|
Name |
Accession |
Description |
Interval |
E-value |
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1-290 |
0e+00 |
|
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: 569.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 1 MTGPLLLGVPTILNEGGFTAENTYDIIERLGVTSLAGSPTAFRLLMAAGPESAARVKGRLRVASSAGEPLNPEVIRWFDA 80
Cdd:cd05973 148 ITGPLALGHPTILLEGGFSVESTWRVIERLGVTNLAGSPTAYRLLMAAGAEVPARPKGRLRRVSSAGEPLTPEVIRWFDA 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 81 CLGAPIHDHYGQTELGMVVNNHHGLEHPVRQGSAGYAMPGYRIAVLDEAGKEVGPNEPGVLAIDIDNSPLLWFTGYYKKD 160
Cdd:cd05973 228 ALGVPIHDHYGQTELGMVLANHHALEHPVHAGSAGRAMPGWRVAVLDDDGDELGPGEPGRLAIDIANSPLMWFRGYQLPD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 161 TPSISGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILAP 240
Cdd:cd05973 308 TPAIDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRG 387
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 492822008 241 GFEGTPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRK 290
Cdd:cd05973 388 GHEGTPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
2-290 |
3.36e-156 |
|
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: 442.93 E-value: 3.36e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 2 TGPLLLGVPTILNEG-GFTAENTYDIIERLGVTSLAGSPTAFRLLMAAGPESaaRVKGRLRVASSAGEPLNPEVIRWFDA 80
Cdd:cd05972 142 FGPWLLGATVFVYEGpRFDAERILELLERYGVTSFCGPPTAYRMLIKQDLSS--YKFSHLRLVVSAGEPLNPEVIEWWRA 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 81 CLGAPIHDHYGQTELGMVVNNHHGLehPVRQGSAGYAMPGYRIAVLDEAGKEVGPNEPGVLAIDI-DNSPLLWFTGYYKK 159
Cdd:cd05972 220 ATGLPIRDGYGQTETGLTVGNFPDM--PVKPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKLpPPGLFLGYVGDPEK 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 160 DTPSISGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILA 239
Cdd:cd05972 298 TEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLT 377
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 492822008 240 PGFEGTPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRK 290
Cdd:cd05972 378 SGYEPSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
3-292 |
7.84e-125 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 367.90 E-value: 7.84e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 3 GPLLLGVPTILNEGGFT---AENTYDIIERLGVTSLAGSPTAFRLLMAAGPESAARVK-GRLRVASSAGEPLNPEVIRWF 78
Cdd:COG0365 247 GPLLNGATVVLYEGRPDfpdPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDlSSLRLLGSAGEPLNPEVWEWW 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 79 DACLGAPIHDHYGQTELGM-VVNNHHGLehPVRQGSAGYAMPGYRIAVLDEAGKEVGPNEPGVLAIDidnSPLL-WFTGY 156
Cdd:COG0365 327 YEAVGVPIVDGWGQTETGGiFISNLPGL--PVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIK---GPWPgMFRGY 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 157 YK-----KDTP-SISGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTE 230
Cdd:COG0365 402 WNdperyRETYfGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQ 481
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492822008 231 IVKAFVILAPGFEGTPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRKAE 292
Cdd:COG0365 482 VVKAFVVLKPGVEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIA 543
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
1-293 |
4.85e-102 |
|
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: 305.58 E-value: 4.85e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 1 MTGPLLLGVPTILNEGGFTAENTYDIIERLGVTSLAGSPTAFRLLMAAGPESAARVK-GRLRVASSAGEPLNPEVIRWFD 79
Cdd:cd05969 149 IWAPWLNGVTNVVYEGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKEGDELARKYDlSSLRFIHSVGEPLNPEAIRWGM 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 80 ACLGAPIHDHYGQTELG-MVVNNHHGLehPVRQGSAGYAMPGYRIAVLDEAGKEVGPNEPGVLAIDIDNSPLlwFTGY-- 156
Cdd:cd05969 229 EVFGVPIHDTWWQTETGsIMIANYPCM--PIKPGSMGKPLPGVKAAVVDENGNELPPGTKGILALKPGWPSM--FRGIwn 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 157 ----YKKdtpSISGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIV 232
Cdd:cd05969 305 deerYKN---SFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEII 381
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492822008 233 KAFVILAPGFEGTPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRKAEV 293
Cdd:cd05969 382 KAFISLKEGFEPSDELKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLKAKEL 442
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
3-292 |
6.79e-99 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 301.43 E-value: 6.79e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 3 GPLLLGVPTILNEGGFTAENTYDIIERLGVTSLAGSPTAFRLLMAAGPESAARVK-GRLRVASSAGEPLNPEVIRWFDAC 81
Cdd:PRK04319 267 APWLNGATNVIDGGRFSPERWYRILEDYKVTVWYTAPTAIRMLMGAGDDLVKKYDlSSLRHILSVGEPLNPEVVRWGMKV 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 82 LGAPIHDHYGQTELG-MVVNNHHGLEhpVRQGSAGYAMPGYRIAVLDEAGKEVGPNEPGVLAIDIDnspllW---FTGY- 156
Cdd:PRK04319 347 FGLPIHDNWWMTETGgIMIANYPAMD--IKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIKKG-----WpsmMRGIw 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 157 -----YKKdtpSISGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEI 231
Cdd:PRK04319 420 nnpekYES---YFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEI 496
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492822008 232 VKAFVILAPGFEGTPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRKAE 292
Cdd:PRK04319 497 IKAFVALRPGYEPSEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLKAWE 557
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
5-289 |
2.09e-87 |
|
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: 268.15 E-value: 2.09e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 5 LLLGVPTILNEG-GFTAENTYDIIERLGVTSLAGSPTAFRLlMAAGPESAARVKGRLRVASSAGEPLNPEVIRWFDACLG 83
Cdd:cd05971 154 LYFGVPVLAHRMtKFDPKAALDLMSRYGVTTAFLPPTALKM-MRQQGEQLKHAQVKLRAIATGGESLGEELLGWAREQFG 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 84 APIHDHYGQTELGMVVNNHHGLeHPVRQGSAGYAMPGYRIAVLDEAGKEVGPNEPGVLAIDIDNSplLWFTGYYKKDTPS 163
Cdd:cd05971 233 VEVNEFYGQTECNLVIGNCSAL-FPIKPGSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVELPDP--VAFLGYWNNPSAT 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 164 ---ISGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILAP 240
Cdd:cd05971 310 ekkMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNP 389
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 492822008 241 GFEGTPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLR 289
Cdd:cd05971 390 GETPSDALAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
1-298 |
6.71e-86 |
|
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: 264.37 E-value: 6.71e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 1 MTGPLLLGVPTILNEGgFTAENTYDIIERLGVTSLAGSPTAFRLLMAAgPESAARVKGRLRVASSAGEPLNPEVIRWFDA 80
Cdd:COG0318 160 LLAPLLAGATLVLLPR-FDPERVLELIERERVTVLFGVPTMLARLLRH-PEFARYDLSSLRLVVSGGAPLPPELLERFEE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 81 CLGAPIHDHYGQTELGMVVNNHHGLEHPVRQGSAGYAMPGYRIAVLDEAGKEVGPNEPGVLAIdidNSPLLwFTGYYKKD 160
Cdd:COG0318 238 RFGVRIVEGYGLTETSPVVTVNPEDPGERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVV---RGPNV-MKGYWNDP 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 161 ---TPSISGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVI 237
Cdd:COG0318 314 eatAEAFRDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVV 393
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492822008 238 LAPGFEGTpelAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRKAEVEKQQQ 298
Cdd:COG0318 394 LRPGAELD---AEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYAAGALE 451
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
1-284 |
9.11e-80 |
|
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: 245.27 E-value: 9.11e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 1 MTGPLLLGVPTILnEGGFTAENTYDIIERLGVTSLAGSPTAFRLLMAAgPESAARVKGRLRVASSAGEPLNPEVIRWFDA 80
Cdd:cd04433 59 LLGALLAGGTVVL-LPKFDPEAALELIEREKVTILLGVPTLLARLLKA-PESAGYDLSSLRALVSGGAPLPPELLERFEE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 81 CLGAPIHDHYGQTELGMVVNNHHGLEHPVRQGSAGYAMPGYRIAVLDEAGKEVGPNEPGVLAIdidNSPLLwFTGYYKKD 160
Cdd:cd04433 137 APGIKLVNGYGLTETGGTVATGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVV---RGPSV-MKGYWNNP 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 161 ---TPSISGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVI 237
Cdd:cd04433 213 eatAAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVV 292
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 492822008 238 LAPGFegtPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQ 284
Cdd:cd04433 293 LRPGA---DLDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
18-289 |
3.44e-79 |
|
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: 249.72 E-value: 3.44e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 18 FTAENTYDIIERLGVTSLAGSPTAFRLLMAagpESAARVK-GRLRVASSAGEPLNPEVIRWFDACLGAPIHDHYGQTELG 96
Cdd:cd05970 263 FDPKALLEKLSKYGVTTFCAPPTIYRFLIR---EDLSRYDlSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETT 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 97 MVVNNHHGLEhpVRQGSAGYAMPGYRIAVLDEAGKEVGPNEPGVLAIDIDNS-PLLWFTGYYK---KDTPSISGGYYRTG 172
Cdd:cd05970 340 LTIATFPWME--PKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSKGkPVGLFGGYYKdaeKTAEVWHDGYYHTG 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 173 DTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILAPGFEGTPELAEEL 252
Cdd:cd05970 418 DAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEELKKEL 497
|
250 260 270
....*....|....*....|....*....|....*..
gi 492822008 253 ALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLR 289
Cdd:cd05970 498 QDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIR 534
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
32-292 |
6.06e-79 |
|
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: 248.92 E-value: 6.06e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 32 VTSLAGSPTAFRLLMAagpESAARVK-GRLRVASSAGEPLNPEVIRWFDACLGAPIHDHYGQTELGMVVNNHHGLEhpVR 110
Cdd:cd05928 267 ITTFCGAPTVYRMLVQ---QDLSSYKfPSLQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGLICANFKGMK--IK 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 111 QGSAGYAMPGYRIAVLDEAGKEVGPNEPGVLAIDID-NSPLLWFTGYY---KKDTPSISGGYYRTGDTVEFEPDGSISFI 186
Cdd:cd05928 342 PGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKpIRPFGLFSGYVdnpEKTAATIRGDFYLTGDRGIMDEDGYFWFM 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 187 GRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILAPGFEG-TPE-LAEELALHVKKQLSAHA 264
Cdd:cd05928 422 GRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLShDPEqLTKELQQHVKSVTAPYK 501
|
250 260
....*....|....*....|....*...
gi 492822008 265 YPRQIDFVAELPKTPSGKIQRFLLRKAE 292
Cdd:cd05928 502 YPRKVEFVQELPKTVTGKIQRNELRDKE 529
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
3-290 |
2.85e-78 |
|
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: 249.02 E-value: 2.85e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 3 GPLLLGVPTILNEGGFT---AENTYDIIERLGVTSLAGSPTAFRLLMAAGPESaarVKGR----LRVASSAGEPLNPEVI 75
Cdd:cd05966 294 GPLANGATTVMFEGTPTypdPGRYWDIVEKHKVTIFYTAPTAIRALMKFGDEW---VKKHdlssLRVLGSVGEPINPEAW 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 76 RWFDACLG---APIHDHYGQTELGMVVNNHHGLEHPVRQGSAGYAMPGYRIAVLDEAGKEVGPNEPGVLAID-------- 144
Cdd:cd05966 371 MWYYEVIGkerCPIVDTWWQTETGGIMITPLPGATPLKPGSATRPFFGIEPAILDEEGNEVEGEVEGYLVIKrpwpgmar 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 145 -IDNSPLLWFTGYYKKDtpsisGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGV 223
Cdd:cd05966 451 tIYGDHERYEDTYFSKF-----PGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGR 525
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492822008 224 PDPQRTEIVKAFVILAPGFEGTPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRK 290
Cdd:cd05966 526 PHDIKGEAIYAFVTLKDGEEPSDELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRK 592
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
3-297 |
5.80e-76 |
|
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: 243.69 E-value: 5.80e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 3 GPLLLGVPTILNEGGFTAENT---YDIIERLGVTSLAGSPTAFRLLMAAGPESAARVKGR-LRVASSAGEPLNPEVIRWF 78
Cdd:TIGR02188 300 GPLANGATTVMFEGVPTYPDPgrfWEIIEKHKVTIFYTAPTAIRALMRLGDEWVKKHDLSsLRLLGSVGEPINPEAWMWY 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 79 DACLG---APIHDHYGQTELGMVVNNHHGLEHPVRQGSAGYAMPGYRIAVLDEAGKEV-GPNEPGVLAID---------I 145
Cdd:TIGR02188 380 YKVVGkerCPIVDTWWQTETGGIMITPLPGATPTKPGSATLPFFGIEPAVVDEEGNPVeGPGEGGYLVIKqpwpgmlrtI 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 146 DNSPLLWFTGYYKKdTPsisgGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPD 225
Cdd:TIGR02188 460 YGDHERFVDTYFSP-FP----GYYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPD 534
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492822008 226 PQRTEIVKAFVILAPGFEGTPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRK-AEVEKQQ 297
Cdd:TIGR02188 535 DIKGQAIYAFVTLKDGYEPDDELRKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRRLLRKiAAGEAEI 607
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
1-289 |
2.46e-75 |
|
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: 238.81 E-value: 2.46e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 1 MTGPLLLGVPTILNEGGFTAENTYDIIERLGVTSLAGSPTAFRLLMAAgPESAARVKGRLRVASSAGEPLNPEVIRWFDA 80
Cdd:cd05959 224 LTFPLSVGATTVLMPERPTPAAVFKRIRRYRPTVFFGVPTLYAAMLAA-PNLPSRDLSSLRLCVSAGEALPAEVGERWKA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 81 CLGAPIHDHYGQTELGMV-VNNhhgLEHPVRQGSAGYAMPGYRIAVLDEAGKEVGPNEPGVLAIDIDNS-PLLWftGYYK 158
Cdd:cd05959 303 RFGLDILDGIGSTEMLHIfLSN---RPGRVRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSaTMYW--NNRD 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 159 KDTPSISGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVIL 238
Cdd:cd05959 378 KTRDTFQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVL 457
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 492822008 239 APGFEGTPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLR 289
Cdd:cd05959 458 RPGYEDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
12-292 |
2.27e-74 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 234.38 E-value: 2.27e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 12 ILNEGGFTAENTYDIIERLGVTSLAGSPTAFRLLMAagpESAARVKGRLRVASSAGEPLNPEVIRWFDACLGAPIHDHYG 91
Cdd:cd05974 157 LFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQ---QDLASFDVKLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYG 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 92 QTELGMVVNNHHGleHPVRQGSAGYAMPGYRIAVLDEAGkevGPNEPGVLAIDI-DNSPLLWFTGYY---KKDTPSISGG 167
Cdd:cd05974 234 QTETTALVGNSPG--QPVKAGSMGRPLPGYRVALLDPDG---APATEGEVALDLgDTRPVGLMKGYAgdpDKTAHAMRGG 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 168 YYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILAPGFEGTPE 247
Cdd:cd05974 309 YYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPE 388
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 492822008 248 LAEELALHVKKQLSAHAYPRQIDFvAELPKTPSGKIQRFLLRKAE 292
Cdd:cd05974 389 TALEIFRFSRERLAPYKRIRRLEF-AELPKTISGKIRRVELRRRE 432
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
4-289 |
4.27e-73 |
|
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: 231.21 E-value: 4.27e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 4 PLLLGVPTILNEGGfTAENTYDIIERLGVTSLAGSPTAFRLlMAAGPESAARVKGRLRVASSAGEPLNPEVIRWFDACLG 83
Cdd:cd05958 161 PFGVGASGVLLEEA-TPDLLLSAIARYKPTVLFTAPTAYRA-MLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATG 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 84 APIHDHYGQTE-LGMVVNNHHGlehPVRQGSAGYAMPGYRIAVLDEAGKEVGPNEPGVLAIdidNSPllwfTGYYKKDTP 162
Cdd:cd05958 239 IPIIDGIGSTEmFHIFISARPG---DARPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAV---RGP----TGCRYLADK 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 163 S----ISGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVIL 238
Cdd:cd05958 309 RqrtyVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVL 388
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 492822008 239 APGFEGTPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLR 289
Cdd:cd05958 389 RPGVIPGPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
3-290 |
2.01e-67 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 221.55 E-value: 2.01e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 3 GPLLLGVPTILNEGGFTAENT---YDIIERLGVTSLAGSPTAFRLLMAAGPESaarVKGR----LRVASSAGEPLNPEVI 75
Cdd:PRK00174 308 GPLANGATTLMFEGVPNYPDPgrfWEVIDKHKVTIFYTAPTAIRALMKEGDEH---PKKYdlssLRLLGSVGEPINPEAW 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 76 RWFDACLGA---PIHDHYGQTELG-MVVNNHHGLeHPVRQGSAGYAMPGYRIAVLDEAGKEVGPNEPGVLAID------- 144
Cdd:PRK00174 385 EWYYKVVGGercPIVDTWWQTETGgIMITPLPGA-TPLKPGSATRPLPGIQPAVVDEEGNPLEGGEGGNLVIKdpwpgmm 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 145 --IDNSPLLWFTGYYKKDtpsisGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVG 222
Cdd:PRK00174 464 rtIYGDHERFVKTYFSTF-----KGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVG 538
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492822008 223 VPDPQRTEIVKAFVILAPGFEGTPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRK 290
Cdd:PRK00174 539 RPDDIKGQGIYAFVTLKGGEEPSDELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRK 606
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
3-290 |
4.71e-66 |
|
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: 217.57 E-value: 4.71e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 3 GPLLLGVPTILNEGGFTAenTYD------IIERLGVTSLAGSPTAFRLLMAAGPEsAARVK----GRLRVASSAGEPLNP 72
Cdd:cd05967 293 GPLLHGATTVLYEGKPVG--TPDpgafwrVIEKYQVNALFTAPTAIRAIRKEDPD-GKYIKkydlSSLRTLFLAGERLDP 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 73 EVIRWFDACLGAPIHDHYGQTELG-MVVNNHHGLE-HPVRQGSAGYAMPGYRIAVLDEAGKEVGPNEPGVLAIDIdnsPL 150
Cdd:cd05967 370 PTLEWAENTLGVPVIDHWWQTETGwPITANPVGLEpLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKL---PL 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 151 -------LWFT-GYYKKDTPSISGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVG 222
Cdd:cd05967 447 ppgclltLWKNdERFKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVG 526
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492822008 223 VPDPQRTEIVKAFVILAPGFEGTPE-LAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRK 290
Cdd:cd05967 527 VRDELKGQVPLGLVVLKEGVKITAEeLEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRK 595
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
1-289 |
4.84e-65 |
|
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: 210.40 E-value: 4.84e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 1 MTGPLLLGVPTILNEGGFTAENTYDIIERLGVTSLAGSPTAFRLLMAAGPESAARVKGrLRVASSAGEPLNPEVIRWFDA 80
Cdd:cd05919 152 LWFPLAVGASAVLNPGWPTAERVLATLARFRPTVLYGVPTFYANLLDSCAGSPDALRS-LRLCVSAGEALPRGLGERWME 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 81 CLGAPIHDHYGQTELGMV-VNNHHGlehPVRQGSAGYAMPGYRIAVLDEAGKEVGPNEPGVLAIdidNSPLLwFTGYYK- 158
Cdd:cd05919 231 HFGGPILDGIGATEVGHIfLSNRPG---AWRLGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLV---RGPSA-AVGYWNn 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 159 --KDTPSISGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFV 236
Cdd:cd05919 304 peKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFV 383
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 492822008 237 ILAPGFEGTPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLR 289
Cdd:cd05919 384 VLKSPAAPQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
3-283 |
1.27e-62 |
|
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: 207.81 E-value: 1.27e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 3 GPLLLGVPTILNEG---GFTAENTYDIIERLGVTSLAGSPTAFRLLMAAGPESAARV-KGRLRVASSAGEPLNPEVIRWF 78
Cdd:cd17634 295 GPLACGATTLLYEGvpnWPTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIEGTdRSSLRILGSVGEPINPEAYEWY 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 79 DACLGA---PIHDHYGQTELG-MVVNNHHGLEhPVRQGSAGYAMPGYRIAVLDEAGKEVGPNEPGVLAIDIDNSP----L 150
Cdd:cd17634 375 WKKIGKekcPVVDTWWQTETGgFMITPLPGAI-ELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPWPGqtrtL 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 151 LWFTGYYKKDTPSISGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTE 230
Cdd:cd17634 454 FGDHERFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQ 533
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 492822008 231 IVKAFVILAPGFEGTPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKI 283
Cdd:cd17634 534 APYAYVVLNHGVEPSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
1-291 |
2.42e-62 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 205.07 E-value: 2.42e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 1 MTGPLLLGVPTILNEGGFTAENTYDIIERLGVTSLAGSPTAFRLLMAAgPESAARVKGRLRVASSAGEPLNPEVIRWFDA 80
Cdd:TIGR02262 222 LTFPMSVGATTVLMGERPTPDAVFDRLRRHQPTIFYGVPTLYAAMLAD-PNLPSEDQVRLRLCTSAGEALPAEVGQRWQA 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 81 CLGAPIHDHYGQTELGMVVNNHhgLEHPVRQGSAGYAMPGYRIAVLDEAGKEVGPNEPGVLAIDIDNSPllwfTGYY--- 157
Cdd:TIGR02262 301 RFGVDIVDGIGSTEMLHIFLSN--LPGDVRYGTSGKPVPGYRLRLVGDGGQDVADGEPGELLISGPSSA----TMYWnnr 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 158 KKDTPSISGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVI 237
Cdd:TIGR02262 375 AKSRDTFQGEWTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVV 454
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 492822008 238 LAPGFEGtpeLAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRKA 291
Cdd:TIGR02262 455 LRPGQTA---LETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQRFKLREG 505
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
1-289 |
2.43e-62 |
|
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: 203.95 E-value: 2.43e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 1 MTGPLLLGVPTILnEGGFTAENTYDIIERLGVTSLAGSPTAFRLLMAAgPESAARVKGRLRVASSAGEPLNPEVIRWFDA 80
Cdd:cd05936 187 LLLPLALGATIVL-IPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLNA-PEFKKRDFSSLRLCISGGAPLPVEVAERFEE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 81 CLGAPIHDHYGQTELGMVVNNHHgLEHPVRQGSAGYAMPGYRIAVLDEAGKEVGPNEPGVLAIDIDNSpllwFTGYYKK- 159
Cdd:cd05936 265 LTGVPIVEGYGLTETSPVVAVNP-LDGPRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQV----MKGYWNRp 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 160 -DTP-SISGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVI 237
Cdd:cd05936 340 eETAeAFVDGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVV 419
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 492822008 238 LAPgfeGTPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLR 289
Cdd:cd05936 420 LKE---GASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
4-289 |
5.58e-61 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 201.95 E-value: 5.58e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 4 PLLLGVPTILNeGGFTAENTYDIIERLGVTSLAGSPTAFRLLMAAgPESAARVKGRLRVASSAGEPLNPEVIRWFDACLG 83
Cdd:PRK06187 229 ALMAGAKQVIP-RRFDPENLLDLIETERVTFFFAVPTIWQMLLKA-PRAYFVDFSSLRLVIYGGAALPPALLREFKEKFG 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 84 APIHDHYGQTELG--MVVN--NHHGLEHPVRQGSAGYAMPGYRIAVLDEAGKEVGPN--EPGVLAIdidNSPllWFT-GY 156
Cdd:PRK06187 307 IDLVQGYGMTETSpvVSVLppEDQLPGQWTKRRSAGRPLPGVEARIVDDDGDELPPDggEVGEIIV---RGP--WLMqGY 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 157 YK--KDTPS-ISGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVK 233
Cdd:PRK06187 382 WNrpEATAEtIDGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPV 461
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 492822008 234 AFVILAPGFEGTpelAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLR 289
Cdd:PRK06187 462 AVVVLKPGATLD---AKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLR 514
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
5-285 |
5.78e-60 |
|
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: 197.06 E-value: 5.78e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 5 LLLGVPTILnEGGFTAENTYDIIERLGVTSLAGSPTAFRLLMAAgPESAARVKGRLRVASSAGEPLNPEVIRWFDAcLGA 84
Cdd:cd17631 162 LLRGGTVVI-LRKFDPETVLDLIERHRVTSFFLVPTMIQALLQH-PRFATTDLSSLRAVIYGGAPMPERLLRALQA-RGV 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 85 PIHDHYGQTELGMVVNNHHGLEHPVRQGSAGYAMPGYRIAVLDEAGKEVGPNEPGVLAIdidNSPLLwFTGYYKK--DTP 162
Cdd:cd17631 239 KFVQGYGMTETSPGVTFLSPEDHRRKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVV---RGPHV-MAGYWNRpeATA 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 163 -SISGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILAPg 241
Cdd:cd17631 315 aAFRDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRP- 393
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 492822008 242 feGTPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQR 285
Cdd:cd17631 394 --GAELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
18-289 |
7.90e-57 |
|
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: 188.65 E-value: 7.90e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 18 FTAENTYDIIERLGVTSLAGSPTAFRLLMAAgPESAARVKGRLRVASSAGEPlnPEVIRWFDACLGAPIHDHYGQTELGM 97
Cdd:cd05934 157 FSASRFWSDVRRYGATVTNYLGAMLSYLLAQ-PPSPDDRAHRLRAAYGAPNP--PELHEEFEERFGVRLLEGYGMTETIV 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 98 VVNNHHGleHPVRQGSAGYAMPGYRIAVLDEAGKEVGPNEPGVLAIDIDNSPLLwFTGYYKKDTPSI---SGGYYRTGDT 174
Cdd:cd05934 234 GVIGPRD--EPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIRGLRGWGF-FKGYYNMPEATAeamRNGWFHTGDL 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 175 VEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILAPGFEGTPelaEELAL 254
Cdd:cd05934 311 GYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDP---EELFA 387
|
250 260 270
....*....|....*....|....*....|....*
gi 492822008 255 HVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLR 289
Cdd:cd05934 388 FCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
3-291 |
3.25e-53 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 183.61 E-value: 3.25e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 3 GPLLLGVPTILNEGGFTAENT---YDIIERLGVTSLAGSPTAFRLLMAAGPESAARVK-GRLRVASSAGEPLNPEVIRWF 78
Cdd:PRK10524 296 APLLAGMATIMYEGLPTRPDAgiwWRIVEKYKVNRMFSAPTAIRVLKKQDPALLRKHDlSSLRALFLAGEPLDEPTASWI 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 79 DACLGAPIHDHYGQTELGM-VVNNHHGLE-HPVRQGSAGYAMPGYRIAVLDEA-GKEVGPNEPGVLAIDidnSPL----- 150
Cdd:PRK10524 376 SEALGVPVIDNYWQTETGWpILAIARGVEdRPTRLGSPGVPMYGYNVKLLNEVtGEPCGPNEKGVLVIE---GPLppgcm 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 151 --LW-----FTGYYKKdtpSISGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGV 223
Cdd:PRK10524 453 qtVWgdddrFVKTYWS---LFGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGV 529
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492822008 224 PDPQRTEIVKAFVIL-----APGFEGTPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKiqrfLLRKA 291
Cdd:PRK10524 530 KDALKGQVAVAFVVPkdsdsLADREARLALEKEIMALVDSQLGAVARPARVWFVSALPKTRSGK----LLRRA 598
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
3-290 |
1.86e-49 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 173.93 E-value: 1.86e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 3 GPLLLGVPTILNEGGFT---AENTYDIIERLGVTSLAGSPTAFRLLMAAGPESAAR-VKGRLRVASSAGEPLNPEVIRWF 78
Cdd:PLN02654 338 GPMLNGATVLVFEGAPNypdSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRhSRKSLRVLGSVGEPINPSAWRWF 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 79 DACLG---APIHDHYGQTELGMVVNNHHGLEHPVRQGSAGYAMPGYRIAVLDEAGKEVGPNEPGVLAIDiDNSPLLWFTG 155
Cdd:PLN02654 418 FNVVGdsrCPISDTWWQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGKEIEGECSGYLCVK-KSWPGAFRTL 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 156 YYKKDTPSIS-----GGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTE 230
Cdd:PLN02654 497 YGDHERYETTyfkpfAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQ 576
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 231 IVKAFVILAPGFEGTPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRK 290
Cdd:PLN02654 577 GIYAFVTLVEGVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRK 636
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
5-298 |
2.24e-47 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 165.46 E-value: 2.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 5 LLLGVPTILNEGgFTAENTYDIIERLGVTSLAGSPTAFRLLMAAGPEsaarVKGR-----LRVASSAGEPLNPEV----I 75
Cdd:PRK08276 209 LALGGTVVVMEK-FDAEEALALIERYRVTHSQLVPTMFVRMLKLPEE----VRARydvssLRVAIHAAAPCPVEVkramI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 76 RWFdaclGAPIHDHYGQTELGM--VVNNHHGLEHPvrqGSAGYAMPGyRIAVLDEAGKEVGPNEPGVLAIDIDNSPllwF 153
Cdd:PRK08276 284 DWW----GPIIHEYYASSEGGGvtVITSEDWLAHP---GSVGKAVLG-EVRILDEDGNELPPGEIGTVYFEMDGYP---F 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 154 TgyYKKD---TPSI--SGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQR 228
Cdd:PRK08276 353 E--YHNDpekTAAArnPHGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEM 430
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 229 TEIVKAFVILAPGFEGTPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRKAEVEKQQQ 298
Cdd:PRK08276 431 GERVKAVVQPADGADAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDRYWEGRQR 500
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
25-285 |
2.53e-47 |
|
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: 164.24 E-value: 2.53e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 25 DIIERLGVTSLAGSPTAFRLLMAAGPESAARvkgRLRVASSAGEPLNPEVIR-WFDACLGAPIHDHYGQTELGMVVNNHH 103
Cdd:cd05930 178 DLLAEEGITVLHLTPSLLRLLLQELELAALP---SLRLVLVGGEALPPDLVRrWRELLPGARLVNLYGPTEATVDATYYR 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 104 GLEHPVRQGSA--GYAMPGYRIAVLDEAGKEVGPNEPGVLAIdidNSPLLwFTGYYKK---------DTPSISGG-YYRT 171
Cdd:cd05930 255 VPPDDEEDGRVpiGRPIPNTRVYVLDENLRPVPPGVPGELYI---GGAGL-ARGYLNRpeltaerfvPNPFGPGErMYRT 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 172 GDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILAPGFEGTpelAEE 251
Cdd:cd05930 331 GDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELD---EEE 407
|
250 260 270
....*....|....*....|....*....|....
