|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
1-286 |
7.89e-161 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 461.53 E-value: 7.89e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 1 MKWGRELAFEHDLSSVRLLGSVGEPI--RAWRWYRLVFGSDKTPVVDTWWQTETGAAMISPLRG-DRLQAGIGDAPAAGI 77
Cdd:PRK00174 354 MKEGDEHPKKYDLSSLRLLGSVGEPInpEAWEWYYKVVGGERCPIVDTWWQTETGGIMITPLPGaTPLKPGSATRPLPGI 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 78 SAKIVDDDGKDLEPspdhgeHVTGYLVLDKPWPAMLRGIWGDPERFKETYWSRFAeqGWYFAGDGARYGSDGEIWVLGRI 157
Cdd:PRK00174 434 QPAVVDEEGNPLEG------GEGGNLVIKDPWPGMMRTIYGDHERFVKTYFSTFK--GMYFTGDGARRDEDGYYWITGRV 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 158 DDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKshHAEMSHEQMVDELRSEVAKEISPIAKPR 237
Cdd:PRK00174 506 DDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLK--GGEEPSDELRKELRNWVRKEIGPIAKPD 583
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2792055509 238 EIHVVPELPKTRSGKIMRRLLRDVAEGRE-LGDTSTLVDPSVFEAIRESK 286
Cdd:PRK00174 584 VIQFAPGLPKTRSGKIMRRILRKIAEGEEiLGDTSTLADPSVVEKLIEAR 633
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
1-285 |
2.02e-144 |
|
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: 419.34 E-value: 2.02e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 1 MKWGRELAFEHDLSSVRLLGSVGEPI--RAWRWYRLVFGSDKTPVVDTWWQTETGAAMISPLRG-DRLQAGIGDAPAAGI 77
Cdd:TIGR02188 346 MRLGDEWVKKHDLSSLRLLGSVGEPInpEAWMWYYKVVGKERCPIVDTWWQTETGGIMITPLPGaTPTKPGSATLPFFGI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 78 SAKIVDDDGKDLEpspdhGEHVTGYLVLDKPWPAMLRGIWGDPERFKETYWSRFaeQGWYFAGDGARYGSDGEIWVLGRI 157
Cdd:TIGR02188 426 EPAVVDEEGNPVE-----GPGEGGYLVIKQPWPGMLRTIYGDHERFVDTYFSPF--PGYYFTGDGARRDKDGYIWITGRV 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 158 DDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKSHHAEmsHEQMVDELRSEVAKEISPIAKPR 237
Cdd:TIGR02188 499 DDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEP--DDELRKELRKHVRKEIGPIAKPD 576
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2792055509 238 EIHVVPELPKTRSGKIMRRLLRDVAEGRE--LGDTSTLVDPSVFEAIRES 285
Cdd:TIGR02188 577 KIRFVPGLPKTRSGKIMRRLLRKIAAGEAeiLGDTSTLEDPSVVEELIEA 626
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
1-275 |
7.00e-138 |
|
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: 401.94 E-value: 7.00e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 1 MKWGRELAFEHDLSSVRLLGSVGEPI--RAWRWYRLVFGSDKTPVVDTWWQTETGAAMISPLRG-DRLQAGIGDAPAAGI 77
Cdd:cd05966 340 MKFGDEWVKKHDLSSLRVLGSVGEPInpEAWMWYYEVIGKERCPIVDTWWQTETGGIMITPLPGaTPLKPGSATRPFFGI 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 78 SAKIVDDDGKDLEPspdhgeHVTGYLVLDKPWPAMLRGIWGDPERFKETYWSRFaeQGWYFAGDGARYGSDGEIWVLGRI 157
Cdd:cd05966 420 EPAILDEEGNEVEG------EVEGYLVIKRPWPGMARTIYGDHERYEDTYFSKF--PGYYFTGDGARRDEDGYYWITGRV 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 158 DDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKSHHAEmsHEQMVDELRSEVAKEISPIAKPR 237
Cdd:cd05966 492 DDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEP--SDELRKELRKHVRKEIGPIATPD 569
|
250 260 270
....*....|....*....|....*....|....*....
gi 2792055509 238 EIHVVPELPKTRSGKIMRRLLRDVAEG-RELGDTSTLVD 275
Cdd:cd05966 570 KIQFVPGLPKTRSGKIMRRILRKIAAGeEELGDTSTLAD 608
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
1-284 |
4.24e-132 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 385.62 E-value: 4.24e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 1 MKWGRELAFEHDLSSVRLLGSVGEPI--RAWRWYRLVFGsdkTPVVDTWWQTETGAAMISPLRGDRLQAG-IGdAPAAGI 77
Cdd:COG0365 293 MKAGDEPLKKYDLSSLRLLGSAGEPLnpEVWEWWYEAVG---VPIVDGWGQTETGGIFISNLPGLPVKPGsMG-KPVPGY 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 78 SAKIVDDDGKDLEPspdhGEhvTGYLVLDKPWPAMLRGIWGDPERFKETYWSRFaeQGWYFAGDGARYGSDGEIWVLGRI 157
Cdd:COG0365 369 DVAVVDEDGNPVPP----GE--EGELVIKGPWPGMFRGYWNDPERYRETYFGRF--PGWYRTGDGARRDEDGYFWILGRS 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 158 DDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKSHHAEmsHEQMVDELRSEVAKEISPIAKPR 237
Cdd:COG0365 441 DDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEP--SDELAKELQAHVREELGPYAYPR 518
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2792055509 238 EIHVVPELPKTRSGKIMRRLLRDVAEGRELGDTSTLVDPSVFEAIRE 284
Cdd:COG0365 519 EIEFVDELPKTRSGKIMRRLLRKIAEGRPLGDTSTLEDPEALDEIKE 565
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
1-280 |
2.45e-85 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 268.69 E-value: 2.45e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 1 MKWGRELAFEHDLSSVRLLGSVGEPIR--AWRWYRLVFGSDKTPVVDTWWQTETGAAMISPLRGDRLQA-GIGDAPAAGI 77
Cdd:PLN02654 384 MRDGDEYVTRHSRKSLRVLGSVGEPINpsAWRWFFNVVGDSRCPISDTWWQTETGGFMITPLPGAWPQKpGSATFPFFGV 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 78 SAKIVDDDGKDLEpspdhGEhVTGYLVLDKPWPAMLRGIWGDPERFKETYWSRFAeqGWYFAGDGARYGSDGEIWVLGRI 157
Cdd:PLN02654 464 QPVIVDEKGKEIE-----GE-CSGYLCVKKSWPGAFRTLYGDHERYETTYFKPFA--GYYFSGDGCSRDKDGYYWLTGRV 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 158 DDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKShhAEMSHEQMVDELRSEVAKEISPIAKPR 237
Cdd:PLN02654 536 DDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVE--GVPYSEELRKSLILTVRNQIGAFAAPD 613
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2792055509 238 EIHVVPELPKTRSGKIMRRLLRDVAEGR--ELGDTSTLVDPSVFE 280
Cdd:PLN02654 614 KIHWAPGLPKTRSGKIMRRILRKIASRQldELGDTSTLADPGVVD 658
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
1-254 |
4.25e-82 |
|
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: 258.28 E-value: 4.25e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 1 MKWGRELAFEHDLSSVRLLGSVGEPI--RAWRWYRLVFGSDKTPVVDTWWQTETGAAMISPLRG-DRLQAGIGDAPAAGI 77
Cdd:cd17634 341 MAAGDDAIEGTDRSSLRILGSVGEPInpEAYEWYWKKIGKEKCPVVDTWWQTETGGFMITPLPGaIELKAGSATRPVFGV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 78 SAKIVDDDGKDLEPSPDhgehvtGYLVLDKPWPAMLRGIWGDPERFKETYWSRFaeQGWYFAGDGARYGSDGEIWVLGRI 157
Cdd:cd17634 421 QPAVVDNEGHPQPGGTE------GNLVITDPWPGQTRTLFGDHERFEQTYFSTF--KGMYFSGDGARRDEDGYYWITGRS 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 158 DDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKshHAEMSHEQMVDELRSEVAKEISPIAKPR 237
Cdd:cd17634 493 DDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLN--HGVEPSPELYAELRNWVRKEIGPLATPD 570
|
250
....*....|....*..
gi 2792055509 238 EIHVVPELPKTRSGKIM 254
Cdd:cd17634 571 VVHWVDSLPKTRSGKIM 587
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
1-275 |
5.68e-80 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 252.12 E-value: 5.68e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 1 MKWGRELAFEHDLSSVRLLGSVGEPI--RAWRWYRLVFGsdkTPVVDTWWQTETGAAMISPLRGDRLQAGIGDAPAAGIS 78
Cdd:PRK04319 310 MGAGDDLVKKYDLSSLRHILSVGEPLnpEVVRWGMKVFG---LPIHDNWWMTETGGIMIANYPAMDIKPGSMGKPLPGIE 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 79 AKIVDDDGKDLEPspdhgeHVTGYLVLDKPWPAMLRGIWGDPERFKETYWSrfaeqGWYFAGDGARYGSDGEIWVLGRID 158
Cdd:PRK04319 387 AAIVDDQGNELPP------NRMGNLAIKKGWPSMMRGIWNNPEKYESYFAG-----DWYVSGDSAYMDEDGYFWFQGRVD 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 159 DVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKSHHAemSHEQMVDELRSEVAKEISPIAKPRE 238
Cdd:PRK04319 456 DVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYE--PSEELKEEIRGFVKKGLGAHAAPRE 533
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2792055509 239 IHVVPELPKTRSGKIMRRLLRdvaeGREL----GDTSTLVD 275
Cdd:PRK04319 534 IEFKDKLPKTRSGKIMRRVLK----AWELglpeGDLSTMED 570
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
2-282 |
9.93e-75 |
|
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: 239.52 E-value: 9.93e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 2 KWGRElafeHDLSSVRLLGSVGEP--IRAWRWYRLVFGsdkTPVVDTWWQTETGAAMISPLRG---DRLQAGIGDAPAAG 76
Cdd:cd05967 347 KYIKK----YDLSSLRTLFLAGERldPPTLEWAENTLG---VPVIDHWWQTETGWPITANPVGlepLPIKAGSPGKPVPG 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 77 ISAKIVDDDGKDLEPSpdhgehVTGYLVLDKPW-PAMLRGIWGDPERFKETYWSRFaeQGWYFAGDGARYGSDGEIWVLG 155
Cdd:cd05967 420 YQVQVLDEDGEPVGPN------ELGNIVIKLPLpPGCLLTLWKNDERFKKLYLSKF--PGYYDTGDAGYKDEDGYLFIMG 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 156 RIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKSHHAEMSHEQmVDELRSEVAKEISPIAK 235
Cdd:cd05967 492 RTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITAEEL-EKELVALVREQIGPVAA 570
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2792055509 236 PREIHVVPELPKTRSGKIMRRLLRDVAEGRELGDTSTLVDPSVFEAI 282
Cdd:cd05967 571 FRLVIFVKRLPKTRSGKILRRTLRKIADGEDYTIPSTIEDPSVLDEI 617
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
1-259 |
7.65e-74 |
|
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: 232.78 E-value: 7.65e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 1 MKWGRELAFEHDLSSVRLLGSVGEPI--RAWRWYRLVFGsdkTPVVDTWWQTETGAAMISPLRGDRLQAGIGDAPAAGIS 78
Cdd:cd05969 194 MKEGDELARKYDLSSLRFIHSVGEPLnpEAIRWGMEVFG---VPIHDTWWQTETGSIMIANYPCMPIKPGSMGKPLPGVK 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 79 AKIVDDDGKDLEPspdhGEHvtGYLVLDKPWPAMLRGIWGDPERFKETYwsrfaEQGWYFAGDGARYGSDGEIWVLGRID 158
Cdd:cd05969 271 AAVVDENGNELPP----GTK--GILALKPGWPSMFRGIWNDEERYKNSF-----IDGWYLTGDLAYRDEDGYFWFVGRAD 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 159 DVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKSHHAemSHEQMVDELRSEVAKEISPIAKPRE 238
Cdd:cd05969 340 DIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFE--PSDELKEEIINFVRQKLGAHVAPRE 417
|
250 260
....*....|....*....|.
gi 2792055509 239 IHVVPELPKTRSGKIMRRLLR 259
Cdd:cd05969 418 IEFVDNLPKTRSGKIMRRVLK 438
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
11-285 |
5.29e-67 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 219.43 E-value: 5.29e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 11 HDLSSVRLLGSVGEPIRA--WRWyrlVFGSDKTPVVDTWWQTETGAAMISPLRG-DRLQAGIGDA--PAAGISAKIVDD- 84
Cdd:PRK10524 352 HDLSSLRALFLAGEPLDEptASW---ISEALGVPVIDNYWQTETGWPILAIARGvEDRPTRLGSPgvPMYGYNVKLLNEv 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 85 DGKDLEPspdhGEHvtGYLVLDKPWP-AMLRGIWGDPERFKETYWSRFAEQgWYFAGDGARYGSDGEIWVLGRIDDVMNI 163
Cdd:PRK10524 429 TGEPCGP----NEK--GVLVIEGPLPpGCMQTVWGDDDRFVKTYWSLFGRQ-VYSTFDWGIRDADGYYFILGRTDDVINV 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 164 SGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKSHHAEMSHEQ---MVDELRSEVAKEISPIAKPREIH 240
Cdd:PRK10524 502 AGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLADREArlaLEKEIMALVDSQLGAVARPARVW 581
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2792055509 241 VVPELPKTRSGKIMRRLLRDVAEGRELGDTSTLVDPSVFEAIRES 285
Cdd:PRK10524 582 FVSALPKTRSGKLLRRAIQAIAEGRDPGDLTTIEDPAALQQIRQA 626
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
4-276 |
1.30e-65 |
|
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: 215.43 E-value: 1.30e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 4 GRELAFEHDLSSVRLLGSVGEPI--RAWRWYRLVFGSDKTPVVDTWWQTET-----GAAMISPLRGDRLqagigDAPAAG 76
Cdd:cd05968 347 GDAPVNAHDLSSLRVLGSTGEPWnpEPWNWLFETVGKGRNPIINYSGGTEIsggilGNVLIKPIKPSSF-----NGPVPG 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 77 ISAKIVDDDGKDLEPSpdhgehvTGYLVLDKPWPAMLRGIWGDPERFKETYWSRFaeQGWYFAGDGARYGSDGEIWVLGR 156
Cdd:cd05968 422 MKADVLDESGKPARPE-------VGELVLLAPWPGMTRGFWRDEDRYLETYWSRF--DNVWVHGDFAYYDEEGYFYILGR 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 157 IDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKSHHAEMshEQMVDELRSEVAKEISPIAKP 236
Cdd:cd05968 493 SDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPT--EALAEELMERVADELGKPLSP 570
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2792055509 237 REIHVVPELPKTRSGKIMRRLLRDVAEGRELGDTSTLVDP 276
Cdd:cd05968 571 ERILFVKDLPKTRNAKVMRRVIRAAYLGKELGDLSSLENP 610
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
3-260 |
2.28e-62 |
|
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: 202.57 E-value: 2.28e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 3 WGRELAFEHDLSSVRLLGSVGEPI--RAWRWYRLVFGsdkTPVVDTWWQTETGAaMISPLRGDRLQAGIGDAPAAGISAK 80
Cdd:cd05972 186 LIKQDLSSYKFSHLRLVVSAGEPLnpEVIEWWRAATG---LPIRDGYGQTETGL-TVGNFPDMPVKPGSMGRPTPGYDVA 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 81 IVDDDGKDLEPSPDhgehvtGYLVLDKPWPAMLRGIWGDPERFKETYwsrfaEQGWYFAGDGARYGSDGEIWVLGRIDDV 160
Cdd:cd05972 262 IIDDDGRELPPGEE------GDIAIKLPPPGLFLGYVGDPEKTEASI-----RGDYYLTGDRAYRDEDGYFWFVGRADDI 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 161 MNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKSHhaEMSHEQMVDELRSEVAKEISPIAKPREIH 240
Cdd:cd05972 331 IKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSG--YEPSEELAEELQGHVKKVLAPYKYPREIE 408
|
250 260
....*....|....*....|
gi 2792055509 241 VVPELPKTRSGKIMRRLLRD 260
Cdd:cd05972 409 FVEELPKTISGKIRRVELRD 428
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
10-268 |
1.16e-54 |
|
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: 183.09 E-value: 1.16e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 10 EHDLSSVRLLGSVGEPIRAWRWYRL--VFGsdkTPVVDTWWQTETGAAMISPLR--GDRLQAGIGdAPAAGISAKIVDDD 85
Cdd:COG0318 211 RYDLSSLRLVVSGGAPLPPELLERFeeRFG---VRIVEGYGLTETSPVVTVNPEdpGERRPGSVG-RPLPGVEVRIVDED 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 86 GKDLEPSpDHGE-HVTGylvldkpwPAMLRGIWGDPERFKETYwsrfaEQGWYFAGDGARYGSDGEIWVLGRIDDVMNIS 164
Cdd:COG0318 287 GRELPPG-EVGEiVVRG--------PNVMKGYWNDPEATAEAF-----RDGWLRTGDLGRLDEDGYLYIVGRKKDMIISG 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 165 GHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKShHAEMSheqmVDELRSEVAKEISPIAKPREIHVVPE 244
Cdd:COG0318 353 GENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRP-GAELD----AEELRAFLRERLARYKVPRRVEFVDE 427
|
250 260
....*....|....*....|....
gi 2792055509 245 LPKTRSGKIMRRLLRDVAEGRELG 268
Cdd:COG0318 428 LPRTASGKIDRRALRERYAAGALE 451
|
|
| propion_prpE |
TIGR02316 |
propionate--CoA ligase; This family contains one of three readily separable clades of proteins ... |
10-285 |
7.62e-53 |
|
propionate--CoA ligase; This family contains one of three readily separable clades of proteins in the group of acetate and propionate--CoA ligases. Characterized members of this family act on propionate. From propionyl-CoA, there is a cyclic degradation pathway: it is ligated by PrpC to the TCA cycle intermediate oxaloacetate, acted upon further by PrpD and an aconitase, then cleaved by PrpB to pyruvate and the TCA cycle intermediate succinate.
Pssm-ID: 131369 [Multi-domain] Cd Length: 628 Bit Score: 182.03 E-value: 7.62e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 10 EHDLSSVRLLGSVGEPIR--AWRWYRLVFGsdkTPVVDTWWQTETGAAMISPLRGDRLQA---GIGDAPAAGISAKIVDD 84
Cdd:TIGR02316 350 KHDLSSLHWLFLAGEPLDepTAHWITDGLG---KPVIDNYWQTETGWPVLAIMPGLDLKPvklGSPGLPMYGYHLRVLDE 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 85 -DGKDLEPSPdhgehvTGYLVLDKPWP-AMLRGIWGDPERFKETYWSRFAEQgWYFAGDGARYGSDGEIWVLGRIDDVMN 162
Cdd:TIGR02316 427 aTGRPCGPNE------KGVLTVVPPLPpGCLSTVWGDDARFLKTYWSHFKRP-LYSSFDWGIRDEDGYTFILGRTDDVIN 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 163 ISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILK-SHHAEMSHEQMVDE--LRSEVAKEISPIAKPREI 239
Cdd:TIGR02316 500 VAGHRLGTREIEESVSSHPSVAEVAVVGVHDELKGQVAVVFAILKeSDSAGDAHDPHAVEtgMMDCVVRQLGAVARPARV 579
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2792055509 240 HVVPELPKTRSGKIMRRLLRDVAEGRELGDTSTLVDPSVFEAIRES 285
Cdd:TIGR02316 580 YFVAALPKTRSGKLLRRSIQALAEGRDPGDLTTIDDPGALEQVRRA 625
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
10-254 |
2.98e-52 |
|
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: 174.01 E-value: 2.98e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 10 EHDLSSVRLLGSVGEPIRAWRWYRLVfGSDKTPVVDTWWQTETGAAMISpLRGDRLQAGIGDA--PAAGISAKIVDDDGK 87
Cdd:cd04433 110 GYDLSSLRALVSGGAPLPPELLERFE-EAPGIKLVNGYGLTETGGTVAT-GPPDDDARKPGSVgrPVPGVEVRIVDPDGG 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 88 DLEPSPdHGE-HVTGylvldkpwPAMLRGIWGDPERfketyWSRFAEQGWYFAGDGARYGSDGEIWVLGRIDDVMNISGH 166
Cdd:cd04433 188 ELPPGE-IGElVVRG--------PSVMKGYWNNPEA-----TAAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIKSGGE 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 167 RISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKShhaemSHEQMVDELRSEVAKEISPIAKPREIHVVPELP 246
Cdd:cd04433 254 NVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRP-----GADLDAEELRAHVRERLAPYKVPRRVVFVDALP 328
|
....*...
gi 2792055509 247 KTRSGKIM 254
Cdd:cd04433 329 RTASGKID 336
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
8-259 |
3.30e-40 |
|
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: 144.93 E-value: 3.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 8 AFEHDLSSVRLLGSVGE--PIRAWRWYRLVFGSdktPVVDTWWQTETGAAMISPlRGDRLQAGIGDAPAAGISAKIVDDD 85
Cdd:cd05958 207 AAGPDLSSLRKCVSAGEalPAALHRAWKEATGI---PIIDGIGSTEMFHIFISA-RPGDARPGATGKPVPGYEAKVVDDE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 86 GKDLepsPDhGEhvTGYLVLDKPwpamlRGIWGDPERFKETYWsrfaEQGWYFAGDGARYGSDGEIWVLGRIDDVMNISG 165
Cdd:cd05958 283 GNPV---PD-GT--IGRLAVRGP-----TGCRYLADKRQRTYV----QGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGG 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 166 HRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKSHHAemSHEQMVDELRSEVAKEISPIAKPREIHVVPEL 245
Cdd:cd05958 348 YNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVI--PGPVLARELQDHAKAHIAPYKYPRAIEFVTEL 425
|
250
....*....|....
