELNRRANRLAHALiaRGV---GPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAA 4650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 164 SIVTSDALAPQVD-AISADCpslqtklLVSDTSRPgWINFrellraasPEHNCVRTRSGDSVA-IYFTSGTTGAPKMVEH 241
Cdd:PRK12316 4651 LLLTQSHLLQRLPiPDGLAS-------LALDRDED-WEGF--------PAHDPAVRLHPDNLAyVIYTSGSTGRPKGVAV 4714
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 26333877 242 SQSSYGLGFVASGRRWmALTESDIFWNTTDTGWVKAAWTLFSAWSNGACIFV 293
Cdd:PRK12316 4715 SHGSLVNHLHATGERY-ELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVI 4765
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
101-307 |
2.04e-05 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 45.95 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 101 AANVLEGvcGLQPEDRMMLVLPRlPDW---WLISVACMrtGVVMIPGVSQLTAKDLKYRLQAARAKSIVTSDALAPQVDA 177
Cdd:PLN02860 46 AAGLLRL--GLRNGDVVAIAALN-SDLyleWLLAVACA--GGIVAPLNYRWSFEEAKSAMLLVRPVMLVTDETCSSWYEE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 178 I-SADCPSLQTKLLVSDTSRPGWINFRELLRaasPEHncVRTRSG------------DSVAIYFTSGTTGAPKMV--EHS 242
Cdd:PLN02860 121 LqNDRLPSLMWQVFLESPSSSVFIFLNSFLT---TEM--LKQRALgtteldyawapdDAVLICFTSGTTGRPKGVtiSHS 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26333877 243 ----QSSYGLGFVASGrrwmaltESDIFWNTT---DTGWVKAAWTLFSAwsnGAC-IFvheLPRVDAKTILNV 307
Cdd:PLN02860 196 alivQSLAKIAIVGYG-------EDDVYLHTAplcHIGGLSSALAMLMV---GAChVL---LPKFDAKAALQA 255
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
110-245 |
2.68e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 45.50 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 110 GLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTSDA-----LAPQVDAISADC-P 183
Cdd:PRK06164 56 GVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVVWPGfkgidFAAILAAVPPDAlP 135
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 184 SLQTKLLVSDTSR--PGWINFRELLRAASP---EHNCVRTRSGDS---VAIYFTSGTTGAPKMVEHSQSS 245
Cdd:PRK06164 136 PLRAIAVVDDAADatPAPAPGARVQLFALPdpaPPAAAGERAADPdagALLFTTSGTTSGPKLVLHRQAT 205
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
88-239 |
2.86e-05 |
|
bacterial long-chain fatty acid CoA synthetase; 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: 341296 [Multi-domain] Cd Length: 569 Bit Score: 45.49 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 88 KWTFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVT 167
Cdd:cd17641 11 EFTWADYADRVRAFALGLLAL-GVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 168 SDAlaPQVD---AISADCPSLQtKLLVSDT------SRPGWINF---RELLRAASPEH-----NCVRTRSGDSVAIY-FT 229
Cdd:cd17641 90 EDE--EQVDkllEIADRIPSVR-YVIYCDPrgmrkyDDPRLISFedvVALGRALDRRDpglyeREVAAGKGEDVAVLcTT 166
|
170
....*....|
gi 26333877 230 SGTTGAPKMV 239
Cdd:cd17641 167 SGTTGKPKLA 176
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
53-291 |
3.33e-05 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 45.17 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 53 NFAHDVLdvwsqlekTGHRPPNPAFWWVNGSGTEVKWTFEELGKQSRKAANVLEgVCGLQPEDRMMLVLPRLPDWWLISV 132
Cdd:PRK03584 87 NYAENLL--------RHRRDDRPAIIFRGEDGPRRELSWAELRRQVAALAAALR-ALGVGPGDRVAAYLPNIPETVVAML 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 133 ACMRTGVVM--------IPGV----SQLTAKDL----KYRLQAaraKSIVTSDALApqvdAISADCPSLQTKLLVSDTSR 196
Cdd:PRK03584 158 ATASLGAIWsscspdfgVQGVldrfGQIEPKVLiavdGYRYGG---KAFDRRAKVA----ELRAALPSLEHVVVVPYLGP 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 197 PG----------WINFRELLRAASPEhnCVRTRSGDSVAIYFTSGTTGAPKMVEHSQSSYGLGFVASGRRWMALTESD-I 265
Cdd:PRK03584 231 AAaaaalpgallWEDFLAPAEAAELE--FEPVPFDHPLWILYSSGTTGLPKCIVHGHGGILLEHLKELGLHCDLGPGDrF 308
|
250 260
....*....|....*....|....*.