gi 492822008 252 LALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQR 285
Cdd:cd05930 408 LRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDR 441
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
1-291 |
6.46e-47 |
|
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: 166.13 E-value: 6.46e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 1 MTGP------LLLGVPTILNEG--GF-TAENTYDIIERLGVTSLAGSPTAFRLLMAAGPESAARV-KGRLRVASSAGEPL 70
Cdd:cd05968 290 MMGPwlifggLILGATMVLYDGapDHpKADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHdLSSLRVLGSTGEPW 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 71 NPEVIRWFDACLGA---PIHDHYGQTEL--GMVVNNhhgLEHPVRQGSAGYAMPGYRIAVLDEAGKEVGPNEpGVLAIDi 145
Cdd:cd05968 370 NPEPWNWLFETVGKgrnPIINYSGGTEIsgGILGNV---LIKPIKPSSFNGPVPGMKADVLDESGKPARPEV-GELVLL- 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 146 dnSPLLWFTGYYKKDTPSISGGYYRT-------GDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEA 218
Cdd:cd05968 445 --APWPGMTRGFWRDEDRYLETYWSRfdnvwvhGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLES 522
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492822008 219 AVVGVPDPQRTEIVKAFVILAPGFEGTPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRKA 291
Cdd:cd05968 523 AAIGVPHPVKGEAIVCFVVLKPGVTPTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAA 595
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
1-290 |
7.65e-47 |
|
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: 162.94 E-value: 7.65e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 1 MTGPLLLGVPTILNEGgFTAENTYDIIERLGVTSLAGSPTAFRLLMAAgPESAARVKGRLRVASSAGEPLNPEVIRWFDA 80
Cdd:cd05903 153 FTLPLLLGAPVVLQDI-WDPDKALALMREHGVTFMMGATPFLTDLLNA-VEEAGEPLSRLRTFVCGGATVPRSLARRAAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 81 CLGAPIHDHYGQTELGMVVNNHHGLEHPVRQGSAGYAMPGYRIAVLDEAGKEVGPNEPGVLAIdidNSPLLwFTGYYKK- 159
Cdd:cd05903 231 LLGAKVCSAYGSTECPGAVTSITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEGELLS---RGPSV-FLGYLDRp 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 160 DTPS--ISGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVI 237
Cdd:cd05903 307 DLTAdaAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVV 386
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 492822008 238 LAPGfeGTPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRK 290
Cdd:cd05903 387 TKSG--ALLTFDELVAYLDRQGVAKQYWPERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
11-289 |
1.12e-46 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 164.55 E-value: 1.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 11 TILNEGGFTAENTYDIIERLGVTSLAGSPTAFRLLMAAGPESAARVKGR-LRVASSAGEPLNPEVIRWFDACLGAPIHDH 89
Cdd:PRK13382 264 TIVTRRRFDPEATLDLIDRHRATGLAVVPVMFDRIMDLPAEVRNRYSGRsLRFAAASGSRMRPDVVIAFMDQFGDVIYNN 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 90 YGQTELGMV-VNNHHGLE-HPvrqGSAGYAMPGYRIAVLDEAGKEVGPNEPGvlAIDIDNSPLlwFTGYYKKDTPSISGG 167
Cdd:PRK13382 344 YNATEAGMIaTATPADLRaAP---DTAGRPAEGTEIRILDQDFREVPTGEVG--TIFVRNDTQ--FDGYTSGSTKDFHDG 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 168 YYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILAPGFEGTPe 247
Cdd:PRK13382 417 FMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATP- 495
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 492822008 248 laEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLR 289
Cdd:PRK13382 496 --ETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQ 535
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
5-289 |
3.12e-46 |
|
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: 161.78 E-value: 3.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 5 LLLGVPTILNEGgFTAENTYDIIERLGVTSLAGSPTAF-RLLMAAGPESAARVKGRLRVASSAGEPLNPEVIRWFDACLG 83
Cdd:cd05929 191 LFMGGTLVLMEK-FDPEEFLRLIERYRVTFAQFVPTMFvRLLKLPEAVRNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGG 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 84 APIHDHYGQTE-LGM-VVNNHHGLEHPvrqGSAGYAMPGyRIAVLDEAGKEVGPNEPGvlAIDIDNSPLLWFTGYYKKDT 161
Cdd:cd05929 270 PIIWEYYGGTEgQGLtIINGEEWLTHP---GSVGRAVLG-KVHILDEDGNEVPPGEIG--EVYFANGPGFEYTNDPEKTA 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 162 PSISGGYYRT-GDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILAP 240
Cdd:cd05929 344 AARNEGGWSTlGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAP 423
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 492822008 241 GFEGTPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLR 289
Cdd:cd05929 424 GADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
9-289 |
3.61e-45 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 160.15 E-value: 3.61e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 9 VPTILNEG------GFTAENTYDIIERLGVTSLAGSPTAFRLLMAAgPESAARVKGRLRVASSAGEPLNP----EVIRWF 78
Cdd:PRK06188 227 LPTLLRGGtvivlaKFDPAEVLRAIEEQRITATFLVPTMIYALLDH-PDLRTRDLSSLETVYYGASPMSPvrlaEAIERF 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 79 daclgAPIH-DHYGQTELGMVVN----NHHGLEHPVRQGSAGYAMPGYRIAVLDEAGKEVGPNEPGVLAIdidNSPLLwF 153
Cdd:PRK06188 306 -----GPIFaQYYGQTEAPMVITylrkRDHDPDDPKRLTSCGRPTPGLRVALLDEDGREVAQGEVGEICV---RGPLV-M 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 154 TGYYKK---DTPSISGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTE 230
Cdd:PRK06188 377 DGYWNRpeeTAEAFRDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGE 456
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 492822008 231 IVKAFVILAPGFEGTPelaEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLR 289
Cdd:PRK06188 457 AVTAVVVLRPGAAVDA---AELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALR 512
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
5-290 |
1.14e-44 |
|
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: 158.24 E-value: 1.14e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 5 LLLGVPTILNEGG-------FTAENTYDIIERLGVTSLAGSPTAFRLLMAAGPESAARVKGRLRVASSAGEPLNPEVIRW 77
Cdd:cd05926 205 LVASLLSTLAAGGsvvlpprFSASTFWPDVRDYNATWYTAVPTIHQILLNRPEPNPESPPPKLRFIRSCSASLPPAVLEA 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 78 FDACLGAPIHDHYGQTELG--MVVNNhhgLEHPVRQ-GSAGYAMpGYRIAVLDEAGKEVGPNEPGVLAIDIDNSPLlwft 154
Cdd:cd05926 285 LEATFGAPVLEAYGMTEAAhqMTSNP---LPPGPRKpGSVGKPV-GVEVRILDEDGEILPPGVVGEICLRGPNVTR---- 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 155 GYYkkDTPSIS------GGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQR 228
Cdd:cd05926 357 GYL--NNPEANaeaafkDGWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKY 434
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492822008 229 TEIVKAFVILApgfEGTPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRK 290
Cdd:cd05926 435 GEEVAAAVVLR---EGASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
2-290 |
1.89e-44 |
|
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: 156.68 E-value: 1.89e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 2 TGPLLLGVPTILnEGGFTAENTYDIIERLGVTSLAGSPTAF-RLL-----MAAGPESAARV-KGRLRVASSAGEPLNPEV 74
Cdd:cd05941 150 LCPLFAGASVEF-LPKFDPKEVAISRLMPSITVFMGVPTIYtRLLqyyeaHFTDPQFARAAaAERLRLMVSGSAALPVPT 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 75 IRWFDACLGAPIHDHYGQTELGMVVNNhhGLEHPVRQGSAGYAMPGYRIAVLDEAGKEVGP-NEPGVLAIdidNSPLLwF 153
Cdd:cd05941 229 LEEWEAITGHTLLERYGMTEIGMALSN--PLDGERRPGTVGMPLPGVQARIVDEETGEPLPrGEVGEIQV---RGPSV-F 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 154 TGYYKK--DTPS--ISGGYYRTGDTVEFEPDGSISFIGR-ADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQR 228
Cdd:cd05941 303 KEYWNKpeATKEefTDDGWFKTGDLGVVDEDGYYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDW 382
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492822008 229 TEIVKAFVILAPGfeGTPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRK 290
Cdd:cd05941 383 GERVVAVVVLRAG--AAALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
4-289 |
4.89e-43 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 154.83 E-value: 4.89e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 4 PLLLGVPTILNEGgFTAENTYDIIERLGVTSLAGSpTAFRLLMAAGPESAARVKGRLRVASSAGEPLNPEVIRWFDACLG 83
Cdd:PRK13295 260 PVMLGATAVLQDI-WDPARAAELIRTEGVTFTMAS-TPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAALG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 84 APIHDHYGQTELGMVVNNHHGLEHPVRQGSAGYAMPGYRIAVLDEAGKEVGPNEPGVLAIdidNSPLLwFTGYYKKdtPS 163
Cdd:PRK13295 338 AKIVSAWGMTENGAVTLTKLDDPDERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQV---RGCSN-FGGYLKR--PQ 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 164 ISG----GYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILA 239
Cdd:PRK13295 412 LNGtdadGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPR 491
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 492822008 240 PGFEGT-PELAEEL-ALHVKKQLsahaYPRQIDFVAELPKTPSGKIQRFLLR 289
Cdd:PRK13295 492 PGQSLDfEEMVEFLkAQKVAKQY----IPERLVVRDALPRTPSGKIQKFRLR 539
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
1-193 |
2.17e-42 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 150.54 E-value: 2.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 1 MTGPLLLGVPTILNEGG--FTAENTYDIIERLGVTSLAGSPTAFRLLMAAGPESAARvKGRLRVASSAGEPLNPEVIRWF 78
Cdd:pfam00501 219 LLGPLLAGATVVLPPGFpaLDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRAL-LSSLRLVLSGGAPLPPELARRF 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 79 DACLGAPIHDHYGQTELGMVVNNH-HGLEHPVRQGSAGYAMPGYRIAVLDEA-GKEVGPNEPGVLAIDidnSPLLwFTGY 156
Cdd:pfam00501 298 RELFGGALVNGYGLTETTGVVTTPlPLDEDLRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVR---GPGV-MKGY 373
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 492822008 157 YKKdtPS------ISGGYYRTGDTVEFEPDGSISFIGRADDVI 193
Cdd:pfam00501 374 LND--PEltaeafDEDGWYRTGDLGRRDEDGYLEIVGRKKDQI 414
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
18-292 |
4.36e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 152.00 E-value: 4.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 18 FTAENTYDIIERLGVTSLAGSPTAFRLLMAAGPESAARVK-GRLRVASSAGEPLNPEVIRWFDACLGAPIHDHYGQTELG 96
Cdd:PRK07788 282 FDPEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKYDtSSLKIIFVSGSALSPELATRALEAFGPVLYNLYGSTEVA 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 97 M--VVNNHHGLEHPvrqGSAGYAMPGYRIAVLDEAGKEVGPNEPGvlAIDIDNSplLWFTGYYKKDTPSISGGYYRTGDT 174
Cdd:PRK07788 362 FatIATPEDLAEAP---GTVGRPPKGVTVKILDENGNEVPRGVVG--RIFVGNG--FPFEGYTDGRDKQIIDGLLSSGDV 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 175 VEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILAPgfeGTPELAEELAL 254
Cdd:PRK07788 435 GYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAP---GAALDEDAIKD 511
|
250 260 270
....*....|....*....|....*....|....*...
gi 492822008 255 HVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRKAE 292
Cdd:PRK07788 512 YVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREMD 549
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
22-294 |
2.22e-41 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 151.26 E-value: 2.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 22 NTYDIIERLGVTSLAGSPTAFRLLMAAGPEsaARVKGRLRVASSAGEPLNPEVIRWFDACLGAPIHDHYGQTElGMVVNN 101
Cdd:PRK07529 299 NFWKIVERYRINFLSGVPTVYAALLQVPVD--GHDISSLRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTE-ATCVSS 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 102 HHGLEHPVRQGSAGYAMPG--YRIAVLDEAG---KEVGPNEPGVLAIDIDNSpllwFTGYYKKDT---PSISGGYYRTGD 173
Cdd:PRK07529 376 VNPPDGERRIGSVGLRLPYqrVRVVILDDAGrylRDCAVDEVGVLCIAGPNV----FSGYLEAAHnkgLWLEDGWLNTGD 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 174 TVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILAPGFEGTPelaEELA 253
Cdd:PRK07529 452 LGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATE---AELL 528
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 492822008 254 LHVKKQLSAH-AYPRQIDFVAELPKTPSGKIQRFLLRKAEVE 294
Cdd:PRK07529 529 AFARDHIAERaAVPKHVRILDALPKTAVGKIFKPALRRDAIR 570
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
5-284 |
2.63e-41 |
|
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: 148.90 E-value: 2.63e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 5 LLLGVPTILnEGGFTAENTYDIIERLGVTSLAGSPTafrlLMAAGPESAARVKGRL---RVASSAGEPLNPEVIRWFDAC 81
Cdd:cd05911 211 LLNGATVII-MPKFDSELFLDLIEKYKITFLYLVPP----IAAALAKSPLLDKYDLsslRVILSGGAPLSKELQELLAKR 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 82 LG-APIHDHYGQTELGMVVNnhHGLEHPVRQGSAGYAMPGYRIAVLDEAGKE-VGPNEPGVLAIdidNSPLLWfTGYYKK 159
Cdd:cd05911 286 FPnATIKQGYGMTETGGILT--VNPDGDDKPGSVGRLLPNVEAKIVDDDGKDsLGPNEPGEICV---RGPQVM-KGYYNN 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 160 DTPSI----SGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAF 235
Cdd:cd05911 360 PEATKetfdEDGWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAY 439
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 492822008 236 VILAPGFEGTpelAEELALHVKKQLSAHaypRQID----FVAELPKTPSGKIQ 284
Cdd:cd05911 440 VVRKPGEKLT---EKEVKDYVAKKVASY---KQLRggvvFVDEIPKSASGKIL 486
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
7-289 |
3.67e-41 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 149.07 E-value: 3.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 7 LGVPTILNEGgFTAENTYDIIERLGVTSLAGSPTAF-RLLMAagPEsAARVK---GRLRVASSAGEPLNPEV----IRWF 78
Cdd:PRK13391 224 LGGTVIVMEH-FDAEQYLALIEEYGVTHTQLVPTMFsRMLKL--PE-EVRDKydlSSLEVAIHAAAPCPPQVkeqmIDWW 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 79 daclGAPIHDHYGQTE-LGM-VVNNHHGLEHPvrqGSAGYAMPGyRIAVLDEAGKEVGPNEPGVLaididnspllWFTG- 155
Cdd:PRK13391 300 ----GPIIHEYYAATEgLGFtACDSEEWLAHP---GTVGRAMFG-DLHILDDDGAELPPGEPGTI----------WFEGg 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 156 ----YYK-----KDTPSISGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDP 226
Cdd:PRK13391 362 rpfeYLNdpaktAEARHPDGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNE 441
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492822008 227 QRTEIVKAFVILAPGFEGTPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLR 289
Cdd:PRK13391 442 DLGEEVKAVVQPVDGVDPGPALAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLR 504
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
11-288 |
4.98e-41 |
|
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: 147.24 E-value: 4.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 11 TILNEGGFTAENTYDIIERLGVTSLAGSPTAFRLLMAAgPESAARVKGRLRVASSAGEPLNPEVIRWFDACLGAPIHDHY 90
Cdd:cd05935 153 TYVLMARWDRETALELIEKYKVTFWTNIPTMLVDLLAT-PEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGY 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 91 GQTE-LGMVVNNHHGleHPVRQgSAGYAMPGYRIAVLD-EAGKEVGPNEPGVLAIdidNSPLLwFTGYYKKDTPS----- 163
Cdd:cd05935 232 GLTEtMSQTHTNPPL--RPKLQ-CLGIP*FGVDARVIDiETGRELPPNEVGEIVV---RGPQI-FKGYWNRPEETeesfi 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 164 -ISGG-YYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILAPG 241
Cdd:cd05935 305 eIKGRrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPE 384
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 492822008 242 FEGTPElAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLL 288
Cdd:cd05935 385 YRGKVT-EEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
3-289 |
1.34e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 146.67 E-value: 1.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 3 GPLLLGvPTILNEGGFTAENtYDIIERLGVTSLAGSPTAF-RLlmAAGPESAARVKG-RLRVASSAgePLNPEVIRWFDA 80
Cdd:PRK07787 190 GPLRIG-NRFVHTGRPTPEA-YAQALSEGGTLYFGVPTVWsRI--AADPEAARALRGaRLLVSGSA--ALPVPVFDRLAA 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 81 CLGAPIHDHYGQTELGMVVNNHHGLEHpvRQGSAGYAMPGYRIAVLDEAGKEVGPNEPGVLAIDIdNSPLLwFTGYYKKD 160
Cdd:PRK07787 264 LTGHRPVERYGMTETLITLSTRADGER--RPGWVGLPLAGVETRLVDEDGGPVPHDGETVGELQV-RGPTL-FDGYLNRP 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 161 TPS----ISGGYYRTGDTVEFEPDGSISFIGR-ADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAF 235
Cdd:PRK07787 340 DATaaafTADGWFRTGDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAY 419
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 492822008 236 VIlapgfEGTPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLR 289
Cdd:PRK07787 420 VV-----GADDVAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
71-285 |
5.12e-40 |
|
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: 142.41 E-value: 5.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 71 NPEVIRWFDACLGAPIHDHYGQTELGMVVNNHHGLEHPvrqGSAGYAMPGYRIAVLDEAGKEVGPNEPGVLAIdidNSPL 150
Cdd:cd17637 124 APETIQRFEETTGATFWSLYGQTETSGLVTLSPYRERP---GSAGRPGPLVRVRIVDDNDRPVPAGETGEIVV---RGPL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 151 LwFTGYYKKDTP---SISGGYYRTGDTVEFEPDGSISFIGR--ADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPD 225
Cdd:cd17637 198 V-FQGYWNLPELtayTFRNGWHHTGDLGRFDEDGYLWYAGRkpEKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPD 276
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 226 PQRTEIVKAFVILAPGFEGTpelAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQR 285
Cdd:cd17637 277 PKWGEGIKAVCVLKPGATLT---ADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
4-289 |
6.66e-40 |
|
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: 144.43 E-value: 6.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 4 PLLLGVPTILNEGG--FTAENTYDIIERLGVTSLAGSPTAFRLLMAAGPESAARVKGRLRVASSAGEPLNPE-VIRWFDA 80
Cdd:cd17649 156 PLICGACVVLRPDElwASADELAEMVRELGVTVLDLPPAYLQQLAEEADRTGDGRPPSLRLYIFGGEALSPElLRRWLKA 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 81 clGAPIHDHYGQTELGMVVNNHHGLEHPVRQGSA---GYAMPGYRIAVLDEAGKEVGPNEPGVLAIdidNSPLLwFTGYY 157
Cdd:cd17649 236 --PVRLFNAYGPTEATVTPLVWKCEAGAARAGASmpiGRPLGGRSAYILDADLNPVPVGVTGELYI---GGEGL-ARGYL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 158 KK----------DTPSISGG-YYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDP 226
Cdd:cd17649 310 GRpeltaerfvpDPFGAPGSrLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGA 389
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492822008 227 QRTEIVkAFVILAPGFEGtPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLR 289
Cdd:cd17649 390 GGKQLV-AYVVLRAAAAQ-PELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
40-293 |
7.91e-40 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 146.06 E-value: 7.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 40 TAFRLLMA------AGPESAARVKGRLRVASSAGEPlnPEVIRWFDACLGAPIHDHYGQTELGMVVNNHHGLEHPvrqGS 113
Cdd:PRK06155 270 TVTYLLGAmvsillSQPARESDRAHRVRVALGPGVP--AALHAAFRERFGVDLLDGYGSTETNFVIAVTHGSQRP---GS 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 114 AGYAMPGYRIAVLDEAGKEVGPNEPGVLAIDIDnSPLLWFTGYYKKDTPSISGG---YYRTGDTVEFEPDGSISFIGRAD 190
Cdd:PRK06155 345 MGRLAPGFEARVVDEHDQELPDGEPGELLLRAD-EPFAFATGYFGMPEKTVEAWrnlWFHTGDRVVRDADGWFRFVDRIK 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 191 DVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILAPGFEGTPelaEELALHVKKQLSAHAYPRQID 270
Cdd:PRK06155 424 DAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEP---VALVRHCEPRLAYFAVPRYVE 500
|
250 260
....*....|....*....|...