gi 2792055509 246 PKTRSGKIMRRLLR 259
Cdd:cd05958 426 PRTATGKLQRFALR 439
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
15-259 |
4.15e-40 |
|
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: 144.58 E-value: 4.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 15 SVRLLGSVGEPI--RAWRWYRLVFGsdkTPVVDTWWQTETGAAMISPLR-GDRLQAGIGDAPAAGISAKIVDDDGKDLep 91
Cdd:cd05973 206 RLRRVSSAGEPLtpEVIRWFDAALG---VPIHDHYGQTELGMVLANHHAlEHPVHAGSAGRAMPGWRVAVLDDDGDEL-- 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 92 spdhGEHVTGYLVLD-KPWPAM-LRGIWGDPerfketywSRFAEQGWYFAGDGARYGSDGEIWVLGRIDDVMNISGHRIS 169
Cdd:cd05973 281 ----GPGEPGRLAIDiANSPLMwFRGYQLPD--------TPAIDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIG 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 170 TAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKSHHAemSHEQMVDELRSEVAKEISPIAKPREIHVVPELPKTR 249
Cdd:cd05973 349 PFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHE--GTPALADELQLHVKKRLSAHAYPRTIHFVDELPKTP 426
|
250
....*....|
gi 2792055509 250 SGKIMRRLLR 259
Cdd:cd05973 427 SGKIQRFLLR 436
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
7-265 |
3.61e-39 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 143.40 E-value: 3.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 7 LAFEHDLSSVRLLGSVGEPI-----RAWRwyrLVFGSDktpVVDTWWQTETG--AAMISPLRGD------RLQAGIgdaP 73
Cdd:PRK06187 274 RAYFVDFSSLRLVIYGGAALppallREFK---EKFGID---LVQGYGMTETSpvVSVLPPEDQLpgqwtkRRSAGR---P 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 74 AAGISAKIVDDDGKDLEPspDHGEhvTGYLVLDKPWpaMLRGIWGDPERFKETYwsrfaEQGWYFAGDGARYGSDGEIWV 153
Cdd:PRK06187 345 LPGVEARIVDDDGDELPP--DGGE--VGEIIVRGPW--LMQGYWNRPEATAETI-----DGGWLHTGDVGYIDEDGYLYI 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 154 LGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKshhAEMSHEQmvDELRSEVAKEISPI 233
Cdd:PRK06187 414 TDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLK---PGATLDA--KELRAFLRGRLAKF 488
|
250 260 270
....*....|....*....|....*....|...
gi 2792055509 234 AKPREIHVVPELPKTRSGKIMRRLLRD-VAEGR 265
Cdd:PRK06187 489 KLPKRIAFVDELPRTSVGKILKRVLREqYAEGK 521
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
10-260 |
5.27e-39 |
|
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: 141.42 E-value: 5.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 10 EHDLSSVRLLGSVGEPIRA--WRWYRLVFGsdkTPVVDTWWQTETGA-----AMISPLRgdrlQAGIGdAPAAGISAKIV 82
Cdd:cd05971 203 KHAQVKLRAIATGGESLGEelLGWAREQFG---VEVNEFYGQTECNLvigncSALFPIK----PGSMG-KPIPGHRVAIV 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 83 DDDGKDLEPSpdhgehVTGYLVLDKPWPAMLRGIWGDPERFKEtywsRFAeQGWYFAGDGARYGSDGEIWVLGRIDDVMN 162
Cdd:cd05971 275 DDNGTPLPPG------EVGEIAVELPDPVAFLGYWNNPSATEK----KMA-GDWLLTGDLGRKDSDGYFWYVGRDDDVIT 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 163 ISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKShhAEMSHEQMVDELRSEVAKEISPIAKPREIHVV 242
Cdd:cd05971 344 SSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNP--GETPSDALAREIQELVKTRLAAHEYPREIEFV 421
|
250
....*....|....*...
gi 2792055509 243 PELPKTRSGKIMRRLLRD 260
Cdd:cd05971 422 NELPRTATGKIRRRELRA 439
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
50-260 |
1.43e-38 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 140.50 E-value: 1.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 50 TETGAAMISPLRGDRLQAGIGdAPAAGISAKIVDDDGKDLEPSPDHGE-HVTGylvldkpwPAMLRGIWGDPERFKETyw 128
Cdd:cd05941 247 TEIGMALSNPLDGERRPGTVG-MPLPGVQARIVDEETGEPLPRGEVGEiQVRG--------PSVFKEYWNKPEATKEE-- 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 129 srFAEQGWYFAGDGARYGSDGEIWVLGRI-DDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILK 207
Cdd:cd05941 316 --FTDDGWFKTGDLGVVDEDGYYWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLR 393
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2792055509 208 SHHAEMSHEqmvdELRSEVAKEISPIAKPREIHVVPELPKTRSGKIMRRLLRD 260
Cdd:cd05941 394 AGAAALSLE----ELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
10-255 |
5.73e-38 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 138.51 E-value: 5.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 10 EHDLSSVRLLGSVGEP-----IRAWRWYRLVFgsdktpvVDTWWQTETGAaMISPLRGDRLQAGIGDA--PAAGISAKIV 82
Cdd:cd17631 209 TTDLSSLRAVIYGGAPmperlLRALQARGVKF-------VQGYGMTETSP-GVTFLSPEDHRRKLGSAgrPVFFVEVRIV 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 83 DDDGKDLEPspdhgeHVTGYLVLDKPwpAMLRGIWGDPERFKETYwsrfaEQGWYFAGDGARYGSDGEIWVLGRIDDvMN 162
Cdd:cd17631 281 DPDGREVPP------GEVGEIVVRGP--HVMAGYWNRPEATAAAF-----RDGWFHTGDLGRLDEDGYLYIVDRKKD-MI 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 163 ISG-HRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKShHAEMSHEQMVDELRSEVAKeispIAKPREIHV 241
Cdd:cd17631 347 ISGgENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRP-GAELDEDELIAHCRERLAR----YKIPKSVEF 421
|
250
....*....|....
gi 2792055509 242 VPELPKTRSGKIMR 255
Cdd:cd17631 422 VDALPRNATGKILK 435
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
10-259 |
1.36e-35 |
|
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: 133.26 E-value: 1.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 10 EHDLSSVRLLGSVGEPIRA--WRWYRLVFGSDktpVVDTWWQTETGAAMISPLRGdRLQAGIGDAPAAGISAKIVDDDGK 87
Cdd:cd05959 276 SRDLSSLRLCVSAGEALPAevGERWKARFGLD---ILDGIGSTEMLHIFLSNRPG-RVRYGTTGKPVPGYEVELRDEDGG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 88 DLEPspdhGEhvTGYLVLDKPWPAMlrGIWGDPERFKETYwsrfaEQGWYFAGDGARYGSDGEIWVLGRIDDVMNISGHR 167
Cdd:cd05959 352 DVAD----GE--PGELYVRGPSSAT--MYWNNRDKTRDTF-----QGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIW 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 168 ISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKSHHAemSHEQMVDELRSEVAKEISPIAKPREIHVVPELPK 247
Cdd:cd05959 419 VSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYE--DSEALEEELKEFVKDRLAPYKYPRWIVFVDELPK 496
|
250
....*....|..
gi 2792055509 248 TRSGKIMRRLLR 259
Cdd:cd05959 497 TATGKIQRFKLR 508
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
11-259 |
1.08e-34 |
|
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: 129.89 E-value: 1.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 11 HDLSSVRLLGSVGEPIRAWRWYRLV--FGsdkTPVVDTWWQTETGAAMISPlRGDRLQAGIGDAPAAGISAKIVDDDGKD 88
Cdd:cd05919 205 DALRSLRLCVSAGEALPRGLGERWMehFG---GPILDGIGATEVGHIFLSN-RPGAWRLGSTGRPVPGYEIRLVDEEGHT 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 89 LEPSpdhgehVTGYLVLDKPwpAMLRGIWGDPERFKETywsrFAEqGWYFAGDGARYGSDGEIWVLGRIDDVMNISGHRI 168
Cdd:cd05919 281 IPPG------EEGDLLVRGP--SAAVGYWNNPEKSRAT----FNG-GWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWV 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 169 STAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKSHHAemSHEQMVDELRSEVAKEISPIAKPREIHVVPELPKT 248
Cdd:cd05919 348 SPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAA--PQESLARDIHRHLLERLSAHKVPRRIAFVDELPRT 425
|
250
....*....|.
gi 2792055509 249 RSGKIMRRLLR 259
Cdd:cd05919 426 ATGKLQRFKLR 436
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
49-260 |
1.50e-34 |
|
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: 130.66 E-value: 1.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 49 QTETGAAMISPlRGDRLQAGIGDAPAAGISAKIVDDDGKDLePSPDHGEhVTGYLVLDKPWpAMLRGIWGDPERFKETYW 128
Cdd:cd05928 325 QTETGLICANF-KGMKIKPGSMGKASPPYDVQIIDDNGNVL-PPGTEGD-IGIRVKPIRPF-GLFSGYVDNPEKTAATIR 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 129 SRFaeqgwYFAGDGARYGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKS 208
Cdd:cd05928 401 GDF-----YLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAP 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2792055509 209 HHAEMSHEQMVDELRSEVAKEISPIAKPREIHVVPELPKTRSGKIMRRLLRD 260
Cdd:cd05928 476 QFLSHDPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
12-259 |
7.04e-34 |
|
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: 127.88 E-value: 7.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 12 DLSSVRLLGSVGEPI------RAWRwyrlVFGsdkTPVVDTWWQTETGAAMISPLRGDRLQAGIGDA-PAAGISAKIVDD 84
Cdd:cd05903 206 PLSRLRTFVCGGATVprslarRAAE----LLG---AKVCSAYGSTECPGAVTSITPAPEDRRLYTDGrPLPGVEIKVVDD 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 85 DGKDLEPSPDHGEHVTGylvldkpwPAMLRGIWGDPERFKetywsRFAEQGWYFAGDGARYGSDGEIWVLGRIDDVMNIS 164
Cdd:cd05903 279 TGATLAPGVEGELLSRG--------PSVFLGYLDRPDLTA-----DAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRG 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 165 GHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKShHAEMSHEQMVDEL-RSEVAKEispiAKPREIHVVP 243
Cdd:cd05903 346 GENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKS-GALLTFDELVAYLdRQGVAKQ----YWPERLVHVD 420
|
250
....*....|....*.
gi 2792055509 244 ELPKTRSGKIMRRLLR 259
Cdd:cd05903 421 DLPRTPSGKVQKFRLR 436
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
10-259 |
9.85e-34 |
|
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: 127.68 E-value: 9.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 10 EHDLSSVRLLGSVGEPIR---AWRWYRlVFGsdkTPVVDTWWQTETG-AAMISPLRGDRLQAGIGdAPAAGISAKIVDDD 85
Cdd:cd05936 238 KRDFSSLRLCISGGAPLPvevAERFEE-LTG---VPIVEGYGLTETSpVVAVNPLDGPRKPGSIG-IPLPGTEVKIVDDD 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 86 GKDLEPspdhGEhvTGYLVLDKPwpAMLRGIWGDPERFKETYwsrfaEQGWYFAGDGARYGSDGEIWVLGRIDDVMNISG 165
Cdd:cd05936 313 GEELPP----GE--VGELWVRGP--QVMKGYWNRPEETAEAF-----VDGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGG 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 166 HRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKSHHAeMSHEQMVDELRSEVAkeisPIAKPREIHVVPEL 245
Cdd:cd05936 380 FNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGAS-LTEEEIIAFCREQLA----GYKVPRQVEFRDEL 454
|
250
....*....|....
gi 2792055509 246 PKTRSGKIMRRLLR 259
Cdd:cd05936 455 PKSAVGKILRRELR 468
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
16-259 |
1.31e-33 |
|
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: 126.64 E-value: 1.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 16 VRLLGSVGEPIRAWRWYRLVFGsdkTPVVDTWWQTETGAAMISPLRGDRLQAGIGdAPAAGISAKIVDDDGKDLepsPDh 95
Cdd:cd05934 198 LRAAYGAPNPPELHEEFEERFG---VRLLEGYGMTETIVGVIGPRDEPRRPGSIG-RPAPGYEVRIVDDDGQEL---PA- 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 96 GEhvTGYLVL--DKPWpAMLRGIWGDPERFKETYwsrfaEQGWYFAGDGARYGSDGEIWVLGRIDDVMNISGHRISTAEV 173
Cdd:cd05934 270 GE--PGELVIrgLRGW-GFFKGYYNMPEATAEAM-----RNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEV 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 174 ESALVGHSGVAEAAVVGATDEHTGQAICAFVILKsHHAEMSHEQMVDELRSEVAkeisPIAKPREIHVVPELPKTRSGKI 253
Cdd:cd05934 342 ERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLR-PGETLDPEELFAFCEGQLA----YFKVPRYIRFVDDLPKTPTEKV 416
|
....*.
gi 2792055509 254 MRRLLR 259
Cdd:cd05934 417 AKAQLR 422
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
5-260 |
4.16e-33 |
|
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: 126.84 E-value: 4.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 5 RELAFEHDLSSVRLLGSVGEPIRAwrwyrLVFGSDKT----PVVDTWWQTETgAAMISPLRGDRLQAGIGDAPAAGISAK 80
Cdd:cd05970 292 REDLSRYDLSSLRYCTTAGEALNP-----EVFNTFKEktgiKLMEGFGQTET-TLTIATFPWMEPKPGSMGKPAPGYEID 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 81 IVDDDGKDLEPSpDHGEHVtgyLVLDKPWP-AMLRGIWGDPERFKETYwsrfaEQGWYFAGDGARYGSDGEIWVLGRIDD 159
Cdd:cd05970 366 LIDREGRSCEAG-EEGEIV---IRTSKGKPvGLFGGYYKDAEKTAEVW-----HDGYYHTGDAAWMDEDGYLWFVGRTDD 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 160 VMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVIL-KSHHAEmshEQMVDELRSEVAKEISPIAKPRE 238
Cdd:cd05970 437 LIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLaKGYEPS---EELKKELQDHVKKVTAPYKYPRI 513
|
250 260
....*....|....*....|..
gi 2792055509 239 IHVVPELPKTRSGKIMRRLLRD 260
Cdd:cd05970 514 VEFVDELPKTISGKIRRVEIRE 535
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
12-258 |
5.60e-33 |
|
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: 125.33 E-value: 5.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 12 DLSSVRLLGSVGEPIRAWRWYRLVFGSDKTPVVDTWWQTETGAAM----ISPLRGDRLQAGIGdAPAAGISAKIVDDDGK 87
Cdd:cd05930 206 ALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDAtyyrVPPDDEEDGRVPIG-RPIPNTRVYVLDENLR 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 88 dlePSPDH--GE-HVTGylvldkpwPAMLRGIWGDPE----RFKETywsRFAEQGWYFA-GDGARYGSDGEIWVLGRIDD 159
Cdd:cd05930 285 ---PVPPGvpGElYIGG--------AGLARGYLNRPEltaeRFVPN---PFGPGERMYRtGDLVRWLPDGNLEFLGRIDD 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 160 VMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKSHhaemsHEQMVDELRSEVAKEISPIAKPREI 239
Cdd:cd05930 351 QVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEG-----GELDEEELRAHLAERLPDYMVPSAF 425
|
250
....*....|....*....
gi 2792055509 240 HVVPELPKTRSGKIMRRLL 258
Cdd:cd05930 426 VVLDALPLTPNGKVDRKAL 444
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
40-260 |
9.02e-32 |
|
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: 122.81 E-value: 9.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 40 KTPVVDTWWQTETGAAMIS-PLRGDRLQAG-IGdaPAAGISAKIVDDDGKDLEPSpdhgehVTGYLVLDKPwpAMLRGIW 117
Cdd:cd05926 290 GAPVLEAYGMTEAAHQMTSnPLPPGPRKPGsVG--KPVGVEVRILDEDGEILPPG------VVGEICLRGP--NVTRGYL 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 118 GDPERFKETywsrFAEQGWYFAGDGARYGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTG 197
Cdd:cd05926 360 NNPEANAEA----AFKDGWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYG 435
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2792055509 198 QAICAFVILKShHAEMSHEQMVDELRSEVAK-EIspiakPREIHVVPELPKTRSGKIMRRLLRD 260
Cdd:cd05926 436 EEVAAAVVLRE-GASVTEEELRAFCRKHLAAfKV-----PKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
10-254 |
2.29e-31 |
|
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: 121.55 E-value: 2.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 10 EHDLSSVRLLGSVGEPIRAwRWYRLVFGS-DKTPVVDTWWQTETGAAMISPLRGDRLQAGIGdAPAAGISAKIVDDDGKD 88
Cdd:cd05911 258 KYDLSSLRVILSGGAPLSK-ELQELLAKRfPNATIKQGYGMTETGGILTVNPDGDDKPGSVG-RLLPNVEAKIVDDDGKD 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 89 LEpspdhGEHVTGYLVLDKPwpAMLRGIWGDPERFKETywsrFAEQGWYFAGDGARYGSDGEIWVLGRIDDVMNISGHRI 168
Cdd:cd05911 336 SL-----GPNEPGEICVRGP--QVMKGYYNNPEATKET----FDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQV 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 169 STAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKsHHAEMSHeqmvDELRSEVAKEISPIAKPR-EIHVVPELPK 247
Cdd:cd05911 405 APAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRK-PGEKLTE----KEVKDYVAKKVASYKQLRgGVVFVDEIPK 479
|
....*..
gi 2792055509 248 TRSGKIM 254
Cdd:cd05911 480 SASGKIL 486
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
12-164 |
2.76e-31 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 120.49 E-value: 2.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 12 DLSSVRLLGSVGEPIRA--WRWYRLVFGsdkTPVVDTWWQTETGAAMISPLRGDRLQAGIGDA--PAAGISAKIVDDDGk 87
Cdd:pfam00501 275 LLSSLRLVLSGGAPLPPelARRFRELFG---GALVNGYGLTETTGVVTTPLPLDEDLRSLGSVgrPLPGTEVKIVDDET- 350
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2792055509 88 dLEPSPDHgehVTGYLVLDKPWpaMLRGIWGDPERFKEtywsRFAEQGWYFAGDGARYGSDGEIWVLGRIDDVMNIS 164
Cdd:pfam00501 351 -GEPVPPG---EPGELCVRGPG--VMKGYLNDPELTAE----AFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
1-276 |
8.88e-31 |
|
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: 120.84 E-value: 8.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 1 MKWGRELAFEHDLSSVRLLGSVGEPIRAwRWYRLVFGSDKTpvvDTWWQTETG----------AAMISPLRGDRLQAgig 70
Cdd:cd05943 356 EKAGLKPAETHDLSSLRTILSTGSPLKP-ESFDYVYDHIKP---DVLLASISGgtdiiscfvgGNPLLPVYRGEIQC--- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 71 daPAAGISAKIVDDDGKDLEpspdhGEhvTGYLVLDKPWPAMLRGIWGDPE--RFKETYWSRFAeqGWYFAGDGARYGSD 148
Cdd:cd05943 429 --RGLGMAVEAFDEEGKPVW-----GE--KGELVCTKPFPSMPVGFWNDPDgsRYRAAYFAKYP--GVWAHGDWIEITPR 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 149 GEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKSHHaEMSHEqMVDELRSEVAK 228
Cdd:cd05943 498 GGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGV-ELDDE-LRKRIRSTIRS 575
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2792055509 229 EISPIAKPREIHVVPELPKTRSGKIMRRLLRDVAEGRELGDTSTLVDP 276
Cdd:cd05943 576 ALSPRHVPAKIIAVPDIPRTLSGKKVEVAVKKIIAGRPVKNAGALANP 623
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
11-264 |
1.31e-30 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 120.16 E-value: 1.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 11 HDLSSVRLLGSVGEPI------RAWRwyrlVFGsdkTPVVDTWWQTETGAA-MISPLRGDRLQAGIGDAPAAGISAKIVD 83
Cdd:PRK13295 309 RPVSSLRTFLCAGAPIpgalveRARA----ALG---AKIVSAWGMTENGAVtLTKLDDPDERASTTDGCPLPGVEVRVVD 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 84 DDGKDLEPspdhGEhvTGYLVLDKPwpAMLRGIWGDPErfketyWSRFAEQGWYFAGDGARYGSDGEIWVLGRIDDVMNI 163
Cdd:PRK13295 382 ADGAPLPA----GQ--IGRLQVRGC--SNFGGYLKRPQ------LNGTDADGWFDTGDLARIDADGYIRISGRSKDVIIR 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 164 SGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKSHHaEMSHEQMVDELRSE-VAKEISpiakPREIHVV 242
Cdd:PRK13295 448 GGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQ-SLDFEEMVEFLKAQkVAKQYI----PERLVVR 522
|
250 260
....*....|....*....|..
gi 2792055509 243 PELPKTRSGKIMRRLLRDVAEG 264
Cdd:PRK13295 523 DALPRTPSGKIQKFRLREMLRG 544
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
73-259 |
5.10e-29 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 115.62 E-value: 5.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 73 PAAGISAKIVDDDGKDLePSPDHGEHVT-GylvldkpwPAMLRGIWGDPERFKETywsrFAEQGWYFAGDGARYGSDGEI 151
Cdd:PRK06087 360 AAAGVEIKVVDEARKTL-PPGCEGEEASrG--------PNVFMGYLDEPELTARA----LDEEGWYYSGDLCRMDEAGYI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 152 WVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKSHHAEMSHEQMVDEL-RSEVAKEI 230
Cdd:PRK06087 427 KITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPHHSLTLEEVVAFFsRKRVAKYK 506
|
170 180
....*....|....*....|....*....