gi 26333877 266 FWNTTdTGWVKAAWtLFSAWSNGACI 291
Cdd:PRK03584 309 FWYTT-CGWMMWNW-LVSGLLVGATL 332
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
165-268 |
3.35e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 45.40 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 165 IVTSDALAPQVDAIsaDCPSLQtkLLVSDTsrPGWinfRELLRAASPEHNCVRTRSGDSVAIYFTSGTTGAPKMVEHSQS 244
Cdd:PRK13388 103 LVTDAEHRPLLDGL--DLPGVR--VLDVDT--PAY---AELVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHG 173
|
90 100
....*....|....*....|....*
gi 26333877 245 SYG-LGFVASGRRwmALTESDIFWN 268
Cdd:PRK13388 174 RLAfAGRALTERF--GLTRDDVCYV 196
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
88-309 |
3.98e-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: 44.85 E-value: 3.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 88 KWTFEELGKQSRKAANVLEGvCGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVT 167
Cdd:cd17645 23 SLTYKQLNEKANQLARHLRG-KGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYMLADSSAKILLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 168 SdalapqvdaisadcpslqtkllvsdtsrpgwinfrellraaspehncvrtrSGDSVAIYFTSGTTGAPK--MVEHSQSs 245
Cdd:cd17645 102 N---------------------------------------------------PDDLAYVIYTSGSTGLPKgvMIEHHNL- 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26333877 246 ygLGFVASGRRWMALTESDIFWNTTDTGWVKAAWTLFSAWSNGACIFVhelprVDAKTILNVRR 309
Cdd:cd17645 130 --VNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHV-----VPSERRLDLDA 186
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
88-269 |
3.99e-05 |
|
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: 44.72 E-value: 3.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 88 KWTFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVT 167
Cdd:cd05939 3 HWTFRELNEYSNKVANFFQAQ-GYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 168 sDALAPQVDAISADCPSLQTKllvsdtsrpgwiNFRELLraaspehncvrtrsgdsVAIYfTSGTTGAPKMVEHSQSSYg 247
Cdd:cd05939 82 -NLLDPLLTQSSTEPPSQDDV------------NFRDKL-----------------FYIY-TSGTTGLPKAAVIVHSRY- 129
|
170 180
....*....|....*....|..
gi 26333877 248 LGFVASGRRWMALTESDIFWNT 269
Cdd:cd05939 130 YRIAAGAYYAFGMRPEDVVYDC 151
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
90-298 |
5.15e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 45.15 E-value: 5.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 90 TFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTSD 169
Cdd:PRK12467 539 SYAELNRQANRLAHVLIAA-GVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQS 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 170 ALAPQVDaISADCPSLQtkllvsdtsrpgwINFRELLRAASPEHNCVRTRSGDSVA-IYFTSGTTGAPKMVEHSQSSYgL 248
Cdd:PRK12467 618 HLLAQLP-VPAGLRSLC-------------LDEPADLLCGYSGHNPEVALDPDNLAyVIYTSGSTGQPKGVAISHGAL-A 682
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 26333877 249 GFVASGRRWMALTESDIFWNTTDTGWVKAAWTLFSAWSNGACifVHELPR 298
Cdd:PRK12467 683 NYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGAT--LHLLPP 730
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
67-247 |
7.24e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 44.39 E-value: 7.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 67 KTGHRPPNPAFWWVNGSGTE-VKWTFEELGKQSRKAANVLEGVCGlqPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGV 145
Cdd:PRK05691 18 RAAQTPDRLALRFLADDPGEgVVLSYRDLDLRARTIAAALQARAS--FGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 146 SQLTAKdlkyRLQAARAKSIVtSDALAPQVDAISADCPSLQTKLLVSDTSRPGWINFRELLRAASPEHNCVRTRSGDSVA 225
Cdd:PRK05691 96 PPESAR----RHHQERLLSII-ADAEPRLLLTVADLRDSLLQMEELAAANAPELLCVDTLDPALAEAWQEPALQPDDIAF 170
|
170 180
....*....|....*....|..