gi 492822008 271 FVAELPKTPSGKIQRFLLRKAEV 293
Cdd:PRK06155 501 FVAALPKTENGKVQKFVLREQGV 523
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
18-290 |
1.18e-38 |
|
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: 142.05 E-value: 1.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 18 FTAENTYDIIERLGVTSLAGSPTAFRLLMAAGPESAARVKGRLRVASsAGEPLNPEVIRWFDACLGAPIHDhYGQTE-LG 96
Cdd:cd12118 208 VDAKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLPHRVHVMT-AGAPPPAAVLAKMEELGFDVTHV-YGLTEtYG 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 97 MVV--------NNHHGLEHPV---RQGSAGYAMPGyrIAVLDEAGKEVGPNEpGVLAIDI---DNSPLLwftGYYKKD-- 160
Cdd:cd12118 286 PATvcawkpewDELPTEERARlkaRQGVRYVGLEE--VDVLDPETMKPVPRD-GKTIGEIvfrGNIVMK---GYLKNPea 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 161 -TPSISGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILA 239
Cdd:cd12118 360 tAEAFRGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELK 439
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 492822008 240 PGFEGTPelaEELALHVKKQLSAHAYPRQIDFVaELPKTPSGKIQRFLLRK 290
Cdd:cd12118 440 EGAKVTE---EEIIAFCREHLAGFMVPKTVVFG-ELPKTSTGKIQKFVLRD 486
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
1-290 |
2.70e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 141.20 E-value: 2.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 1 MTGPLLLGVpTILNEGGFTAENTYDIIERLGVTSLAGSPTAFRLLMAAgPESAARVKGRLRVASSAGEPLNPEVIRWFDA 80
Cdd:PRK07656 226 VNAPLMRGA-TILPLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQH-PDRSAEDLSSLRLAVTGAASMPVALLERFES 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 81 CLGAP-IHDHYGQTE-LGMVVNNHHGLEHPVRQGSAGYAMPGYRIAVLDEAGKEVGPNEPGVLAIDIDNSpllwFTGYYK 158
Cdd:PRK07656 304 ELGVDiVLTGYGLSEaSGVTTFNRLDDDRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNV----MKGYYD 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 159 --KDTP-SISG-GYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKA 234
Cdd:PRK07656 380 dpEATAaAIDAdGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKA 459
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 492822008 235 FVILAPGFEGTpelAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRK 290
Cdd:PRK07656 460 YVVLKPGAELT---EEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
90-281 |
4.20e-38 |
|
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: 137.05 E-value: 4.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 90 YGQTEL-GMVVNNHHGLEhpvRQGSAGYAMPGYRIAVLDEAGKEVGPNEPGVLAIDidnSPLLwFTGYYkkDTPSIS--- 165
Cdd:cd17636 143 YGQTEVmGLATFAALGGG---AIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVAR---GPTV-MAGYW--NRPEVNarr 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 166 --GGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILAPGFE 243
Cdd:cd17636 214 trGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGAS 293
|
170 180 190
....*....|....*....|....*....|....*...
gi 492822008 244 GTPelaEELALHVKKQLSAHAYPRQIDFVAELPKTPSG 281
Cdd:cd17636 294 VTE---AELIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
5-289 |
8.79e-38 |
|
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: 139.11 E-value: 8.79e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 5 LLLGVPTILNEGGFTAENTYDIIERLGVTSLAGSPTAFRLLMAAG--PESAARvkgrLRVASSAGEPLNPEVIRWF-DAC 81
Cdd:cd05922 180 LLRGATLVLTNDGVLDDAFWEDLREHGATGLAGVPSTYAMLTRLGfdPAKLPS----LRYLTQAGGRLPQETIARLrELL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 82 LGAPIHDHYGQTE---LGMVVNNHHGLEHPvrqGSAGYAMPGYRIAVLDEAGKEVGPNEPGVLAIDIDNSPLLWFTGYYK 158
Cdd:cd05922 256 PGAQVYVMYGQTEatrRMTYLPPERILEKP---GSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPNVMKGYWNDPPY 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 159 KDTPSISGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQrTEIVKAFVIL 238
Cdd:cd05922 333 RRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPL-GEKLALFVTA 411
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 492822008 239 APGFEgtpelAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLR 289
Cdd:cd05922 412 PDKID-----PKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
21-295 |
3.03e-37 |
|
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: 135.69 E-value: 3.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 21 ENTYDIIERLGVTSLAGSPTAFRLLMAAgPESAArvKGRLRVASSAGEPLNPEVIRWFDACLGAPIHDHYGQTELGMVVN 100
Cdd:cd05944 87 DNFWKLVERYRITSLSTVPTVYAALLQV-PVNAD--ISSLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 101 NHHGlEHPVRQGSAGYAMP--GYRIAVLDEAG---KEVGPNEPGVLAIdidNSPLLwFTGYYKKD---TPSISGGYYRTG 172
Cdd:cd05944 164 VNPP-DGPKRPGSVGLRLPyaRVRIKVLDGVGrllRDCAPDEVGEICV---AGPGV-FGGYLYTEgnkNAFVADGWLNTG 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 173 DTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILAPGFEGTPelaEEL 252
Cdd:cd05944 239 DLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVEE---EEL 315
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 492822008 253 ALHVKKQLSAH-AYPRQIDFVAELPKTPSGKIQRFLLRKAEVEK 295
Cdd:cd05944 316 LAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPALRADAIHR 359
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
12-289 |
3.82e-37 |
|
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: 135.10 E-value: 3.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 12 ILNEGGFTAENTYDIIERLGVTSLAGSPTAFrLLMAAGPESAARVKGRLRVASSAGEPLNPEVIRWFDACLGAP-IHDHY 90
Cdd:cd05917 73 VFPSPSFDPLAVLEAIEKEKCTALHGVPTMF-IAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKdVTIAY 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 91 GQTELGMVVNNHH-GLEHPVRQGSAGYAMPGYRIAVLDEAGKEV-GPNEPGVLAIDIDNSPLlwftGYYK---KDTPSIS 165
Cdd:cd05917 152 GMTETSPVSTQTRtDDSIEKRVNTVGRIMPHTEAKIVDPEGGIVpPVGVPGELCIRGYSVMK----GYWNdpeKTAEAID 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 166 G-GYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILAPGFEG 244
Cdd:cd05917 228 GdGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAEL 307
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 492822008 245 TpelAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLR 289
Cdd:cd05917 308 T---EEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
5-290 |
5.48e-37 |
|
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: 137.76 E-value: 5.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 5 LLLGVPTILNEGGFTAENTYDIIERLGVTSLAGSPTAFRLLMAAgPESAARVKGRLRVASSAGEPLNPEVIRWFDAcLGA 84
Cdd:cd12119 228 AMVGAKLVLPGPYLDPASLAELIEREGVTFAAGVPTVWQGLLDH-LEANGRDLSSLRRVVIGGSAVPRSLIEAFEE-RGV 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 85 PIHDHYGQTE---LGMVV---NNHHGL---EHPVRQGSAGYAMPGYRIAVLDEAGKEV--GPNEPGVLAIdidNSPllWF 153
Cdd:cd12119 306 RVIHAWGMTEtspLGTVArppSEHSNLsedEQLALRAKQGRPVPGVELRIVDDDGRELpwDGKAVGELQV---RGP--WV 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 154 T-GYYKKDTPSI---SGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRT 229
Cdd:cd12119 381 TkSYYKNDEESEaltEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWG 460
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492822008 230 EIVKAFVILAPGFEGTPelaEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRK 290
Cdd:cd12119 461 ERPLAVVVLKEGATVTA---EELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
4-291 |
1.60e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 136.09 E-value: 1.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 4 PLLLGVPTILNEGGFTAENTYDII--ERLGVTSLAGSPTAFRLLMAAgPESAARVKGRLRVASSAGEPLNPEVIR-WFDA 80
Cdd:PRK09088 197 PVLAVGGSILVSNGFEPKRTLGRLgdPALGITHYFCVPQMAQAFRAQ-PGFDAAALRHLTALFTGGAPHAAEDILgWLDD 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 81 clGAPIHDHYGQTELGMVvnnhhgLEHPV-------RQGSAGYAMPGYRIAVLDEAGKEVGPNEPGVLAIDIDNspllWF 153
Cdd:PRK09088 276 --GIPMVDGFGMSEAGTV------FGMSVdcdviraKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPN----LS 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 154 TGYYKKDTPS----ISGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRT 229
Cdd:PRK09088 344 PGYWRRPQATarafTGDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWG 423
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492822008 230 EIVKAFVILAPgfeGTPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRKA 291
Cdd:PRK09088 424 EVGYLAIVPAD---GAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRDA 482
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
5-290 |
1.79e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 136.60 E-value: 1.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 5 LLLGVPTILNEGGfTAENTYDIIERLGVTSLAGSPTAFrLLMAAGPESAARVKGRLRVASSAGEPLNPEVIRWFDACL-G 83
Cdd:PRK08316 235 LYVGATNVILDAP-DPELILRTIEAERITSFFAPPTVW-ISLLRHPDFDTRDLSSLRKGYYGASIMPVEVLKELRERLpG 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 84 APIHDHYGQTELG---MVVNNHHGLEHPvrqGSAGyaMPGYRI--AVLDEAGKEVGPNEPGVLaidIDNSPLLwFTGYYK 158
Cdd:PRK08316 313 LRFYNCYGQTEIAplaTVLGPEEHLRRP---GSAG--RPVLNVetRVVDDDGNDVAPGEVGEI---VHRSPQL-MLGYWD 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 159 KD---TPSISGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAF 235
Cdd:PRK08316 384 DPektAEAFRGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAV 463
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 492822008 236 VILAPGFEGTPelaEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRK 290
Cdd:PRK08316 464 VVPKAGATVTE---DELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRE 515
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
18-288 |
9.00e-36 |
|
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: 134.17 E-value: 9.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 18 FTAENTYDIIERLGVTSLAGSPTAFRLLMAAGPESAARVKGrLRVASSAGEPLNPEVIRWFDACLGAPIHDHYGQTELGM 97
Cdd:cd05923 228 FDPADALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSS-LRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTEAMN 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 98 VVNNHHglehpVRQGSAGyaMPGY----RIAVLDEAGKEVGPN-EPGVLAIDIDNSPLlwFTGYYKK---DTPSISGGYY 169
Cdd:cd05923 307 SLYMRD-----ARTGTEM--RPGFfsevRIVRIGGSPDEALANgEEGELIVAAAADAA--FTGYLNQpeaTAKKLQDGWY 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 170 RTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILAPGfegtPELA 249
Cdd:cd05923 378 RTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREG----TLSA 453
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 492822008 250 EEL-ALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLL 288
Cdd:cd05923 454 DELdQFCRASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
5-290 |
3.05e-35 |
|
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: 129.37 E-value: 3.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 5 LLLGVPTILNEGGFTAENTydiIERLGVTSLAGSPTAFRLLMAAGPESAARvkGRLRVASSAGEPLNPEVIRWFdACLGA 84
Cdd:cd17630 63 LLAGAELVLLERNQALAED---LAPPGVTHVSLVPTQLQRLLDSGQGPAAL--KSLRAVLLGGAPIPPELLERA-ADRGI 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 85 PIHDHYGQTELGMVVNNHHGLEHpvRQGSAGYAMPGYRIAVLDeagkevgpnePGVLAIdidnSPLLWFTGYYKKDTPSI 164
Cdd:cd17630 137 PLYTTYGMTETASQVATKRPDGF--GRGGVGVLLPGRELRIVE----------DGEIWV----GGASLAMGYLRGQLVPE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 165 --SGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILAPgf 242
Cdd:cd17630 201 fnEDGWFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRG-- 278
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 492822008 243 egtPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRK 290
Cdd:cd17630 279 ---PADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
18-289 |
7.37e-35 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 131.67 E-value: 7.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 18 FTAENTYDIIERLGVTSLAGSPTAFRLLMAAGPESAARVK-GRLRVASSAGEPLNPEVIRWFDACLGAPIHDHYGQTEL- 95
Cdd:PRK13390 229 FDAQATLGHVERYRITVTQMVPTMFVRLLKLDADVRTRYDvSSLRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTEAh 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 96 GM-VVNNHHGLEHPvrqGSAGYAMPGyRIAVLDEAGKEVGPNEPGVLAIDIDNSPLLWFTGYYKKDTPSISGGYYRT--G 172
Cdd:PRK13390 309 GMtFIDSPDWLAHP---GSVGRSVLG-DLHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHPAHPFWTtvG 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 173 DTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILAPGFEGTPELAEEL 252
Cdd:PRK13390 385 DLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDELAREL 464
|
250 260 270
....*....|....*....|....*....|....*..
gi 492822008 253 ALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLR 289
Cdd:PRK13390 465 IDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
20-291 |
8.50e-35 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 131.81 E-value: 8.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 20 AENTYDIIERLGVTSLAGSPTAFRLLMAAGPESAARVKGrLRVASSAGEPLNPEVIRWFDACLGAPIHDHYGQTElGMVv 99
Cdd:COG1021 263 PDTAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSS-LRVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE-GLV- 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 100 nNHHGLEHP--VRQGSAGYAM-PGYRIAVLDEAGKEVGPNEPGVLaididnspllW------FTGYYKKD-------TPS 163
Cdd:COG1021 340 -NYTRLDDPeeVILTTQGRPIsPDDEVRIVDEDGNPVPPGEVGEL----------LtrgpytIRGYYRAPehnarafTPD 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 164 isgGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILApgfe 243
Cdd:COG1021 409 ---GFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPR---- 481
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 492822008 244 GTPELAEELALHVKKQ-LSAHAYPRQIDFVAELPKTPSGKIQRFLLRKA 291
Cdd:COG1021 482 GEPLTLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKALRAA 530
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
1-290 |
1.25e-34 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 131.79 E-value: 1.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 1 MTGPLLLGVPTILNEGgFTAENTYDIIERLGVT-SLAGSPTAFRLLMAAgPESAARVKGrLRVASSAGEPLNPEVIRwfd 79
Cdd:PRK06087 247 VTAPFLIGARSVLLDI-FTPDACLALLEQQRCTcMLGATPFIYDLLNLL-EKQPADLSA-LRFFLCGGTTIPKKVAR--- 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 80 ACLGAPIH--DHYGQTELG--MVVNNHHGLEHPVrqGSAGYAMPGYRIAVLDEAGKEVgpnEPGVLAIDIDNSPLLwFTG 155
Cdd:PRK06087 321 ECQQRGIKllSVYGSTESSphAVVNLDDPLSRFM--HTDGYAAAGVEIKVVDEARKTL---PPGCEGEEASRGPNV-FMG 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 156 YYkkDTPSISG------GYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRT 229
Cdd:PRK06087 395 YL--DEPELTAraldeeGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLG 472
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492822008 230 EIVKAFVILAPGfEGTPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRK 290
Cdd:PRK06087 473 ERSCAYVVLKAP-HHSLTLEEVVAFFSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
1-285 |
1.26e-34 |
|
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: 130.91 E-value: 1.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 1 MTGPLLLGVPTILNEGGfTAENTYDIIERLGVTSLAGSPTAFRLLMAAGpESAARVKGRLRVASSAGEPLNPEVIRWFDA 80
Cdd:cd05920 200 VLGTLLAGGRVVLAPDP-SPDAAFPLIEREGVTVTALVPALVSLWLDAA-ASRRADLSSLRLLQVGGARLSPALARRVPP 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 81 CLGAPIHDHYGQTElGMVvnNHHGLEHP--VRQGSAGYAM-PGYRIAVLDEAGKEVGPNEPGVLaidIDNSPLLwFTGYY 157
Cdd:cd05920 278 VLGCTLQQVFGMAE-GLL--NYTRLDDPdeVIIHTQGRPMsPDDEIRVVDEEGNPVPPGEEGEL---LTRGPYT-IRGYY 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 158 KKD-------TPSisgGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTE 230
Cdd:cd05920 351 RAPehnarafTPD---GFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGE 427
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 492822008 231 IVKAFVILapgfEGTPELAEELALHVKKQ-LSAHAYPRQIDFVAELPKTPSGKIQR 285
Cdd:cd05920 428 RSCAFVVL----RDPPPSAAQLRRFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDK 479
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
24-285 |
1.35e-34 |
|
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: 130.86 E-value: 1.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 24 YDIIERLGVTSLAGSPTAFRLLMA-AGPESAARvkgrLRVASSAGEPLNPEVIRWFDACLGAPIHDHYGQTELGMVVNnH 102
Cdd:cd17646 222 AALIREHGVTTCHFVPSMLRVFLAePAAGSCAS----LRRVFCSGEALPPELAARFLALPGAELHNLYGPTEAAIDVT-H 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 103 HGLEHPVRQGSA--GYAMPGYRIAVLDEAGKEVGPNEPGVLAIdidnSPLLWFTGYYKK---------DTPSISGG-YYR 170
Cdd:cd17646 297 WPVRGPAETPSVpiGRPVPNTRLYVLDDALRPVPVGVPGELYL----GGVQLARGYLGRpaltaerfvPDPFGPGSrMYR 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 171 TGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILAPGfeGTPELAE 250
Cdd:cd17646 373 TGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAG--AAGPDTA 450
|
250 260 270
....*....|....*....|....*....|....*
gi 492822008 251 ELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQR 285
Cdd:cd17646 451 ALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDR 485
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
39-285 |
1.50e-34 |
|
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: 130.93 E-value: 1.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 39 PTAFRLLMAAGPESAARVKGRLRVASSAGEPL--NPEVIRWFDACLGAPIHDHYGQTElgmvvnNHHGLEHPVRQGSAGY 116
Cdd:cd17651 234 PTVALRALAEHGRPLGVRLAALRYLLTGGEQLvlTEDLREFCAGLPGLRLHNHYGPTE------THVVTALSLPGDPAAW 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 117 --------AMPGYRIAVLDEAGKEVGPNEPGVLAIDID-------NSPLLwfTGYYKKDTPSISGG-YYRTGDTVEFEPD 180
Cdd:cd17651 308 papppigrPIDNTRVYVLDAALRPVPPGVPGELYIGGAglargylNRPEL--TAERFVPDPFVPGArMYRTGDLARWLPD 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 181 GSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILAPGFEGTPelaEELALHVKKQL 260
Cdd:cd17651 386 GELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDA---AELRAALATHL 462
|
250 260
....*....|....*....|....*
gi 492822008 261 SAHAYPRQIDFVAELPKTPSGKIQR 285
Cdd:cd17651 463 PEYMVPSAFVLLDALPLTPNGKLDR 487
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
1-285 |
5.27e-34 |
|
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: 128.58 E-value: 5.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 1 MTGPLLLG-----VPtilNEGGFTAENTYDIIERLGVTSLAGSPTAFRLLMAAGpESAARVKGRLRVASSAGEPLNPEVI 75
Cdd:cd17643 152 IWGALLHGgrlvvVP---YEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEAA-DRDGRDPLALRYVIFGGEALEAAML 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 76 R-WFdaclGAPIHDH------YGQTELgMVVNNHHGLEHPVRQGSA----GYAMPGYRIAVLDEAGKEVGPNEPGVLAID 144
Cdd:cd17643 228 RpWA----GRFGLDRpqlvnmYGITET-TVHVTFRPLDAADLPAAAaspiGRPLPGLRVYVLDADGRPVPPGVVGELYVS 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 145 ID-------NSPLLwFTGYYKKDTPSISGG-YYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVN 216
Cdd:cd17643 303 GAgvargylGRPEL-TAERFVANPFGGPGSrMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVR 381
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 217 EAAVVGVPD-PQRTEIVKAFVilapGFEGTPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQR 285
Cdd:cd17643 382 DAAVIVREDePGDTRLVAYVV----ADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDR 447
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
26-291 |
7.17e-34 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 129.23 E-value: 7.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 26 IIERLG-VTSLAGSPTAF-RLLMAAG--PESAARVkgRLRVASSAgePLNPEVIRWFDACLGAPIHDHYGQTELGMVVNN 101
Cdd:PRK07514 237 VLALMPrATVMMGVPTFYtRLLQEPRltREAAAHM--RLFISGSA--PLLAETHREFQERTGHAILERYGMTETNMNTSN 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 102 HHGLEHpvRQGSAGYAMPGYRIAVLD-EAGKEVGPNEPGVLAIDIDNSpllwFTGYY----KKDTPSISGGYYRTGDTVE 176
Cdd:PRK07514 313 PYDGER--RAGTVGFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNV----FKGYWrmpeKTAEEFRADGFFITGDLGK 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 177 FEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILAPGFEGTPelaEELALHV 256
Cdd:PRK07514 387 IDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDE---AAILAAL 463
|
250 260 270
....*....|....*....|....*....|....*
gi 492822008 257 KKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRKA 291
Cdd:PRK07514 464 KGRLARFKQPKRVFFVDELPRNTMGKVQKNLLREQ 498
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
1-289 |
1.40e-33 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 128.28 E-value: 1.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 1 MTGPLLLGVP------------TILNEGGFTAENTYDIIERLGVTSLAGSPTAFRLLMAAGPESAARVK-GRLRVASSAG 67
Cdd:PRK12406 201 LTGPLYHSAPnayglragrlggVLVLQPRFDPEELLQLIERHRITHMHMVPTMFIRLLKLPEEVRAKYDvSSLRHVIHAA 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 68 EPLNPEVIRWFDACLGAPIHDHYGQTELGMVV--NNHHGLEHPvrqGSAGYAMPGYRIAVLDEAGKEVGPNEPGVLAIDI 145
Cdd:PRK12406 281 APCPADVKRAMIEWWGPVIYEYYGSTESGAVTfaTSEDALSHP---GTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRI 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 146 DNSPLLWFTGYYKKDTPSISGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPD 225
Cdd:PRK12406 358 AGNPDFTYHNKPEKRAEIDRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPD 437
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492822008 226 PQRTEIVKAFVILAPGfeGTPElAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLR 289
Cdd:PRK12406 438 AEFGEALMAVVEPQPG--ATLD-EADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLR 498
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
1-290 |
5.16e-33 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 126.58 E-value: 5.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 1 MTGPLLLGVpTILNEGGFTAENTYDIIERLGVTSLAGSPTAFrLLMAAGPESAARVKGRLRVASSAGEPLNPEVIRWFDA 80
Cdd:cd05904 220 ALGLLRLGA-TVVVMPRFDLEELLAAIERYKVTHLPVVPPIV-LALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRA 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 81 CL-GAPIHDHYGQTELGMVVNNHHG-LEHPVRQGSAGYAMPGYRIAVLD-EAGKEVGPNEPGVLAIdidNSPLLwFTGYY 157
Cdd:cd05904 298 KFpNVDLGQGYGMTESTGVVAMCFApEKDRAKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWI---RGPSI-MKGYL 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 158 K--KDTPS--ISGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVK 233
Cdd:cd05904 374 NnpEATAAtiDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPM 453
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 492822008 234 AFVILAPGfegtPELAE-ELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIqrflLRK 290
Cdd:cd05904 454 AFVVRKPG----SSLTEdEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKI----LRK 503
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
8-296 |
5.75e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 124.00 E-value: 5.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 8 GVPTILNEG-GFTAENTYDIIERLGVTSLAGSPTAFRLlMAAGPESAARVKGRLRVASSAGEPLNPEVIRWFDACLGAPI 86
Cdd:PRK07470 230 GAATVLLPSeRFDPAEVWALVERHRVTNLFTVPTILKM-LVEHPAVDRYDHSSLRYVIYAGAPMYRADQKRALAKLGKVL 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 87 HDHYGqteLGMVVNN--------HHGLEHP-VRQGSAGYAMPGYRIAVLDEAGKEVGPNEPGVLAIdidNSPLLwFTGYY 157
Cdd:PRK07470 309 VQYFG---LGEVTGNitvlppalHDAEDGPdARIGTCGFERTGMEVQIQDDEGRELPPGETGEICV---IGPAV-FAGYY 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 158 ---KKDTPSISGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKA 234
Cdd:PRK07470 382 nnpEANAKAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVA 461
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492822008 235 FVILApgfEGTPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRkAEVEKQ 296
Cdd:PRK07470 462 VCVAR---DGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVR-EELEER 519
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
18-300 |
6.29e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 124.38 E-value: 6.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 18 FTAENTYDIIERLGVTSLAGSPTAFRLLMAAgPESAARVKGRLRVASSAGEPLNPEVIRWFDACLGAPIHDHYGQTELGM 97
Cdd:PRK06710 284 FDMKMVFEAIKKHKVTLFPGAPTIYIALLNS-PLLKEYDISSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSP 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 98 VVNNHHGLEHPVrQGSAGYAMPGYRIAVLD-EAGKEVGPNEPGVLAIdidNSPLLwFTGYYKKDTPS---ISGGYYRTGD 173
Cdd:PRK06710 363 VTHSNFLWEKRV-PGSIGVPWPDTEAMIMSlETGEALPPGEIGEIVV---KGPQI-MKGYWNKPEETaavLQDGWLHTGD 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 174 TVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILApgfEGTPELAEELA 253
Cdd:PRK06710 438 VGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLK---EGTECSEEELN 514
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 492822008 254 LHVKKQLSAHAYPRQIDFVAELPKTPSGKIqrflLRKAEVEKQQQQN 300
Cdd:PRK06710 515 QFARKYLAAYKVPKVYEFRDELPKTTVGKI----LRRVLIEEEKRKN 557
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
4-285 |
1.12e-31 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 123.05 E-value: 1.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 4 PLLLGVPTILNEGGFTAENTYDIIERLGVTSLAGSPTAFRLLMAAgPESAARVKGRLRVASSAGEPLNPEVIRWFDAcLG 83
Cdd:PRK06839 211 PTLFAGGVIIVPRKFEPTKALSMIEKHKVTVVMGVPTIHQALINC-SKFETTNLQSVRWFYNGGAPCPEELMREFID-RG 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 84 APIHDHYGQTELGMVVNNHHGLEHPVRQGSAGYAMPGYRIAVLDEAGKEVGPNEPGVLAIDIDNSpllwFTGYY---KKD 160
Cdd:PRK06839 289 FLFGQGFGMTETSPTVFMLSEEDARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNV----MKEYWnrpDAT 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 161 TPSISGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILAP 240
Cdd:PRK06839 365 EETIQDGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKS 444
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 492822008 241 GFEGTpelAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQR 285
Cdd:PRK06839 445 SSVLI---EKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQK 486
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
13-288 |
1.93e-31 |
|
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: 121.66 E-value: 1.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 13 LNEGG--FTAENTYDIIE---RLGVTSLAGSPTAFRLLMAAGPesaarVKGRLRVASSAGEPLNPE-VIRWFDACLGAPI 86
Cdd:cd12115 168 LATGGkvVLADNVLALPDlpaAAEVTLINTVPSAAAELLRHDA-----LPASVRVVNLAGEPLPRDlVQRLYARLQVERV 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 87 HDHYGQTELGMVVNNHHGLEHPVRQGSAGYAMPGYRIAVLDEAGKEVGPNEPGVLAIDIDNSPLlwftGYYKKDT----- 161
Cdd:cd12115 243 VNLYGPSEDTTYSTVAPVPPGASGEVSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVAR----GYLGRPGltaer 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 162 ----PSISGGY-YRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFV 236
Cdd:cd12115 319 flpdPFGPGARlYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYI 398
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 492822008 237 ILAPGFEGTPelaEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLL 288
Cdd:cd12115 399 VAEPGAAGLV---EDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
59-299 |
2.06e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 122.95 E-value: 2.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 59 RLRVASSAGEPLNPEVIRWFDACLGAPIHDHYGQTELGMV--VNNHHGlehpVRQGSAGYAMPGYRIAVLDEAGKEVGPN 136
Cdd:PRK05677 327 ALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVvsVNPSQA----IQVGTIGIPVPSTLCKVIDDDGNELPLG 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 137 EPGVLAIdidNSPLLwFTGYYKK--DTPSI--SGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEH 212
Cdd:PRK05677 403 EVGELCV---KGPQV-MKGYWQRpeATDEIldSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAAL 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 213 PAVNEAAVVGVPDPQRTEIVKAFVILAPGFEGTpelAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRKAE 292
Cdd:PRK05677 479 PGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLT---KEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRDEE 555
|
....*..