gi 2792055509 231 SpiakPREIHVVPELPKTRSGKIMRRLLR 259
Cdd:PRK06087 507 Y----PEHIVVIDKLPRTASGKIQKFLLR 531
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
172-252 |
5.46e-29 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 105.32 E-value: 5.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 172 EVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKShhaemSHEQMVDELRSEVAKEISPIAKPREIHVVPELPKTRSG 251
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKP-----GVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSG 75
|
.
gi 2792055509 252 K 252
Cdd:pfam13193 76 K 76
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
49-264 |
1.44e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 113.87 E-value: 1.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 49 QTETG--AAMISPLRGDRlQAGIGDAPAAGISAKIVDDDGKDLEPspdhGEhvTGYLVLDKPwPAMLrGIWGDPERFKET 126
Cdd:PRK08316 321 QTEIAplATVLGPEEHLR-RPGSAGRPVLNVETRVVDDDGNDVAP----GE--VGEIVHRSP-QLML-GYWDDPEKTAEA 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 127 YwsrfaEQGWYFAGDGARYGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVIL 206
Cdd:PRK08316 392 F-----RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVP 466
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2792055509 207 KShhaemSHEQMVDELRSEVAKEISPIAKPREIHVVPELPKTRSGKIMRRLLRDVAEG 264
Cdd:PRK08316 467 KA-----GATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRERYAG 519
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
73-258 |
1.50e-28 |
|
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: 113.11 E-value: 1.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 73 PAAGISAKIVDDDGKDLEPsPDHGE-HVTGylvldkpwPAMLRGIWGDPERFKETyWSRFAEQGWYFAGDGARYGSDGEI 151
Cdd:cd05945 277 AKPGAKLVILDEDGRPVPP-GEKGElVISG--------PSVSKGYLNNPEKTAAA-FFPDEGQRAYRTGDLVRLEADGLL 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 152 WVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKsHHAEMsheQMVDELRSEVAKEIS 231
Cdd:cd05945 347 FYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPK-PGAEA---GLTKAIKAELAERLP 422
|
170 180
....*....|....*....|....*..
gi 2792055509 232 PIAKPREIHVVPELPKTRSGKIMRRLL 258
Cdd:cd05945 423 PYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
1-284 |
3.08e-27 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 110.66 E-value: 3.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 1 MKWGRELAFEHDLSSVRLLGSVGEPI--RAWRW-YRLVFGsdktpvvDTWWQTETG----------AAMISPLRGDRLQA 67
Cdd:PRK03584 370 EKAGLVPGETHDLSALRTIGSTGSPLppEGFDWvYEHVKA-------DVWLASISGgtdicscfvgGNPLLPVYRGEIQC 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 68 gigdaPAAGISAKIVDDDGKDLEpspdhGEhvTGYLVLDKPWPAMLRGIWGDP--ERFKETYWSRFAeqGWYFAGDGARY 145
Cdd:PRK03584 443 -----RGLGMAVEAWDEDGRPVV-----GE--VGELVCTKPFPSMPLGFWNDPdgSRYRDAYFDTFP--GVWRHGDWIEI 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 146 GSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKsHHAEMShEQMVDELRSE 225
Cdd:PRK03584 509 TEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLA-EGVTLD-DALRARIRTT 586
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2792055509 226 VAKEISPIAKPREIHVVPELPKTRSGKIM----RRLL--RDVAEGRELGdtsTLVDPSVFEAIRE 284
Cdd:PRK03584 587 IRTNLSPRHVPDKIIAVPDIPRTLSGKKVelpvKKLLhgRPVKKAVNRD---ALANPEALDWFAD 648
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
62-259 |
3.54e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 109.69 E-value: 3.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 62 GDRlQAGIGDAPAAGISAKIVDDDGkdlEPSPDHGEHVTGYLVLDkpwPAMLRGIWGDPERFKETywsrFAEQGWYFAGD 141
Cdd:PRK07787 288 GER-RPGWVGLPLAGVETRLVDEDG---GPVPHDGETVGELQVRG---PTLFDGYLNRPDATAAA----FTADGWFRTGD 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 142 GARYGSDGEIWVLGRID-DVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKSHHAEmsheqmvD 220
Cdd:PRK07787 357 VAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVAA-------D 429
|
170 180 190
....*....|....*....|....*....|....*....
gi 2792055509 221 ELRSEVAKEISPIAKPREIHVVPELPKTRSGKIMRRLLR 259
Cdd:PRK07787 430 ELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
42-260 |
1.93e-26 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 107.05 E-value: 1.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 42 PVVDTWWQTETgAAMISPLRGDRLQAGIGDA--PAAGISAKIVDDDGkdlePSPDHGEhvtgylVLDKPwPAMLRGIWGD 119
Cdd:cd05912 215 PVYQSYGMTET-CSQIVTLSPEDALNKIGSAgkPLFPVELKIEDDGQ----PPYEVGE------ILLKG-PNVTKGYLNR 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 120 PERFKETYwsrfaEQGWYFAGDGARYGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQA 199
Cdd:cd05912 283 PDATEESF-----ENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQV 357
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2792055509 200 ICAFVILKShhaEMSHEQMVDELRSEVAKeispIAKPREIHVVPELPKTRSGKIMRRLLRD 260
Cdd:cd05912 358 PVAFVVSER---PISEEELIAYCSEKLAK----YKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
10-260 |
2.61e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 107.68 E-value: 2.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 10 EHDLSSVRLL--GSVGEPIRAWRWYRLVFGSDKtpVVDTWWQTE-TGAAMISPLRGDR-LQAGIGDAPAAGISAKIVDDD 85
Cdd:PRK07656 277 AEDLSSLRLAvtGAASMPVALLERFESELGVDI--VLTGYGLSEaSGVTTFNRLDDDRkTVAGTIGTAIAGVENKIVNEL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 86 GKDLePSPDHGE-HVTGYLVLdkpwpamlRGIWGDPERFKETywsrFAEQGWYFAGDGARYGSDGEIWVLGRIDDVMNIS 164
Cdd:PRK07656 355 GEEV-PVGEVGElLVRGPNVM--------KGYYDDPEATAAA----IDADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVG 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 165 GHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKsHHAEMSHEQMVDELRSEVAKeispIAKPREIHVVPE 244
Cdd:PRK07656 422 GFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLK-PGAELTEEELIAYCREHLAK----YKVPRSIEFLDE 496
|
250
....*....|....*.
gi 2792055509 245 LPKTRSGKIMRRLLRD 260
Cdd:PRK07656 497 LPKNATGKVLKRALRE 512
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
24-260 |
3.46e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 107.20 E-value: 3.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 24 EPIRAWRwyrlvfgSDKTPVVDTWWQTETGAAMISPLRGDRLQAGIGDA--PAAGISAKIVDDDGKDLEPSpdhgehVTG 101
Cdd:PRK09088 267 EDILGWL-------DDGIPMVDGFGMSEAGTVFGMSVDCDVIRAKAGAAgiPTPTVQTRVVDDQGNDCPAG------VPG 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 102 YLVLDKPwpAMLRGIWGDPERFKETywsrFAEQGWYFAGDGARYGSDGEIWVLGRIDDvMNISG-HRISTAEVESALVGH 180
Cdd:PRK09088 334 ELLLRGP--NLSPGYWRRPQATARA----FTGDGWFRTGDIARRDADGFFWVVDRKKD-MFISGgENVYPAEIEAVLADH 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 181 SGVAEAAVVGATDEHTGQAICAFVilkSHHAEMSHEqmVDELRSEVAKEISPIAKPREIHVVPELPKTRSGKIMRRLLRD 260
Cdd:PRK09088 407 PGIRECAVVGMADAQWGEVGYLAI---VPADGAPLD--LERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRD 481
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
80-259 |
1.20e-25 |
|
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: 105.61 E-value: 1.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 80 KIVDDDGKDLEPspdhGEhvTGYLVLDKPWpaMLRGIWGDPErfketYWSR-FAEQGWYFAGDGARYGSDGEIWVLGRID 158
Cdd:COG1021 366 RIVDEDGNPVPP----GE--VGELLTRGPY--TIRGYYRAPE-----HNARaFTPDGFYRTGDLVRRTPDGYLVVEGRAK 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 159 DVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKShhAEMSHEQMVDELRSevakeiSPIAK--- 235
Cdd:COG1021 433 DQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPRG--EPLTLAELRRFLRE------RGLAAfkl 504
|
170 180
....*....|....*....|....
gi 2792055509 236 PREIHVVPELPKTRSGKIMRRLLR 259
Cdd:COG1021 505 PDRLEFVDALPLTAVGKIDKKALR 528
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
12-269 |
2.21e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 105.23 E-value: 2.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 12 DLSSVRLLGSVGEPIR---AWRWYRLVfgsdKTPVVDTWWQTETG-AAMISPLRGdrLQAGIGDAPAAGISAKIVDDDGK 87
Cdd:PRK05677 324 DFSALKLTLSGGMALQlatAERWKEVT----GCAICEGYGMTETSpVVSVNPSQA--IQVGTIGIPVPSTLCKVIDDDGN 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 88 DLePSPDHGEH-VTGylvldkpwPAMLRGIWGDPERFKETywsrFAEQGWYFAGDGARYGSDGEIWVLGRIDDVMNISGH 166
Cdd:PRK05677 398 EL-PLGEVGELcVKG--------PQVMKGYWQRPEATDEI----LDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGF 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 167 RISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKShHAEMSHEQMVDELRSEVakeiSPIAKPREIHVVPELP 246
Cdd:PRK05677 465 NVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKP-GETLTKEQVMEHMRANL----TGYKVPKAVEFRDELP 539
|
250 260
....*....|....*....|...
gi 2792055509 247 KTRSGKIMRRLLRDvAEGRELGD 269
Cdd:PRK05677 540 TTNVGKILRRELRD-EELKKAGL 561
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
42-264 |
3.52e-25 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 104.27 E-value: 3.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 42 PVVDTWWQTETgAAMISPLRGDRLQAGIGDA--PAAGISAKIVDDdGKDLEPSpDHGEhvtgylVLDKPwPAMLRGIWGD 119
Cdd:PRK03640 280 PVYQSYGMTET-ASQIVTLSPEDALTKLGSAgkPLFPCELKIEKD-GVVVPPF-EEGE------IVVKG-PNVTKGYLNR 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 120 PERFKETYwsrfaEQGWYFAGDGARYGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQA 199
Cdd:PRK03640 350 EDATRETF-----QDGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQV 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2792055509 200 ICAFVIlksHHAEMSHEQMVDELRSEVAKeispIAKPREIHVVPELPKTRSGKIMRRLLRDVAEG 264
Cdd:PRK03640 425 PVAFVV---KSGEVTEEELRHFCEEKLAK----YKVPKRFYFVEELPRNASGKLLRHELKQLVEE 482
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
80-258 |
1.56e-24 |
|
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: 102.41 E-value: 1.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 80 KIVDDDGKDLEPspdhGEhvTGYLVLDKPWpaMLRGIWGDPERFKETywsrFAEQGWYFAGDGARYGSDGEIWVLGRIDD 159
Cdd:cd05920 321 RVVDEEGNPVPP----GE--EGELLTRGPY--TIRGYYRAPEHNARA----FTPDGFYRTGDLVRRTPDGYLVVEGRIKD 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 160 VMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKShhAEMSHEQMVDELRsevAKEISPIAKPREI 239
Cdd:cd05920 389 QINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRD--PPPSAAQLRRFLR---ERGLAAYKLPDRI 463
|
170
....*....|....*....
gi 2792055509 240 HVVPELPKTRSGKIMRRLL 258
Cdd:cd05920 464 EFVDSLPLTAVGKIDKKAL 482
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
15-259 |
1.62e-24 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 102.06 E-value: 1.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 15 SVRLLGSVGE---PIRAWRWY----RLV--FGSDKTPVVDTWWQTETGAAMISPlrgdrlQAGIGdAPAAGISAKIVDdd 85
Cdd:cd17649 213 SLRLYIFGGEalsPELLRRWLkapvRLFnaYGPTEATVTPLVWKCEAGAARAGA------SMPIG-RPLGGRSAYILD-- 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 86 gKDLEPSPDHgehVTGYLVLDKPwpAMLRGIWGDPERFKETYWSR-FAEQG--WYFAGDGARYGSDGEIWVLGRIDDVMN 162
Cdd:cd17649 284 -ADLNPVPVG---VTGELYIGGE--GLARGYLGRPELTAERFVPDpFGAPGsrLYRTGDLARWRDDGVIEYLGRVDHQVK 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 163 ISGHRISTAEVESALVGHSGVAEAAVVgATDEHTGQAICAFVILKshhAEMSHEQMVDELRSEVAKEISPIAKPREIHVV 242
Cdd:cd17649 358 IRGFRIELGEIEAALLEHPGVREAAVV-ALDGAGGKQLVAYVVLR---AAAAQPELRAQLRTALRASLPDYMVPAHLVFL 433
|
250
....*....|....*..
gi 2792055509 243 PELPKTRSGKIMRRLLR 259
Cdd:cd17649 434 ARLPLTPNGKLDRKALP 450
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
12-262 |
1.97e-24 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 102.59 E-value: 1.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 12 DLSSVRLLGSVGEPI---RAWRWYRLVfgsdKTPVVDTWWQTETGAAMISPLRGDRLQAGIGDAPAAGISAKIVDDDGKD 88
Cdd:PRK12492 331 DFSALKLTNSGGTALvkaTAERWEQLT----GCTIVEGYGLTETSPVASTNPYGELARLGTVGIPVPGTALKVIDDDGNE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 89 LePSPDHGEhvtgylvLDKPWPAMLRGIWGDPERFKETywsrFAEQGWYFAGDGARYGSDGEIWVLGRIDDVMNISGHRI 168
Cdd:PRK12492 407 L-PLGERGE-------LCIKGPQVMKGYWQQPEATAEA----LDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNV 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 169 STAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKSHHAEmsheqmVDELRSEVAKEISPIAKPREIHVVPELPKT 248
Cdd:PRK12492 475 YPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDPGLS------VEELKAYCKENFTGYKVPKHIVLRDSLPMT 548
|
250
....*....|....
gi 2792055509 249 RSGKIMRRLLRDVA 262
Cdd:PRK12492 549 PVGKILRRELRDIA 562
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
131-260 |
2.14e-24 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 100.10 E-value: 2.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 131 FAEQGWYFAGDGARYGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVilkshh 210
Cdd:cd17630 201 FNEDGWFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVI------ 274
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2792055509 211 aEMSHEQMVDELRSEVAKEISPIAKPREIHVVPELPKTRSGKIMRRLLRD 260
Cdd:cd17630 275 -VGRGPADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
10-258 |
3.68e-24 |
|
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: 101.02 E-value: 3.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 10 EHDLSSVRLLGSVGEPIRAWRWYRL--VFGSDktpVVDTWWQTETGAA--MISPLRGDRLQAGIgdaPAAGISAKIVD-D 84
Cdd:cd05935 195 TRDLSSLKVLTGGGAPMPPAVAEKLlkLTGLR---FVEGYGLTETMSQthTNPPLRPKLQCLGI---P*FGVDARVIDiE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 85 DGKDLEPSpdhgehVTGYLVLDKPwpAMLRGIWGDPERFKETYWSRFAEQgwYF-AGDGARYGSDGEIWVLGRIDDVMNI 163
Cdd:cd05935 269 TGRELPPN------EVGEIVVRGP--QIFKGYWNRPEETEESFIEIKGRR--FFrTGDLGYMDEEGYFFFVDRVKRMINV 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 164 SGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKShhaEMSHEQMVDELRSEVAKEISPIAKPREIHVVP 243
Cdd:cd05935 339 SGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRP---EYRGKVTEEDIIEWAREQMAAYKYPREVEFVD 415
|
250
....*....|....*
gi 2792055509 244 ELPKTRSGKIMRRLL 258
Cdd:cd05935 416 ELPRSASGKILWRLL 430
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
131-259 |
5.40e-24 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 99.35 E-value: 5.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 131 FAEQGWyFAGDGARYGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKSHH 210
Cdd:PRK07824 230 FAEPGW-FRTDDLGALDDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGP 308
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2792055509 211 AEmsheqMVDELRSEVAKEISPIAKPREIHVVPELPKTRSGKIMRRLLR 259
Cdd:PRK07824 309 AP-----TLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALV 352
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
77-259 |
7.36e-24 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 98.89 E-value: 7.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 77 ISAKIVDDDGKDLEPSPDHGE-HVTGYLVldkpwpaMLrGIWGDPERFKETywsrFAEQGWYFAGDGARYGSDGEIWVLG 155
Cdd:cd05917 183 TEAKIVDPEGGIVPPVGVPGElCIRGYSV-------MK-GYWNDPEKTAEA----IDGDGWLHTGDLAVMDEDGYCRIVG 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 156 RIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKShHAEMSHEqmvdELRSEVAKEISPIAK 235
Cdd:cd05917 251 RIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKE-GAELTEE----DIKAYCKGKIAHYKV 325
|
170 180
....*....|....*....|....
gi 2792055509 236 PREIHVVPELPKTRSGKIMRRLLR 259
Cdd:cd05917 326 PRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
73-258 |
2.39e-23 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 98.81 E-value: 2.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 73 PAAGISAKIVDDDGKDLEPSpdhgehVTGYLVLDKPWPAmlRGIWGDPERFKEtywsRFAEQGW------YFAGDGARYG 146
Cdd:cd12117 311 PIANTRVYVLDEDGRPVPPG------VPGELYVGGDGLA--LGYLNRPALTAE----RFVADPFgpgerlYRTGDLARWL 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 147 SDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKshhaemsHEQMVDELRSEV 226
Cdd:cd12117 379 PDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAE-------GALDAAELRAFL 451
|
170 180 190
....*....|....*....|....*....|..
gi 2792055509 227 AKEISPIAKPREIHVVPELPKTRSGKIMRRLL 258
Cdd:cd12117 452 RERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
74-261 |
6.76e-23 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 97.99 E-value: 6.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 74 AAGISAKIVDDDGKDLEPSPDHGEHvtgylvldkpW---PAMLRGIWGDPERFKetywSRFAEQGWYFAGDGARYGSDGE 150
Cdd:PLN02574 380 APNMQAKVVDWSTGCLLPPGNCGEL----------WiqgPGVMKGYLNNPKATQ----STIDKDGWLRTGDIAYFDEDGY 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 151 IWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKSHHAeMSHEQMVDelrsEVAKEI 230
Cdd:PLN02574 446 LYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGST-LSQEAVIN----YVAKQV 520
|
170 180 190
....*....|....*....|....*....|.
gi 2792055509 231 SPIAKPREIHVVPELPKTRSGKIMRRLLRDV 261
Cdd:PLN02574 521 APYKKVRKVVFVQSIPKSPAGKILRRELKRS 551
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
52-260 |
1.15e-22 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 97.14 E-value: 1.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 52 TGAAMISPLRGDRLQAGIGDA--PAAGISAKIVDDDGKDLepsPDhGEHVTGYLVLDkpwpAMLRGIwgDPERFKETYws 129
Cdd:PRK13382 347 TEAGMIATATPADLRAAPDTAgrPAEGTEIRILDQDFREV---PT-GEVGTIFVRND----TQFDGY--TSGSTKDFH-- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 130 rfaeQGWYFAGDGARYGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKSH 209
Cdd:PRK13382 415 ----DGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPG 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2792055509 210 HAEmsheqMVDELRSEVAKEISPIAKPREIHVVPELPKTRSGKIMRRLLRD 260
Cdd:PRK13382 491 ASA-----TPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQA 536
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
14-258 |
1.17e-22 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 96.62 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 14 SSVRLLGSVGEPIRAWRWYRLvfgSDKTPVV----------DTWWQTetgAAMISPlrGDRLQAGIGdAPAAGISAKIVD 83
Cdd:cd12115 213 ASVRVVNLAGEPLPRDLVQRL---YARLQVErvvnlygpseDTTYST---VAPVPP--GASGEVSIG-RPLANTQAYVLD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 84 DDgkdLEPSPDHgehVTGYLVLDKPWPAmlRGIWGDPERFKETYWSRFAEQG--WYFAGDGARYGSDGEIWVLGRIDDVM 161
Cdd:cd12115 284 RA---LQPVPLG---VPGELYIGGAGVA--RGYLGRPGLTAERFLPDPFGPGarLYRTGDLVRWRPDGLLEFLGRADNQV 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 162 NISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVIlkshhAEMSHEQMVDELRSEVAKEISPIAKPREIHV 241
Cdd:cd12115 356 KVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIV-----AEPGAAGLVEDLRRHLGTRLPAYMVPSRFVR 430
|
250
....*....|....*..
gi 2792055509 242 VPELPKTRSGKIMRRLL 258
Cdd:cd12115 431 LDALPLTPNGKIDRSAL 447
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
8-260 |
1.36e-22 |
|
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: 96.93 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 8 AFEHDLSSVRLL---GSVGEP--IRAWRwYRLVfgsdktPVVDTWWQTETGAAMISPLRGDRLQAGIGDA---------- 72
Cdd:cd12119 274 ANGRDLSSLRRVvigGSAVPRslIEAFE-ERGV------RVIHAWGMTETSPLGTVARPPSEHSNLSEDEqlalrakqgr 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 73 PAAGISAKIVDDDGKDLepsPDHGEHVtGYLVLDKPWPAmlRGIWGDPERfKETYWsrfaEQGWYFAGDGARYGSDGEIW 152
Cdd:cd12119 347 PVPGVELRIVDDDGREL---PWDGKAV-GELQVRGPWVT--KSYYKNDEE-SEALT----EDGWLRTGDVATIDEDGYLT 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 153 VLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKShHAEMSHEQMVDELRSEVAKEisp 232
Cdd:cd12119 416 ITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKE-GATVTAEELLEFLADKVAKW--- 491
|
250 260
....*....|....*....|....*...