gi 26333877 226 IYFTSGTTGAPKMVehsQSSYG 247
Cdd:PRK05691 171 LQYTSGSTALPKGV---QVSHG 189
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
90-293 |
8.61e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 44.18 E-value: 8.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 90 TFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTSD 169
Cdd:PRK12316 2030 SYAELDSRANRLAHRLRAR-GVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQR 2108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 170 ALapqvdaiSADCPsLQTKLLVSDTSRPGWInfrellrAASPEHNCVRTRSGDSVA-IYFTSGTTGAPKMVEHSQSSYGL 248
Cdd:PRK12316 2109 HL-------LERLP-LPAGVARLPLDRDAEW-------ADYPDTAPAVQLAGENLAyVIYTSGSTGLPKGVAVSHGALVA 2173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 26333877 249 GFVASGRRWmALTESDIFWNTTDTGWVKAAWTLFSAWSNGACIFV 293
Cdd:PRK12316 2174 HCQAAGERY-ELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLI 2217
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
90-237 |
1.10e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 43.76 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 90 TFEELGKQSRKAANVLEGVcGLQPEDRMMlVLPRLPDWWLIS-VACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTS 168
Cdd:PRK07788 76 TYAELDEQSNALARGLLAL-GVRAGDGVA-VLARNHRGFVLAlYAAGKVGARIILLNTGFSGPQLAEVAAREGVKALVYD 153
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26333877 169 DALAPQVDAISADCPSLQTKLLVSD---TSRPGWINFRELLRAASPEHNCVRTRSGDSVAIyfTSGTTGAPK 237
Cdd:PRK07788 154 DEFTDLLSALPPDLGRLRAWGGNPDddePSGSTDETLDDLIAGSSTAPLPKPPKPGGIVIL--TSGTTGTPK 223
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
86-304 |
1.12e-04 |
|
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: 43.44 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 86 EVKWTFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKsi 165
Cdd:cd12118 27 DRRYTWRQTYDRCRRLASALAAL-GISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAK-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 166 vtsdalapqvdaisadcpslqtkLLVSDTSrpgwINFRELLRAASPEHNCVRTRSG-DSVAIYFTSGTTGAPKMVEHSQS 244
Cdd:cd12118 104 -----------------------VLFVDRE----FEYEDLLAEGDPDFEWIPPADEwDPIALNYTSGTTGRPKGVVYHHR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26333877 245 SYGLGFVASGRRWMALTESDIFWNTTD---TGWVkAAWTLFSAWSNGACifvheLPRVDAKTI 304
Cdd:cd12118 157 GAYLNALANILEWEMKQHPVYLWTLPMfhcNGWC-FPWTVAAVGGTNVC-----LRKVDAKAI 213
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
90-289 |
1.22e-04 |
|
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: 43.45 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 90 TFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPgvsqltakdLKYRLQAARAKSIV-TS 168
Cdd:cd17653 24 TYGELDAASNALANRLLQL-GVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVP---------LDAKLPSARIQAILrTS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 169 DAlapqvdaisadcpslqtKLLVSDTSrpgwinfrellraaspehncvrtrsGDSVA-IYFTSGTTGAPK--MVEH---- 241
Cdd:cd17653 94 GA-----------------TLLLTTDS-------------------------PDDLAyIIFTSGSTGIPKgvMVPHrgvl 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 26333877 242 ---SQSSYGLgFVASGRRwMALTESDIFWnttdtgwvKAAWTLFSAWSNGA 289
Cdd:cd17653 132 nyvSQPPARL-DVGPGSR-VAQVLSIAFD--------ACIGEIFSTLCNGG 172
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
70-237 |
1.78e-04 |
|
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: 42.88 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 70 HRPPNPAFWWVNGSGTEVKWTfEELGKQSRKAANVLEGvcGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLT 149
Cdd:cd05923 12 SRAPDACAIADPARGLRLTYS-ELRARIEAVAARLHAR--GLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 150 AKDLKYRLQAARAKSIVTSDAlAPQVDAISAdcpSLQTKLLVSDTSRPGWI-NFRELLRAASPehncvrtRSGDSVAIYF 228
Cdd:cd05923 89 AAELAELIERGEMTAAVIAVD-AQVMDAIFQ---SGVRVLALSDLVGLGEPeSAGPLIEDPPR-------EPEQPAFVFY 157
|
....*....