gi 492822008 293 VEKQQQQ 299
Cdd:PRK05677 556 LKKAGLK 562
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
25-298 |
3.42e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 121.99 E-value: 3.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 25 DIIERLGVTSLAGSPTAFRLLMAAgPESAARVKGRLRVASSAGEPLnPEVI--RWFDAClGAPIHDHYGQTELgMVVNNH 102
Cdd:PRK08314 273 RLIERYRVTHWTNIPTMVVDFLAS-PGLAERDLSSLRYIGGGGAAM-PEAVaeRLKELT-GLDYVEGYGLTET-MAQTHS 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 103 HGLEHPVRQgSAGYAMPGYRIAVLD-EAGKEVGPNEPGVLAIdidNSPLLwFTGYYKKDTPS------ISGG-YYRTGDT 174
Cdd:PRK08314 349 NPPDRPKLQ-CLGIPTFGVDARVIDpETLEELPPGEVGEIVV---HGPQV-FKGYWNRPEATaeafieIDGKrFFRTGDL 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 175 VEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILAPGFEGTPElAEELAL 254
Cdd:PRK08314 424 GRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEARGKTT-EEEIIA 502
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 492822008 255 HVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRKAEVEKQQQ 298
Cdd:PRK08314 503 WAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQLQEQEKARAAK 546
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
3-293 |
3.82e-31 |
|
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: 123.04 E-value: 3.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 3 GPLLLGVPTIL--NEGGFTAENTYDIIERLGVTSLAGSPTAFRLLMAAGPESAARvkgrLRVASSAGEPLNPE-VIRWFD 79
Cdd:COG1020 678 GALLSGATLVLapPEARRDPAALAELLARHRVTVLNLTPSLLRALLDAAPEALPS----LRLVLVGGEALPPElVRRWRA 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 80 ACLGAPIHDHYGQTElGMVVNNHHGLEHPVRQGSA---GYAMPGYRIAVLDEAGKEVGPNEPGVLAI------Didnspl 150
Cdd:COG1020 754 RLPGARLVNLYGPTE-TTVDSTYYEVTPPDADGGSvpiGRPIANTRVYVLDAHLQPVPVGVPGELYIggaglaR------ 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 151 lwftGYYKK----------DTPSISGG-YYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAA 219
Cdd:COG1020 827 ----GYLNRpeltaerfvaDPFGFPGArLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAV 902
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492822008 220 VVGVPDPQRTEIVKAFVILAPgfeGTPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRKAEV 293
Cdd:COG1020 903 VVAREDAPGDKRLVAYVVPEA---GAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAA 973
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
3-285 |
7.54e-31 |
|
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: 120.38 E-value: 7.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 3 GPLLLGVPTILNEGGF--TAENTYDIIERLGVTSLAGSPTAFRLLMAAGPESAARvkgrLRVASSAGEPLNPE-VIRWFD 79
Cdd:cd12117 196 GALLNGARLVLAPKGTllDPDALGALIAEEGVTVLWLTAALFNQLADEDPECFAG----LRELLTGGEVVSPPhVRRVLA 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 80 ACLGAPIHDHYGQTElGMVVNNHHGLEHPVRQGSA---GYAMPGYRIAVLDEAGKEVGPNEPGVLAIDIDNSPLlwftGY 156
Cdd:cd12117 272 ACPGLRLVNGYGPTE-NTTFTTSHVVTELDEVAGSipiGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLAL----GY 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 157 YKKDT---------PSISGG-YYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPD- 225
Cdd:cd12117 347 LNRPAltaerfvadPFGPGErLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDa 426
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 226 PQRTEIVkAFVILAPGFEgtpelAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQR 285
Cdd:cd12117 427 GGDKRLV-AYVVAEGALD-----AAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDR 480
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
1-220 |
8.49e-31 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 119.29 E-value: 8.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 1 MTGPLLLGVPTIL---NEGGFTAENTYDIIERLGVTSLAGSPTAFRLLMAAGPESAARvkgrLRVASSAGEPLNPEVI-R 76
Cdd:TIGR01733 179 IFGALLAGATLVVppeDEERDDAALLAALIAEHPVTVLNLTPSLLALLAAALPPALAS----LRLVILGGEALTPALVdR 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 77 WFDACLGAPIHDHYGQTElGMVVNNHHGLEHPVRQGSA----GYAMPGYRIAVLDEAGKEVGPNEPGVLAIdidnspllw 152
Cdd:TIGR01733 255 WRARGPGARLINLYGPTE-TTVWSTATLVDPDDAPRESpvpiGRPLANTRLYVLDDDLRPVPVGVVGELYI--------- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 153 fTGyykkdtPSISGGY------------------------YRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESA 208
Cdd:TIGR01733 325 -GG------PGVARGYlnrpeltaerfvpdpfaggdgarlYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAA 397
|
250
....*....|..
gi 492822008 209 LLEHPAVNEAAV 220
Cdd:TIGR01733 398 LLRHPGVREAVV 409
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
27-285 |
2.79e-30 |
|
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: 118.50 E-value: 2.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 27 IERLGVTSLAGSPTAFRLLMAAGPESAARVKgRLRVASSAGEPL-NPEVIRWFDACLGAPIHDHYGQTELGMVVNNHHGL 105
Cdd:cd05945 184 LAEHGITVWVSTPSFAAMCLLSPTFTPESLP-SLRHFLFCGEVLpHKTARALQQRFPDARIYNTYGPTEATVAVTYIEVT 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 106 EHPVRQG---SAGYAMPGYRIAVLDEAGKEVGPNEPGVLAIdidnspllwfTGyykkdtPSISGGY-------------- 168
Cdd:cd05945 263 PEVLDGYdrlPIGYAKPGAKLVILDEDGRPVPPGEKGELVI----------SG------PSVSKGYlnnpektaaaffpd 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 169 -----YRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILAPGFE 243
Cdd:cd05945 327 egqraYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAE 406
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 492822008 244 --GTPELAEELAlhvkKQLSAHAYPRQIDFVAELPKTPSGKIQR 285
Cdd:cd05945 407 agLTKAIKAELA----ERLPPYMIPRRFVYLDELPLNANGKIDR 446
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
76-289 |
5.95e-30 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 118.58 E-value: 5.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 76 RWFdACLGAPIHDHYGQTELGMVVNNHHgLEHPVRQGSAGYAMPGYRIAVLDEAGKEVGPNEPGVLAIdidNSPLLwFTG 155
Cdd:PRK07059 346 RWL-EMTGCPITEGYGLSETSPVATCNP-VDATEFSGTIGLPLPSTEVSIRDDDGNDLPLGEPGEICI---RGPQV-MAG 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 156 YYKK--DTPSI--SGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEI 231
Cdd:PRK07059 420 YWNRpdETAKVmtADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEA 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 492822008 232 VKAFVIlapgfEGTPEL-AEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLR 289
Cdd:PRK07059 500 VKLFVV-----KKDPALtEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
4-299 |
1.08e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 117.83 E-value: 1.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 4 PLLLGVPTILnEGGFTAENTYDIIERLGVTSLAGSPTAFRLLMAAgPESAARVKGRLRV--ASSAGEPLNPEV-IRWFDA 80
Cdd:PRK06178 273 PLFSGATLVL-LARWDAVAFMAAVERYRVTRTVMLVDNAVELMDH-PRFAEYDLSSLRQvrVVSFVKKLNPDYrQRWRAL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 81 CLGAPIHDHYGQTE--------LGMVVNNHHGLEHPVrqgSAGYAMPGYRIAVLD-EAGKEVGPNEPGVLAIdidNSPLL 151
Cdd:PRK06178 351 TGSVLAEAAWGMTEthtcdtftAGFQDDDFDLLSQPV---FVGLPVPGTEFKICDfETGELLPLGAEGEIVV---RTPSL 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 152 wFTGYYKK---DTPSISGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQR 228
Cdd:PRK06178 425 -LKGYWNKpeaTAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDK 503
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492822008 229 TEIVKAFVILAPGFEGTpelAEELALHVKKQLSAHAYPrQIDFVAELPKTPSGKIqrfllRKAEVEKQQQQ 299
Cdd:PRK06178 504 GQVPVAFVQLKPGADLT---AAALQAWCRENMAVYKVP-EIRIVDALPMTATGKV-----RKQDLQALAEE 565
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
2-282 |
1.45e-29 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 115.17 E-value: 1.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 2 TGPLLLGVPTILNEGGFTAENTYDIIERLGVTSLAGSPTAF-RLLMAAGPESAARVKGRLRVASSAGEPLNPEV-IRWFD 79
Cdd:cd05924 77 FGGLLGGQTVVLPDDRFDPEEVWRTIEKHKVTSMTIVGDAMaRPLIDALRDAGPYDLSSLFAISSGGALLSPEVkQGLLE 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 80 ACLGAPIHDHYGQTELGMVVNNHHGLEHPvrqGSAGYAMPGYRIAVLDEAGKEV--GPNEPGVLAIDiDNSPLlwftGYY 157
Cdd:cd05924 157 LVPNITLVDAFGSSETGFTGSGHSAGSGP---ETGPFTRANPDTVVLDDDGRVVppGSGGVGWIARR-GHIPL----GYY 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 158 K--KDT----PSISGGYYR-TGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTE 230
Cdd:cd05924 229 GdeAKTaetfPEVDGVRYAvPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQ 308
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 492822008 231 IVKAFVILAPGFEGTpelAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGK 282
Cdd:cd05924 309 EVVAVVQLREGAGVD---LEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
11-285 |
1.84e-29 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 117.02 E-value: 1.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 11 TILNEGGFTAENTydiierLGVTSL--AGSPTAFRLLMAAGPESAARVKGR-----LRVASSAGEPLNPEVIRWFDACLG 83
Cdd:PRK13383 244 TVLTHRHFDAEAA------LAQASLhrADAFTAVPVVLARILELPPRVRARnplpqLRVVMSSGDRLDPTLGQRFMDTYG 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 84 APIHDHYGQTELGMvvnnhHGLEHPVRQGSA----GYAMPGYRIAVLDEAGKEVGPNEPGVLAIDIDnsplLWFTGYYKK 159
Cdd:PRK13383 318 DILYNGYGSTEVGI-----GALATPADLRDApetvGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGE----LAGTRYTDG 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 160 DTPSISGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILA 239
Cdd:PRK13383 389 GGKAVVDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLH 468
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 492822008 240 PGFEGTpelAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQR 285
Cdd:PRK13383 469 PGSGVD---AAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLR 511
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
5-282 |
2.08e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 116.91 E-value: 2.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 5 LLLGVPTILNEGG-FTAENTYDIIERLGVTSLAGSPTAFrllmaAGPESAARVKGR------LRVASSAGEPLNPEV-IR 76
Cdd:PRK07798 241 LFSGQTVVLLPDVrFDADEVWRTIEREKVNVITIVGDAM-----ARPLLDALEARGpydlssLFAIASGGALFSPSVkEA 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 77 WFDACLGAPIHDHYGQTELGmvvNNHHGLEHPVRQGSAG-YAMPGYRIAVLDEAGKEVGP--NEPGVLAIDiDNSPLlwf 153
Cdd:PRK07798 316 LLELLPNVVLTDSIGSSETG---FGGSGTVAKGAVHTGGpRFTIGPRTVVLDEDGNPVEPgsGEIGWIARR-GHIPL--- 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 154 tGYYK------KDTPSISGGYYR-TGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDP 226
Cdd:PRK07798 389 -GYYKdpektaETFPTIDGVRYAiPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDE 467
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 492822008 227 QRTEIVKAFVILAPGfeGTPELaEELALHVKKQLSAHAYPRQIDFVAELPKTPSGK 282
Cdd:PRK07798 468 RWGQEVVAVVQLREG--ARPDL-AELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
25-285 |
2.59e-29 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 115.85 E-value: 2.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 25 DIIERLGVTSLAGSPTAFRLLMAAGPESAARVKgrlrvASSAGEPLNPEVIRWFDAcLGAPIHDHYGQTElGMVVNNHHG 104
Cdd:cd12116 211 RLIEAHSITVMQATPATWRMLLDAGWQGRAGLT-----ALCGGEALPPDLAARLLS-RVGSLWNLYGPTE-TTIWSTAAR 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 105 LEHPVRQGSAGYAMPGYRIAVLDEAGKEVGPNEPGVLAIDIDNSPllwfTGYYKK---------DTPSISGG--YYRTGD 173
Cdd:cd12116 284 VTAAAGPIPIGRPLANTQVYVLDAALRPVPPGVPGELYIGGDGVA----QGYLGRpaltaerfvPDPFAGPGsrLYRTGD 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 174 TVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVkAFVILApgfEGTPELAEELA 253
Cdd:cd12116 360 LVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLV-AYVVLK---AGAAPDAAALR 435
|
250 260 270
....*....|....*....|....*....|..
gi 492822008 254 LHVKKQLSAHAYPRQIDFVAELPKTPSGKIQR 285
Cdd:cd12116 436 AHLRATLPAYMVPSAFVRLDALPLTANGKLDR 467
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
25-285 |
4.05e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 116.25 E-value: 4.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 25 DIIERLGVTSLAGSPTAFRLLMAAGPESAARVKGrLRVASSAGEPLNPEVIRWFDACLGAPIHDHYGQTE-----LGMVV 99
Cdd:PRK05605 304 DAMKKHPPTWLPGVPPLYEKIAEAAEERGVDLSG-VRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTEtspiiVGNPM 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 100 NNHHglehpvRQGSAGYAMPG--YRIAVLDEAGKEVGPNEPGVLAIdidNSPLLwFTGYYKK---DTPSISGGYYRTGDT 174
Cdd:PRK05605 383 SDDR------RPGYVGVPFPDteVRIVDPEDPDETMPDGEEGELLV---RGPQV-FKGYWNRpeeTAKSFLDGWFRTGDV 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 175 VEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILAPGFEGTPELAEElal 254
Cdd:PRK05605 453 VVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEGLRA--- 529
|
250 260 270
....*....|....*....|....*....|.
gi 492822008 255 HVKKQLSAHAYPRQIDFVAELPKTPSGKIQR 285
Cdd:PRK05605 530 YCREHLTRYKVPRRFYHVDELPRDQLGKVRR 560
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
90-299 |
9.90e-29 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 115.15 E-value: 9.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 90 YGQTELG-MVVNNHHGLEHpvRQGSAGYAMPGYRIAVLDEAGKEVGPNEPGVLAIdidNSPLLwFTGYYKK--DTPS-IS 165
Cdd:PRK08974 357 YGLTECSpLVSVNPYDLDY--YSGSIGLPVPSTEIKLVDDDGNEVPPGEPGELWV---KGPQV-MLGYWQRpeATDEvIK 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 166 GGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVIlapgfEGT 245
Cdd:PRK08974 431 DGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVV-----KKD 505
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 492822008 246 PEL-AEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRKAEVEKQQQQ 299
Cdd:PRK08974 506 PSLtEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARAKVDNK 560
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
5-291 |
9.97e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 115.26 E-value: 9.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 5 LLLGVPTILNE-GGFTAENTYDIIERLGVTSLAGSPTAFRLLMAAgpesaARVKGR---LRVASSAGEPLNPEVIRWFDA 80
Cdd:PRK07786 238 LLLGAPTVIYPlGAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAE-----QQARPRdlaLRVLSWGAAPASDTLLRQMAA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 81 CL-GAPIHDHYGQTELGMVVNNHHGLEHPVRQGSAGYAMPGYRIAVLDEAGKEVGPNEPGVLaidIDNSPLLwFTGYYKK 159
Cdd:PRK07786 313 TFpEAQILAAFGQTEMSPVTCMLLGEDAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEI---VYRAPTL-MSGYWNN 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 160 DTPS---ISGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFV 236
Cdd:PRK07786 389 PEATaeaFAGGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVA 468
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 492822008 237 ILAPgfeGTPELA-EELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRKA 291
Cdd:PRK07786 469 AVRN---DDAALTlEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRER 521
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
16-289 |
2.16e-28 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 114.15 E-value: 2.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 16 GGFTAEntydiIERLGVTSLAGSPTAFRLLMAAgPESAARVKGRLRVASSAGEPLNPEVIRWFDACLGAPIHDHYGQTEL 95
Cdd:PRK12492 297 PGFIKE-----LGKWRFSALLGLNTLFVALMDH-PGFKDLDFSALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTET 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 96 GMVVN-NHHGleHPVRQGSAGYAMPGYRIAVLDEAGKEVGPNEPGVLAIdidNSPLLwFTGYYKKDTPSI----SGGYYR 170
Cdd:PRK12492 371 SPVAStNPYG--ELARLGTVGIPVPGTALKVIDDDGNELPLGERGELCI---KGPQV-MKGYWQQPEATAealdAEGWFK 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 171 TGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVIL-APGFEgtpelA 249
Cdd:PRK12492 445 TGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVArDPGLS-----V 519
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 492822008 250 EELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLR 289
Cdd:PRK12492 520 EELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELR 559
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
57-297 |
3.50e-28 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 113.54 E-value: 3.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 57 KGRLRVASSAGEPLNPEVIRWFDACL-GAPIHDHYGQTELGMVVNNH------HGLehpVRQGSAGYAMPGYRIAVLD-E 128
Cdd:PLN02330 302 KLKLQAIMTAAAPLAPELLTAFEAKFpGVQVQEAYGLTEHSCITLTHgdpekgHGI---AKKNSVGFILPNLEVKFIDpD 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 129 AGKEVGPNEPGVLAIdidNSPLLwFTGYY--KKDTPSI--SGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFD 204
Cdd:PLN02330 379 TGRSLPKNTPGELCV---RSQCV-MQGYYnnKEETDRTidEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAE 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 205 VESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILAPgfeGTPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQ 284
Cdd:PLN02330 455 LEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINP---KAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIM 531
|
250
....*....|...