gi 2792055509 233 iAKPREIHVVPELPKTRSGKIMRRLLRD 260
Cdd:cd12119 492 -WLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
11-267 |
1.83e-22 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 96.95 E-value: 1.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 11 HDLSSVR--LLGSVGEPIRAWRWYRlvfgsDKT--PVVDTWWQTE-TGAAMISPLRGDRLQAGIG-DAPAAGISAKIVDD 84
Cdd:PRK07529 330 HDISSLRyaLCGAAPLPVEVFRRFE-----AATgvRIVEGYGLTEaTCVSSVNPPDGERRIGSVGlRLPYQRVRVVILDD 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 85 DGKDLEPSPDHGEHV---------TGYLVLDKPwpamlRGIWgdperfketywsrfAEQGWYFAGDGARYGSDGEIWVLG 155
Cdd:PRK07529 405 AGRYLRDCAVDEVGVlciagpnvfSGYLEAAHN-----KGLW--------------LEDGWLNTGDLGRIDADGYFWLTG 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 156 RIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKShHAEMSHEQMVDELRSEVAKeisPIAK 235
Cdd:PRK07529 466 RAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKP-GASATEAELLAFARDHIAE---RAAV 541
|
250 260 270
....*....|....*....|....*....|..
gi 2792055509 236 PREIHVVPELPKTRSGKIMRRLLRDVAEGREL 267
Cdd:PRK07529 542 PKHVRILDALPKTAVGKIFKPALRRDAIRRVL 573
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
12-262 |
2.01e-22 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 96.48 E-value: 2.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 12 DLSSVRLLGSVGEPIR---AWRWYRLVfgsdKTPVVDTWWQTETG-AAMISPLRGDRLQAGIGdAPAAGISAKIVDDDGK 87
Cdd:PRK08751 327 DFSSLKMTLGGGMAVQrsvAERWKQVT----GLTLVEAYGLTETSpAACINPLTLKEYNGSIG-LPIPSTDACIKDDAGT 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 88 DLePSPDHGEhvtgylvLDKPWPAMLRGIWGDPErfkETYWSRFAEqGWYFAGDGARYGSDGEIWVLGRIDDVMNISGHR 167
Cdd:PRK08751 402 VL-AIGEIGE-------LCIKGPQVMKGYWKRPE---ETAKVMDAD-GWLHTGDIARMDEQGFVYIVDRKKDMILVSGFN 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 168 ISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAfVILKSHHAEMSheqmvDELRSEVAKEISPIAKPREIHVVPELPK 247
Cdd:PRK08751 470 VYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKV-VIVKKDPALTA-----EDVKAHARANLTGYKQPRIIEFRKELPK 543
|
250
....*....|....*
gi 2792055509 248 TRSGKIMRRLLRDVA 262
Cdd:PRK08751 544 TNVGKILRRELRDAA 558
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
7-258 |
2.47e-22 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 96.15 E-value: 2.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 7 LAFEHDLSSVRLLGSVGEP-----IRAWRwyrlvfgsDKTPVVDT---WWQTETGA--AMISPLRGDRLQAGIGDAPAAG 76
Cdd:cd05904 268 IVDKYDLSSLRQIMSGAAPlgkelIEAFR--------AKFPNVDLgqgYGMTESTGvvAMCFAPEKDRAKYGSVGRLVPN 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 77 ISAKIVD-DDGKDLEPSPdhgehvTGYLvldkpW---PAMLRGIWGDPERFKETywsrFAEQGWYFAGDGARYGSDGEIW 152
Cdd:cd05904 340 VEAKIVDpETGESLPPNQ------TGEL-----WirgPSIMKGYLNNPEATAAT----IDKEGWLHTGDLCYIDEDGYLF 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 153 VLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILK--SHHAEmsheqmvDELRSEVAKEI 230
Cdd:cd05904 405 IVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKpgSSLTE-------DEIMDFVAKQV 477
|
250 260
....*....|....*....|....*...
gi 2792055509 231 SPIAKPREIHVVPELPKTRSGKIMRRLL 258
Cdd:cd05904 478 APYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
73-258 |
3.22e-22 |
|
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: 95.80 E-value: 3.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 73 PAAGISAKIVDDDGKDLepsPDHgehVTGYLVLDKPWPAmlRGIWGDPERFKETYWSRFAEQGWYFAGDGARYGSDGEIW 152
Cdd:cd12114 305 PLANQRYRVLDPRGRDC---PDW---VPGELWIGGRGVA--LGYLGDPELTAARFVTHPDGERLYRTGDLGRYRPDGTLE 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 153 VLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVgATDEHTGQAICAFVILKSHHAEMSheqmVDELRSEVAKEISP 232
Cdd:cd12114 377 FLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVV-VLGDPGGKRLAAFVVPDNDGTPIA----PDALRAFLAQTLPA 451
|
170 180
....*....|....*....|....*.
gi 2792055509 233 IAKPREIHVVPELPKTRSGKIMRRLL 258
Cdd:cd12114 452 YMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
12-265 |
3.73e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 95.72 E-value: 3.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 12 DLSSVRLLGSVG----EPIRAwRWYRLVfgsdktP---VVDTWWQTETGAAMISPLRGDRLQAGiGDAPAAGISAKIVDD 84
Cdd:PRK07798 294 DLSSLFAIASGGalfsPSVKE-ALLELL------PnvvLTDSIGSSETGFGGSGTVAKGAVHTG-GPRFTIGPRTVVLDE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 85 DGKDLEPspdhGEHVTGYLVLDKPWPAmlrGIWGDPERFKETYwSRFAEQGWYFAGDGARYGSDGEIWVLGRIDDVMNIS 164
Cdd:PRK07798 366 DGNPVEP----GSGEIGWIARRGHIPL---GYYKDPEKTAETF-PTIDGVRYAIPGDRARVEADGTITLLGRGSVCINTG 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 165 GHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAfVILKSHHAEMSheqmVDELRSEVAKEISPIAKPREIHVVPE 244
Cdd:PRK07798 438 GEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVA-VVQLREGARPD----LAELRAHCRSSLAGYKVPRAIWFVDE 512
|
250 260
....*....|....*....|.
gi 2792055509 245 LPKTRSGKIMRRLLRDVAEGR 265
Cdd:PRK07798 513 VQRSPAGKADYRWAKEQAAER 533
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
42-258 |
1.32e-21 |
|
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: 94.11 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 42 PVVDTWWQTETGAAMISPlrgdrlQAGIGDAPAAGISA--KIVDDDGKDLEPSPDHGEhvtGYLVLDKPWPAMLRGIWGD 119
Cdd:cd05923 294 EKVNIYGTTEAMNSLYMR------DARTGTEMRPGFFSevRIVRIGGSPDEALANGEE---GELIVAAAADAAFTGYLNQ 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 120 PERFKETYwsrfaEQGWYFAGDGARYGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQA 199
Cdd:cd05923 365 PEATAKKL-----QDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQS 439
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2792055509 200 ICAFVILksHHAEMSHEQMVDELRsevAKEISPIAKPREIHVVPELPKTRSGKIMRRLL 258
Cdd:cd05923 440 VTACVVP--REGTLSADELDQFCR---ASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
23-258 |
1.67e-21 |
|
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: 93.53 E-value: 1.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 23 GEPIRAWR---WYRlVFGSDKTPVVDTWWQTETGA-AMISPLRGDRLQAG----IGdAPAAGISAKIVDDDGKDLEPSpd 94
Cdd:cd17643 219 GEALEAAMlrpWAG-RFGLDRPQLVNMYGITETTVhVTFRPLDAADLPAAaaspIG-RPLPGLRVYVLDADGRPVPPG-- 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 95 hgehVTGYLVLDKPWPAmlRGIWGDP----ERFKETYWSRFAEQGwYFAGDGARYGSDGEIWVLGRIDDVMNISGHRIST 170
Cdd:cd17643 295 ----VVGELYVSGAGVA--RGYLGRPeltaERFVANPFGGPGSRM-YRTGDLARRLPDGELEYLGRADEQVKIRGFRIEL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 171 AEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKShhaemSHEQMVDELRSEVAKEISPIAKPREIHVVPELPKTRS 250
Cdd:cd17643 368 GEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADD-----GAAADIAELRALLKELLPDYMVPARYVPLDALPLTVN 442
|
....*...
gi 2792055509 251 GKIMRRLL 258
Cdd:cd17643 443 GKLDRAAL 450
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
11-252 |
1.72e-21 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 92.45 E-value: 1.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 11 HDLSSVRLLGSVGEPIRAWRWYRLVFGSDKTPVVDTWWQTETGAAMISPLRGDRLQAGIGDAPAAGisAKIVDDDGKDLE 90
Cdd:cd05924 131 YDLSSLFAISSGGALLSPEVKQGLLELVPNITLVDAFGSSETGFTGSGHSAGSGPETGPFTRANPD--TVVLDDDGRVVP 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 91 PSPDHGEHV--TGYLVLdkpwpamlrGIWGDPERFKETYwSRFAEQGWYFAGDGARYGSDGEIWVLGRIDDVMNISGHRI 168
Cdd:cd05924 209 PGSGGVGWIarRGHIPL---------GYYGDEAKTAETF-PEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKV 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 169 STAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKShhaemSHEQMVDELRSEVAKEISPIAKPREIHVVPELPKT 248
Cdd:cd05924 279 FPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQLRE-----GAGVDLEELREHCRTRIARYKLPKQVVFVDEIERS 353
|
....
gi 2792055509 249 RSGK 252
Cdd:cd05924 354 PAGK 357
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
77-266 |
1.73e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 93.69 E-value: 1.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 77 ISAKIVDDDGKDLEPspdhGEhvTGYLVLDKPwpAMLRGIWGDPERFKETYwsrfaEQGWYFAGDGARYGSDGEIWVLGR 156
Cdd:PRK07786 354 VAARVVDENMNDVPV----GE--VGEIVYRAP--TLMSGYWNNPEATAEAF-----AGGWFHSGDLVRQDEEGYVWVVDR 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 157 IDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKSHHAEMSHEQMVDELRSEVAKeispIAKP 236
Cdd:PRK07786 421 KKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDAALTLEDLAEFLTDRLAR----YKHP 496
|
170 180 190
....*....|....*....|....*....|....*.
gi 2792055509 237 REIHVVPELPKTRSGKIMRRLLR------DVAEGRE 266
Cdd:PRK07786 497 KALEIVDALPRNPAGKVLKTELRerygacVNVERRS 532
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
80-262 |
2.31e-21 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 93.68 E-value: 2.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 80 KIVDDDGKDLePSPDHGEHVT-GYLVLdkpwpamlRGIWGDPERFKETywsrFAEQGWYFAGDGARYGSDGEIWVLGRID 158
Cdd:PRK12583 385 KVVDPDGATV-PRGEIGELCTrGYSVM--------KGYWNNPEATAES----IDEDGWMHTGDLATMDEQGYVRIVGRSK 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 159 DVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKSHHAEMSheqmvDELRSEVAKEISPIAKPRE 238
Cdd:PRK12583 452 DMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASE-----EELREFCKARIAHFKVPRY 526
|
170 180
....*....|....*....|....
gi 2792055509 239 IHVVPELPKTRSGKIMRRLLRDVA 262
Cdd:PRK12583 527 FRFVDEFPMTVTGKVQKFRMREIS 550
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
10-260 |
3.54e-21 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 92.81 E-value: 3.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 10 EHDLSSVRLLGSVGEPIR---AWRWYRLVfgsdKTPVVDTWWQTETgAAMIS--PLRGDRLQAGIGdAPAAGISAKIVDD 84
Cdd:PRK08974 321 ELDFSSLKLSVGGGMAVQqavAERWVKLT----GQYLLEGYGLTEC-SPLVSvnPYDLDYYSGSIG-LPVPSTEIKLVDD 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 85 DGKDLEPspdhGEhvTGYLvldkpW---PAMLRGIWGDPERFKETYwsrfaEQGWYFAGDGARYGSDGEIWVLGRIDDVM 161
Cdd:PRK08974 395 DGNEVPP----GE--PGEL-----WvkgPQVMLGYWQRPEATDEVI-----KDGWLATGDIAVMDEEGFLRIVDRKKDMI 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 162 NISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKshhaEMSHEQmvDELRSEVAKEISPIAKPREIHV 241
Cdd:PRK08974 459 LVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKK----DPSLTE--EELITHCRRHLTGYKVPKLVEF 532
|
250
....*....|....*....
gi 2792055509 242 VPELPKTRSGKIMRRLLRD 260
Cdd:PRK08974 533 RDELPKSNVGKILRRELRD 551
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
50-261 |
4.71e-21 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 92.59 E-value: 4.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 50 TETGAAMISPLRGDrlqagigDAPAA------GISAKIVD-DDGKDLEPSpDHGE-HVTGylvldkpwPAMLRGIWGDPE 121
Cdd:cd17642 337 TETTSAILITPEGD-------DKPGAvgkvvpFFYAKVVDlDTGKTLGPN-ERGElCVKG--------PMIMKGYVNNPE 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 122 RFKETywsrFAEQGWYFAGDGARYGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAIC 201
Cdd:cd17642 401 ATKAL----IDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPA 476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2792055509 202 AFVILKsHHAEMSHEQMVDElrseVAKEISPIAKPRE-IHVVPELPKTRSGKIMRRLLRDV 261
Cdd:cd17642 477 AVVVLE-AGKTMTEKEVMDY----VASQVSTAKRLRGgVKFVDEVPKGLTGKIDRRKIREI 532
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
15-255 |
5.03e-21 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 91.17 E-value: 5.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 15 SVRLLGSVGE-PIRAWRWYRLVFGSdkTPVVDTWWQTETGAAMISPLRGDRLQAGIGDAPAAGISAKIVDDDGKDLePSP 93
Cdd:cd17635 118 SLRLIGYGGSrAIAADVRFIEATGL--TNTAQVYGLSETGTALCLPTDDDSIEINAVGRPYPGVDVYLAATDGIAG-PSA 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 94 DHGEhvtgyLVLDKPWpaMLRGIWGDPERFKETYwsrfaEQGWYFAGDGARYGSDGEIWVLGRIDDVMNISGHRISTAEV 173
Cdd:cd17635 195 SFGT-----IWIKSPA--NMLGYWNNPERTAEVL-----IDGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEV 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 174 ESALVGHSGVAEAAVVGATDEHTGQAICAFVILkshhAEMSHEQMVDELRSEVAKEISPIAKPREIHVVPELPKTRSGKI 253
Cdd:cd17635 263 ERIAEGVSGVQECACYEISDEEFGELVGLAVVA----SAELDENAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKV 338
|
..
gi 2792055509 254 MR 255
Cdd:cd17635 339 KR 340
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
133-260 |
6.23e-21 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 92.35 E-value: 6.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 133 EQGWYFAGDGARYGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILkSHHAE 212
Cdd:PLN02330 415 EDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVI-NPKAK 493
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2792055509 213 MSHEQMVDELRSEVAKeispIAKPREIHVVPELPKTRSGKIMRRLLRD 260
Cdd:PLN02330 494 ESEEDILNFVAANVAH----YKKVRVVQFVDSIPKSLSGKIMRRLLKE 537
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
10-265 |
6.82e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 91.95 E-value: 6.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 10 EHDLSSVRLLGSVGEPI------RAWRWYRLVFgsdktpvVDTWWQTETGAAMIS-PLRGDRLQ-AGIgdaPAAGISAKI 81
Cdd:PRK08314 301 ERDLSSLRYIGGGGAAMpeavaeRLKELTGLDY-------VEGYGLTETMAQTHSnPPDRPKLQcLGI---PTFGVDARV 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 82 VD-DDGKDLePSPDHGEHVT-GylvldkpwPAMLRGIWGDPERFKETywsrFAE-QGWYF--AGDGARYGSDGEIWVLGR 156
Cdd:PRK08314 371 IDpETLEEL-PPGEVGEIVVhG--------PQVFKGYWNRPEATAEA----FIEiDGKRFfrTGDLGRMDEEGYFFITDR 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 157 IDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKSHH-AEMSHEQMVDELRSEVA--Keispi 233
Cdd:PRK08314 438 LKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEArGKTTEEEIIAWAREHMAayK----- 512
|
250 260 270
....*....|....*....|....*....|..
gi 2792055509 234 aKPREIHVVPELPKTRSGKIMRRLLRDVAEGR 265
Cdd:PRK08314 513 -YPRIVEFVDSLPKSGSGKILWRQLQEQEKAR 543
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
12-260 |
1.58e-20 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 91.07 E-value: 1.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 12 DLSSVRLLGSVGEP-----IRAWRWYRLVFGSDktpvvdtWWQTETGAAMISPLRGD-RLQAGIGDAPAAGISAKIVDDD 85
Cdd:PRK06839 262 NLQSVRWFYNGGAPcpeelMREFIDRGFLFGQG-------FGMTETSPTVFMLSEEDaRRKVGSIGKPVLFCDYELIDEN 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 86 GKDLEPspdhGEhvTGYLVLDKPwpAMLRGIWGDPERFKETywsrfAEQGWYFAGDGARYGSDGEIWVLGRIDDVMNISG 165
Cdd:PRK06839 335 KNKVEV----GE--VGELLIRGP--NVMKEYWNRPDATEET-----IQDGWLCTGDLARVDEDGFVYIVGRKKEMIISGG 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 166 HRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKShHAEMSHEQMVDELRSEVAKeispIAKPREIHVVPEL 245
Cdd:PRK06839 402 ENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKS-SSVLIEKDVIEHCRLFLAK----YKIPKEIVFLKEL 476
|
250
....*....|....*....
gi 2792055509 246 PKTRSGKIMR----RLLRD 260
Cdd:PRK06839 477 PKNATGKIQKaqlvNQLKS 495
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
69-259 |
2.04e-20 |
|
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: 90.48 E-value: 2.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 69 IGdAPAAGISAKIVDDDGkdlEPSPDHgehVTGYLVLDKPWPAmlRGIWGDP----ERFKETYWSrfAEQGWYFAGDGAR 144
Cdd:cd17651 313 IG-RPIDNTRVYVLDAAL---RPVPPG---VPGELYIGGAGLA--RGYLNRPeltaERFVPDPFV--PGARMYRTGDLAR 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 145 YGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVIlkshhAEMSHEQMVDELRS 224
Cdd:cd17651 382 WLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVV-----GDPEAPVDAAELRA 456
|
170 180 190
....*....|....*....|....*....|....*
gi 2792055509 225 EVAKEISPIAKPREIHVVPELPKTRSGKIMRRLLR 259
Cdd:cd17651 457 ALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
12-263 |
3.32e-20 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 89.91 E-value: 3.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 12 DLSSVRLLGSVGEPIRAwrwyrlvfgsdktPVVDTWWQ----------TETGAAMISPLRGDRLQAG-IGdaPAAGISAK 80
Cdd:cd05918 213 DVPSLRTLVLGGEALTQ-------------SDVDTWADrvrlinaygpAECTIAATVSPVVPSTDPRnIG--RPLGATCW 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 81 IVDDDgkdlepspDHGEHV----TGYLVLDKPwpAMLRGIWGDPERFKETY-----WSRFAEQGW----YFAGDGARYGS 147
Cdd:cd05918 278 VVDPD--------NHDRLVpigaVGELLIEGP--ILARGYLNDPEKTAAAFiedpaWLKQEGSGRgrrlYRTGDLVRYNP 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 148 DGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQA---ICAFVILKSHHAEMSHEQMVDELRS 224
Cdd:cd05918 348 DGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVVKPKDGSSspqLVAFVVLDGSSSGSGDGDSLFLEPS 427
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2792055509 225 EVAKEISPIAKPREIHVVP------------ELPKTRSGKIMRRLLRDVAE 263
Cdd:cd05918 428 DEFRALVAELRSKLRQRLPsymvpsvflplsHLPLTASGKIDRRALRELAE 478
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
14-260 |
3.64e-20 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 89.82 E-value: 3.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 14 SSVRLLGSVGEPIRAWRWYRLVFGsdkTPVVDTWWQTETGAAMISPLRGDRlqAGIGDAPAAGISAKIVDDDGKDLEPSp 93
Cdd:PRK06155 294 HRVRVALGPGVPAALHAAFRERFG---VDLLDGYGSTETNFVIAVTHGSQR--PGSMGRLAPGFEARVVDEHDQELPDG- 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 94 dhgehVTGYLVL--DKPWpAMLRGIWGDPERFKETyWSRFaeqgWYFAGDGARYGSDGEIWVLGRIDDVMNISGHRISTA 171
Cdd:PRK06155 368 -----EPGELLLraDEPF-AFATGYFGMPEKTVEA-WRNL----WFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSF 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 172 EVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKSHHAeMSHEQMVDELRSEVAKeispIAKPREIHVVPELPKTRSG 251
Cdd:PRK06155 437 EVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTA-LEPVALVRHCEPRLAY----FAVPRYVEFVAALPKTENG 511
|
....*....