gi 26333877 229 TSGTTGAPK 237
Cdd:cd05923 158 TSGTTGLPK 166
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
90-289 |
2.63e-04 |
|
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: 42.29 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 90 TFEELGKQSRKAANVL--EGVcglQPEDRMMLVLPRLPDwwlisvacMRTGVVMIpgvsqltakdlkyrLQAARAksIVT 167
Cdd:cd17643 14 TYGELDARANRLARTLraEGV---GPGDRVALALPRSAE--------LIVALLAI--------------LKAGGA--YVP 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 168 SDALAP--QVDAISADCpslQTKLLVSDTSRPGWInfrellraaspehncvrtrsgdsvaIYfTSGTTGAPK--MVEHSQ 243
Cdd:cd17643 67 IDPAYPveRIAFILADS---GPSLLLTDPDDLAYV-------------------------IY-TSGSTGRPKgvVVSHAN 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 26333877 244 SsygLGFVASGRRWMALTESDIFWNTTDTGWVKAAWTLFSAWSNGA 289
Cdd:cd17643 118 V---LALFAATQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGG 160
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
33-289 |
2.64e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 42.64 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 33 EVVATWEAislgrqpVPEYFNFAHDVLDVW-SQLEKTghrPPNPAFwwVNGsgtEVKWTFEELGKQSRKAANVLEGvCGL 111
Cdd:PRK12316 495 QLVEGWNA-------TAAEYPLQRGVHRLFeEQVERT---PEAPAL--AFG---EETLDYAELNRRANRLAHALIE-RGV 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 112 QPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTSDALAPQVDaisadcpsLQTKLLV 191
Cdd:PRK12316 559 GPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKLP--------LAAGVQV 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 192 SDTSRPG-WInfrellrAASPEHNCVRTRSGDSVA-IYFTSGTTGAPKMVEHSQSSyglgfVASGRRWM----ALTESDI 265
Cdd:PRK12316 631 LDLDRPAaWL-------EGYSEENPGTELNPENLAyVIYTSGSTGKPKGAGNRHRA-----LSNRLCWMqqayGLGVGDT 698
|
250 260
....*....|....*....|....
gi 26333877 266 FWNTTDTGWVKAAWTLFSAWSNGA 289
Cdd:PRK12316 699 VLQKTPFSFDVSVWEFFWPLMSGA 722
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
91-239 |
2.76e-04 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 42.38 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 91 FEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVT-SD 169
Cdd:PRK12406 14 FDELAQRAARAAGGLAAL-GVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAhAD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 170 ALAPQVDAISADC--------PSLQTKLLVSD---TSRPGWINFRELLrAASPEHNCVRTRSGDSVaIYfTSGTTGAPKM 238
Cdd:PRK12406 93 LLHGLASALPAGVtvlsvptpPEIAAAYRISPallTPPAGAIDWEGWL-AQQEPYDGPPVPQPQSM-IY-TSGTTGHPKG 169
|
.
gi 26333877 239 V 239
Cdd:PRK12406 170 V 170
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
210-293 |
3.98e-04 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 42.04 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 210 SPEHNCVRTRSGDSVAIYFTSGTTGAPKMVEHSQSSYGLGFVASGRRWMALTESDIFWNTTDTGWVKAAWTLFSAWSNGa 289
Cdd:PTZ00237 243 SPFYEYVPVESSHPLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHGFLYGSLSLG- 321
|
....
gi 26333877 290 CIFV 293
Cdd:PTZ00237 322 NTFV 325
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
88-269 |
4.19e-04 |
|
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: 41.57 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 88 KWTFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVt 167
Cdd:cd05940 3 ALTYAELDAMANRYARWLKSL-GLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 168 sdalapqVDAisadcpslqtkllvsdtsrpgwinfrellraaspehncvrtrsgdsvAIY-FTSGTTGAPK--MVEHSQS 244
Cdd:cd05940 81 -------VDA-----------------------------------------------ALYiYTSGTTGLPKaaIISHRRA 106
|
170 180
....*....|....*....|....*
gi 26333877 245 SYGLGFVASgrrWMALTESDIFWNT 269
Cdd:cd05940 107 WRGGAFFAG---SGGALPSDVLYTC 128
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
90-243 |
5.25e-04 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 41.65 E-value: 5.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 90 TFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPgVS---QLTAKDLKyRLQAARAK--- 163
Cdd:cd05921 27 TYAEALRQVRAIAQGLLDL-GLSAERPLLILSGNSIEHALMALAAMYAGVPAAP-VSpaySLMSQDLA-KLKHLFELlkp 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 164 SIVTSDALAPQVDAISADCPsLQTKLLVSDTSRPG--WINFRELL----RAASPEhncVRTRSG-DSVAIY-FTSGTTGA 235
Cdd:cd05921 104 GLVFAQDAAPFARALAAIFP-LGTPLVVSRNAVAGrgAISFAELAatppTAAVDA---AFAAVGpDTVAKFlFTSGSTGL 179
|
....*...
gi 26333877 236 PKMVEHSQ 243
Cdd:cd05921 180 PKAVINTQ 187
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
86-169 |
8.78e-04 |
|
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: 40.89 E-value: 8.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 86 EVKWTFEELGKQSRKAANVLEgVCGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSI 165
Cdd:cd05914 5 GEPLTYKDLADNIAKFALLLK-INGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAI 83
|
....