gi 492822008 285 RFLLRKAEVEKQQ 297
Cdd:PLN02330 532 RRLLKEKMLSINK 544
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
5-290 |
3.99e-28 |
|
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: 112.05 E-value: 3.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 5 LLLGVPTILNEGgFTAENTYDIIERLGVTSLAGSPTAFRLLMAAGPESAARvkgRLRVASSAGEPLNPEVIrwfDACL-- 82
Cdd:cd05912 140 VIYGMTVYLVDK-FDAEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYPN---NLRCILLGGGPAPKPLL---EQCKek 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 83 GAPIHDHYGQTELGMVVNNHHGLEHPVRQGSAGYAMPGYRIAVLDEAGKEVGPNEPGVLAIDIDNspllwftGYYKKDTP 162
Cdd:cd05912 213 GIPVYQSYGMTETCSQIVTLSPEDALNKIGSAGKPLFPVELKIEDDGQPPYEVGEILLKGPNVTK-------GYLNRPDA 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 163 ---SISGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILA 239
Cdd:cd05912 286 teeSFENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSE 365
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 492822008 240 PGFEgtpelAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRK 290
Cdd:cd05912 366 RPIS-----EEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
1-298 |
1.06e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 112.95 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 1 MTGPLLLGVPtilNEGGFTAENTYDIIERLGVTSLAGSPTAFRLLMAAGpeSAARVKGRLRVASSaGEPLNPE-VIRWFD 79
Cdd:PRK12467 720 ASGATLHLLP---PDCARDAEAFAALMADQGVTVLKIVPSHLQALLQAS--RVALPRPQRALVCG-GEALQVDlLARVRA 793
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 80 ACLGAPIHDHYGQTELGMVVNNHH--GLEHPVRQGSAGYAMPGYRIAVLDeagKEVGPNEPGV----------LAIDIDN 147
Cdd:PRK12467 794 LGPGARLINHYGPTETTVGVSTYElsDEERDFGNVPIGQPLANLGLYILD---HYLNPVPVGVvgelyiggagLARGYHR 870
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 148 SPLLWFTgYYKKDTPSISGG-YYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDP 226
Cdd:PRK12467 871 RPALTAE-RFVPDPFGADGGrLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGD 949
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492822008 227 QRTEIVkAFVILAPGFEGT--PELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRKAEVEKQQQ 298
Cdd:PRK12467 950 AGLQLV-AYLVPAAVADGAehQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAVQA 1022
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
18-291 |
1.11e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 111.96 E-value: 1.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 18 FTAENTYDIIERLGVTSLAGSPTAFRLLMAAGPESAARVKGRLRVASsAGEPLNPEVIRWFDAcLGAPIHDHYGQTEL-G 96
Cdd:PRK08162 257 VDPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAGIDHPVHAMV-AGAAPPAAVIAKMEE-IGFDLTHVYGLTETyG 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 97 MVVNNhhgLEHP--------------VRQGSAGYAMPGyrIAVLD-EAGKEVgPNepgvlaidiDNSPL--------LWF 153
Cdd:PRK08162 335 PATVC---AWQPewdalplderaqlkARQGVRYPLQEG--VTVLDpDTMQPV-PA---------DGETIgeimfrgnIVM 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 154 TGYYKKDTPS---ISGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTE 230
Cdd:PRK08162 400 KGYLKNPKATeeaFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGE 479
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492822008 231 IVKAFVILAPGFEGTpelAEELALHVKKQLSAHAYPRQIDFvAELPKTPSGKIQRFLLRKA 291
Cdd:PRK08162 480 VPCAFVELKDGASAT---EEEIIAHCREHLAGFKVPKAVVF-GELPKTSTGKIQKFVLREQ 536
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
204-282 |
1.30e-27 |
|
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: 102.24 E-value: 1.30e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492822008 204 DVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILAPgfeGTPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGK 282
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKP---GVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
11-285 |
1.96e-27 |
|
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: 108.65 E-value: 1.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 11 TILNEGGFTAENTYDIIERLGVTSLAGSPTAFRLLMAAG-PESAarvkgrLRVASSAGEPLNPEVIRWFDAclGAP---I 86
Cdd:cd17633 68 TFIGQRKFNPKSWIRKINQYNATVIYLVPTMLQALARTLePESK------IKSIFSSGQKLFESTKKKLKN--IFPkanL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 87 HDHYGQTELGMVVNNHHGLEHPVrqGSAGYAMPGYRIAVLDEAGKEVGpnepgVLAIdidNSPLLwFTGYYKKDTpSISG 166
Cdd:cd17633 140 IEFYGTSELSFITYNFNQESRPP--NSVGRPFPNVEIEIRNADGGEIG-----KIFV---KSEMV-FSGYVRGGF-SNPD 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 167 GYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVilapgfEGTP 246
Cdd:cd17633 208 GWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALY------SGDK 281
|
250 260 270
....*....|....*....|....*....|....*....
gi 492822008 247 ELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQR 285
Cdd:cd17633 282 LTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
84-290 |
6.44e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 109.48 E-value: 6.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 84 APIHDHYGQTELGMVVNNHHGlEHPVRQGSAGYAMPGYRIAVLDEAGKEVGPNEPGVLAIdidNSPLLwFTGYYK--KDT 161
Cdd:PRK07638 280 AKLYEFYGASELSFVTALVDE-ESERRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYV---KSPQF-FMGYIIggVLA 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 162 PSISGGYYRTGDTVEFE-PDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVilap 240
Cdd:PRK07638 355 RELNADGWMTVRDVGYEdEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII---- 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 492822008 241 gfEGTpELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRK 290
Cdd:PRK07638 431 --KGS-ATKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKS 477
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
18-294 |
9.85e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 109.48 E-value: 9.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 18 FTAENTYDIIERLGVTSLAGSPTAFrLLMAAGPESAARVKGRLRVASSAGEPLNPEVIRWFDACLGAP-IHDHYGQTELG 96
Cdd:PRK12583 278 FDPLATLQAVEEERCTALYGVPTMF-IAELDHPQRGNFDLSSLRTGIMAGAPCPIEVMRRVMDEMHMAeVQIAYGMTETS 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 97 mVVNNHHGLEHPV--RQGSAGYAMPGYRIAVLDEAGKEVGPNEPGVLAIdidnSPLLWFTGYYKKDTPSISG----GYYR 170
Cdd:PRK12583 357 -PVSLQTTAADDLerRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCT----RGYSVMKGYWNNPEATAESidedGWMH 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 171 TGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILAPGFEGTpelAE 250
Cdd:PRK12583 432 TGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAAS---EE 508
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 492822008 251 ELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRKAEVE 294
Cdd:PRK12583 509 ELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREISIE 552
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
6-285 |
3.25e-26 |
|
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: 105.28 E-value: 3.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 6 LLGVPTILNEGGFTAENTYDIIERLGVTSLAGSPTAFRLLMAAGPESAARVKGrLRVASSAGEPLNPEVIRW------FD 79
Cdd:cd17638 64 LLTGATVVPVAVFDVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSS-LRAAVTGAATVPVELVRRmrselgFE 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 80 ACLGApihdhYGQTELGMVVNNHHGLEHPVRQGSAGYAMPGYRIAVLDEAgkEV---GPN---------EPGVLAIDIDn 147
Cdd:cd17638 143 TVLTA-----YGLTEAGVATMCRPGDDAETVATTCGRACPGFEVRIADDG--EVlvrGYNvmqgylddpEATAEAIDAD- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 148 spllwftgyykkdtpsisgGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQ 227
Cdd:cd17638 215 -------------------GWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDER 275
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 492822008 228 RTEIVKAFVILAPGFEGTpelAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQR 285
Cdd:cd17638 276 MGEVGKAFVVARPGVTLT---EEDVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
4-289 |
4.31e-26 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 108.20 E-value: 4.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 4 PLLLGVPTILNEGGFTAENTYDIIERLGVTSLAGSPTAF-RLLMAAGPESAARVkgrlRVASSAGEPLNPEVI-RWFDAC 81
Cdd:PRK06060 209 PLATGGSAVINSAPVTPEAAAILSARFGPSVLYGVPNFFaRVIDSCSPDSFRSL----RCVVSAGEALELGLAeRLMEFF 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 82 LGAPIHDHYGQTELGMVVNNHHGLEHpvRQGSAGYAMPGYRIAVLDEAGKEVGPNEPGVLaididnspllWFTG------ 155
Cdd:PRK06060 285 GGIPILDGIGSTEVGQTFVSNRVDEW--RLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDL----------WVRGpaiakg 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 156 YYKKDTPSIS-GGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKA 234
Cdd:PRK06060 353 YWNRPDSPVAnEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQA 432
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 492822008 235 FVILAPGfEGtpeLAEELALHVKK----QLSAHAYPRQIDFVAELPKTPSGKIQRFLLR 289
Cdd:PRK06060 433 FLVATSG-AT---IDGSVMRDLHRgllnRLSAFKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
58-226 |
7.34e-26 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 107.11 E-value: 7.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 58 GRLRVASSAGEPLNPEVIRWFDAcLGAPIHDHYGQTELGMVVNNHHglEHPVRQGSAGYAMPGYRIAvLDEAGkEV---G 134
Cdd:COG1022 347 GRLRFAVSGGAALGPELARFFRA-LGIPVLEGYGLTETSPVITVNR--PGDNRIGTVGPPLPGVEVK-IAEDG-EIlvrG 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 135 PNepgVlaididnspllwFTGYYKKD-------TPsisGGYYRTGDTVEFEPDGSISFIGRADDVI-TSSGYRIGPFDVE 206
Cdd:COG1022 422 PN---V------------MKGYYKNPeataeafDA---DGWLHTGDIGELDEDGFLRITGRKKDLIvTSGGKNVAPQPIE 483
|
170 180 190
....*....|....*....|....*....|
gi 492822008 207 SALLEHPAVNEAAVVG----------VPDP 226
Cdd:COG1022 484 NALKASPLIEQAVVVGdgrpflaaliVPDF 513
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
24-289 |
8.15e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 106.71 E-value: 8.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 24 YDIIERLGVTSLAGSPTAFrlLMAAGPESAARVK-GRLRVASSAGEPLNPEVIRWFDACLGAPIHDHYGQTE---LGMVV 99
Cdd:PRK07008 260 YELIEAERVTFSAGVPTVW--LGLLNHMREAGLRfSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEmspLGTLC 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 100 ---NNHHGLEHPVR------QGSAGYampGYRIAVLDEAGKEVgPNEpGVLAIDID-NSPllW-FTGYYKKDTPSISGGY 168
Cdd:PRK07008 338 klkWKHSQLPLDEQrkllekQGRVIY---GVDMKIVGDDGREL-PWD-GKAFGDLQvRGP--WvIDRYFRGDASPLVDGW 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 169 YRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILAPGFEGTpel 248
Cdd:PRK07008 411 FPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVT--- 487
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 492822008 249 AEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLR 289
Cdd:PRK07008 488 REELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLR 528
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
18-289 |
1.95e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 105.35 E-value: 1.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 18 FTAENTYDIIERLGVTSLAGSPTAFRLLMAAgPESAARVKGRLRVASSAGEPLNPEVIRWFDACL-GAPIHDHYGQTEL- 95
Cdd:PRK06145 225 FDPEAVLAAIERHRLTCAWMAPVMLSRVLTV-PDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVFtRARYIDAYGLTETc 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 96 --GMVVNNHHGLEhpvRQGSAGYAMPGYRIAVLDEAGKEVGPNEPGVLAIdidNSPLLwFTGYYK---KDTPSISGGYYR 170
Cdd:PRK06145 304 sgDTLMEAGREIE---KIGSTGRALAHVEIRIADGAGRWLPPNMKGEICM---RGPKV-TKGYWKdpeKTAEAFYGDWFR 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 171 TGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILAPGfeGTPELaE 250
Cdd:PRK06145 377 SGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPG--ATLTL-E 453
|
250 260 270
....*....|....*....|....*....|....*....
gi 492822008 251 ELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLR 289
Cdd:PRK06145 454 ALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLR 492
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
3-290 |
5.36e-25 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 104.82 E-value: 5.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 3 GPLLLGVPTILNEGGFTAENTYD-----IIERLGVTSLAGSPTAFRLLMAAGPEsAARVKG-----RLRVASSAGEPLNP 72
Cdd:PTZ00237 316 GSLSLGNTFVMFEGGIIKNKHIEddlwnTIEKHKVTHTLTLPKTIRYLIKTDPE-ATIIRSkydlsNLKEIWCGGEVIEE 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 73 EVIRWFDACLGAPIHDHYGQTELGMV-VNNHHGLEHPVRqgSAGYAMPGYRIAVLDEAGKEVGPNEPGVLAIDIDNSPLl 151
Cdd:PTZ00237 395 SIPEYIENKLKIKSSRGYGQTEIGITyLYCYGHINIPYN--ATGVPSIFIKPSILSEDGKELNVNEIGEVAFKLPMPPS- 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 152 WFTGYYKKDTP-----SISGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDP 226
Cdd:PTZ00237 472 FATTFYKNDEKfkqlfSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDP 551
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492822008 227 QRTEIVKAFVILAPGFEGTP----ELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRK 290
Cdd:PTZ00237 552 DCYNVPIGLLVLKQDQSNQSidlnKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISK 619
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
60-290 |
7.92e-25 |
|
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: 103.76 E-value: 7.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 60 LRVASSAGEPLNPEVIRWFDACLGAP-IHDHYGQTE--LGMVVNNhhglEHPVRQGSAGYAMPGYRIAVLD-EAGKEVGP 135
Cdd:cd17642 303 LHEIASGGAPLSKEVGEAVAKRFKLPgIRQGYGLTEttSAILITP----EGDDKPGAVGKVVPFFYAKVVDlDTGKTLGP 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 136 NEPGVLAIdidNSPLLwFTGYYKK----DTPSISGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLE 211
Cdd:cd17642 379 NERGELCV---KGPMI-MKGYVNNpeatKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQ 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 212 HPAVNEAAVVGVPDPQRTEIVKAFVILAPGFEGTpelAEELALHVKKQLSAHAYPR-QIDFVAELPKTPSGKIQRFLLRK 290
Cdd:cd17642 455 HPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMT---EKEVMDYVASQVSTAKRLRgGVKFVDEVPKGLTGKIDRRKIRE 531
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
90-289 |
8.42e-25 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 103.61 E-value: 8.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 90 YGQTE-LGMVVNNHHGLEHpvRQGSAGYAMPGYRIAVLDEAGKEVGPNEPGVLAID-IDNSPLlwFTGYYK--KDTPSI- 164
Cdd:PRK08008 319 YGMTEtIVGIIGDRPGDKR--RWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKgVPGKTI--FKEYYLdpKATAKVl 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 165 -SGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILAPGFE 243
Cdd:PRK08008 395 eADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGET 474
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 492822008 244 GTPelaEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLR 289
Cdd:PRK08008 475 LSE---EEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
90-295 |
9.52e-25 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 103.74 E-value: 9.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 90 YGQTElGMVVNNHHGLEHPV--RQGSAGYAMPGYRIAVLD-EAGKEVGPNEPGVLAididnspllwfT-------GYYK- 158
Cdd:PRK08315 348 YGMTE-TSPVSTQTRTDDPLekRVTTVGRALPHLEVKIVDpETGETVPRGEQGELC-----------TrgysvmkGYWNd 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 159 --KDTPSI-SGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAF 235
Cdd:PRK08315 416 peKTAEAIdADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAW 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 236 VILAPGFEGTpelAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRKAEVEK 295
Cdd:PRK08315 496 IILRPGATLT---EEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREMMIEE 552
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
112-295 |
1.06e-24 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 103.12 E-value: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 112 GSAGYAMPGYRIAVLDEaGKEVGPNEPGVLAIdidNSPLLwFTGYYKKDTP---SISGGYYRTGDTVEFEPDGSISFIGR 188
Cdd:PRK03640 307 GSAGKPLFPCELKIEKD-GVVVPPFEEGEIVV---KGPNV-TKGYLNREDAtreTFQDGWFKTGDIGYLDEEGFLYVLDR 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 189 ADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILAPGFEgtpelAEELALHVKKQLSAHAYPRQ 268
Cdd:PRK03640 382 RSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGEVT-----EEELRHFCEEKLAKYKVPKR 456
|
170 180
....*....|....*....|....*..
gi 492822008 269 IDFVAELPKTPSGKIQRFLLRKAEVEK 295
Cdd:PRK03640 457 FYFVEELPRNASGKLLRHELKQLVEEM 483
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
5-285 |
1.32e-24 |
|
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: 102.67 E-value: 1.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 5 LLLGVPTILneggftaENTYDIIERLGVTSLAGsptafRLLMAAgpesaarVKGRLRVASSAGEPLNPEVIRWFDAcLGA 84
Cdd:cd05907 177 VFLAVPRVW-------EKVYAAIKVKAVPGLKR-----KLFDLA-------VGGRLRFAASGGAPLPAELLHFFRA-LGI 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 85 PIHDHYGQTELGMVVNNHHGleHPVRQGSAGYAMPGYRIAvldeagkevgpnepgvlaIDIDNSPLLW----FTGYYKKD 160
Cdd:cd05907 237 PVYEGYGLTETSAVVTLNPP--GDNRIGTVGKPLPGVEVR------------------IADDGEILVRgpnvMLGYYKNP 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 161 TPS----ISGGYYRTGDTVEFEPDGSISFIGRADDVI-TSSGYRIGPFDVESALLEHPAVNEAAVVG----------VPD 225
Cdd:cd05907 297 EATaealDADGWLHTGDLGEIDEDGFLHITGRKKDLIiTSGGKNISPEPIENALKASPLISQAVVIGdgrpflvaliVPD 376
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492822008 226 PqrtEIVKAFVILAPGFEGTP-ELAEELALH---------VKKQLSAHAYPRQIDFVAELP------KTPSGKIQR 285
Cdd:cd05907 377 P---EALEAWAEEHGIAYTDVaELAANPAVRaeieaaveaANARLSRYEQIKKFLLLPEPFtiengeLTPTLKLKR 449
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
3-298 |
1.36e-24 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 103.88 E-value: 1.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 3 GPLLLGVPTILNEGGFT-AENTYDIIERLGVTSLAGSPTAFRLLmAAGPESAARVkGRLRVASSAGEPLNPEVIR-WFDA 80
Cdd:PRK12316 4755 HPLINGASVVIRDDSLWdPERLYAEIHEHRVTVLVFPPVYLQQL-AEHAERDGEP-PSLRVYCFGGEAVAQASYDlAWRA 4832
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 81 CLGAPIHDHYGQTELGMVVNNHHGLEHPVRQGSA---GYAMPGYRIAVLDEAGKEVGPNEPGVLAIDIDnsplLWFTGYY 157
Cdd:PRK12316 4833 LKPVYLFNGYGPTETTVTVLLWKARDGDACGAAYmpiGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGE----GVARGYL 4908
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 158 KKdtPSIS-------------GGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVP 224
Cdd:PRK12316 4909 ER--PALTaerfvpdpfgapgGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQE 4986
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492822008 225 DPQRTEIVkAFVI-----LAPGFEGTPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRKAEVEKQQQ 298
Cdd:PRK12316 4987 GAVGKQLV-GYVVpqdpaLADADEAQAELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDASLLQQ 5064
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
2-289 |
1.51e-24 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 103.00 E-value: 1.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 2 TGPLLLGvPTILNEGGFTAENTYDIIERLGVTSLAGSPTAFRLLMAAGPESAARVKGRLRVASSAGEPLNPEVIRWFDAC 81
Cdd:PLN02574 264 VGLLSLG-STIVVMRRFDASDMVKVIDRFKVTHFPVVPPILMALTKKAKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQT 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 82 LgaPIHDH---YGQTELGMVVNNHHGLEHPVRQGSAGYAMPGYRIAVLD-EAGKEVGPNEPGVLAIDIDNSPLLWFTGYY 157
Cdd:PLN02574 343 L--PHVDFiqgYGMTESTAVGTRGFNTEKLSKYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPK 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 158 KKDTPSISGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVI 237
Cdd:PLN02574 421 ATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVV 500
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 492822008 238 LAPGfegtPELAEELAL-HVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLR 289
Cdd:PLN02574 501 RRQG----STLSQEAVInYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELK 549
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
25-285 |
1.61e-24 |
|
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: 102.33 E-value: 1.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 25 DIIERLGVTSLAGSPTAFRLLMAAGPESaarvkgrLRVASSAGEPLNPE-VIRWfdaCLGAPIHDHYGQTELgMVVNNHH 103
Cdd:cd17652 178 DLLREHRITHVTLPPAALAALPPDDLPD-------LRTLVVAGEACPAElVDRW---APGRRMINAYGPTET-TVCATMA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 104 GLEHPVRQGSAGYAMPGYRIAVLDEAGKEVGPNEPGVLAIdidNSPLLwFTGY----------YKKDTPSISGG-YYRTG 172
Cdd:cd17652 247 GPLPGGGVPPIGRPVPGTRVYVLDARLRPVPPGVPGELYI---AGAGL-ARGYlnrpgltaerFVADPFGAPGSrMYRTG 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 173 DTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILAPgfeGTPELAEEL 252
Cdd:cd17652 323 DLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAP---GAAPTAAEL 399
|
250 260 270
....*....|....*....|....*....|...
gi 492822008 253 ALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQR 285
Cdd:cd17652 400 RAHLAERLPGYMVPAAFVVLDALPLTPNGKLDR 432
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
18-289 |
2.60e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 102.41 E-value: 2.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 18 FTAENTYDIIERLGVTSL--AGSPTAFRLlmaAGPESAARVKGRLRVAssAGEPLNPEVIRWFDACLGAPIHDHYGQTEL 95
Cdd:PRK13388 226 FSASGFLDDVRRYGATYFnyVGKPLAYIL---ATPERPDDADNPLRVA--FGNEASPRDIAEFSRRFGCQVEDGYGSSEG 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 96 GMVVNnhhgLEHPVRQGSAGYAMPGYRI-----------AVLDEAGKEVGPNEpgvlAID--IDNSPLLWFTGYYKKDTP 162
Cdd:PRK13388 301 AVIVV----REPGTPPGSIGRGAPGVAIynpetltecavARFDAHGALLNADE----AIGelVNTAGAGFFEGYYNNPEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 163 S---ISGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILA 239
Cdd:PRK13388 373 TaerMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLR 452
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 492822008 240 PGFEGTPELAEELaLHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLR 289
Cdd:PRK13388 453 DGATFDPDAFAAF-LAAQPDLGTKAWPRYVRIAADLPSTATNKVLKRELI 501
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
29-292 |
3.25e-24 |
|
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: 102.02 E-value: 3.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 29 RLGVTSLagSPTAFRLLMAAGPESAARvkgrLRVASSAGEPLNPEVIR-WFDACLGAP-IHDHYGQTELGMVVNNHHGLE 106
Cdd:cd17655 228 RITIIDL--TPAHLKLLDAADDSEGLS----LKHLIVGGEALSTELAKkIIELFGTNPtITNAYGPTETTVDASIYQYEP 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 107 HPVRQGSA--GYAMPGYRIAVLDEAGKEVGPNEPGVLAIDIDNSPllwfTGYYKK---------DTPSISGG-YYRTGDT 174
Cdd:cd17655 302 ETDQQVSVpiGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVA----RGYLNRpeltaekfvDDPFVPGErMYRTGDL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 175 VEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILAPGFEgTPELAEELAl 254
Cdd:cd17655 378 ARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELP-VAQLREFLA- 455
|
250 260 270
....*....|....*....|....*....|....*...