gi 2792055509 252 KIMRRLLRD 260
Cdd:PRK06155 512 KVQKFVLRE 520
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
12-260 |
6.89e-20 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 89.31 E-value: 6.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 12 DLSSVRL-LG---SVGEPIrAWRWYRLVfgsdKTPVVDTWWQTETG-AAMISPLRGDRLQAGIGdAPAAGISAKIVDDDG 86
Cdd:PRK07059 325 DFSKLIVaNGggmAVQRPV-AERWLEMT----GCPITEGYGLSETSpVATCNPVDATEFSGTIG-LPLPSTEVSIRDDDG 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 87 KDLePSPDHGE-HVTGylvldkpwPAMLRGIWGDPErfkETYWSRFAEqGWYFAGDGARYGSDGEIWVLGRIDDVMNISG 165
Cdd:PRK07059 399 NDL-PLGEPGEiCIRG--------PQVMAGYWNRPD---ETAKVMTAD-GFFRTGDVGVMDERGYTKIVDRKKDMILVSG 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 166 HRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKshhaemSHEQMVDELRSEVAKEISPIAKPREIHVVPEL 245
Cdd:PRK07059 466 FNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVVKK------DPALTEEDVKAFCKERLTNYKRPKFVEFRTEL 539
|
250
....*....|....*
gi 2792055509 246 PKTRSGKIMRRLLRD 260
Cdd:PRK07059 540 PKTNVGKILRRELRD 554
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
111-260 |
7.01e-20 |
|
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: 88.90 E-value: 7.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 111 AMLRGIWGDPERFKETYwsrfaEQGWYFAGDGARYGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVG 190
Cdd:cd12118 348 IVMKGYLKNPEATAEAF-----RGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVA 422
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 191 ATDEHTGQAICAFVILKShHAEMSHEQMVDELRSEVAKEISpiakPREIhVVPELPKTRSGKIMRRLLRD 260
Cdd:cd12118 423 RPDEKWGEVPCAFVELKE-GAKVTEEEIIAFCREHLAGFMV----PKTV-VFGELPKTSTGKIQKFVLRD 486
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
33-269 |
7.06e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 88.97 E-value: 7.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 33 RLVFGSDKTP-------------VVDTWWQTETGAAmISPLRGDRLQAgIGDAPAaGIsaKIVDDDGkdLEPSP------ 93
Cdd:PRK07867 270 RIVYGNEGAPgdiarfarrfgcvVVDGFGSTEGGVA-ITRTPDTPPGA-LGPLPP-GV--AIVDPDT--GTECPpaedad 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 94 ---DHGEHVTGYLVlDKPWPAMLRGIWGDPERFKEtywsRFAEqGWYFAGDGARYGSDGEIWVLGRIDDVMNISGHRIST 170
Cdd:PRK07867 343 grlLNADEAIGELV-NTAGPGGFEGYYNDPEADAE----RMRG-GVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGT 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 171 AEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKShHAEMSHEQMVDELRSEvaKEISPIAKPREIHVVPELPKTRS 250
Cdd:PRK07867 417 APIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAP-GAKFDPDAFAEFLAAQ--PDLGPKQWPSYVRVCAELPRTAT 493
|
250
....*....|....*....
gi 2792055509 251 GKIMRRLLRdvAEGRELGD 269
Cdd:PRK07867 494 FKVLKRQLS--AEGVDCAD 510
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
131-265 |
8.26e-20 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 87.92 E-value: 8.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 131 FAEQGWYFAGDGARYGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKShH 210
Cdd:cd05944 229 FVADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKP-G 307
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2792055509 211 AEMSHEQMVDELRSEVAKEispIAKPREIHVVPELPKTRSGKIMRRLLRDVAEGR 265
Cdd:cd05944 308 AVVEEEELLAWARDHVPER---AAVPKHIEVLEELPVTAVGKVFKPALRADAIHR 359
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
45-259 |
1.04e-19 |
|
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: 88.39 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 45 DTWWQTETgAAMISPLRGDRLQAGIGDAPAAGISAKIVDDDGKDLepspDHGEHVtgyLVLDKPWPA-MLRGIWGDPERF 123
Cdd:cd05974 230 DGYGQTET-TALVGNSPGQPVKAGSMGRPLPGYRVALLDPDGAPA----TEGEVA---LDLGDTRPVgLMKGYAGDPDKT 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 124 KETYwsrfaEQGWYFAGDGARYGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAF 203
Cdd:cd05974 302 AHAM-----RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAF 376
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2792055509 204 VILKShHAEMSHEQMVDELRSEVAKeISPIAKPREIHVVpELPKTRSGKIMRRLLR 259
Cdd:cd05974 377 IVLRA-GYEPSPETALEIFRFSRER-LAPYKRIRRLEFA-ELPKTISGKIRRVELR 429
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
50-260 |
1.91e-19 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 87.62 E-value: 1.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 50 TETGaaMIS--PLRGDRLQAGIGdAPAAGISAKIVD-DDGKDLEPspdhGE----HVTGylvldkpwPAMLRGIWGDPER 122
Cdd:PRK07514 304 TETN--MNTsnPYDGERRAGTVG-FPLPGVSLRVTDpETGAELPP----GEigmiEVKG--------PNVFKGYWRMPEK 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 123 FKEtywsRFAEQGWYFAGDGARYGSDGEIWVLGRIDDVMnISG-HRISTAEVESALVGHSGVAEAAVVGATDEHTGQAIC 201
Cdd:PRK07514 369 TAE----EFRADGFFITGDLGKIDERGYVHIVGRGKDLI-ISGgYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVT 443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2792055509 202 AFVILKShHAEMSHEQMVDELRSEVAKeispIAKPREIHVVPELPKTRSGKIMRRLLRD 260
Cdd:PRK07514 444 AVVVPKP-GAALDEAAILAALKGRLAR----FKQPKRVFFVDELPRNTMGKVQKNLLRE 497
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
80-270 |
2.93e-19 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 87.17 E-value: 2.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 80 KIVD-DDGKDLEPSpDHGEHVT-GYLVldkpwpaMLrGIWGDPERFKETywsrFAEQGWYFAGDGARYGSDGEIWVLGRI 157
Cdd:PRK08315 383 KIVDpETGETVPRG-EQGELCTrGYSV-------MK-GYWNDPEKTAEA----IDADGWMHTGDLAVMDEEGYVNIVGRI 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 158 DDvMNI-SGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKSHHaEMSHEQMVDELRSEVAK-EIspiak 235
Cdd:PRK08315 450 KD-MIIrGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGA-TLTEEDVRDFCRGKIAHyKI----- 522
|
170 180 190
....*....|....*....|....*....|....*
gi 2792055509 236 PREIHVVPELPKTRSGKIMRRLLRDVAEgRELGDT 270
Cdd:PRK08315 523 PRYIRFVDEFPMTVTGKIQKFKMREMMI-EELGLQ 556
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
75-264 |
4.50e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 86.86 E-value: 4.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 75 AGISAKIVDDDGKDLEPSPDHGEHVTGylvldkpwPAMLRGIWGDPERFKETYWSrfaeqGWYFAGDGARYGSDGEIWVL 154
Cdd:PRK06145 326 AHVEIRIADGAGRWLPPNMKGEICMRG--------PKVTKGYWKDPEKTAEAFYG-----DWFRSGDVGYLDEEGFLYLT 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 155 GRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKShhaemSHEQMVDELRSEVAKEISPIA 234
Cdd:PRK06145 393 DRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNP-----GATLTLEALDRHCRQRLASFK 467
|
170 180 190
....*....|....*....|....*....|
gi 2792055509 235 KPREIHVVPELPKTRSGKIMRRLLRDVAEG 264
Cdd:PRK06145 468 VPRQLKVRDELPRNPSGKVLKRVLRDELNG 497
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
73-259 |
4.80e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 86.58 E-value: 4.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 73 PAAGISAKIVDDDGKDLEPspdhGEH----VTGYLVLDkpwpamlrGIWGDPERFKETYwsrfaEQGWYFAGDGARYGSD 148
Cdd:PRK06188 344 PTPGLRVALLDEDGREVAQ----GEVgeicVRGPLVMD--------GYWNRPEETAEAF-----RDGWLHTGDVAREDED 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 149 GEIWVLGRIDDvMNISG-HRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKShhaemshEQMVD--ELRSE 225
Cdd:PRK06188 407 GFYYIVDRKKD-MIVTGgFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRP-------GAAVDaaELQAH 478
|
170 180 190
....*....|....*....|....*....|....
gi 2792055509 226 VAKEISPIAKPREIHVVPELPKTRSGKIMRRLLR 259
Cdd:PRK06188 479 VKERKGSVHAPKQVDFVDSLPLTALGKPDKKALR 512
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
50-258 |
5.39e-19 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 86.15 E-value: 5.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 50 TET--GAAMISPLRGDRlQAGIGdAPAAGISAKIVDDDgkdLEPSPD--HGE-HVTGylvldkpwPAMLRGIWGDP---- 120
Cdd:cd17652 237 TETtvCATMAGPLPGGG-VPPIG-RPVPGTRVYVLDAR---LRPVPPgvPGElYIAG--------AGLARGYLNRPglta 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 121 ERFKEtywSRFAEQG--WYFAGDGARYGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQ 198
Cdd:cd17652 304 ERFVA---DPFGAPGsrMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDK 380
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 199 AICAFVILKSHHAeMSHEqmvdELRSEVAKEISPIAKPREIHVVPELPKTRSGKIMRRLL 258
Cdd:cd17652 381 RLVAYVVPAPGAA-PTAA----ELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
12-260 |
5.72e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 86.52 E-value: 5.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 12 DLSSVRLLGSVGEPIRAWRWYRL--VFGsdktPVV-DTWWQTETGAAMISPLRGDRLQAGIGDAPAAGISAKIVDDDGKD 88
Cdd:PRK07788 321 DTSSLKIIFVSGSALSPELATRAleAFG----PVLyNLYGSTEVAFATIATPEDLAEAPGTVGRPPKGVTVKILDENGNE 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 89 LEPspdhgeHVTGYLVLDKPWPamLRGIWGDpeRFKETywsrfaEQGWYFAGDGARYGSDGEIWVLGRiDDVMNISG-HR 167
Cdd:PRK07788 397 VPR------GVVGRIFVGNGFP--FEGYTDG--RDKQI------IDGLLSSGDVGYFDEDGLLFVDGR-DDDMIVSGgEN 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 168 ISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKSHHAEMSheqmvDELRSEVAKEISPIAKPREIHVVPELPK 247
Cdd:PRK07788 460 VFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDE-----DAIKDYVRDNLARYKVPRDVVFLDELPR 534
|
250
....*....|...
gi 2792055509 248 TRSGKIMRRLLRD 260
Cdd:PRK07788 535 NPTGKVLKRELRE 547
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
85-268 |
5.90e-19 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 86.44 E-value: 5.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 85 DGKDLEPSPDHGEHVtGYLVLDKPwpAMLRGIWGDPERFKETYwsrfaEQGWYFAGDGARYGSDGEIWVLGRIDDVMNIS 164
Cdd:PLN02479 388 DTKTMKPVPADGKTM-GEIVMRGN--MVMKGYLKNPKANEEAF-----ANGWFHSGDLGVKHPDGYIEIKDRSKDIIISG 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 165 GHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKSHHAEMSHEQMVDELRSEVAKEISPIAKPREIhVVPE 244
Cdd:PLN02479 460 GENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSDEAALAEDIMKFCRERLPAYWVPKSV-VFGP 538
|
170 180
....*....|....*....|....
gi 2792055509 245 LPKTRSGKIMRRLLRdvAEGRELG 268
Cdd:PLN02479 539 LPKTATGKIQKHVLR--AKAKEMG 560
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
12-188 |
1.23e-18 |
|
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: 85.01 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 12 DLSSVRLLGSVGEPIRAW---RWyRLVFGSdkTPVVDTWWQTET--GAAMISPLRGDRLQAG---IGdAPAAGISAKIVD 83
Cdd:TIGR01733 233 ALASLRLVILGGEALTPAlvdRW-RARGPG--ARLINLYGPTETtvWSTATLVDPDDAPRESpvpIG-RPLANTRLYVLD 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 84 DDgkdLEPSPDHgehVTGYLVLDKPWPAmlRGIWGDP----ERFKETYWSRFAEQGWYFAGDGARYGSDGEIWVLGRIDD 159
Cdd:TIGR01733 309 DD---LRPVPVG---VVGELYIGGPGVA--RGYLNRPeltaERFVPDPFAGGDGARLYRTGDLVRYLPDGNLEFLGRIDD 380
|
170 180
....*....|....*....|....*....
gi 2792055509 160 VMNISGHRISTAEVESALVGHSGVAEAAV 188
Cdd:TIGR01733 381 QVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
10-258 |
1.28e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 85.47 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 10 EHDLSSVR--LLGSVGEPIRAWRWYRLVFGSDktpVVDTWWQTETGAAMISPLRGDRLQAGIGDAPAAGISAKIVDDDGK 87
Cdd:PRK06710 319 EYDISSIRacISGSAPLPVEVQEKFETVTGGK---LVEGYGLTESSPVTHSNFLWEKRVPGSIGVPWPDTEAMIMSLETG 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 88 DLEPSPDHGEHVTgylvldkPWPAMLRGIWGDPErfkETywSRFAEQGWYFAGDGARYGSDGEIWVLGRIDDVMNISGHR 167
Cdd:PRK06710 396 EALPPGEIGEIVV-------KGPQIMKGYWNKPE---ET--AAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFN 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 168 ISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKsHHAEMSHEqmvdELRSEVAKEISPIAKPREIHVVPELPK 247
Cdd:PRK06710 464 VYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLK-EGTECSEE----ELNQFARKYLAAYKVPKVYEFRDELPK 538
|
250
....*....|.
gi 2792055509 248 TRSGKIMRRLL 258
Cdd:PRK06710 539 TTVGKILRRVL 549
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
73-264 |
2.20e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 84.71 E-value: 2.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 73 PAAGISAKIVDDDGKDLEPSPDHGEHVTGYlvldkpwPAMLRGIWGDPERFKETYwsrfaEQGWYFAGDGARYGSDGEIW 152
Cdd:PRK06178 392 PVPGTEFKICDFETGELLPLGAEGEIVVRT-------PSLLKGYWNKPEATAEAL-----RDGWLHTGDIGKIDEQGFLH 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 153 VLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKSHHAEMSHeqmvdELRSEVAKEISP 232
Cdd:PRK06178 460 YLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTAA-----ALQAWCRENMAV 534
|
170 180 190
....*....|....*....|....*....|..
gi 2792055509 233 IAKPrEIHVVPELPKTRSGKIMRRLLRDVAEG 264
Cdd:PRK06178 535 YKVP-EIRIVDALPMTATGKVRKQDLQALAEE 565
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
50-258 |
4.06e-18 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 83.92 E-value: 4.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 50 TETGA-AMISPLRGDRLQAG---IGdAPAAGISAKIVDDDGKdLEPSPDHGE-HVTGYLVLdkpwpamlRGIWGDPERFK 124
Cdd:cd17655 288 TETTVdASIYQYEPETDQQVsvpIG-KPLGNTRIYILDQYGR-PQPVGVAGElYIGGEGVA--------RGYLNRPELTA 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 125 ETYWSRFAEQG--WYFAGDGARYGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICA 202
Cdd:cd17655 358 EKFVDDPFVPGerMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCA 437
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2792055509 203 FVILKSHHAemsheqmVDELRSEVAKEISPIAKPREIHVVPELPKTRSGKIMRRLL 258
Cdd:cd17655 438 YIVSEKELP-------VAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
80-260 |
1.04e-17 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 82.43 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 80 KIVDDDGKDLEPspdhGEHVTGYLvldKPWPAMLrgIWGDPERFKETYwsrfAEQGWYFAGDGARYGSDGEIWVLGRIDD 159
Cdd:cd05929 308 HILDEDGNEVPP----GEIGEVYF---ANGPGFE--YTNDPEKTAAAR----NEGGWSTLGDVGYLDEDGYLYLTDRRSD 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 160 vMNISGHR-ISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVilKSHHAEMSHEQMVDELRSEVAKEISPIAKPRE 238
Cdd:cd05929 375 -MIISGGVnIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVV--QPAPGADAGTALAEELIAFLRDRLSRYKCPRS 451
|
170 180
....*....|....*....|..
gi 2792055509 239 IHVVPELPKTRSGKIMRRLLRD 260
Cdd:cd05929 452 IEFVAELPRDDTGKLYRRLLRD 473
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
114-258 |
1.15e-17 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 82.52 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 114 RGIWGDPERFKETYW-SRFAEQG-WYFAGDGARYGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGA 191
Cdd:cd17650 308 RGYLNRPELTAERFVeNPFAPGErMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVR 387
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2792055509 192 TDEHTGQAICAFVIlkshhaeMSHEQMVDELRSEVAKEISPIAKPREIHVVPELPKTRSGKIMRRLL 258
Cdd:cd17650 388 EDKGGEARLCAYVV-------AAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
137-258 |
1.16e-17 |
|
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: 82.32 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 137 YFAGDGARYGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKSHHAEMShe 216
Cdd:cd17646 371 YRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAGPD-- 448
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2792055509 217 qmVDELRSEVAKEISPIAKPREIHVVPELPKTRSGKIMRRLL 258
Cdd:cd17646 449 --TAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
12-270 |
1.44e-17 |
|
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: 82.60 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 12 DLSSVRLLGSVGEPIRAW---RWYRLVFGsdkTPVVDTWWQTETG-AAMISPLRGDRLQAG---IGdAPAAGISAKIVDD 84
Cdd:COG1020 729 ALPSLRLVLVGGEALPPElvrRWRARLPG---ARLVNLYGPTETTvDSTYYEVTPPDADGGsvpIG-RPIANTRVYVLDA 804
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 85 DgkdLEPSPD--HGE-HVTGYLVldkpwpAmlRGIWGDP----ERFKEtywSRFAEQG--WYFAGDGARYGSDGEIWVLG 155
Cdd:COG1020 805 H---LQPVPVgvPGElYIGGAGL------A--RGYLNRPeltaERFVA---DPFGFPGarLYRTGDLARWLPDGNLEFLG 870
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 156 RIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKSHHAEMSheqmvDELRSEVAKEISPIAK 235
Cdd:COG1020 871 RADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAA-----ALLRLALALLLPPYMV 945
|
250 260 270
....*....|....*....|....*....|....*
gi 2792055509 236 PREIHVVPELPKTRSGKIMRRLLRDVAEGRELGDT 270
Cdd:COG1020 946 PAAVVLLLPLPLTGNGKLDRLALPAPAAAAAAAAA 980
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
12-255 |
1.62e-17 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 81.16 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 12 DLSSVRLLGSVGEPIRAWRWYRLVFGsdktpvvdTWW----QTET-GAAMISPLRGDRLQAGigdAPAAGISAKIVDDDG 86
Cdd:cd17637 112 DLSSLRHVLGLDAPETIQRFEETTGA--------TFWslygQTETsGLVTLSPYRERPGSAG---RPGPLVRVRIVDDND 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 87 KDLEPspdhGEhvTGYLVLDKPwpAMLRGIWGDPERFKETYwsrfaEQGWYFAGDGARYGSDGEIWVLGRI--DDVMNIS 164
Cdd:cd17637 181 RPVPA----GE--TGEIVVRGP--LVFQGYWNLPELTAYTF-----RNGWHHTGDLGRFDEDGYLWYAGRKpeKELIKPG 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 165 GHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKSHHAEMSheqmvDELRSEVAKEISPIAKPREIHVVPE 244
Cdd:cd17637 248 GENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLTA-----DELIEFVGSRIARYKKPRYVVFVEA 322
|
250
....*....|.
gi 2792055509 245 LPKTRSGKIMR 255
Cdd:cd17637 323 LPKTADGSIDR 333
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
12-260 |
1.79e-17 |
|
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: 81.94 E-value: 1.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 12 DLSSVRLLGSVGEPIRAWRWYRLV-----FGSDKTPVVDTWWQTETGAAMI---SPLRGDRLQAG----IGdAPAAGISA 79
Cdd:cd05906 287 DLSSLRYLVNAGEAVVAKTIRRLLrllepYGLPPDAIRPAFGMTETCSGVIysrSFPTYDHSQALefvsLG-RPIPGVSM 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 80 KIVDDDGkDLEPSPDHGE-HVTGylvldkpwPAMLRGIWGDPERFKETywsrFAEQGWYFAGDGArYGSDGEIWVLGRID 158
Cdd:cd05906 366 RIVDDEG-QLLPEGEVGRlQVRG--------PVVTKGYYNNPEANAEA----FTEDGWFRTGDLG-FLDNGNLTITGRTK 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 159 DVMNISGHRISTAEVESAL-----VGHSGVAEAAVVGATDEhTGQAICAFVILKSHHAEMSheQMVDELRSEVAKEISpi 233
Cdd:cd05906 432 DTIIVNGVNYYSHEIEAAVeevpgVEPSFTAAFAVRDPGAE-TEELAIFFVPEYDLQDALS--ETLRAIRSVVSREVG-- 506
|
250 260 270
....*....|....*....|....*....|.