gi 26333877 166 VTSD 169
Cdd:cd05914 84 FVSD 87
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
90-180 |
1.15e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 40.40 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 90 TFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTSD 169
Cdd:PRK06710 51 TFSVFHDKVKRFANYLQKL-GVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLD 129
|
90
....*....|.
gi 26333877 170 ALAPQVDAISA 180
Cdd:PRK06710 130 LVFPRVTNVQS 140
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
90-241 |
2.49e-03 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 39.27 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 90 TFEELGKQSRKAANVLEGVCGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIpGVSQL-TAKDLKYRLQAARAKSIVTS 168
Cdd:PRK08974 50 TFRKLEERSRAFAAYLQNGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVV-NVNPLyTPRELEHQLNDSGAKAIVIV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 169 DALAPQVDAISADCP-----------SLQT-------------KLLVSDTSRPGWINFRELLRAASPEHNCVRTRSGDSV 224
Cdd:PRK08974 129 SNFAHTLEKVVFKTPvkhviltrmgdQLSTakgtlvnfvvkyiKRLVPKYHLPDAISFRSALHKGRRMQYVKPELVPEDL 208
|
170 180
....*....|....*....|
gi 26333877 225 A-IYFTSGTTGAPK--MVEH 241
Cdd:PRK08974 209 AfLQYTGGTTGVAKgaMLTH 228
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
84-265 |
2.68e-03 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 39.35 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 84 GTEVKWTFEELGKQSRKAANVLEGVcGLQPEDRMMLVL----PRLPDWWLIsvacMRTGVVMIPGVSQLTAKDLKYRLQA 159
Cdd:PRK06018 35 GPIVRTTYAQIHDRALKVSQALDRD-GIKLGDRVATIAwntwRHLEAWYGI----MGIGAICHTVNPRLFPEQIAWIINH 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 160 ARAKSIVTSDALAPQVDAISADCPSLQTKLLVSD------TSRPGWINFRELLRAASPEHNCVRTRSGDSVAIYFTSGTT 233
Cdd:PRK06018 110 AEDRVVITDLTFVPILEKIADKLPSVERYVVLTDaahmpqTTLKNAVAYEEWIAEADGDFAWKTFDENTAAGMCYTSGTT 189
|
170 180 190
....*....|....*....|....*....|...
gi 26333877 234 GAPKMVEHSQSSYGL-GFVASGRRWMALTESDI 265
Cdd:PRK06018 190 GDPKGVLYSHRSNVLhALMANNGDALGTSAADT 222
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
80-254 |
5.30e-03 |
|
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: 38.18 E-value: 5.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 80 VNGSGT--EVKWTFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRL 157
Cdd:cd05915 14 VSRLHTgeVHRTTYAEVYQRARRLMGGLRAL-GVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 158 QAARAKSI-VTSDALApqvdaISADCPSLQTKLLVSDTSRPGWINFRELLRAASPEHNCVR-TRSGDSVAIYFTSGTTGA 235
Cdd:cd05915 93 NHAEDKVLlFDPNLLP-----LVEAIRGELKTVQHFVVMDEKAPEGYLAYEEALGEEADPVrVPERAACGMAYTTGTTGL 167
|
170
....*....|....*....
gi 26333877 236 PKMVEHSQSSYGLGFVASG 254
Cdd:cd05915 168 PKGVVYSHRALVLHSLAAS 186
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
86-246 |
6.64e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 38.00 E-value: 6.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 86 EVKWTFEELGKQSRKAANVLEGVcGLQPEDRMMLVLPRLPDwwlisvacM---RTGVVMIPGV-----SQLTAKDLKYRL 157
Cdd:PRK08162 41 DRRRTWAETYARCRRLASALARR-GIGRGDTVAVLLPNIPA--------MveaHFGVPMAGAVlntlnTRLDAASIAFML 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333877 158 QAARAKSIVTSDALAPQVDAISADCPSLqtKLLVSD--------TSRPGWINFRELLRAASPEHNCVRTRSG-DSVAIYF 228
Cdd:PRK08162 112 RHGEAKVLIVDTEFAEVAREALALLPGP--KPLVIDvddpeypgGRFIGALDYEAFLASGDPDFAWTLPADEwDAIALNY 189
|
170
....*....|....*....
gi 26333877 229 TSGTTGAPK-MVEHSQSSY 246
Cdd:PRK08162 190 TSGTTGNPKgVVYHHRGAY 208
|
|
| |