gi 492822008 255 hvkKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRKAE 292
Cdd:cd17655 456 ---RELPDYMIPSYFIKLDEIPLTPNGKVDRKALPEPD 490
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
18-290 |
8.82e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 100.91 E-value: 8.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 18 FTAENTYDIIERLGVTSL--AGSPTAFRLlmaAGPESAARVKGRLRVAssAGEPLNPEVIRWFDACLGAPIHDHYGQTEL 95
Cdd:PRK07867 228 FSASGFLPDVRRYGATYAnyVGKPLSYVL---ATPERPDDADNPLRIV--YGNEGAPGDIARFARRFGCVVVDGFGSTEG 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 96 GMVVNNHHGlehpVRQGSAGYAMPGyrIAVLD-EAGKEVGPNE---PGVLAIDIDNSPLL------WFTGYYKK---DTP 162
Cdd:PRK07867 303 GVAITRTPD----TPPGALGPLPPG--VAIVDpDTGTECPPAEdadGRLLNADEAIGELVntagpgGFEGYYNDpeaDAE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 163 SISGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILAPGF 242
Cdd:PRK07867 377 RMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGA 456
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 492822008 243 EGTPELAEELaLHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRK 290
Cdd:PRK07867 457 KFDPDAFAEF-LAAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
21-298 |
2.74e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 100.24 E-value: 2.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 21 ENTYDIIERLGVTSLAGSPTAFRLLMAAGPESAARVKgrLRVASSAGEPLNPEVIR-WFDACLGAPIHDHYGQTELGMVV 99
Cdd:PRK12467 1799 EQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHPLS--LRRVVCGGEALEVEALRpWLERLPDTGLFNLYGPTETAVDV 1876
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 100 NnHHGLEHPVRQGSA----GYAMPGYRIAVLDEagkEVGPNEPGV----------LAIDIDNSPLLWFTGYYKKDTPSIS 165
Cdd:PRK12467 1877 T-HWTCRRKDLEGRDsvpiGQPIANLSTYILDA---SLNPVPIGVagelylggvgLARGYLNRPALTAERFVADPFGTVG 1952
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 166 GGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILAPGFEGT 245
Cdd:PRK12467 1953 SRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQDGANGKQLVAYVVPTDPGLVDD 2032
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 492822008 246 PE----LAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRKAEVEKQQQ 298
Cdd:PRK12467 2033 DEaqvaLRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDASELQQ 2089
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
4-298 |
4.27e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 99.65 E-value: 4.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 4 PLLLGVPTILNEGG-FTAENTYDIIERLGVTSLAGSPTAFRLLMaagpeSAARVKGR---LRVASSAGEPLNPEVIR-WF 78
Cdd:PRK12316 2208 PLLNGARVLIRDDElWDPEQLYDEMERHGVTILDFPPVYLQQLA-----EHAERDGRppaVRVYCFGGEAVPAASLRlAW 2282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 79 DACLGAPIHDHYGQTELGMVVNNHHGleHPVRQGSAGYAMPGYRIA-----VLDEAGKEVGPNEPGVLAIDID------- 146
Cdd:PRK12316 2283 EALRPVYLFNGYGPTEAVVTPLLWKC--RPQDPCGAAYVPIGRALGnrrayILDADLNLLAPGMAGELYLGGEglargyl 2360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 147 NSPLLWFTGYYKKDTPSISGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDP 226
Cdd:PRK12316 2361 NRPGLTAERFVPDPFSASGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGA 2440
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492822008 227 QRTEIVkAFVIlapGFEGTPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRKAEVEKQQQ 298
Cdd:PRK12316 2441 SGKQLV-AYVV---PDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLRQ 2508
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
1-283 |
5.52e-23 |
|
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: 98.24 E-value: 5.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 1 MTGPLLLGVPtilNEGGFTAENTYDIIERLGVTSLAGSPTAFRLLMAAGPESaarvkgrLRVASSAGEPLNPEVIRWFDA 80
Cdd:cd17648 160 LNGQKLVVPP---DEMRFDPDRFYAYINREKVTYLSGTPSVLQQYDLARLPH-------LKRVDAAGEEFTAPVFEKLRS 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 81 CLGAPIHDHYGQTElgMVVNNHHGLEHPVRQ--GSAGYAMPGYRIAVLDEAGKEVGPNEPGVLAIDID-------NSPLL 151
Cdd:cd17648 230 RFAGLIINAYGPTE--TTVTNHKRFFPGDQRfdKSLGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDgvargylNRPEL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 152 ----WFTGYYKKDTPSISGGY---YRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVP 224
Cdd:cd17648 308 taerFLPNPFQTEQERARGRNarlYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKE 387
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492822008 225 DPQRTE--IVKAFVILAPGFEGTPELAEELAlHVKKQLSAHAYPRQIDFVAELPKTPSGKI 283
Cdd:cd17648 388 DASQAQsrIQKYLVGYYLPEPGHVPESDLLS-FLRAKLPRYMVPARLVRLEGIPVTINGKL 447
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
83-291 |
8.95e-23 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 98.03 E-value: 8.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 83 GAPIHDHYGQTEL--GMVVNNHHGLEHpvrQGSAGYAMPGYRIAVLDEAGKEVGPNEPGVLAIdidNSPLLwFTGYYKK- 159
Cdd:PRK08751 354 GLTLVEAYGLTETspAACINPLTLKEY---NGSIGLPIPSTDACIKDDAGTVLAIGEIGELCI---KGPQV-MKGYWKRp 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 160 -DTPSI--SGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFV 236
Cdd:PRK08751 427 eETAKVmdADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVI 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 492822008 237 IlapgfEGTPEL-AEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRKA 291
Cdd:PRK08751 507 V-----KKDPALtAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRDA 557
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
4-299 |
3.02e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 96.95 E-value: 3.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 4 PLLLGVPTILNeGGFTAENTYDIIERLGVTSLAGSPTAFRLLMAAGPESAARVKGRLRVASSAGEPLNPEVI-RWFdacL 82
Cdd:PRK12316 3258 PLMSGARVVLA-GPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQqQVF---A 3333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 83 GAPIHDHYGQTELGMVVNNHHGLEHPVRQGSAGYAMPGYRIAVLDEAGKEVGPNEPG-------VLAIDIDNSPLLwFTG 155
Cdd:PRK12316 3334 GLPLYNLYGPTEATITVTHWQCVEEGKDAVPIGRPIANRACYILDGSLEPVPVGALGelylggeGLARGYHNRPGL-TAE 3412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 156 YYKKDTPSISGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQrteiVKAF 235
Cdd:PRK12316 3413 RFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDGRQ----LVAY 3488
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492822008 236 VILApgfEGTPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRKAEVEKQQQQ 299
Cdd:PRK12316 3489 VVPE---DEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQQD 3549
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
19-289 |
3.26e-22 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 96.63 E-value: 3.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 19 TAENTYDIIERLGVTSLAGSPTAFRLLMAAGPESAARVKGRLRVASSAGEPlnPEVIRWFDACLGAPIHDHYGQTE-LGM 97
Cdd:PLN03102 262 TAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPP--PAALVKKVQRLGFQVMHAYGLTEaTGP 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 98 VV-----------NNHHGLEHPVRQGSAGYAMPgyRIAVLDEAGKEVGPNEPGVLA-IDIDNSPLLwfTGYYKKDTPSIS 165
Cdd:PLN03102 340 VLfcewqdewnrlPENQQMELKARQGVSILGLA--DVDVKNKETQESVPRDGKTMGeIVIKGSSIM--KGYLKNPKATSE 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 166 G---GYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILAPGF 242
Cdd:PLN03102 416 AfkhGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGE 495
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 492822008 243 EGTPELAEELAL-------HVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLR 289
Cdd:PLN03102 496 TTKEDRVDKLVTrerdlieYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLR 549
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
11-289 |
4.80e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 95.97 E-value: 4.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 11 TILNEGGFTAENTYDIIERLGVTSLAGSPTAFRLLMAAGPESA----ARVKGRLRVASSAGEplnpeVIRWFDAcLGAPI 86
Cdd:PRK06164 249 PLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERAdfpsARLFGFASFAPALGE-----LAALARA-RGVPL 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 87 HDHYGQTELGMVVNNHHgLEHPVR---QGSAGYAMPGYRIAVLDEAGKEVGPN-EPGVLAIdidNSPLLwFTGYYkkDTP 162
Cdd:PRK06164 323 TGLYGSSEVQALVALQP-ATDPVSvriEGGGRPASPEARVRARDPQDGALLPDgESGEIEI---RAPSL-MRGYL--DNP 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 163 SISG------GYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVkAFV 236
Cdd:PRK06164 396 DATAraltddGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGKTVPV-AFV 474
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 492822008 237 ILAPgfeGTPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSG---KIQRFLLR 289
Cdd:PRK06164 475 IPTD---GASPDEAGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLR 527
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
155-289 |
5.02e-22 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 95.68 E-value: 5.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 155 GYYKK---DTPSISGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEI 231
Cdd:PLN02479 415 GYLKNpkaNEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGES 494
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 232 VKAFVILAPGFEGTPE--LAEELALHVKKQLSAHAYPRQIDFvAELPKTPSGKIQRFLLR 289
Cdd:PLN02479 495 PCAFVTLKPGVDKSDEaaLAEDIMKFCRERLPAYWVPKSVVF-GPLPKTATGKIQKHVLR 553
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
20-290 |
7.08e-22 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 95.44 E-value: 7.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 20 AENTYDIIERLGVTSLAGSPTAFRLLMAAGPESAARVKGR-LRVASSAGEPLNPEVIRWFDACLGAPIHDHYGQTElGMV 98
Cdd:PRK10946 261 ATLCFPLIEKHQVNVTALVPPAVSLWLQAIAEGGSRAQLAsLKLLQVGGARLSETLARRIPAELGCQLQQVFGMAE-GLV 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 99 vnNHHGLEHPVRQ--GSAGYAM-PGYRIAVLDEAGKEVGPNEPGVLAIdidNSPLLwFTGYYKkdTPSI------SGGYY 169
Cdd:PRK10946 340 --NYTRLDDSDERifTTQGRPMsPDDEVWVADADGNPLPQGEVGRLMT---RGPYT-FRGYYK--SPQHnasafdANGFY 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 170 RTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILApgfegTPELA 249
Cdd:PRK10946 412 CSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVK-----EPLKA 486
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 492822008 250 EELALHVKKQLSA-HAYPRQIDFVAELPKTPSGKIQRFLLRK 290
Cdd:PRK10946 487 VQLRRFLREQGIAeFKLPDRVECVDSLPLTAVGKVDKKQLRQ 528
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
3-296 |
7.43e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 96.00 E-value: 7.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 3 GPLLLGVPTILNEGG-FTAENTYDIIERLGVTSLAGSPTAFRLLMA-AGPESAARVKgrlRVASSaGEPLNPEVIRWFDA 80
Cdd:PRK12467 3298 WTLICGGCLVVRDNDlWDPEELWQAIHAHRISIACFPPAYLQQFAEdAGGADCASLD---IYVFG-GEAVPPAAFEQVKR 3373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 81 CLG-APIHDHYGQTELGMVVNNHHGLEHPVRQGSA---GYAMPGYRIAVLDEAGKEVGPNEPGVLAIDIDnsplLWFTGY 156
Cdd:PRK12467 3374 KLKpRGLTNGYGPTEAVVTVTLWKCGGDAVCEAPYapiGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGV----GLARGY 3449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 157 YKK----------DTPSISGG-YYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPD 225
Cdd:PRK12467 3450 HQRpsltaerfvaDPFSGSGGrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDG 3529
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492822008 226 PQRTEIVKAFVILAPGfegtPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRKAEVEKQ 296
Cdd:PRK12467 3530 AGGKQLVAYVVPADPQ----GDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKGS 3596
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
16-285 |
8.01e-22 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 95.34 E-value: 8.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 16 GGFTAENTYDIIERLGVTSLAGSPTAFRLLMA-AGPESAARVKGRLRVASSAGEPLNPEVIRWFDACLGAPIHDHYGQTE 94
Cdd:PRK05852 252 GRFSAHTFWDDIKAVGATWYTAVPTIHQILLErAATEPSGRKPAALRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 95 LGMVVNN------HHGLEHPVRQGSAGYAMpGYRIAVLDEAGKEVGPNEPGVLaididnspllWFTGY-----YKKDtPS 163
Cdd:PRK05852 332 ATHQVTTtqiegiGQTENPVVSTGLVGRST-GAQIRIVGSDGLPLPAGAVGEV----------WLRGTtvvrgYLGD-PT 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 164 ISG-----GYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVIL 238
Cdd:PRK05852 400 ITAanftdGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVP 479
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 492822008 239 ApgfEGTPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQR 285
Cdd:PRK05852 480 R---ESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDR 523
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
5-295 |
8.48e-22 |
|
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: 95.42 E-value: 8.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 5 LLLGVPTILNEG--GFTAENT-YDIIERLGVTSLAGSPTAFRLLMAAGPESAARVK-GRLRVASSAGEPLNPEVIRWFDA 80
Cdd:cd05943 312 LAVGATIVLYDGspFYPDTNAlWDLADEEGITVFGTSAKYLDALEKAGLKPAETHDlSSLRTILSTGSPLKPESFDYVYD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 81 CLGAPIH--DHYGQTEL-----GMVVNnhhgleHPVRQGSAGYAMPGYRIAVLDEAGKEVgPNEPGVLAI---------- 143
Cdd:cd05943 392 HIKPDVLlaSISGGTDIiscfvGGNPL------LPVYRGEIQCRGLGMAVEAFDEEGKPV-WGEKGELVCtkpfpsmpvg 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 144 ---DIDNSPllwftgyYKKDTPSISGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAV 220
Cdd:cd05943 465 fwnDPDGSR-------YRAAYFAKYPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLV 537
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492822008 221 VGVPDPQRTEIVKAFVILAPGFEGTPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRK----AEVEK 295
Cdd:cd05943 538 VGQEWKDGDERVILFVKLREGVELDDELRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKVEVAVKKiiagRPVKN 616
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
113-297 |
9.11e-22 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 94.68 E-value: 9.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 113 SAGYAMPGYRIavldeagkEVGPNEPGVLAIDidnSPLLwFTGYYkkdtPSI--SGGYYRTGDTVEFEPDGSISFIGRAD 190
Cdd:PRK07445 284 SSGQVLPHAQI--------TIPANQTGNITIQ---AQSL-ALGYY----PQIldSQGIFETDDLGYLDAQGYLHILGRNS 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 191 DVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILAPGfEGTPelaEELALHVKKQLSAHAYPRQID 270
Cdd:PRK07445 348 QKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDP-SISL---EELKTAIKDQLSPFKQPKHWI 423
|
170 180
....*....|....*....|....*..
gi 492822008 271 FVAELPKTPSGKIQRFLLRKAEVEKQQ 297
Cdd:PRK07445 424 PVPQLPRNPQGKINRQQLQQIAVQRLG 450
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
167-290 |
3.53e-21 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 92.03 E-value: 3.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 167 GYYRTGDTVEFEpDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILAPGfeGTP 246
Cdd:PRK07824 234 GWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGG--PAP 310
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 492822008 247 ELaEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRK 290
Cdd:PRK07824 311 TL-EALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVR 353
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
115-285 |
3.60e-21 |
|
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: 93.10 E-value: 3.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 115 GYAMPGYRIAVLDEAGKEVGPNEPGVLAIDIDNSPLlwftGYY----KKDTPSIS----GGYYRTGDTVEFEPDGSISFI 186
Cdd:cd12114 303 GRPLANQRYRVLDPRGRDCPDWVPGELWIGGRGVAL----GYLgdpeLTAARFVThpdgERLYRTGDLGRYRPDGTLEFL 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 187 GRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVkAFVILAPGfeGTPELAEELALHVKKQLSAHAYP 266
Cdd:cd12114 379 GRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRLA-AFVVPDND--GTPIAPDALRAFLAQTLPAYMIP 455
|
170
....*....|....*....
gi 492822008 267 RQIDFVAELPKTPSGKIQR 285
Cdd:cd12114 456 SRVIALEALPLTANGKVDR 474
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
3-298 |
5.33e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 93.48 E-value: 5.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 3 GPLLLGVPTIL--NEGGFTAENTYDIIERLGVTSLAGSPTAFR-LLMAAGPESAARvkgrLRVASSAGEPLNPEVIRWFD 79
Cdd:PRK12316 716 WPLMSGARLVVaaPGDHRDPAKLVELINREGVDTLHFVPSMLQaFLQDEDVASCTS----LRRIVCSGEALPADAQEQVF 791
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 80 ACL-GAPIHDHYGQTELGMVVNNHHGLEHPVRQGSAGYAMPGYRIAVLDEAGkevGPNEPGVLA-IDIDNSPLLwfTGYY 157
Cdd:PRK12316 792 AKLpQAGLYNLYGPTEAAIDVTHWTCVEEGGDSVPIGRPIANLACYILDANL---EPVPVGVLGeLYLAGRGLA--RGYH 866
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 158 KKD---------TPSISGG-YYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVpdpQ 227
Cdd:PRK12316 867 GRPgltaerfvpSPFVAGErMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV---D 943
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492822008 228 RTEIVKAFVILAPGfegtPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRKAEVEKQQQ 298
Cdd:PRK12316 944 GKQLVGYVVLESEG----GDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASVAQQ 1010
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
21-290 |
1.48e-20 |
|
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: 91.34 E-value: 1.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 21 ENTYDIIERLGVTSLAGSPTAFRLLMAAGPESAARVKGRLRVASSAGEPlnPEVIRWFDACLGAPIHDHYGQTE---LGM 97
Cdd:cd05915 234 ASLVELFDGEGVTFTAGVPTVWLALADYLESTGHRLKTLRRLVVGGSAA--PRSLIARFERMGVEVRQGYGLTEtspVVV 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 98 ---------VVNNHHGLEHPVRQGSAGYAMPgyrIAVLDEAGKEVGPNEPGVLAIDIDNSPLLwfTGYYK----KDTPSI 164
Cdd:cd05915 312 qnfvkshleSLSEEEKLTLKAKTGLPIPLVR---LRVADEEGRPVPKDGKALGEVQLKGPWIT--GGYYGneeaTRSALT 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 165 SGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILapgfEG 244
Cdd:cd05915 387 PDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVP----RG 462
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 492822008 245 TPELAEELALHVKKQL-SAHAYPRQIDFVAELPKTPSGKIQRFLLRK 290
Cdd:cd05915 463 EKPTPEELNEHLLKAGfAKWQLPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
19-285 |
1.49e-20 |
|
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: 90.01 E-value: 1.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 19 TAENTYDIIERLGVTSLAGSPTAFRLLMAAGPESAARVKgRLRVASSAGEPLNPEVIRWFDACLGAPIHDHYGQTELGMV 98
Cdd:cd17635 79 TYKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVP-SLRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSETGTA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 99 --VNNHHGLehpVRQGSAGYAMPGYRIAVLDEAGKEVGPNEPGVLAIdidNSPllWF-TGYYK--KDTPSI-SGGYYRTG 172
Cdd:cd17635 158 lcLPTDDDS---IEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWI---KSP--ANmLGYWNnpERTAEVlIDGWVNTG 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 173 DTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILAPgfEGTPELAEEL 252
Cdd:cd17635 230 DLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASA--ELDENAIRAL 307
|
250 260 270
....*....|....*....|....*....|...
gi 492822008 253 ALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQR 285
Cdd:cd17635 308 KHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
25-295 |
7.06e-20 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 89.47 E-value: 7.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 25 DIIERLGVTSLAGSPTAFRLLMAAG--PESAARVkGRLRVASSAGEPLNPEVIRWF------DACLgAPIHdhyGQTEL- 95
Cdd:PRK03584 349 DLAAEEGVTVFGTSAKYLDACEKAGlvPGETHDL-SALRTIGSTGSPLPPEGFDWVyehvkaDVWL-ASIS---GGTDIc 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 96 -GMVVNNHhglEHPVRQGSAGYAMPGYRIAVLDEAGKEVGpNEPGVLAI-------------DIDNSPLL--WFTGYykk 159
Cdd:PRK03584 424 sCFVGGNP---LLPVYRGEIQCRGLGMAVEAWDEDGRPVV-GEVGELVCtkpfpsmplgfwnDPDGSRYRdaYFDTF--- 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 160 dtPsisgGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILA 239
Cdd:PRK03584 497 --P----GVWRHGDWIEITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLA 570
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 240 PGFEGTPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQ----RFLLRKAEVEK 295
Cdd:PRK03584 571 EGVTLDDALRARIRTTIRTNLSPRHVPDKIIAVPDIPRTLSGKKVelpvKKLLHGRPVKK 630
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
9-293 |
7.93e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 88.55 E-value: 7.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 9 VPTILneggfTAENTYDIIERLGVTS---LAGSPTAFRLLMAAGPEsaarvKGRLRVASSAGEPLnPEviRWFDACLGAP 85
Cdd:PRK08308 170 KPVII-----TNKNPKFALNILRNTPqhiLYAVPLMLHILGRLLPG-----TFQFHAVMTSGTPL-PE--AWFYKLRERT 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 86 IH--DHYGQTELGMVVNNHHGLEHpvrqGSAGYAMPGYRIavldEAGKevGPNEPGVLAIDIDNSPLlwftgyykkdtps 163
Cdd:PRK08308 237 TYmmQQYGCSEAGCVSICPDMKSH----LDLGNPLPHVSV----SAGS--DENAPEEIVVKMGDKEI------------- 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 164 isggyyRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVIlAPGFE 243
Cdd:PRK08308 294 ------FTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVI-SHEEI 366
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 492822008 244 GTPELAEelalHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRKAEV 293
Cdd:PRK08308 367 DPVQLRE----WCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLELGEV 412
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
59-288 |
6.34e-19 |
|
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: 86.71 E-value: 6.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 59 RLRVASSAGEPLNPEVIRWFDAcLGAPIHDHYGQTELGMVVNNHHglEHPVRQGSAGYAMPGYRIAVlDEAGkEVGPNEP 138
Cdd:cd17641 325 RLRSAATGGAALGPDTFRFFHA-IGVPLKQLYGQTELAGAYTVHR--DGDVDPDTVGVPFPGTEVRI-DEVG-EILVRSP 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 139 GVlaididnspllwFTGYYKKDTPSIS----GGYYRTGDTVEFEPDGSISFIGRADDV-ITSSGYRIGPFDVESALLEHP 213
Cdd:cd17641 400 GV------------FVGYYKNPEATAEdfdeDGWLHTGDAGYFKENGHLVVIDRAKDVgTTSDGTRFSPQFIENKLKFSP 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 214 AVNEAAVVGVPDPQRTEIVKA-FVILAPGFE-------------GTPELAEELALHVKKqlsahayprqidFVAELPktP 279
Cdd:cd17641 468 YIAEAVVLGAGRPYLTAFICIdYAIVGKWAEqrgiafttytdlaSRPEVYELIRKEVEK------------VNASLP--E 533
|
....*....