gi 2792055509 234 AKPReiHVVP----ELPKTRSGKIMRRLLRD 260
Cdd:cd05906 507 VSPA--YLIPlpkeEIPKTSLGKIQRSKLKA 535
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
64-268 |
3.02e-17 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 81.59 E-value: 3.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 64 RLQAGIGDAPAAGISAKIVDDDGKDlePSPDHGEHVTGYLVLDKPWPAMLRGIWGDPERFKETYwsrfaEQGWYFAGDGA 143
Cdd:PRK05857 338 KIEAGAVGRPYPGVDVYLAATDGIG--PTAPGAGPSASFGTLWIKSPANMLGYWNNPERTAEVL-----IDGWVNTGDLL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 144 RYGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKSHHAEMSHEQMVDELR 223
Cdd:PRK05857 411 ERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVASAELDESAARALKHTIA 490
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2792055509 224 SEVAKEISPIAKPREIHVVPELPKTRSGKIMRRLLRDVAEGRELG 268
Cdd:PRK05857 491 ARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASLAAAATADKAR 535
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
110-259 |
3.54e-17 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 81.18 E-value: 3.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 110 PAMLRGIWGDPERFKETywsrFAEQGWYFAGDGARYGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVV 189
Cdd:PLN02246 391 PQIMKGYLNDPEATANT----IDKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVV 466
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 190 GATDEHTGQAICAFVIlKSHHAEMSHeqmvDELRSEVAKEISPIAKPREIHVVPELPKTRSGKIMRRLLR 259
Cdd:PLN02246 467 PMKDEVAGEVPVAFVV-RSNGSEITE----DEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLR 531
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
73-258 |
5.11e-17 |
|
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: 80.41 E-value: 5.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 73 PAAGISAKIVDDDGKdlePSPdhgEHVTGYLVLDKPWPAmlRGIWGDP----ERFKEtywSRFAEQG--WYFAGDGARYG 146
Cdd:cd12116 296 PLANTQVYVLDAALR---PVP---PGVPGELYIGGDGVA--QGYLGRPaltaERFVP---DPFAGPGsrLYRTGDLVRRR 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 147 SDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQaICAFVILKSHHAemsheQMVDELRSEV 226
Cdd:cd12116 365 ADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRR-LVAYVVLKAGAA-----PDAAALRAHL 438
|
170 180 190
....*....|....*....|....*....|..
gi 2792055509 227 AKEISPIAKPREIHVVPELPKTRSGKIMRRLL 258
Cdd:cd12116 439 RATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
50-260 |
1.00e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 80.04 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 50 TETGA-AMISPLRGDRLQAGIGdAPAAGISAKIVDDDGKDlEPSPDhGEhvTGYLVLDKPwpAMLRGIWGDPERFKETYw 128
Cdd:PRK05605 371 TETSPiIVGNPMSDDRRPGYVG-VPFPDTEVRIVDPEDPD-ETMPD-GE--EGELLVRGP--QVFKGYWNRPEETAKSF- 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 129 srfaEQGWYFAGDGARYGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKS 208
Cdd:PRK05605 443 ----LDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEP 518
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2792055509 209 hHAEMSHEQMVDELRSEVAKeispIAKPREIHVVPELPKTRSGKIMRRLLRD 260
Cdd:PRK05605 519 -GAALDPEGLRAYCREHLTR----YKVPRRFYHVDELPRDQLGKVRRREVRE 565
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
137-258 |
1.23e-16 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 79.44 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 137 YFAGDGARYGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVIlkshhaeMSHE 216
Cdd:cd17656 364 YRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFV-------MEQE 436
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2792055509 217 QMVDELRSEVAKEISPIAKPREIHVVPELPKTRSGKIMRRLL 258
Cdd:cd17656 437 LNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
80-265 |
1.53e-16 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 79.26 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 80 KIVDDDGKDLEpspdHGEhvTGYLVLDKPWpaMLRGIWGDPERFKetywSRFAEQGWYFAGDGARYGSDGEIWVLGRIDD 159
Cdd:PRK10946 366 WVADADGNPLP----QGE--VGRLMTRGPY--TFRGYYKSPQHNA----SAFDANGFYCSGDLVSIDPDGYITVVGREKD 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 160 VMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKshhaemsheqmvDELRSEVAKE------ISPI 233
Cdd:PRK10946 434 QINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVK------------EPLKAVQLRRflreqgIAEF 501
|
170 180 190
....*....|....*....|....*....|..
gi 2792055509 234 AKPREIHVVPELPKTRSGKIMRRLLRDVAEGR 265
Cdd:PRK10946 502 KLPDRVECVDSLPLTAVGKVDKKQLRQWLASR 533
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
49-258 |
2.84e-16 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 78.63 E-value: 2.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 49 QTETGAAMISPLRGDRLQAGIGDAPAAGISAKIVDDDGKDLepspdhGEHVTGYLVLDKPWP-AMLRGIWGDPERFKETY 127
Cdd:PTZ00237 414 QTEIGITYLYCYGHINIPYNATGVPSIFIKPSILSEDGKEL------NVNEIGEVAFKLPMPpSFATTFYKNDEKFKQLF 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 128 wSRFaeQGWYFAGDGARYGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILK 207
Cdd:PTZ00237 488 -SKF--PGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLK 564
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2792055509 208 ----SHHAEMSHEQmvDELRSEVAKEISPIAKPREIHVVPELPKTRSGKIMRRLL 258
Cdd:PTZ00237 565 qdqsNQSIDLNKLK--NEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQII 617
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
80-260 |
3.39e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 78.02 E-value: 3.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 80 KIVDDDGKDLEPspdhGEHVTGYLVLDKPWPAMLrgiwGDPERFKETYwsrfAEQGWYFAGDGARYGSDGEIWVLGRIDD 159
Cdd:PRK08276 326 RILDEDGNELPP----GEIGTVYFEMDGYPFEYH----NDPEKTAAAR----NPHGWVTVGDVGYLDEDGYLYLTDRKSD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 160 vMNISGH-RISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKSHHAemSHEQMVDELRSEVAKEISPIAKPRE 238
Cdd:PRK08276 394 -MIISGGvNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGAD--AGDALAAELIAWLRGRLAHYKCPRS 470
|
170 180
....*....|....*....|..
gi 2792055509 239 IHVVPELPKTRSGKIMRRLLRD 260
Cdd:PRK08276 471 IDFEDELPRTPTGKLYKRRLRD 492
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
12-260 |
3.54e-16 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 78.20 E-value: 3.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 12 DLSSVRLLGSVGEP--IRAWRWyrLVFGSDKTPVVDTWWQTETGAAMISplrGDRLQA---GIGDAPAAGISAKIVDDDG 86
Cdd:PLN03052 469 DWSSIRCFGSTGEAssVDDYLW--LMSRAGYKPIIEYCGGTELGGGFVT---GSLLQPqafAAFSTPAMGCKLFILDDSG 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 87 KdlePSPDHgEHVTGYLVLDkpwpamlrgiwgdPERFKETYWSRFAE-QGWYFAG----DGA---RYG------SDGEIW 152
Cdd:PLN03052 544 N---PYPDD-APCTGELALF-------------PLMFGASSTLLNADhYKVYFKGmpvfNGKilrRHGdifertSGGYYR 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 153 VLGRIDDVMNISGHRISTAEVESAL-VGHSGVAEAAVVGATDEHTG-QAICAFVILKShhaEMSHEQMVDELR----SEV 226
Cdd:PLN03052 607 AHGRADDTMNLGGIKVSSVEIERVCnAADESVLETAAIGVPPPGGGpEQLVIAAVLKD---PPGSNPDLNELKkifnSAI 683
|
250 260 270
....*....|....*....|....*....|....
gi 2792055509 227 AKEISPIAKPREIHVVPELPKTRSGKIMRRLLRD 260
Cdd:PLN03052 684 QKKLNPLFKVSAVVIVPSFPRTASNKVMRRVLRQ 717
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
13-259 |
4.08e-16 |
|
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: 77.87 E-value: 4.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 13 LSSVRLLGSVGEPIRAWRWYRLVFGSDKTPVVDTWWQTETGAAM--ISPLRGDRLQAGIGdAPAAGISAKIVDDDGKDLE 90
Cdd:cd05922 230 LPSLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMtyLPPERILEKPGSIG-LAIPGGEFEILDDDGTPTP 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 91 PspdhGEhvTGYLVLDKPWPAMlrGIWGDPErfKETYWSRFAEQGWyfAGDGARYGSDGEIWVLGRIDDVMNISGHRIST 170
Cdd:cd05922 309 P----GE--PGEIVHRGPNVMK--GYWNDPP--YRRKEGRGGGVLH--TGDLARRDEDGFLFIVGRRDRMIKLFGNRISP 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 171 AEVESALVGHSGVAEAAVVGAtDEHTGQAICAFVILKShhaemshEQMVDELRSEVAKEISPIAKPREIHVVPELPKTRS 250
Cdd:cd05922 377 TEIEAAARSIGLIIEAAAVGL-PDPLGEKLALFVTAPD-------KIDPKDVLRSLAERLPPYKVPATVRVVDELPLTAS 448
|
....*....
gi 2792055509 251 GKIMRRLLR 259
Cdd:cd05922 449 GKVDYAALR 457
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
87-264 |
4.86e-16 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 77.75 E-value: 4.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 87 KDLEPSPDHGEhVTGYLVLDKPwpAMLRGIWGDPERFKETYwsrfaEQGWYFAGDGARYGSDGEIWVLGRIDDVMNISGH 166
Cdd:PLN03102 380 ETQESVPRDGK-TMGEIVIKGS--SIMKGYLKNPKATSEAF-----KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGE 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 167 RISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKShhAEMSHEQMVDELRS------EVAKEISP-IAKPREI 239
Cdd:PLN03102 452 NISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEK--GETTKEDRVDKLVTrerdliEYCRENLPhFMCPRKV 529
|
170 180
....*....|....*....|....*
gi 2792055509 240 HVVPELPKTRSGKIMRRLLRDVAEG 264
Cdd:PLN03102 530 VFLQELPKNGNGKILKPKLRDIAKG 554
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
135-255 |
5.63e-16 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 76.68 E-value: 5.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 135 GWYFAGDGARYGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQaICAFVILKShhaEMS 214
Cdd:cd17633 208 GWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGE-IAVALYSGD---KLT 283
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2792055509 215 HEQMVDELRSEVAK-EIspiakPREIHVVPELPKTRSGKIMR 255
Cdd:cd17633 284 YKQLKRFLKQKLSRyEI-----PKKIIFVDSLPYTSSGKIAR 320
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
50-259 |
6.48e-16 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 77.42 E-value: 6.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 50 TETGAAMISPLRGD-RLQAGIGdAPAAGISAKIVDDDGKDLEPSpdhgehVTGYL-VLDKPWPAMLRGIWGDPERFKETy 127
Cdd:PRK08008 322 TETIVGIIGDRPGDkRRWPSIG-RPGFCYEAEIRDDHNRPLPAG------EIGEIcIKGVPGKTIFKEYYLDPKATAKV- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 128 wsrFAEQGWYFAGDGARYGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILK 207
Cdd:PRK08008 394 ---LEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLN 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2792055509 208 ShHAEMSHEQMVDELRSEVAKeispIAKPREIHVVPELPKTRSGKIMRRLLR 259
Cdd:PRK08008 471 E-GETLSEEEFFAFCEQNMAK----FKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
140-258 |
6.51e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 77.34 E-value: 6.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 140 GDGARYGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKShHAEMSHEQMV 219
Cdd:PRK13383 401 GDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHP-GSGVDAAQLR 479
|
90 100 110
....*....|....*....|....*....|....*....
gi 2792055509 220 DELRSEVAKeispIAKPREIHVVPELPKTRSGKIMRRLL 258
Cdd:PRK13383 480 DYLKDRVSR----FEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
83-273 |
9.24e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 76.99 E-value: 9.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 83 DDDGKDLEPSPDHGEHVtgylvlDKPWPAMLRGIWGDPERFKEtywsRFAeQGWYFAGDGARYGSDGEIWVLGRIDDVMN 162
Cdd:PRK13388 339 DAHGALLNADEAIGELV------NTAGAGFFEGYYNNPEATAE----RMR-HGMYWSGDLAYRDADGWIYFAGRTADWMR 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 163 ISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKShHAEMSHEQMVDELRSEvaKEISPIAKPREIHVV 242
Cdd:PRK13388 408 VDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRD-GATFDPDAFAAFLAAQ--PDLGTKAWPRYVRIA 484
|
170 180 190
....*....|....*....|....*....|.
gi 2792055509 243 PELPKTRSGKIMRRLLRdvAEGRELGDTSTL 273
Cdd:PRK13388 485 ADLPSTATNKVLKRELI--AQGWATGDPVTL 513
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
135-262 |
1.67e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 76.14 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 135 GWYFAGDGARYGSDGEIWVLGRIDDVMnISG-HRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKShHAEM 213
Cdd:PRK08162 416 GWFHTGDLAVLHPDGYIKIKDRSKDII-ISGgENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKD-GASA 493
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2792055509 214 SHEQMVDELRSEVAkeisPIAKPREIhVVPELPKTRSGKIMRRLLRDVA 262
Cdd:PRK08162 494 TEEEIIAHCREHLA----GFKVPKAV-VFGELPKTSTGKIQKFVLREQA 537
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
36-260 |
2.71e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 75.97 E-value: 2.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 36 FGSDKTPVVDTWWQTETGAAMISPlrgdrlQAGIGdAPAAGISAKIVDDDgkdLEPSPdhgEHVTGYLVLDKPWPAmlRG 115
Cdd:PRK12467 3384 YGPTEAVVTVTLWKCGGDAVCEAP------YAPIG-RPVAGRSIYVLDGQ---LNPVP---VGVAGELYIGGVGLA--RG 3448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 116 IWGDP----ERFKETYWSRFAEQgWYFAGDGARYGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVgA 191
Cdd:PRK12467 3449 YHQRPsltaERFVADPFSGSGGR-LYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVL-A 3526
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2792055509 192 TDEHTGQAICAFVILKSHHAEMSheqmvDELRSEVAKEISPIAKPREIHVVPELPKTRSGKIMRRLLRD 260
Cdd:PRK12467 3527 RDGAGGKQLVAYVVPADPQGDWR-----ETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPD 3590
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
12-260 |
3.53e-15 |
|
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: 75.35 E-value: 3.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 12 DLSSVRLLGSVGEPIRA--------------WRW------YRL----VFGSdkTPVVDTWWQTETGAAMISPLRGDRLQA 67
Cdd:cd05931 269 DLSSWRVALNGAEPVRPatlrrfaeafapfgFRPeafrpsYGLaeatLFVS--GGPPGTGPVVLRVDRDALAGRAVAVAA 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 68 GIGDA--------PAAGISAKIVDDDGKDLEPSPDHGE-HVTGylvldkpwPAMLRGIWGDPERFKETYWSRFA--EQGW 136
Cdd:cd05931 347 DDPAArelvscgrPLPDQEVRIVDPETGRELPDGEVGEiWVRG--------PSVASGYWGRPEATAETFGALAAtdEGGW 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 137 YFAGD-GARYgsDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGV---AEAAVVGATDEHTGQAIcAFVILKSHHAE 212
Cdd:cd05931 419 LRTGDlGFLH--DGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHPAlrpGCVAAFSVPDDGEERLV-VVAEVERGADP 495
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2792055509 213 MSHEQMVDELRSEVAKEISpiAKPREIHVVP--ELPKTRSGKIMRRLLRD 260
Cdd:cd05931 496 ADLAAIAAAIRAAVAREHG--VAPADVVLVRpgSIPRTSSGKIQRRACRA 543
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
74-256 |
4.10e-15 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 74.92 E-value: 4.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 74 AAGISAKIVDDDGKDLEPSPDHGEHVTGylvldkpwPAMLRGIWGDPERFKETYwsrfaEQGWYFAGDGARYGSDGEIWV 153
Cdd:PRK05852 360 STGAQIRIVGSDGLPLPAGAVGEVWLRG--------TTVVRGYLGDPTITAANF-----TDGWLRTGDLGSLSAAGDLSI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 154 LGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAfVILKSHHAEMSHEQMVDELRSEVAkeisPI 233
Cdd:PRK05852 427 RGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAA-VIVPRESAPPTAEELVQFCRERLA----AF 501
|
170 180
....*....|....*....|...
gi 2792055509 234 AKPREIHVVPELPKTRSGKIMRR 256
Cdd:PRK05852 502 EIPASFQEASGLPHTAKGSLDRR 524
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
8-251 |
6.23e-15 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 73.49 E-value: 6.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 8 AFEHDLSSVRllgsvgEPIRAWRWYRLVfgsdktPVVDTWW--------QTE-TGAAMISPLRGDrlqaGIGDA--PAAG 76
Cdd:cd17636 108 DGLYDLSSLR------SSPAAPEWNDMA------TVDTSPWgrkpggygQTEvMGLATFAALGGG----AIGGAgrPSPL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 77 ISAKIVDDDGKDLepsPDhGEhvTGYLVLDKPwpAMLRGIWGDPERFKEtywsRFAEqGWYFAGDGARYGSDGEIWVLGR 156
Cdd:cd17636 172 VQVRILDEDGREV---PD-GE--VGEIVARGP--TVMAGYWNRPEVNAR----RTRG-GWHHTNDLGRREPDGSLSFVGP 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 157 IDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKShHAEMSHEQMVDELRSEVAKeispIAKP 236
Cdd:cd17636 239 KTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKP-GASVTEAELIEHCRARIAS----YKKP 313
|
250
....*....|....*
gi 2792055509 237 REIHVVPELPKTRSG 251
Cdd:cd17636 314 KSVEFADALPRTAGG 328
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
11-260 |
6.39e-15 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 74.47 E-value: 6.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 11 HDLSSVRLLGSVGEPIRA--WRWYRLVFGSDKtPVVDTWWQTETGAAMISplrGDRLQA---GIGDAPAAGISAKIVDDD 85
Cdd:PLN03051 233 LDWSKLRVFASTGEASAVddVLWLSSVRGYYK-PVIEYCGGTELASGYIS---STLLQPqapGAFSTASLGTRFVLLNDN 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 86 GkdlEPSPDhGEHVTGYLVLDKPwpamlrgIWGDPERF-----KETYWS---RFAEQGWYFA--GDGARYGSDGEIWVLG 155
Cdd:PLN03051 309 G---VPYPD-DQPCVGEVALAPP-------MLGASDRLlnadhDKVYYKgmpMYGSKGMPLRrhGDIMKRTPGGYFCVQG 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 156 RIDDVMNISGHRISTAEVESALV-GHSGVAEAAVVGATDEHTGQAICAFVI----LKSHHAEMSHEQMVDELRSEVAKEI 230
Cdd:PLN03051 378 RADDTMNLGGIKTSSVEIERACDrAVAGIAETAAVGVAPPDGGPELLVIFLvlgeEKKGFDQARPEALQKKFQEAIQTNL 457
|
250 260 270
....*....|....*....|....*....|
gi 2792055509 231 SPIAKPREIHVVPELPKTRSGKIMRRLLRD 260
Cdd:PLN03051 458 NPLFKVSRVKIVPELPRNASNKLLRRVLRD 487
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
66-267 |
1.02e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 73.92 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 66 QAGIGDA--PAAGISAKIVDDDGKDLEPSpDHGE-HVTGylvldkpwPAMLRGIWGDPERFKETYwsrfaEQGWYFAGDG 142
Cdd:PRK07470 336 DARIGTCgfERTGMEVQIQDDEGRELPPG-ETGEiCVIG--------PAVFAGYYNNPEANAKAF-----RDGWFRTGDL 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 143 ARYGSDGEIWVLGRIDDvMNISG-HRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAfVILKSHHAEMSHEQMVDE 221
Cdd:PRK07470 402 GHLDARGFLYITGRASD-MYISGgSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVA-VCVARDGAPVDEAELLAW 479
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2792055509 222 LRSEVAKeispIAKPREIHVVPELPKTRSGKIMRRLLRDVAEGREL 267
Cdd:PRK07470 480 LDGKVAR----YKLPKRFFFWDALPKSGYGKITKKMVREELEERGL 521
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
133-266 |
1.57e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 73.27 E-value: 1.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 133 EQGWYFAGDGARYGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAfVILKSHHAE 212
Cdd:PRK07638 359 ADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVA-IIKGSATKQ 437
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2792055509 213 msheqmvdELRSEVAKEISPIAKPREIHVVPELPKTRSGKIMRRLLRDVAEGRE 266
Cdd:PRK07638 438 --------QLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWIENQE 483
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
148-258 |
2.19e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 72.76 E-value: 2.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 148 DGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVIlkSHHAEMSheqmvDELRSEVA 227
Cdd:PRK08308 304 RGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVI--SHEEIDP-----VQLREWCI 376
|
90 100 110
....*....|....*....|....*....|.
gi 2792055509 228 KEISPIAKPREIHVVPELPKTRSGKIMRRLL 258
Cdd:PRK08308 377 QHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
73-256 |
2.25e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 72.72 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 73 PAAGISAKIVDDDGKDLEPSPD-----HGEHVT-GYLVLDKPWPAMlrgiwgdperfketywsrfAEQGWYFAGDGARYG 146
Cdd:PRK07768 365 PLPGLEVRVVDEDGQVLPPRGVgvielRGESVTpGYLTMDGFIPAQ-------------------DADGWLDTGDLGYLT 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 147 SDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVgATDEHTGQAICAF-VILKSHHAEmsHEQMVDELRSE 225
Cdd:PRK07768 426 EEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAV-AVRLDAGHSREGFaVAVESNAFE--DPAEVRRIRHQ 502
|
170 180 190
....*....|....*....|....*....|....*
gi 2792055509 226 VAKEISPI--AKPREIHVVP--ELPKTRSGKIMRR 256
Cdd:PRK07768 503 VAHEVVAEvgVRPRNVVVLGpgSIPKTPSGKLRRA 537
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
70-265 |
2.79e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 72.47 E-value: 2.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 70 GDAPA-AGISAKIVDDDGKDLEPSPDHGE-HVTGylvldkpwPAMLRGIWGDPERFKETywsrFAEQGWYFAGDGARYGS 147
Cdd:PRK06164 351 GGRPAsPEARVRARDPQDGALLPDGESGEiEIRA--------PSLMRGYLDNPDATARA----LTDDGYFRTGDLGYTRG 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 148 DGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATdeHTGQAIC-AFVILKShHAEMSHEQMVDELRSEV 226
Cdd:PRK06164 419 DGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGAT--RDGKTVPvAFVIPTD-GASPDEAGLMAACREAL 495
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2792055509 227 AkeisPIAKPREIHVVPELPKTRSG---KIMRRLLRDVAEGR 265
Cdd:PRK06164 496 A----GFKVPARVQVVEAFPVTESAngaKIQKHRLREMAQAR 533
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
110-255 |
3.24e-14 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 71.76 E-value: 3.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 110 PAMLRGIWGDPERFKETywsrFAEQGWYFAGDGARYGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVV 189
Cdd:cd17638 194 YNVMQGYLDDPEATAEA----IDADGWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVI 269
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2792055509 190 GATDEHTGQAICAFVILKSHHAeMSHEQMVDELRSEVAKeispIAKPREIHVVPELPKTRSGKIMR 255
Cdd:cd17638 270 GVPDERMGEVGKAFVVARPGVT-LTEEDVIAWCRERLAN----YKVPRFVRFLDELPRNASGKVMK 330
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
73-262 |
4.41e-14 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 71.98 E-value: 4.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 73 PAAGISAKIVDDDGKDLEPSPDHGehvtgyLVLDKPwPAMLRGIWGDPERFKETYwsrfaEQGWYFAGDGARYGSDGEIW 152
Cdd:cd05909 319 PLPGMEVKIVSVETHEEVPIGEGG------LLLVRG-PNVMLGYLNEPELTSFAF-----GDGWYDTGDIGKIDGEGFLT 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 153 VLGRIDDVMNISGHRISTAEVESALVGHSGV-AEAAVVGATDEHTGQAICAFVIlkshHAEMSHEQMVDELRsevAKEIS 231
Cdd:cd05909 387 ITGRLSRFAKIAGEMVSLEAIEDILSEILPEdNEVAVVSVPDGRKGEKIVLLTT----TTDTDPSSLNDILK---NAGIS 459
|
170 180 190
....*....|....*....|....*....|.
gi 2792055509 232 PIAKPREIHVVPELPKTRSGKIMRRLLRDVA 262
Cdd:cd05909 460 NLAKPSYIHQVEEIPLLGTGKPDYVTLKALA 490
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
135-259 |
4.52e-14 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 72.08 E-value: 4.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 135 GWYFAGDGARYGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKshHAEMS 214
Cdd:cd05915 389 GFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPR--GEKPT 466
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2792055509 215 HEQMVDELRSEVA--KEIspiakPREIHVVPELPKTRSGKIMRRLLR 259
Cdd:cd05915 467 PEELNEHLLKAGFakWQL-----PDAYVFAEEIPRTSAGKFLKRALR 508
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
15-259 |
6.06e-14 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 71.60 E-value: 6.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 15 SVRLLGSVGEPIRAWRWYRLV--FGSdkTPVVDTWWQTETGAAMISPLRGDRLQAGIGDA-PAAGIsaKIVDDDGKDLEP 91
Cdd:PRK06060 261 SLRCVVSAGEALELGLAERLMefFGG--IPILDGIGSTEVGQTFVSNRVDEWRLGTLGRVlPPYEI--RVVAPDGTTAGP 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 92 SPDHGEHVTGylvldkpwPAMLRGIWGDPErfketywSRFAEQGWYFAGDGARYGSDGEIWVLGRIDDVMNISGHRISTA 171
Cdd:PRK06060 337 GVEGDLWVRG--------PAIAKGYWNRPD-------SPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPR 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 172 EVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKShhAEMSHEQMVDELRSEVAKEISPIAKPREIHVVPELPKTRSG 251
Cdd:PRK06060 402 EVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATS--GATIDGSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNG 479
|
....*...
gi 2792055509 252 KIMRRLLR 259
Cdd:PRK06060 480 KLVRGALR 487
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
73-260 |
6.72e-14 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 71.27 E-value: 6.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 73 PAAGISAKIVDDDGKDLEPSpDHGE---HVTG-----YLvldkpwpamlrgiwGDPERFKETywsrfAEQGWYFAGDGAR 144
Cdd:PRK12406 329 AAPGAELRFVDEDGRPLPQG-EIGEiysRIAGnpdftYH--------------NKPEKRAEI-----DRGGFITSGDVGY 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 145 YGSDGEIWVLGRIDDvMNISGH-RISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKShHAEMSHEQMVDELR 223
Cdd:PRK12406 389 LDADGYLFLCDRKRD-MVISGGvNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQP-GATLDEADIRAQLK 466
|
170 180 190
....*....|....*....|....*....|....*..
gi 2792055509 224 SEVAKeispIAKPREIHVVPELPKTRSGKIMRRLLRD 260
Cdd:PRK12406 467 ARLAG----YKVPKHIEIMAELPREDSGKIFKRRLRD 499
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
123-258 |
8.46e-14 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 70.93 E-value: 8.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 123 FKETYWSRFaeqgwYFAGDGARYGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICA 202
Cdd:cd17644 339 FNSSESERL-----YKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVA 413
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2792055509 203 FVIlkshhAEMSHEQMVDELRSEVAKEISPIAKPREIHVVPELPKTRSGKIMRRLL 258
Cdd:cd17644 414 YIV-----PHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
42-260 |
9.33e-14 |
|
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: 70.80 E-value: 9.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 42 PVVDTWWQ----------TET--GAAMISPLRGDRLQAGigdAPAAGISAKIVDddgKDLEPSPdhgEHVTGYLVLDKPw 109
Cdd:cd17653 224 SLLDRWSPgrrlynaygpTECtiSSTMTELLPGQPVTIG---KPIPNSTCYILD---ADLQPVP---EGVVGEICISGV- 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 110 pAMLRGIWGDPERFKETYWSRFAEQGW--YFAGDGARYGSDGEIWVLGRIDDVMNISGHRISTAEVES-ALVGHSGVAEA 186
Cdd:cd17653 294 -QVARGYLGNPALTASKFVPDPFWPGSrmYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEvVLQSQPEVTQA 372
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2792055509 187 AVVgatdeHTGQAICAFVilkshhaeMSHEQMVDELRSEVAKEISPIAKPREIHVVPELPKTRSGKIMRRLLRD 260
Cdd:cd17653 373 AAI-----VVNGRLVAFV--------TPETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
30-258 |
1.39e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 70.96 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 30 RWYRLvfgSDKTPVVDTWWQTETGA-AMISPLRGDRLQAG---IGdAPAAGISAKIVDddgKDLEPSPDH--GE-HVTGy 102
Cdd:PRK12467 790 RVRAL---GPGARLINHYGPTETTVgVSTYELSDEERDFGnvpIG-QPLANLGLYILD---HYLNPVPVGvvGElYIGG- 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 103 lvldkpwPAMLRGIWGDP----ERFKEtywSRFAEQG--WYFAGDGARYGSDGEIWVLGRIDDVMNISGHRISTAEVESA 176
Cdd:PRK12467 862 -------AGLARGYHRRPaltaERFVP---DPFGADGgrLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEAR 931
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 177 LVGHSGVAEAAVVgATDEHTGQAICAFVILKSHHAEMSHEQMVDELRSEVAKEISPIAKPREIHVVPELPKTRSGKIMRR 256
Cdd:PRK12467 932 LLAQPGVREAVVL-AQPGDAGLQLVAYLVPAAVADGAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRK 1010
|
..
gi 2792055509 257 LL 258
Cdd:PRK12467 1011 AL 1012
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
35-258 |
2.77e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 69.99 E-value: 2.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 35 VFGSDKTPVVDTWWQTETGAAMIsplrgdRLQAGIGdAPAAGISAKIVDDDgkdLEPSPdhgEHVTGYLVLDKPWPAmlR 114
Cdd:PRK12316 4841 GYGPTETTVTVLLWKARDGDACG------AAYMPIG-TPLGNRSGYVLDGQ---LNPLP---VGVAGELYLGGEGVA--R 4905
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 115 GIWGDP----ERFKEtywSRFAEQG--WYFAGDGARYGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAV 188
Cdd:PRK12316 4906 GYLERPaltaERFVP---DPFGAPGgrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVV 4982
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2792055509 189 VgATDEHTGQAICAFVILKSHH---AEMSHEQMVDELRSEVAKEISPIAKPREIHVVPELPKTRSGKIMRRLL 258
Cdd:PRK12316 4983 I-AQEGAVGKQLVGYVVPQDPAladADEAQAELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKAL 5054
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
131-266 |
3.03e-13 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 69.25 E-value: 3.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 131 FAEQGWYFAGDGARYGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKshH 210
Cdd:PRK07445 320 LDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPK--D 397
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2792055509 211 AEMSheqmVDELRSEVAKEISPIAKPREIHVVPELPKTRSGKIMRRLLRDVAEGRE 266
Cdd:PRK07445 398 PSIS----LEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQIAVQRL 449
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
7-258 |
3.21e-13 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 69.81 E-value: 3.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 7 LAFEHDLSSVRLLGSVGEPIRAWRWYRLVFGSDKTPVVDTWWQTETGAAMISPLRGDRLQAGIGDAPAAGI----SAKIV 82
Cdd:PRK05691 2441 LAGQGEQLPVRMCITGGEALTGEHLQRIRQAFAPQLFFNAYGPTETVVMPLACLAPEQLEEGAASVPIGRVvgarVAYIL 2520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 83 DDDgkdLEPSPDHGehvTGYLVLDKPwpAMLRGIWGDP----ERFKEtywSRFAEQG--WYFAGDGARYGSDGEIWVLGR 156
Cdd:PRK05691 2521 DAD---LALVPQGA---TGELYVGGA--GLAQGYHDRPgltaERFVA---DPFAADGgrLYRTGDLVRLRADGLVEYVGR 2589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 157 IDDVMNISGHRISTAEVESALVGHSGVAEAAVVgATDEHTGQAICAFVILK-SHHAEMSHEQMVDELRSEVAKEISPIAK 235
Cdd:PRK05691 2590 IDHQVKIRGFRIELGEIESRLLEHPAVREAVVL-ALDTPSGKQLAGYLVSAvAGQDDEAQAALREALKAHLKQQLPDYMV 2668
|
250 260
....*....|....*....|...
gi 2792055509 236 PREIHVVPELPKTRSGKIMRRLL 258
Cdd:PRK05691 2669 PAHLILLDSLPLTANGKLDRRAL 2691
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
137-258 |
9.29e-13 |
|
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: 67.96 E-value: 9.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 137 YFAGDGARYGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKShhaEMSHE 216
Cdd:cd17645 325 YRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPE---EIPHE 401
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2792055509 217 qmvdELRSEVAKEISPIAKPREIHVVPELPKTRSGKIMRRLL 258
Cdd:cd17645 402 ----ELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
137-258 |
1.25e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 68.06 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 137 YFAGDGARYGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVgATDEHTGQAICAFVILKShhaemSHE 216
Cdd:PRK12316 2383 YRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVV-AQDGASGKQLVAYVVPDD-----AAE 2456
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2792055509 217 QMVDELRSEVAKEISPIAKPREIHVVPELPKTRSGKIMRRLL 258
Cdd:PRK12316 2457 DLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKAL 2498
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
81-259 |
2.21e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 66.96 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 81 IVDDDGKDLePSpdhGEHVTGYLVLDK-PWPAMlrgiwGDPERFKETywSRFAEQGWYFAGDGARYGSDGEIWVLGRiDD 159
Cdd:PRK13390 335 ICDDDGNEL-PA---GRIGTVYFERDRlPFRYL-----NDPEKTAAA--QHPAHPFWTTVGDLGSVDEDGYLYLADR-KS 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 160 VMNISGH-RISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKS--HHAEMSHEQMVDELRSEVAKeispIAKP 236
Cdd:PRK13390 403 FMIISGGvNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEgiRGSDELARELIDYTRSRIAH----YKAP 478
|
170 180
....*....|....*....|...
gi 2792055509 237 REIHVVPELPKTRSGKIMRRLLR 259
Cdd:PRK13390 479 RSVEFVDELPRTPTGKLVKGLLR 501
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
69-258 |
2.32e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 67.29 E-value: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 69 IGdAPAAGISAKIVDddgKDLEPSPdhgEHVTGYLVLDKPwpAMLRGIWGDP----ERFKEtywSRFAE-QGWYFAGDGA 143
Cdd:PRK12316 827 IG-RPIANLACYILD---ANLEPVP---VGVLGELYLAGR--GLARGYHGRPgltaERFVP---SPFVAgERMYRTGDLA 894
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 144 RYGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGAtdehTGQAICAFVILKSHHAEmsheqMVDELR 223
Cdd:PRK12316 895 RYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV----DGKQLVGYVVLESEGGD-----WREALK 965
|
170 180 190
....*....|....*....|....*....|....*
gi 2792055509 224 SEVAKEISPIAKPREIHVVPELPKTRSGKIMRRLL 258
Cdd:PRK12316 966 AHLAASLPEYMVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
76-260 |
2.36e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 66.65 E-value: 2.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 76 GISAKIVDDDGKDLepspdhgehvtgylvldkPWPA------MLRGIWGDPERFKETywSRFAEQGWYFAGDGARYGSDG 149
Cdd:PRK07008 364 GVDMKIVGDDGREL------------------PWDGkafgdlQVRGPWVIDRYFRGD--ASPLVDGWFPTGDVATIDADG 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 150 EIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGAT----DEHTgqaicAFVILKSHHAEMSHEQMVDELRSE 225
Cdd:PRK07008 424 FMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAhpkwDERP-----LLVVVKRPGAEVTREELLAFYEGK 498
|
170 180 190
....*....|....*....|....*....|....*.
gi 2792055509 226 VAK-EIspiakPREIHVVPELPKTRSGKIMRRLLRD 260
Cdd:PRK07008 499 VAKwWI-----PDDVVFVDAIPHTATGKLQKLKLRE 529
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
73-260 |
3.11e-12 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 66.31 E-value: 3.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 73 PAAGISAKIVDDDGKDLepsPDHGEhVTGYLvldkpwpaMLRGIWGDPERFKETYwSRFAEQGWYFAGDGARYGSDGEIW 152
Cdd:PRK06018 361 PPFGVEMKITDDAGKEL---PWDGK-TFGRL--------KVRGPAVAAAYYRVDG-EILDDDGFFDTGDVATIDAYGYMR 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 153 VLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKSHHaEMSHEQMVDELRSEVAKeisp 232
Cdd:PRK06018 428 ITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGE-TATREEILKYMDGKIAK---- 502
|
170 180
....*....|....*....|....*...
gi 2792055509 233 IAKPREIHVVPELPKTRSGKIMRRLLRD 260
Cdd:PRK06018 503 WWMPDDVAFVDAIPHTATGKILKTALRE 530
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
81-260 |
4.18e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 65.87 E-value: 4.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 81 IVDDDGKDLEPspdhGEHVTGYLVLDKPWPAMlrgiwGDPERFKEtywSRFAEQGWYFAGDGARYGSDGEIWVLGRIDDv 160
Cdd:PRK13391 340 ILDDDGAELPP----GEPGTIWFEGGRPFEYL-----NDPAKTAE---ARHPDGTWSTVGDIGYVDEDGYLYLTDRAAF- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 161 MNISGH-RISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILkshhAEMSH--EQMVDELRSEVAKEISPIAKPR 237
Cdd:PRK13391 407 MIISGGvNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQP----VDGVDpgPALAAELIAFCRQRLSRQKCPR 482
|
170 180
....*....|....*....|...
gi 2792055509 238 EIHVVPELPKTRSGKIMRRLLRD 260
Cdd:PRK13391 483 SIDFEDELPRLPTGKLYKRLLRD 505
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
136-260 |
4.78e-12 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 65.92 E-value: 4.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 136 WYFAGDGARYGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGAT-DEHTGQAICAFVILKSHHAEMS 214
Cdd:cd05937 339 YFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKvPGHDGRAGCAAITLEESSAVPT 418
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2792055509 215 HEQMvDELRSEVAKEISPIAKPREIHVVPELPKTRSGKIMRRLLRD 260
Cdd:cd05937 419 EFTK-SLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRD 463
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
110-259 |
2.87e-11 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 63.66 E-value: 2.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 110 PAMLRGIWGDPerfKETYWSRFAEqGWYFAGDGARYGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVV 189
Cdd:PLN02860 393 PHVMLGYWGQN---SETASVLSND-GWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVV 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 190 GATDEHTGQAICAFVILKSH----HAEMSHEQMVDELRSEV------AKEISPIAKPREIHVVPE-LPKTRSGKIMRRLL 258
Cdd:PLN02860 469 GVPDSRLTEMVVACVRLRDGwiwsDNEKENAKKNLTLSSETlrhhcrEKNLSRFKIPKLFVQWRKpFPLTTTGKIRRDEV 548
|
.
gi 2792055509 259 R 259
Cdd:PLN02860 549 R 549
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
137-257 |
4.48e-11 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 62.80 E-value: 4.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 137 YFAGDGARYGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQA------ICAFVilkshh 210
Cdd:cd17648 332 YKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQSriqkylVGYYL------ 405
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2792055509 211 aemSHEQMVDE--LRSEVAKEISPIAKPREIHVVPELPKTRSGKI-MRRL 257
Cdd:cd17648 406 ---PEPGHVPEsdLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLdVRAL 452
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
80-261 |
6.71e-11 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 62.22 E-value: 6.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 80 KIVDDDGKDLePSPDHGE-HVTGylvldkpwPAMLRGIWGDPERFKETYwsrFAEQGW--YFAGDGArYGSDGEIWVLGR 156
Cdd:PRK04813 330 LIIDEEGTKL-PDGEQGEiVISG--------PSVSKGYLNNPEKTAEAF---FTFDGQpaYHTGDAG-YLEDGLLFYQGR 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 157 IDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILKSHHAEmSHEQMVDELRSEVAKEISPIAKP 236
Cdd:PRK04813 397 IDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVPKEEDFE-REFELTKAIKKELKERLMEYMIP 475
|
170 180
....*....|....*....|....*.
gi 2792055509 237 REIHVVPELPKTRSGKIMR-RLLRDV 261
Cdd:PRK04813 476 RKFIYRDSLPLTPNGKIDRkALIEEV 501
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
14-258 |
8.99e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 62.49 E-value: 8.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 14 SSVRLLGSVGEPIRAWRWYRLV-----------FGSDKTPVVDTWWQTETGAAMISPlrgdrlqagIGdAPAAGISAKIV 82
Cdd:PRK05691 1388 TSLRRLFSGGEALPAELRNRVLqrlpqvqlhnrYGPTETAINVTHWQCQAEDGERSP---------IG-RPLGNVLCRVL 1457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 83 DDDgkdLEPSPdhgEHVTGYLVLDKPwpAMLRGIWGDP----ERFKEtywSRFAEQG--WYFAGDGARYGSDGEIWVLGR 156
Cdd:PRK05691 1458 DAE---LNLLP---PGVAGELCIGGA--GLARGYLGRPaltaERFVP---DPLGEDGarLYRTGDRARWNADGALEYLGR 1526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 157 IDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVilkshhAEMSHEQMVDELRSEVAKEISPIAKP 236
Cdd:PRK05691 1527 LDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGAQLVGYYT------GEAGQEAEAERLKAALAAELPEYMVP 1600
|
250 260
....*....|....*....|..
gi 2792055509 237 REIHVVPELPKTRSGKIMRRLL 258
Cdd:PRK05691 1601 AQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
73-265 |
1.26e-10 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 61.86 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 73 PAAGISAKIVD-DDGKDLEPspdhGEhvTGyLVLDKPwPAMLRGIWGDPERFKETYwSRFAEQGWYFAGDGARYGSDGEI 151
Cdd:PRK08633 965 PLPGVAVRIVDpETFEELPP----GE--DG-LILIGG-PQVMKGYLGDPEKTAEVI-KDIDGIGWYVTGDKGHLDEDGFL 1035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 152 WVLGRIDDVMNISGHRISTAEVESALVGHSGVAEA--AVVGATDEHTGQAICAFVilkshhaeMSHEQMVDELRSEVAK- 228
Cdd:PRK08633 1036 TITDRYSRFAKIGGEMVPLGAVEEELAKALGGEEVvfAVTAVPDEKKGEKLVVLH--------TCGAEDVEELKRAIKEs 1107
|
170 180 190
....*....|....*....|....*....|....*..
gi 2792055509 229 EISPIAKPREIHVVPELPKTRSGKIMRRLLRDVAEGR 265
Cdd:PRK08633 1108 GLPNLWKPSRYFKVEALPLLGSGKLDLKGLKELALAL 1144
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
42-256 |
1.38e-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: 61.46 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 42 PVVDTWWQTETGAAmISPLRGDRLQAGIGDAPAAGISAKIVDDdgkdlepspdhGEhvtgylVLDKPwPAMLRGIWGDPE 121
Cdd:cd05907 237 PVYEGYGLTETSAV-VTLNPPGDNRIGTVGKPLPGVEVRIADD-----------GE------ILVRG-PNVMLGYYKNPE 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 122 RFKETywsrFAEQGWYFAGDGARYGSDGEIWVLGRIDDVM-NISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAI 200
Cdd:cd05907 298 ATAEA----LDADGWLHTGDLGEIDEDGFLHITGRKKDLIiTSGGKNISPEPIENALKASPLISQAVVIGDGRPFLVALI 373
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2792055509 201 CAFVILKSHHAEM------------SHEQMVDELRSEVA---KEISPIAKPREIHVVPELP------KTRSGKIMRR 256
Cdd:cd05907 374 VPDPEALEAWAEEhgiaytdvaelaANPAVRAEIEAAVEaanARLSRYEQIKKFLLLPEPFtiengeLTPTLKLKRP 450
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
11-258 |
1.55e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 61.90 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 11 HDLSSVRLLGSVGEPIRAWRWYRLVFGSdktPVVDTWWQTETgaaMISPLRGDRLQAGIGDA----PAAGISAKIVDDDg 86
Cdd:PRK12316 3308 HRCTSLKRIVCGGEALPADLQQQVFAGL---PLYNLYGPTEA---TITVTHWQCVEEGKDAVpigrPIANRACYILDGS- 3380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 87 kdLEPSPdhgEHVTGYLVLDKPWPAmlRGIWGDPERFKETYW-SRFAEQG-WYFAGDGARYGSDGEIWVLGRIDDVMNIS 164
Cdd:PRK12316 3381 --LEPVP---VGALGELYLGGEGLA--RGYHNRPGLTAERFVpDPFVPGErLYRTGDLARYRADGVIEYIGRVDHQVKIR 3453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 165 GHRISTAEVESALVGHSGVAEAAVVGAtdehTGQAICAFVILKSHHAEMSheqmvDELRSEVAKEISPIAKPREIHVVPE 244
Cdd:PRK12316 3454 GFRIELGEIEARLLEHPWVREAVVLAV----DGRQLVAYVVPEDEAGDLR-----EALKAHLKASLPEYMVPAHLLFLER 3524
|
250
....*....|....