gi 492822008 280 SGKIQRFLL 288
Cdd:cd17641 534 AQRIRRFLL 542
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
18-285 |
6.93e-19 |
|
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: 86.33 E-value: 6.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 18 FTAENTYDIIERLGVTSLAGSPTAFRLLMAAGPESAARVKGRLRVASSAGEPLNPE-VIRWFDACLGAP-IHDHYGQTEL 95
Cdd:cd17644 184 SSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLPSSLRLVIVGGEAVQPElVRQWQKNVGNFIqLINVYGPTEA 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 96 GMVVNNHHGLEHPVRQGSA---GYAMPGYRIAVLDEAGKEVGPNEPGVLAI-------DIDNSPLL----WFTGYYKKDT 161
Cdd:cd17644 264 TIAATVCRLTQLTERNITSvpiGRPIANTQVYILDENLQPVPVGVPGELHIggvglarGYLNRPELtaekFISHPFNSSE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 162 PSisgGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVIlaPG 241
Cdd:cd17644 344 SE---RLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIV--PH 418
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 492822008 242 FEGTPeLAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQR 285
Cdd:cd17644 419 YEESP-STVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDR 461
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
58-288 |
2.94e-18 |
|
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: 84.42 E-value: 2.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 58 GRLRVASSAGEPLNPEVIRWFDAcLGAPIHDHYGQTELGMVV-----NNhhglehpVRQGSAGYAMPGYRIAVLDEAGKe 132
Cdd:cd05914 234 GNIKEFVIGGAKINPDVEEFLRT-IGFPYTIGYGMTETAPIIsysppNR-------IRLGSAGKVIDGVEVRIDSPDPA- 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 133 vgpNEPGVLAIDIDNSPLlwftGYYKKD--TPSI--SGGYYRTGDTVEFEPDGSISFIGRADDVI-TSSGYRIGPFDVES 207
Cdd:cd05914 305 ---TGEGEIIVRGPNVMK----GYYKNPeaTAEAfdKDGWFHTGDLGKIDAEGYLYIRGRKKEMIvLSSGKNIYPEEIEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 208 ALLEHPAVNEAAVVgvpdpQRTEIVKAFVILAPGFE-----GTPELAEELALHVKKQLS--AHAYPRQIDFV---AELPK 277
Cdd:cd05914 378 KINNMPFVLESLVV-----VQEKKLVALAYIDPDFLdvkalKQRNIIDAIKWEVRDKVNqkVPNYKKISKVKivkEEFEK 452
|
250
....*....|.
gi 492822008 278 TPSGKIQRFLL 288
Cdd:cd05914 453 TPKGKIKRFLY 463
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
27-291 |
3.22e-18 |
|
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: 84.52 E-value: 3.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 27 IERLGVTSLAGSPTAFRLLmaaGPESAARvkgrLRVASSAGEPLNPEVI-RWfdaCLGAPIHDHYGQTE--LGMVVNNHH 103
Cdd:cd05918 191 INRLRVTWAFLTPSVARLL---DPEDVPS----LRTLVLGGEALTQSDVdTW---ADRVRLINAYGPAEctIAATVSPVV 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 104 GLEHPvrqGSAGYAMPGyRIAVLDEA--GKEVGPNEPGVLAIDidnSPLLwFTGYY-----------------KKDTPSI 164
Cdd:cd05918 261 PSTDP---RNIGRPLGA-TCWVVDPDnhDRLVPIGAVGELLIE---GPIL-ARGYLndpektaaafiedpawlKQEGSGR 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 165 SGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGV---PDPQRTEIVKAFVILAPG 241
Cdd:cd05918 333 GRRLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVvkpKDGSSSPQLVAFVVLDGS 412
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492822008 242 FEGTP----------ELAEELALHVKKQLSAH--AY--PRQIDFVAELPKTPSGKIQRFLLRKA 291
Cdd:cd05918 413 SSGSGdgdslflepsDEFRALVAELRSKLRQRlpSYmvPSVFLPLSHLPLTASGKIDRRALREL 476
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
152-290 |
4.43e-18 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 84.06 E-value: 4.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 152 WFTG-YYKKDTPSISG--------------------GYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALL 210
Cdd:PRK05620 394 WVTAsYYHSPTEEGGGaastfrgedvedandrftadGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIM 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 211 EHPAVNEAAVVGVPDPQRTEIVKAFVILAPGFEGTPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRK 290
Cdd:PRK05620 474 AAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQ 553
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
58-222 |
4.94e-18 |
|
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: 83.95 E-value: 4.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 58 GRLRVASSAGEPLNPEVIRWFDAcLGAPIHDHYGQTELGMVVNNHHgLEHPVRqGSAGYAMPGYRIAVLDEAGKEVGPne 137
Cdd:cd17640 213 GIFKFGISGGGALPPHVDTFFEA-IGIEVLNGYGLTETSPVVSARR-LKCNVR-GSVGRPLPGTEIKIVDPEGNVVLP-- 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 138 PGVLAIDIDNSPLLwFTGYYKK--DTPSI--SGGYYRTGDTVEFEPDGSISFIGRADDVIT-SSGYRIGPFDVESALLEH 212
Cdd:cd17640 288 PGEKGIVWVRGPQV-MKGYYKNpeATSKVldSDGWFNTGDLGWLTCGGELVLTGRAKDTIVlSNGENVEPQPIEEALMRS 366
|
170
....*....|
gi 492822008 213 PAVNEAAVVG 222
Cdd:cd17640 367 PFIEQIMVVG 376
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
4-283 |
6.81e-18 |
|
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: 83.53 E-value: 6.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 4 PLLLGVPTILNEGGFTAENTYDIIERLGVTSLAGSPTAFR-LLMAAGPESAARvkgrLRVASSAGEPLNPEVIRWFDACL 82
Cdd:cd05909 210 PLLSGIKVVFHPNPLDYKKIPELIYDKKATILLGTPTFLRgYARAAHPEDFSS----LRLVVAGAEKLKDTLRQEFQEKF 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 83 GAPIHDHYGQTELGMV--VNNHhglEHPVRQGSAGYAMPGYRIAVLDEAGK-EVGPNEPGVLAIDIDNSpllwFTGYYKK 159
Cdd:cd05909 286 GIRILEGYGTTECSPVisVNTP---QSPNKEGTVGRPLPGMEVKIVSVETHeEVPIGEGGLLLVRGPNV----MLGYLNE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 160 DTPS---ISGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEH-PAVNEAAVVGVPDPQRTEIVKAF 235
Cdd:cd05909 359 PELTsfaFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLL 438
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 492822008 236 VilapgfegTPELAEELALH--VKK-QLSAHAYPRQIDFVAELPKTPSGKI 283
Cdd:cd05909 439 T--------TTTDTDPSSLNdiLKNaGISNLAKPSYIHQVEEIPLLGTGKP 481
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
160-299 |
9.75e-18 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 83.68 E-value: 9.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 160 DTPSISGG-YYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFV-- 236
Cdd:PRK05691 2560 DPFAADGGrLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPSGKQLAGYLVsa 2639
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492822008 237 ILAPGFEGTPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRKAEVEKQQQQ 299
Cdd:PRK05691 2640 VAGQDDEAQAALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPDPELNRQA 2702
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
18-290 |
1.80e-17 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 82.54 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 18 FTAENTYDIIERLGVTSLAGSPTAFRLLMAAGPESAAR-----VKGRLRVASSAGEPLNPEVIRWFDAclgAPIHDHYGQ 92
Cdd:PLN02860 247 FDAKAALQAIKQHNVTSMITVPAMMADLISLTRKSMTWkvfpsVRKILNGGGSLSSRLLPDAKKLFPN---AKLFSAYGM 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 93 TE----LGMVVNNHHGLEHPvRQGSAGYAMPgYRIAVLDEAGKEVGPNEPGV-LAIDIDNSPLLW--FT------GYYKK 159
Cdd:PLN02860 324 TEacssLTFMTLHDPTLESP-KQTLQTVNQT-KSSSVHQPQGVCVGKPAPHVeLKIGLDESSRVGriLTrgphvmLGYWG 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 160 DTPSISG-----GYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKA 234
Cdd:PLN02860 402 QNSETASvlsndGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVA 481
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492822008 235 FVIL----------APGFEGTPELAEE-LALHVKKQ-LSAHAYPRQIDFVAE-LPKTPSGKIQRFLLRK 290
Cdd:PLN02860 482 CVRLrdgwiwsdneKENAKKNLTLSSEtLRHHCREKnLSRFKIPKLFVQWRKpFPLTTTGKIRRDEVRR 550
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
25-290 |
3.05e-17 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 81.57 E-value: 3.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 25 DIIERLGVTSLAGSPTAFrLLMAAGPESAARVKGRLRVASSAGEPLNPEVIRWFDACL-GAPIHDHYGQTELGMVVNNHH 103
Cdd:PLN02246 266 ELIQRHKVTIAPFVPPIV-LAIAKSPVVEKYDLSSIRMVLSGAAPLGKELEDAFRAKLpNAVLGQGYGMTEAGPVLAMCL 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 104 GLEH---PVRQGSAGYAMPGYRIAVLD-EAGKEVGPNEPGvlAIDIDNSPLLwfTGYYK----------KDtpsisgGYY 169
Cdd:PLN02246 345 AFAKepfPVKSGSCGTVVRNAELKIVDpETGASLPRNQPG--EICIRGPQIM--KGYLNdpeatantidKD------GWL 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 170 RTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILAPGFEGTpelA 249
Cdd:PLN02246 415 HTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEIT---E 491
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 492822008 250 EELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRK 290
Cdd:PLN02246 492 DEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRA 532
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
25-285 |
3.96e-17 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 81.63 E-value: 3.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 25 DIIERLGVTSLAGSPT---AFrlLMAAGPESAARVKGRLRVASSAGEPLNPEVIRWFDACLGAPIHDHYGQTELGMVVNN 101
Cdd:PRK10252 683 QFFAEYGVTTTHFVPSmlaAF--VASLTPEGARQSCASLRQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAVDVSW 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 102 H--HGLEHPVRQGSA---GYAMPGYRIAVLDEAGKEVGPNEPGVLAI-------------DIDNSPLLwftgyykkDTPS 163
Cdd:PRK10252 761 YpaFGEELAAVRGSSvpiGYPVWNTGLRILDARMRPVPPGVAGDLYLtgiqlaqgylgrpDLTASRFI--------ADPF 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 164 ISGG-YYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEI---VKAFVILA 239
Cdd:PRK10252 833 APGErMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACVINQAAATggdARQLVGYL 912
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 492822008 240 PGFEGTPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQR 285
Cdd:PRK10252 913 VSQSGLPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDR 958
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
39-285 |
7.86e-17 |
|
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: 80.21 E-value: 7.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 39 PTAFRLLMAAGPESAARVKGRLRVASSAGEPL--NPEVIRWFDAcLGAPIHDHYGQTELGMVVNN--HHGLEHPvRQGSA 114
Cdd:cd17656 226 PVAFLKFIFSEREFINRFPTCVKHIITAGEQLviTNEFKEMLHE-HNVHLHNHYGPSETHVVTTYtiNPEAEIP-ELPPI 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 115 GYAMPGYRIAVLDEAGKEVGPNEPGVLAIdidnSPLLWFTGYYKKDTPS----ISGGY------YRTGDTVEFEPDGSIS 184
Cdd:cd17656 304 GKPISNTWIYILDQEQQLQPQGIVGELYI----SGASVARGYLNRQELTaekfFPDPFdpnermYRTGDLARYLPDGNIE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 185 FIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILAPGFEgTPELAEELAlhvkKQLSAHA 264
Cdd:cd17656 380 FLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQELN-ISQLREYLA----KQLPEYM 454
|
250 260
....*....|....*....|.
gi 492822008 265 YPRQIDFVAELPKTPSGKIQR 285
Cdd:cd17656 455 IPSFFVPLDQLPLTPNGKVDR 475
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
24-290 |
1.05e-16 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 80.18 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 24 YDIIERLGVTSLAGSPTAFRLLMAAGPESAARVKgRLRVASSAGEPLNPEVIRWFDAcLGAPIHDHYGQTE---LGMVVN 100
Cdd:PRK06018 261 YELLDTEKVTFTAGVPTVWLMLLQYMEKEGLKLP-HLKMVVCGGSAMPRSMIKAFED-MGVEVRHAWGMTEmspLGTLAA 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 101 NHHGLEH-------PVRQgSAGYAMPGYRIAVLDEAGKEVgPNEPGVlaididnspllwfTGYYKKDTPSISGGYYR--- 170
Cdd:PRK06018 339 LKPPFSKlpgdarlDVLQ-KQGYPPFGVEMKITDDAGKEL-PWDGKT-------------FGRLKVRGPAVAAAYYRvdg 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 171 ----------TGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILAP 240
Cdd:PRK06018 404 eildddgffdTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKP 483
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 492822008 241 GFEGTPelaEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRK 290
Cdd:PRK06018 484 GETATR---EEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALRE 530
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
21-291 |
3.63e-16 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 78.51 E-value: 3.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 21 ENTYDIIERLGVTSLAGS---PTAFRLLMAAgPESAARVKGRLRVASSAGEPLNPEVIRWFDAClGAPIHDHYGQTELG- 96
Cdd:PRK05857 247 ENTTSLLEILTTNAVATTclvPTLLSKLVSE-LKSANATVPSLRLVGYGGSRAIAADVRFIEAT-GVRTAQVYGLSETGc 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 97 --MVVNNHHGLEHPVRQGSAGYAMPGYRIAVLDEAGKevGPNEP--------GVLAIdidNSP--LLWFTGYYKKDTPSI 164
Cdd:PRK05857 325 taLCLPTDDGSIVKIEAGAVGRPYPGVDVYLAATDGI--GPTAPgagpsasfGTLWI---KSPanMLGYWNNPERTAEVL 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 165 SGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILAPGFE- 243
Cdd:PRK05857 400 IDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVASAELDe 479
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 492822008 244 -GTPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRKA 291
Cdd:PRK05857 480 sAARALKHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASLAAA 528
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
25-286 |
7.80e-16 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 77.11 E-value: 7.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 25 DIIERLGVTSLAGSPT-AFRLLMAAGPESAARVKGRLRVASSAGEPLNPEVIRWFDACLGAPIHDHYGQTELGMVVnnhh 103
Cdd:COG1541 169 RLMQDFGPTVLVGTPSyLLYLAEVAEEEGIDPRDLSLKKGIFGGEPWSEEMRKEIEERWGIKAYDIYGLTEVGPGV---- 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 104 GLEHPVRQGsaGYAMPGYRIA-VLD-EAGKEVGPNEPGVLAididnspllwFTGYYKKDTPSISggyYRTGDTVEFEPDG 181
Cdd:COG1541 245 AYECEAQDG--LHIWEDHFLVeIIDpETGEPVPEGEEGELV----------VTTLTKEAMPLIR---YRTGDLTRLLPEP 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 182 S--------ISFI-GRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILAPGFEgTPELAEEL 252
Cdd:COG1541 310 CpcgrthprIGRIlGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYQIVVDREGGLDELTVRVELAPGAS-LEALAEAI 388
|
250 260 270
....*....|....*....|....*....|....*.
gi 492822008 253 ALHVKKQLSAHAyprQIDFVA--ELPKTPsGKIQRF 286
Cdd:COG1541 389 AAALKAVLGLRA---EVELVEpgSLPRSE-GKAKRV 420
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
160-285 |
1.43e-15 |
|
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: 76.35 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 160 DTPSISGG-YYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVIL 238
Cdd:cd17650 323 ENPFAPGErMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVA 402
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 492822008 239 ApgfeGTPELAeELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQR 285
Cdd:cd17650 403 A----ATLNTA-ELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDR 444
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
59-290 |
2.34e-15 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 75.81 E-value: 2.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 59 RLRVASSAGEPLNPEVI-RWFdacLGAPIHDHYGQTELGMVVNnhHGLEHPVRQGSAGYAMPGYRIAVLDEAGKEVGPNE 137
Cdd:cd17653 210 NLKTIFLGGEAVPPSLLdRWS---PGRRLYNAYGPTECTISST--MTELLPGQPVTIGKPIPNSTCYILDADLQPVPEGV 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 138 PGVLAIdidnSPLLWFTGYYKKD---------TPSISGG-YYRTGDTVEFEPDGSISFIGRADDVITSSGYRIG-PFDVE 206
Cdd:cd17653 285 VGEICI----SGVQVARGYLGNPaltaskfvpDPFWPGSrMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINlEEIEE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 207 SALLEHPAVNEAAVVGVPDpqrtEIVkAFVilapgfegTPELAEELALH--VKKQLSAHAYPRQIDFVAELPKTPSGKIQ 284
Cdd:cd17653 361 VVLQSQPEVTQAAAIVVNG----RLV-AFV--------TPETVDVDGLRseLAKHLPSYAVPDRIIALDSFPLTANGKVD 427
|
....*.
gi 492822008 285 RFLLRK 290
Cdd:cd17653 428 RKALRE 433
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
169-285 |
1.49e-14 |
|
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: 73.36 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 169 YRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILAPGFEgtpel 248
Cdd:cd17645 325 YRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEIP----- 399
|
90 100 110
....*....|....*....|....*....|....*..
gi 492822008 249 AEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQR 285
Cdd:cd17645 400 HEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDR 436
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
26-299 |
2.27e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 73.66 E-value: 2.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 26 IIERLGVTSLAGSPTAFRLLMAagpESAARVKGRLRVASSAGEPLNPEVI-RWFDACLGAPIHDHYGQTELGMVVNNHH- 103
Cdd:PRK05691 1359 LVQQYGVTTLHFVPPLLQLFID---EPLAAACTSLRRLFSGGEALPAELRnRVLQRLPQVQLHNRYGPTETAINVTHWQc 1435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 104 ----GLEHPVrqgsaGYAMPGYRIAVLDEAGKEVGPNEPGVLAID-------IDNSPLLWFTGYYKKDTPSISGGYYRTG 172
Cdd:PRK05691 1436 qaedGERSPI-----GRPLGNVLCRVLDAELNLLPPGVAGELCIGgaglargYLGRPALTAERFVPDPLGEDGARLYRTG 1510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 173 DTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVV---GVPDPQrteivkaFVILAPGFEGTPELA 249
Cdd:PRK05691 1511 DRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLvreGAAGAQ-------LVGYYTGEAGQEAEA 1583
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 492822008 250 EELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQrfllRKAEVEKQQQQ 299
Cdd:PRK05691 1584 ERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLD----RRALPEPVWQQ 1629
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
61-291 |
2.44e-14 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 72.89 E-value: 2.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 61 RVASSAGEPLNPEVIRWFDAcLGAPIHDHYGQTELGMVvnNHhgLEHPVRQ--GSAGYAMPGYRIAVLDEAgkEVGPNEP 138
Cdd:cd05932 278 RLAGCGSAPVPPALLEWYRS-LGLNILEAYGMTENFAY--SH--LNYPGRDkiGTVGNAGPGVEVRISEDG--EILVRSP 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 139 GVlaididnspllwFTGYYKKDTPSISG----GYYRTGDTVEFEPDGSISFIGRADDVI-TSSGYRIGPFDVESALLEHP 213
Cdd:cd05932 351 AL------------MMGYYKDPEATAEAftadGFLRTGDKGELDADGNLTITGRVKDIFkTSKGKYVAPAPIENKLAEHD 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 214 AVNEAAVVG--VPDPQRTEIVKAFVILAPGFEGTPELAEELALH---VKKQLSAHaypRQIDFVAELPK---------TP 279
Cdd:cd05932 419 RVEMVCVIGsgLPAPLALVVLSEEARLRADAFARAELEASLRAHlarVNSTLDSH---EQLAGIVVVKDpwsidngilTP 495
|
250
....*....|..
gi 492822008 280 SGKIQRFLLRKA 291
Cdd:cd05932 496 TLKIKRNVLEKA 507
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
58-291 |
4.06e-14 |
|
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: 72.31 E-value: 4.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 58 GRLRVASSAGEPLNPEVIRWFDACL---GAP---IHDHYGQTELG-MVVNNHHGLEHPVRQG----SAGYAMPGYRIAVL 126
Cdd:cd05906 289 SSLRYLVNAGEAVVAKTIRRLLRLLepyGLPpdaIRPAFGMTETCsGVIYSRSFPTYDHSQAlefvSLGRPIPGVSMRIV 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 127 DEAGKEVGPNEPGVLAIdidnSPLLWFTGYYKKDTPS----ISGGYYRTGDtVEFEPDGSISFIGRADDVITSSGYRIGP 202
Cdd:cd05906 369 DDEGQLLPEGEVGRLQV----RGPVVTKGYYNNPEANaeafTEDGWFRTGD-LGFLDNGNLTITGRTKDTIIVNGVNYYS 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 203 FDVESALLEHP--AVNEAAVVGVPDPQRT--EIVKAFVILAPGFEGTPELAEELALHVKKQLS---AHAYPRQIDfvaEL 275
Cdd:cd05906 444 HEIEAAVEEVPgvEPSFTAAFAVRDPGAEteELAIFFVPEYDLQDALSETLRAIRSVVSREVGvspAYLIPLPKE---EI 520
|
250
....*....|....*.
gi 492822008 276 PKTPSGKIQRFLLRKA 291
Cdd:cd05906 521 PKTSLGKIQRSKLKAA 536
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
169-299 |
5.80e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 72.51 E-value: 5.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 169 YRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAvVGVPDPQRTEIVKAFVILAPGFEGTPEL 248
Cdd:PRK05691 4104 YRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAA-VAVQEGVNGKHLVGYLVPHQTVLAQGAL 4182
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 492822008 249 AEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRKAEVEKQQQQ 299
Cdd:PRK05691 4183 LERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQLQSQ 4233
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
5-291 |
3.43e-13 |
|
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: 69.30 E-value: 3.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 5 LLLGVPTILNEGG-------FTAENTYDIIERLGVTSLAGSPTAFRLLMAAGPESAARvKGRLRVASSAGepLNPEVIRW 77
Cdd:cd05940 137 LIVGWSACLASGAtlvirkkFSASNFWDDIRKYQATIFQYIGELCRYLLNQPPKPTER-KHKVRMIFGNG--LRPDIWEE 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 78 FDACLGAP-IHDHYGQTELGMVVNNHHGlehpvRQGSAG----YAMPGYRIAVL-----------DEAG--KEVGPNEPG 139
Cdd:cd05940 214 FKERFGVPrIAEFYAATEGNSGFINFFG-----KPGAIGrnpsLLRKVAPLALVkydlesgepirDAEGrcIKVPRGEPG 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 140 VLAIDIdnSPLLWFTGYYK--KDTPSI-------SGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALL 210
Cdd:cd05940 289 LLISRI--NPLEPFDGYTDpaATEKKIlrdvfkkGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLG 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 211 EHPAVNEAAVVGVPDPqRTE--IVKAFVILAPgfeGTPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLL 288
Cdd:cd05940 367 AFPGVEEANVYGVQVP-GTDgrAGMAAIVLQP---NEEFDLSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDL 442
|
...
gi 492822008 289 RKA 291
Cdd:cd05940 443 RNE 445
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
115-285 |
4.39e-13 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 69.15 E-value: 4.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 115 GYAMPGYRIAVLDEAGKEVGPNEPGVLAIdidnspllwfTGyykkdtPSISGGY-------------------YRTGDTV 175
Cdd:PRK04813 321 GYAKPDSPLLIIDEEGTKLPDGEQGEIVI----------SG------PSVSKGYlnnpektaeafftfdgqpaYHTGDAG 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 176 EFEpDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTEIVKAFVILAPG-----FEGTPELAE 250
Cdd:PRK04813 385 YLE-DGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVPKEEdfereFELTKAIKK 463
|
170 180 190
....*....|....*....|....*....|....*
gi 492822008 251 ELalhvKKQLSAHAYPRQIDFVAELPKTPSGKIQR 285
Cdd:PRK04813 464 EL----KERLMEYMIPRKFIYRDSLPLTPNGKIDR 494
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
27-291 |
9.16e-13 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 68.42 E-value: 9.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 27 IERLGVTSLAGSPTAFRL-LMAAGPESAARVK-GRLRVASSAGEPLNPEVIRWF---------------------DACL- 82
Cdd:cd05931 238 ISRYRATISAAPNFAYDLcVRRVRDEDLEGLDlSSWRVALNGAEPVRPATLRRFaeafapfgfrpeafrpsyglaEATLf 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 83 --GAPIHDHYGQTELGMVVNNHHGLEHP------VRQGSAGYAMPGYRIAVLDEAG-KEVGPNEPGVlaididnsplLWF 153
Cdd:cd05931 318 vsGGPPGTGPVVLRVDRDALAGRAVAVAaddpaaRELVSCGRPLPDQEVRIVDPETgRELPDGEVGE----------IWV 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 154 ------TGYYKKDTPSI----------SGGYYRTGDtVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLE-HPAVN 216
Cdd:cd05931 388 rgpsvaSGYWGRPEATAetfgalaatdEGGWLRTGD-LGFLHDGELYITGRLKDLIIVRGRNHYPQDIEATAEEaHPALR 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 217 E--AAVVGVPDPQ-RTEIVKAFVILAPGFEGTPELAEELALHVkkqLSAHAY-PRQIDFVA--ELPKTPSGKIQRFLLRK 290
Cdd:cd05931 467 PgcVAAFSVPDDGeERLVVVAEVERGADPADLAAIAAAIRAAV---AREHGVaPADVVLVRpgSIPRTSSGKIQRRACRA 543
|
.