gi 2792055509 245 LPKTRSGKIMRRLL 258
Cdd:PRK12316 3525 MPLTPNGKLDRKAL 3538
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
114-258 |
1.55e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 61.72 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 114 RGIWGDPERFKETYWSR-FAEQG--WYFAGDGARYGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAvVG 190
Cdd:PRK05691 4078 RGYVGDPLRTALAFVPHpFGAPGerLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAA-VA 4156
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2792055509 191 ATDEHTGQAICAFviLKSHHAEMSHEQMVDELRSEVAKEISPIAKPREIHVVPELPKTRSGKIMRRLL 258
Cdd:PRK05691 4157 VQEGVNGKHLVGY--LVPHQTVLAQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
42-256 |
1.91e-10 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 60.88 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 42 PVVDTWWQTETgAAMISPLRGDRLQAG-IGdAPAAGISAKIVDDdgkdlepspdhGE-HVTGylvldkpwPAMLRGIWGD 119
Cdd:COG1022 373 PVLEGYGLTET-SPVITVNRPGDNRIGtVG-PPLPGVEVKIAED-----------GEiLVRG--------PNVMKGYYKN 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 120 PERFKETywsrFAEQGWYFAGDGARYGSDGEIWVLGRIDDVM-NISGHRISTAEVESALVGHSGVAEAAVVGAtdehtGQ 198
Cdd:COG1022 432 PEATAEA----FDADGWLHTGDIGELDEDGFLRITGRKKDLIvTSGGKNVAPQPIENALKASPLIEQAVVVGD-----GR 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 199 -AICAFVIL---------KSHH------AEMS-HEQMVDELRSEVA---KEISPIAKPREIHVVP--------ELpkTRS 250
Cdd:COG1022 503 pFLAALIVPdfealgewaEENGlpytsyAELAqDPEVRALIQEEVDranAGLSRAEQIKRFRLLPkeftiengEL--TPT 580
|
....*.
gi 2792055509 251 GKIMRR 256
Cdd:COG1022 581 LKLKRK 586
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
137-258 |
2.57e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 60.95 E-value: 2.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 137 YFAGDGARYGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVgATDEHTGQAICAFVILKSH---HAEM 213
Cdd:PRK12467 1956 YRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVI-AQDGANGKQLVAYVVPTDPglvDDDE 2034
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2792055509 214 SHEQMVDELRSEVAKEISPIAKPREIHVVPELPKTRSGKIMRRLL 258
Cdd:PRK12467 2035 AQVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKAL 2079
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
50-258 |
1.94e-09 |
|
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: 57.84 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 50 TETGAaMISPLRGDRLQAGIGDAPAAGISAKIVDDDgkdlePSPDHGE-HVTGylvldkpwPAMLRGIWGDPERFKETyw 128
Cdd:cd05914 268 TETAP-IISYSPPNRIRLGSAGKVIDGVEVRIDSPD-----PATGEGEiIVRG--------PNVMKGYYKNPEATAEA-- 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 129 srFAEQGWYFAGDGARYGSDGEIWVLGRIDDVMNI-SGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILK 207
Cdd:cd05914 332 --FDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNMPFVLESLVVVQEKKLVALAYIDPDFLD 409
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2792055509 208 SHHAEMSH--EQMVDELRSEVAKEISPIAKPREIHVVPE-LPKTRSGKIMRRLL 258
Cdd:cd05914 410 VKALKQRNiiDAIKWEVRDKVNQKVPNYKKISKVKIVKEeFEKTPKGKIKRFLY 463
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
129-260 |
6.73e-09 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 56.33 E-value: 6.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 129 SRFAEQGWYFAGDGARYGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVILkS 208
Cdd:PRK05620 424 DRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVL-A 502
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2792055509 209 HHAEMSHEqMVDELRSEVAKEISPIAKPREIHVVPELPKTRSGKI----MRRLLRD 260
Cdd:PRK05620 503 PGIEPTRE-TAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFdkkdLRQHLAD 557
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
137-258 |
2.90e-08 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 54.67 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 137 YFAGDGARYGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAA----VVGATDEHTGQA--ICAFVIlkshh 210
Cdd:PRK10252 839 YRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVthacVINQAAATGGDArqLVGYLV----- 913
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2792055509 211 AEMSHEQMVDELRSEVAKEISPIAKPREIHVVPELPKTRSGKIMRRLL 258
Cdd:PRK10252 914 SQSGLPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
133-266 |
3.04e-08 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 54.33 E-value: 3.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 133 EQGWYFAGDGARYGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFvilkSHHAE 212
Cdd:PRK08043 589 ERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASKGEALVLF----TTDSE 664
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2792055509 213 MSHEQMVDELRSEVAKEispIAKPREIHVVPELPKTRSGKIMRRLLRDVAEGRE 266
Cdd:PRK08043 665 LTREKLQQYAREHGVPE---LAVPRDIRYLKQLPLLGSGKPDFVTLKSMVDEPE 715
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
80-255 |
1.31e-07 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 52.31 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 80 KIVDDDGKDLepspdhGEHVTGylvldKPW---PAMLRGIWGDPERFKEtywsrFAEQGWYFAGDGArYGSDGEIWVLGR 156
Cdd:PRK09192 397 EIRNEAGMPL------PERVVG-----HICvrgPSLMSGYFRDEESQDV-----LAADGWLDTGDLG-YLLDGYLYITGR 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 157 IDDVMNISGHRI------STAEVESALvgHSGvaEAAVVgATDEHTGQAICAFVilkshHAEMSHEQMVDELRSEVAkei 230
Cdd:PRK09192 460 AKDLIIINGRNIwpqdieWIAEQEPEL--RSG--DAAAF-SIAQENGEKIVLLV-----QCRISDEERRGQLIHALA--- 526
|
170 180 190
....*....|....*....|....*....|....
gi 2792055509 231 spiAKPREIH-------VVP--ELPKTRSGKIMR 255
Cdd:PRK09192 527 ---ALVRSEFgveaaveLVPphSLPRTSSGKLSR 557
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
110-260 |
3.17e-07 |
|
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: 51.27 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 110 PAMLRGIWGDPERFKETywsrFAEQGWYFAGDGARYGSDGEIWVLGRIDDVMNIS-GHRISTAEVESALVGHSGVAEAAV 188
Cdd:cd17641 399 PGVFVGYYKNPEATAED----FDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSdGTRFSPQFIENKLKFSPYIAEAVV 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 189 VGATDEHTGQAICAFVILKSHHAE------------MSHEQMVDELRSEVAKEISPIAKPREIHVVPELPK--------- 247
Cdd:cd17641 475 LGAGRPYLTAFICIDYAIVGKWAEqrgiafttytdlASRPEVYELIRKEVEKVNASLPEAQRIRRFLLLYKeldaddgel 554
|
170
....*....|...
gi 2792055509 248 TRSGKIMRRLLRD 260
Cdd:cd17641 555 TRTRKVRRGVIAE 567
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
13-191 |
6.60e-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: 50.16 E-value: 6.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 13 LSSVRLLGSVGEPI--RAWRWYRLVfgsdKTPVVDTWWQTETGAAMISPLRGDRLQAGIGDApAAGISAKIvDDDGKDLE 90
Cdd:cd05932 274 LDQCRLAGCGSAPVppALLEWYRSL----GLNILEAYGMTENFAYSHLNYPGRDKIGTVGNA-GPGVEVRI-SEDGEILV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 91 PSPdhgehvtgylvldkpwpAMLRGIWGDPERFKETywsrFAEQGWYFAGDGARYGSDGEIWVLGRIDDVMNIS-GHRIS 169
Cdd:cd05932 348 RSP-----------------ALMMGYYKDPEATAEA----FTADGFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVA 406
|
170 180
....*....|....*....|..
gi 2792055509 170 TAEVESALVGHSGVAEAAVVGA 191
Cdd:cd05932 407 PAPIENKLAEHDRVEMVCVIGS 428
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
136-248 |
1.01e-06 |
|
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: 49.66 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 136 WYFAGDGARYGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDE-HTGQAICAFVILKShhaemS 214
Cdd:cd05940 324 WFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPgTDGRAGMAAIVLQP-----N 398
|
90 100 110
....*....|....*....|....*....|....
gi 2792055509 215 HEQMVDELRSEVAKEISPIAKPREIHVVPELPKT 248
Cdd:cd05940 399 EEFDLSALAAHLEKNLPGYARPLFLRLQPEMEIT 432
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
73-266 |
1.79e-06 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 49.02 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 73 PAAGISAKIVDDDGKDLEpspdhgEHVTGYLVLDKPwpAMLRGIWGDPERFKETywsrFAEQGWYFAGDGArYGSDGEIW 152
Cdd:cd05908 319 PIDETDIRICDEDNKILP------DGYIGHIQIRGK--NVTPGYYNNPEATAKV----FTDDGWLKTGDLG-FIRNGRLV 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 153 VLGRIDDVMNISGHRISTAEVESALVGHSGV--AEAAVVGATDEHTGQA-ICAFVIlkshhaemsHEQMVDELrSEVAKE 229
Cdd:cd05908 386 ITGREKDIIFVNGQNVYPHDIERIAEELEGVelGRVVACGVNNSNTRNEeIFCFIE---------HRKSEDDF-YPLGKK 455
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2792055509 230 ISPIAKPR---EIH-VVP--ELPKTRSGKIMRRLLRDVAEGRE 266
Cdd:cd05908 456 IKKHLNKRggwQINeVLPirRIPKTTSGKVKRYELAQRYQSGE 498
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
136-253 |
4.39e-06 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 47.47 E-value: 4.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 136 WYFAGDGARYgSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVaEAAVVGATDEhtgQAICAFVILKSHHAEMSH 215
Cdd:cd17654 340 MRATGDFVTV-KDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGV-ESCAVTLSDQ---QRLIAFIVGESSSSRIHK 414
|
90 100 110
....*....|....*....|....*....|....*...
gi 2792055509 216 EQMVDELrsevakeiSPIAKPREIHVVPELPKTRSGKI 253
Cdd:cd17654 415 ELQLTLL--------SSHAIPDTFVQIDKLPLTSHGKV 444
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
42-190 |
7.06e-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: 46.97 E-value: 7.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 42 PVVDTWWQTETGAaMISPLRGDRLQAGIGDAPAAGISAKIVDDDGKDLEPSPDHGehvtgyLVLDKPwPAMLRGIWGDPE 121
Cdd:cd17640 239 EVLNGYGLTETSP-VVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVLPPGEKG------IVWVRG-PQVMKGYYKNPE 310
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 122 RFKETywsrFAEQGWYFAGDGARYGSDGEIWVLGRIDDVMNIS-GHRISTAEVESALVGHSGVAEAAVVG 190
Cdd:cd17640 311 ATSKV----LDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIMVVG 376
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
115-253 |
8.90e-06 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 46.74 E-value: 8.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 115 GIWGDPERFKETYWSRFaeqgW-------YFAGDGARYGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAA 187
Cdd:cd17647 349 DHWNYLDKDNNEPWRQF----WlgprdrlYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENI 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 188 VVGATDEHTGQAICAFVILK------------SHHAEMSHEQMV----------DELRSEVAKEISPIAKPREIHVVPEL 245
Cdd:cd17647 425 TLVRRDKDEEPTLVSYIVPRfdkpddesfaqeDVPKEVSTDPIVkgligyrkliKDIREFLKKRLASYAIPSLIVVLDKL 504
|
....*...
gi 2792055509 246 PKTRSGKI 253
Cdd:cd17647 505 PLNPNGKV 512
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
133-266 |
1.24e-05 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 46.50 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 133 EQGWYFAGDGARYGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAIcafvILKSHHAE 212
Cdd:PRK06814 1008 ADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDARKGERI----ILLTTASD 1083
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2792055509 213 MSHEQMVDELRsevAKEISPIAKPREIHVVPELPKTRSGKI----MRRLLRDVAEGRE 266
Cdd:PRK06814 1084 ATRAAFLAHAK---AAGASELMVPAEIITIDEIPLLGTGKIdyvaVTKLAEEAAAKPE 1138
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
2-257 |
4.75e-05 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 44.37 E-value: 4.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 2 KWGRELAfEHDLSSVRLLGSVGEPIRAWRWYRLV-----FGSDKTPVVDTWWQTETGAAMISP-----LRGDRLQAGIGD 71
Cdd:PRK05851 261 KYARRVS-DVDLGALRVALNGGEPVDCDGFERFAtamapFGFDAGAAAPSYGLAESTCAVTVPvpgigLRVDEVTTDDGS 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 72 ---------APAAGISAKIVDDDGKDLEPSPDHGE-HVTGylvldkpwPAMLRGIWGDPErfketywsrFAEQGWYFAGD 141
Cdd:PRK05851 340 garrhavlgNPIPGMEVRISPGDGAAGVAGREIGEiEIRG--------ASMMSGYLGQAP---------IDPDDWFPTGD 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 142 GArYGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVG-ATDEhtGQAICAFVILkshhAEMSHEQMvD 220
Cdd:PRK05851 403 LG-YLVDGGLVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAvGTGE--GSARPGLVIA----AEFRGPDE-A 474
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2792055509 221 ELRSEVAKEISPiakprEIHVVP---------ELPKTRSGKiMRRL 257
Cdd:PRK05851 475 GARSEVVQRVAS-----ECGVVPsdvvfvapgSLPRTSSGK-LRRL 514
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
101-259 |
4.81e-05 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 44.72 E-value: 4.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 101 GYLVLDKPWPamlRG--IWGDP----------ERFKETYwsRFAEQG--WYFAGDGARYGSDGEIWVLGRIDDVMNIS-G 165
Cdd:PLN02387 492 GYLISDKPMP---RGeiVIGGPsvtlgyfknqEKTDEVY--KVDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQhG 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 166 HRISTAEVESALVGhSGVAEAAVVGATDEHTgqaICAFVILKSHHA--EMSHEQMVD-----------ELRSEVAKEISP 232
Cdd:PLN02387 567 EYVSLGKVEAALSV-SPYVDNIMVHADPFHS---YCVALVVPSQQAleKWAKKAGIDysnfaelcekeEAVKEVQQSLSK 642
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2792055509 233 IAK---------PREIHVVPELPKTRSG------KIMRRLLR 259
Cdd:PLN02387 643 AAKaarlekfeiPAKIKLLPEPWTPESGlvtaalKLKREQIR 684
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
156-259 |
5.78e-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: 44.34 E-value: 5.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 156 RIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGATDEHT-GQAICAFVilkshhAEMSHEQMVDELRSEVAKEISPIA 234
Cdd:cd05939 370 RTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVEVPGVeGRAGMAAI------VDPERKVDLDRFSAVLAKSLPPYA 443
|
90 100
....*....|....*....|....*
gi 2792055509 235 KPREIHVVPELPKTRSGKIMRRLLR 259
Cdd:cd05939 444 RPQFIRLLPEVDKTGTFKLQKTDLQ 468
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
110-259 |
2.41e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 42.85 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 110 PAMLRGIWGDPERFKETYWSRfAEQGWYFAGDGArYGSDGEIWVLGRIDDVMNISGHRI------STAEVESALVGHSGV 183
Cdd:PRK05691 405 PSIAHGYWRNPEASAKTFVEH-DGRTWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLypqdieKTVEREVEVVRKGRV 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 184 AEAAVVGATDEHTGQAIcafVILKSHHAEMSHEQMVDELRSEVAKEIspiakpREIHVV-----P-ELPKTRSGKIMRRL 257
Cdd:PRK05691 483 AAFAVNHQGEEGIGIAA---EISRSVQKILPPQALIKSIRQAVAEAC------QEAPSVvlllnPgALPKTSSGKLQRSA 553
|
..
gi 2792055509 258 LR 259
Cdd:PRK05691 554 CR 555
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
114-259 |
2.50e-04 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 42.42 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 114 RGIWGDPERFKETYWSRF--------------AEQGWYFAGDGARYgSDGEIWVLGRIDDVMNISG-----HRI-STAEV 173
Cdd:PRK12476 441 RGYWGRPEETERTFGAKLqsrlaegshadgaaDDGTWLRTGDLGVY-LDGELYITGRIADLIVIDGrnhypQDIeATVAE 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 174 ESALVGHSGVAEAAVVGatDEHTGQAICAFVILKSHHAEMSheQMVDELRSEVAKEISpiAKPREIHVVPE--LPKTRSG 251
Cdd:PRK12476 520 ASPMVRRGYVTAFTVPA--EDNERLVIVAERAAGTSRADPA--PAIDAIRAAVSRRHG--LAVADVRLVPAgaIPRTTSG 593
|
....*...
gi 2792055509 252 KIMRRLLR 259
Cdd:PRK12476 594 KLARRACR 601
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
50-256 |
9.37e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 40.31 E-value: 9.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 50 TETGAAMISplrgdrlqAGIGDAPAAgisaKIVDDDGKdLEPSPD-------HGEHVTgylvldkpwpamlRGIWGDPER 122
Cdd:PRK05850 364 TGGGTPLVS--------YGSPRSPTV----RIVDPDTC-IECPAGtvgeiwvHGDNVA-------------AGYWQKPEE 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 123 FKETYWSRFA-------EQGWYFAGDGArYGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSG--VAEAAVvgaTD 193
Cdd:PRK05850 418 TERTFGATLVdpspgtpEGPWLRTGDLG-FISEGELFIVGRIKDLLIVDGRNHYPDDIEATIQEITGgrVAAISV---PD 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 194 EHTGQAICAFVILKSHHAEMSHEQMVDELRSEVakeISPIAKPREIHV-----VP--ELPKTRSGKIMRR 256
Cdd:PRK05850 494 DGTEKLVAIIELKKRGDSDEEAMDRLRTVKREV---TSAISKSHGLSVadlvlVApgSIPITTSGKIRRA 560
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
11-192 |
1.32e-03 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 39.75 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 11 HDLSSVRLLGSVGEPIRAW---RWYRLVfgSDKTPVVDTWWQTEtgAAMISPLRGDRLQAGIGDAPA-----------AG 76
Cdd:cd05910 196 ITLPSLRRVLSAGAPVPIAlaaRLRKML--SDEAEILTPYGATE--ALPVSSIGSRELLATTTAATSggagtcvgrpiPG 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 77 ISAKIVD-DDGKDLEPSPDH-------GE-HVTGYLV----LDKPWPAMLRGIWGDPERFketywsrfaeqgWYFAGDGA 143
Cdd:cd05910 272 VRVRIIEiDDEPIAEWDDTLelprgeiGEiTVTGPTVtptyVNRPVATALAKIDDNSEGF------------WHRMGDLG 339
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2792055509 144 RYGSDGEIWVLGRIDDVMNISGHRISTAEVESALVGHSGVAEAAVVGAT 192
Cdd:cd05910 340 YLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVG 388
|
|
| PRK09188 |
PRK09188 |
serine/threonine protein kinase; Provisional |
147-262 |
1.85e-03 |
|
serine/threonine protein kinase; Provisional
Pssm-ID: 236400 [Multi-domain] Cd Length: 365 Bit Score: 39.36 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 147 SDGEiwvlGRIDDVMNiSGHRIStaeveSALVGHSGVAEAAVVGATDEHTGQAICAFVilkshhaEMSHEQMVDELRSEV 226
Cdd:PRK09188 229 SDGE----GTGDRIDN-EAPAIQ-----AALKSDPAVSDVAIALFSLPAKGVGLYAFV-------EAELPADEKSLRARL 291
|
90 100 110
....*....|....*....|....*....|....*.
gi 2792055509 227 AKEISPIAkPREIHVVPELPKTRSGKIMRRLLRDVA 262
Cdd:PRK09188 292 AGAKPPKP-PEHIQPVAALPRDADGTVRDDILRLIA 326
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
133-260 |
4.27e-03 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 38.31 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792055509 133 EQGWYFAGDGARYgSDGEIWVLGRIDDvMNIS-GHRISTAEVESALVGHSGVAEAAVVGATDEHTGQAICAFVilkshha 211
Cdd:PRK09029 330 DEGWFATRDRGEW-QNGELTILGRLDN-LFFSgGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVV------- 400
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2792055509 212 EMSHEQMVDELRSEVAKEISPIAKPREIHVVPELPKTRSGKIMRRLLRD 260
Cdd:PRK09029 401 ESDSEAAVVNLAEWLQDKLARFQQPVAYYLLPPELKNGGIKISRQALKE 449
|
|
| |