gi 492822008 291 A 291
Cdd:cd05931 544 A 544
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
58-290 |
2.95e-11 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 63.63 E-value: 2.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 58 GRLRVASSAGEPLNPEVIRWF---------DACLGAPihdHYGQTE-----------LGMVVNNHHGLEHPVRQGSA--G 115
Cdd:PRK05851 272 GALRVALNGGEPVDCDGFERFatamapfgfDAGAAAP---SYGLAEstcavtvpvpgIGLRVDEVTTDDGSGARRHAvlG 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 116 YAMPGY--RIAVLDEAgkeVGPNEPGVLAIDIDNSPLLwfTGYYKkDTPSISGGYYRTGDtVEFEPDGSISFIGRADDVI 193
Cdd:PRK05851 349 NPIPGMevRISPGDGA---AGVAGREIGEIEIRGASMM--SGYLG-QAPIDPDDWFPTGD-LGYLVDGGLVVCGRAKELI 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 194 TSSGYRIGPFDVESALLEHPAVNEAAVVGVPDPQRTeiVKAFVILAPGFEGTPELA--EELALHVKKQLSahAYPRQIDF 271
Cdd:PRK05851 422 TVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGS--ARPGLVIAAEFRGPDEAGarSEVVQRVASECG--VVPSDVVF 497
|
250 260
....*....|....*....|.
gi 492822008 272 VA--ELPKTPSGKIQRFLLRK 290
Cdd:PRK05851 498 VApgSLPRTSSGKLRRLAVKR 518
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
58-237 |
4.00e-11 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 63.39 E-value: 4.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 58 GRLRVASSAGEPLNPEVIRWFDACLGaPIHDHYGQTEL--GMVVNNHHGLEHpvrqGSAGYAMPGYRIAVLD--EAGKEV 133
Cdd:cd17639 250 GRLRYMLSGGAPLSADTQEFLNIVLC-PVIQGYGLTETcaGGTVQDPGDLET----GRVGPPLPCCEIKLVDweEGGYST 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 134 GPNEP-GVLAIdidNSPLLwFTGYYKKD-------TPsisGGYYRTGDTVEFEPDGSISFIGRADD-VITSSGYRIGPFD 204
Cdd:cd17639 325 DKPPPrGEILI---RGPNV-FKGYYKNPektkeafDG---DGWFHTGDIGEFHPDGTLKIIDRKKDlVKLQNGEYIALEK 397
|
170 180 190
....*....|....*....|....*....|...
gi 492822008 205 VESALLEHPAVNEAAVVGvpDPQRTEIVkAFVI 237
Cdd:cd17639 398 LESIYRSNPLVNNICVYA--DPDKSYPV-AIVV 427
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
42-285 |
5.25e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 63.09 E-value: 5.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 42 FRLLMAAGPESAARVKGR---------------LRVASSAGEPLNPEVIRWF-DAclGAP-------IHDHYGQTEL--- 95
Cdd:PRK07768 245 YRGTMTAAPNFAYALLARrlrrqakpgafdlssLRFALNGAEPIDPADVEDLlDA--GARfglrpeaILPAYGMAEAtla 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 96 --------GMVVNNHH-------GLEHPVRQGSA------GYAMPGYRIAVLDEAGKEVGPNEPGVLAIDIDN-SPllwf 153
Cdd:PRK07768 323 vsfspcgaGLVVDEVDadllaalRRAVPATKGNTrrlatlGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESvTP---- 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 154 tGYYKKDTP---SISGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNE--AAVVGVPDPQR 228
Cdd:PRK07768 399 -GYLTMDGFipaQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPgnAVAVRLDAGHS 477
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492822008 229 TEivkAFVILAPG-FEGTPELAEELALHVKKQLSAH--AYPRQIDFVA--ELPKTPSGKIQR 285
Cdd:PRK07768 478 RE---GFAVAVESnAFEDPAEVRRIRHQVAHEVVAEvgVRPRNVVVLGpgSIPKTPSGKLRR 536
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
1-289 |
5.35e-11 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 62.91 E-value: 5.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 1 MTGPLLL------GVPTILNEGGFTAENTYDIIERLGVTSLAGSPTAFRLLMAAGPESAARVK-GRLRVASSAGEPLNPE 73
Cdd:PLN03051 172 MMGPWLLysaflnGATLALYGGAPLGRGFGKFVQDAGVTVLGLVPSIVKAWRHTGAFAMEGLDwSKLRVFASTGEASAVD 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 74 VIRWFDACLG--APIHDHYGQTEL--GMVVNNhhgLEHPVRQGSAGYAMPGYRIAVLDEAGKEVGPNEPGVLAIDIdNSP 149
Cdd:PLN03051 252 DVLWLSSVRGyyKPVIEYCGGTELasGYISST---LLQPQAPGAFSTASLGTRFVLLNDNGVPYPDDQPCVGEVAL-APP 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 150 LLWFTG----------YYKKDTPSISGG--YYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLE-HPAVN 216
Cdd:PLN03051 328 MLGASDrllnadhdkvYYKGMPMYGSKGmpLRRHGDIMKRTPGGYFCVQGRADDTMNLGGIKTSSVEIERACDRaVAGIA 407
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492822008 217 EAAVVGVPDPQRTEIVKAFVILAPGFEGTPELAEELALH------VKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLR 289
Cdd:PLN03051 408 ETAAVGVAPPDGGPELLVIFLVLGEEKKGFDQARPEALQkkfqeaIQTNLNPLFKVSRVKIVPELPRNASNKLLRRVLR 486
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
4-283 |
1.24e-10 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 62.25 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 4 PLLLGVPTILNEGGFTAENTYDIIERLGVTSLAGSPTAFRLLMaagpeSAARVK----GRLRVASSAGEPLNPEVIRWFD 79
Cdd:PRK08633 845 PLLEGIKVVYHPDPTDALGIAKLVAKHRATILLGTPTFLRLYL-----RNKKLHplmfASLRLVVAGAEKLKPEVADAFE 919
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 80 ACLGAPIHDHYGQTELGMV--VN--NH----HGLEHPVRQGSAGYAMPGYRIAVLD-EAGKEVGPNEPGVLAIDIDNSpl 150
Cdd:PRK08633 920 EKFGIRILEGYGATETSPVasVNlpDVlaadFKRQTGSKEGSVGMPLPGVAVRIVDpETFEELPPGEDGLILIGGPQV-- 997
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 151 lwFTGYYK---------KDTPSIsgGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEhpAVNEA--- 218
Cdd:PRK08633 998 --MKGYLGdpektaeviKDIDGI--GWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAK--ALGGEevv 1071
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492822008 219 -AVVGVPDPQRTEivKAFVILAPGFEGTPELAEELAlhvKKQLSAHAYPRQIDFVAELPKTPSGKI 283
Cdd:PRK08633 1072 fAVTAVPDEKKGE--KLVVLHTCGAEDVEELKRAIK---ESGLPNLWKPSRYFKVEALPLLGSGKL 1132
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
43-295 |
1.71e-10 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 61.29 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 43 RLLMAAGPESAARvKGRLRVASSAGepLNPEVIRWFDACLGAP-IHDHYGQTE--LGMVVNN----------HHGL---- 105
Cdd:cd05937 188 RYLLSTPPSPYDR-DHKVRVAWGNG--LRPDIWERFRERFNVPeIGEFYAATEgvFALTNHNvgdfgagaigHHGLirrw 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 106 ---------------EHPVRQGSAGYAmpgyriavldeagKEVGPNEPGVLAIDIDNSPLLWFTGYYKKDTPSIS----- 165
Cdd:cd05937 265 kfenqvvlvkmdpetDDPIRDPKTGFC-------------VRAPVGEPGEMLGRVPFKNREAFQGYLHNEDATESklvrd 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 166 -----GGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVpdpqrteivkafviLAP 240
Cdd:cd05937 332 vfrkgDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGV--------------KVP 397
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492822008 241 GFEG----------------TPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRKAEVEK 295
Cdd:cd05937 398 GHDGragcaaitleessavpTEFTKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRDEGVDP 468
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
28-288 |
2.31e-10 |
|
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: 60.95 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 28 ERLGVTSLAGSPTAFRLLMAAGPESaaRVKGR---LRVASSAGEPL--NPEVIRWFDACLGAPIHDHYGQTELGMVVNNH 102
Cdd:cd17654 207 KRHRITVLQATPTLFRRFGSQSIKS--TVLSAtssLRVLALGGEPFpsLVILSSWRGKGNRTRIFNIYGITEVSCWALAY 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 103 H--GLEHPVRQGSAgyaMPGYRIAVLDEAGKEVgpnePGVLAIDIDNspLLWFTGYYKkDTPSisGGYYRTGDTVEFEpD 180
Cdd:cd17654 285 KvpEEDSPVQLGSP---LLGTVIEVRDQNGSEG----TGQVFLGGLN--RVCILDDEV-TVPK--GTMRATGDFVTVK-D 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 181 GSISFIGRADDVITSSGYRIGPFDVESALLEHPAVnEAAVVGVPDPQRteiVKAFVIlapGFEGTPELAEELALHvkkQL 260
Cdd:cd17654 352 GELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGV-ESCAVTLSDQQR---LIAFIV---GESSSSRIHKELQLT---LL 421
|
250 260
....*....|....*....|....*...
gi 492822008 261 SAHAYPRQIDFVAELPKTPSGKIQRFLL 288
Cdd:cd17654 422 SSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
58-274 |
9.62e-10 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 59.01 E-value: 9.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 58 GRLRVASSAGEPLNPEVIRWFDACLGAPIHDHYGQTELGMVVNNHHGLEHPVRQgsagyampgYRIAVLDEAGKEV--GP 135
Cdd:cd17632 362 GRLLAAVCGSAPLSAEMKAFMESLLDLDLHDGYGSTEAGAVILDGVIVRPPVLD---------YKLVDVPELGYFRtdRP 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 136 NEPGVLAIDIDNspllWFTGYYK--KDTPSI--SGGYYRTGDTV-EFEPDgSISFIGRADDVIT-SSGYRIGPFDVESAL 209
Cdd:cd17632 433 HPRGELLVKTDT----LFPGYYKrpEVTAEVfdEDGFYRTGDVMaELGPD-RLVYVDRRNNVLKlSQGEFVTVARLEAVF 507
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492822008 210 LEHPAVNE-------------AAVVGVPDPQRTEivkafvilaPGFEGTPELAEELALHVKK-QLSAHAYPRqiDFVAE 274
Cdd:cd17632 508 AASPLVRQifvygnserayllAVVVPTQDALAGE---------DTARLRAALAESLQRIAREaGLQSYEIPR--DFLIE 575
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
6-226 |
9.67e-10 |
|
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: 59.01 E-value: 9.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 6 LLGVPTILNEGGFTA------ENTYDIIERLGVTSLAGSPTAFRLLMAAGpESAARVKGRLRVASSAGEPLNPEVIRWFD 79
Cdd:cd05910 142 ALGLTSVIPDMDPTRparadpQKLVGAIRQYGVSIVFGSPALLERVARYC-AQHGITLPSLRRVLSAGAPVPIALAARLR 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 80 ACL--GAPIHDHYGQTE-LGMVVNNHHGLE----HPVRQGSA---GYAMPGYRIAVLDeagkevgPNEPGVLAIDIDNSP 149
Cdd:cd05910 221 KMLsdEAEILTPYGATEaLPVSSIGSRELLatttAATSGGAGtcvGRPIPGVRVRIIE-------IDDEPIAEWDDTLEL 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 150 LLWFTGYYKKDTPSISGGYY--------------------RTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESAL 209
Cdd:cd05910 294 PRGEIGEITVTGPTVTPTYVnrpvatalakiddnsegfwhRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVF 373
|
250
....*....|....*..
gi 492822008 210 LEHPAVNEAAVVGVPDP 226
Cdd:cd05910 374 NTHPGVRRSALVGVGKP 390
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
58-290 |
2.60e-09 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 57.61 E-value: 2.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 58 GRLRVASSAGEPLNPEVIRWFDACLGAPIHDHYGQTE-LGMVVNNHHGlEHPVrqGSAGYAMP------------GYRIA 124
Cdd:cd05927 274 GNVRLMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTEcTAGATLTLPG-DTSV--GHVGGPLPcaevklvdvpemNYDAK 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 125 VLDEAGkEV---GPNEpgvlaididnspllwFTGYYK---KDTPSI-SGGYYRTGDTVEFEPDGSISFIGRADDVIT-SS 196
Cdd:cd05927 351 DPNPRG-EVcirGPNV---------------FSGYYKdpeKTAEALdEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKlSQ 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 197 GYRIGPFDVESALLEHPAVNEAAVVG-----------VPDPqrtEIVKAFVILAPGFEGT-------PELAEE-----LA 253
Cdd:cd05927 415 GEYVAPEKIENIYARSPFVAQIFVYGdslksflvaivVPDP---DVLKEWAASKGGGTGSfeelcknPEVKKAiledlVR 491
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 492822008 254 LHVKKQLSAHAYPRQIDFVAELPK------TPSGKIQRFLLRK 290
Cdd:cd05927 492 LGKENGLKGFEQVKAIHLEPEPFSvengllTPTFKLKRPQLKK 534
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
169-285 |
3.26e-09 |
|
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: 57.53 E-value: 3.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 169 YRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNE----------------AAVVGVPDPQRTEIV 232
Cdd:cd17647 374 YRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVREnitlvrrdkdeeptlvSYIVPRFDKPDDESF 453
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492822008 233 KAFV--------ILAPGFEGTPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQR 285
Cdd:cd17647 454 AQEDvpkevstdPIVKGLIGYRKLIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDK 514
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
27-232 |
5.23e-09 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 56.83 E-value: 5.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 27 IERLGVTSLAGSPTAFRLLMAAGPESAARVKGRLRVAsSAGEPLNPEVIRWFDACL--GAPIHDHYGQTE---LGMVVNN 101
Cdd:PRK09274 258 IERYGVTNLFGSPALLERLGRYGEANGIKLPSLRRVI-SAGAPVPIAVIERFRAMLppDAEILTPYGATEalpISSIESR 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 102 HHGLEHpvRQGSA-------GYAMPGYRIAVLD---------EAGKEVGPNE--------PGVLaididnspllwfTGYY 157
Cdd:PRK09274 337 EILFAT--RAATDngagicvGRPVDGVEVRIIAisdapipewDDALRLATGEigeivvagPMVT------------RSYY 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 158 KKDT-------PSISGG-YYRTGDTVEFEPDGSISFIGR-ADDVITSSGyRIGPFDVESALLEHPAVNEAAVVGVPDPQR 228
Cdd:PRK09274 403 NRPEatrlakiPDGQGDvWHRMGDLGYLDAQGRLWFCGRkAHRVETAGG-TLYTIPCERIFNTHPGVKRSALVGVGVPGA 481
|
....
gi 492822008 229 TEIV 232
Cdd:PRK09274 482 QRPV 485
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
115-291 |
7.27e-09 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 56.55 E-value: 7.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 115 GYAMPGYRIAVLDEAGKEVGPNEPGVLaididnspllWFTGyykkdtPSISGGYYR---------------TGDtVEFEP 179
Cdd:PRK09192 388 GKALPGHEIEIRNEAGMPLPERVVGHI----------CVRG------PSLMSGYFRdeesqdvlaadgwldTGD-LGYLL 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 180 DGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVN--EAAVVGVPDPQRTEIVkaFVILAPGfeGTPE----LAEELA 253
Cdd:PRK09192 451 DGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRsgDAAAFSIAQENGEKIV--LLVQCRI--SDEErrgqLIHALA 526
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 492822008 254 LHVKkqlSAHAYPRQIDFVA--ELPKTPSGKIQRFLLRKA 291
Cdd:PRK09192 527 ALVR---SEFGVEAAVELVPphSLPRTSSGKLSRAKAKKR 563
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
169-283 |
1.23e-08 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 56.23 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 169 YRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAV------------NEAAVVG--VPDPQRTEiVKA 234
Cdd:TIGR03443 680 YRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVrenvtlvrrdkdEEPTLVSyiVPQDKSDE-LEE 758
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 492822008 235 FVILAP----------GFEGTPELAEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKI 283
Cdd:TIGR03443 759 FKSEVDdeessdpvvkGLIKYRKLIKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKV 817
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
7-290 |
2.27e-08 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 54.55 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 7 LGVPTILNEGGFTaENTYDIIERLGVTSLAGSPT-AFRLLMAAGPESAARVKGRLRVASSAGEPLNPEVIRWFDACLGAP 85
Cdd:cd05913 147 LGALVIPAGGGNT-ERQLQLIKDFGPTVLCCTPSyALYLAEEAEEEGIDPRELSLKVGIFGAEPWTEEMRKRIERRLGIK 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 86 IHDHYGQTEL-GMVVnnhhGLEHPVRQGSaGYAMPGYRIAVLD-EAGKEVGPNEPGVLAididnspllwFTGYYKKDTPS 163
Cdd:cd05913 226 AYDIYGLTEIiGPGV----AFECEEKDGL-HIWEDHFIPEIIDpETGEPVPPGEVGELV----------FTTLTKEAMPL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 164 ISggyYRTGDTV--EFEPDGSISF-------IGRADDVITSSGYRIGPFDVESALLEHPAVNEAA--VVGVPDPQRTEIV 232
Cdd:cd05913 291 IR---YRTRDITrlLPGPCPCGRThrridriTGRSDDMLIIRGVNVFPSQIEDVLLKIPGLGPHYqlILTRQEHLDELTI 367
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492822008 233 KafVILAPGF---EGTPELAEELALHVKKQLSAHAyprQIDFVA--ELPKTPsGKIQRFL-LRK 290
Cdd:cd05913 368 K--VEVRPEAdddEKLEALKQRLERHIKSVLGVTV---EVELVEpgSLPRSE-GKAKRVIdKRK 425
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
60-283 |
2.62e-08 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 54.97 E-value: 2.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 60 LRVASSAGEPLNPEVIRWFDACLGAPIHDHYGQTELGMVVnnhhGLEHPV--RQGSAGYAMPG--YRiavLDeagKEVGP 135
Cdd:PRK06814 909 LRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETAPVI----ALNTPMhnKAGTVGRLLPGieYR---LE---PVPGI 978
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 136 NEPGVLAIDIDNSPLlwftGYYKKDTPSI----SGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLE 211
Cdd:PRK06814 979 DEGGRLFVRGPNVML----GYLRAENPGVleppADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAE 1054
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492822008 212 HPAVNEAAVVGVPDPQRTEIVkafVILAPGFEGTpelAEELALHVKK-QLSAHAYPRQIDFVAELPKTPSGKI 283
Cdd:PRK06814 1055 LWPDALHAAVSIPDARKGERI---ILLTTASDAT---RAAFLAHAKAaGASELMVPAEIITIDEIPLLGTGKI 1121
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
113-290 |
4.87e-08 |
|
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: 54.03 E-value: 4.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 113 SAGYAMPGYRIAVLDEAGKEVGPNEPGVLAIDIDNSPllwfTGYYK--KDTPSI--SGGYYRTGDtVEFEPDGSISFIGR 188
Cdd:cd05908 315 EVGKPIDETDIRICDEDNKILPDGYIGHIQIRGKNVT----PGYYNnpEATAKVftDDGWLKTGD-LGFIRNGRLVITGR 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 189 ADDVITSSGYRIGPFDVESALLEHPAVN--EAAVVGVPDPQ-RTEIVKAFVILAPGFEGTPELAEELALHVKKQLSAH-- 263
Cdd:cd05908 390 EKDIIFVNGQNVYPHDIERIAEELEGVElgRVVACGVNNSNtRNEEIFCFIEHRKSEDDFYPLGKKIKKHLNKRGGWQin 469
|
170 180
....*....|....*....|....*...
gi 492822008 264 -AYPrqidfVAELPKTPSGKIQRFLLRK 290
Cdd:cd05908 470 eVLP-----IRRIPKTTSGKVKRYELAQ 492
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
59-290 |
1.47e-07 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 52.39 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 59 RLRVASSAGEPLNPEVIRWFDACLG-APIHDHYGQTELG-MVVnnHHGLEHPvrQGSAGYAMP--GYRIAVLDEAGKEVG 134
Cdd:PLN03052 472 SIRCFGSTGEASSVDDYLWLMSRAGyKPIIEYCGGTELGgGFV--TGSLLQP--QAFAAFSTPamGCKLFILDDSGNPYP 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 135 PNEPGV--LAIDidnsPLLWFTGY----------YKKDTPSISGGYYRT-GDTVEFEPDGSISFIGRADDVITSSGYRIG 201
Cdd:PLN03052 548 DDAPCTgeLALF----PLMFGASStllnadhykvYFKGMPVFNGKILRRhGDIFERTSGGYYRAHGRADDTMNLGGIKVS 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 202 PFDVE----SAlleHPAVNEAAVVGVPDPQR-TEIVKAFVILAPGFEGTPELaEELAL----HVKKQLSAHAYPRQIDFV 272
Cdd:PLN03052 624 SVEIErvcnAA---DESVLETAAIGVPPPGGgPEQLVIAAVLKDPPGSNPDL-NELKKifnsAIQKKLNPLFKVSAVVIV 699
|
250
....*....|....*...
gi 492822008 273 AELPKTPSGKIQRFLLRK 290
Cdd:PLN03052 700 PSFPRTASNKVMRRVLRQ 717
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
3-290 |
2.58e-07 |
|
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: 51.66 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 3 GPLLLGVPTILNEGGFTAENTYDIIERLGVTSLAGSPTAFRLLMAAgPESAARVKGRLRVAssAGEPLNPEVIRWFDACL 82
Cdd:cd05939 165 GQALLHGSTVVIRKKFSASNFWDDCVKYNCTIVQYIGEICRYLLAQ-PPSEEEQKHNVRLA--VGNGLRPQIWEQFVRRF 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 83 GAP-IHDHYGQTELGMVVNNHHGlehpvRQGSAGYaMPGY-------RIAVLDEAGKEV-----------GPNEPGVLAI 143
Cdd:cd05939 242 GIPqIGEFYGATEGNSSLVNIDN-----HVGACGF-NSRIlpsvypiRLIKVDEDTGELirdsdglcipcQPGEPGLLVG 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 144 DID-NSPLLWFTGYYKK---------DTPSISGGYYRTGDTVEFEPDGSISFIGRADDVITSSGYRIGPFDVESALLEHP 213
Cdd:cd05939 316 KIIqNDPLRRFDGYVNEgatnkkiarDVFKKGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVL 395
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492822008 214 AVNEAAVVGVPDPQRTEIVKAFVILAPgfEGTPELaEELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRK 290
Cdd:cd05939 396 GLEDVVVYGVEVPGVEGRAGMAAIVDP--ERKVDL-DRFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQK 469
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
59-300 |
7.57e-07 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 50.48 E-value: 7.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 59 RLRVASSAGEPLNPEVIR-WFDAcLGAPIHDHYGQTELGMVVnnhhGLEHPV--RQGSAGYAMPGYRIAVLDEAGKE--- 132
Cdd:PRK08043 480 RLRYVVAGAEKLQESTKQlWQDK-FGLRILEGYGVTECAPVV----SINVPMaaKPGTVGRILPGMDARLLSVPGIEqgg 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 133 ----VGPN---------EPGVLaididnspllwftgyykkDTPS-------ISGGYYRTGDTVEFEPDGSISFIGRADDV 192
Cdd:PRK08043 555 rlqlKGPNimngylrveKPGVL------------------EVPTaenargeMERGWYDTGDIVRFDEQGFVQIQGRAKRF 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 193 ITSSGYRIGPFDVES-ALLEHPAVNEAAVVgVPDPQRTEivkAFVIlapgFEGTPELAEELALHVKKQLSAH--AYPRQI 269
Cdd:PRK08043 617 AKIAGEMVSLEMVEQlALGVSPDKQHATAI-KSDASKGE---ALVL----FTTDSELTREKLQQYAREHGVPelAVPRDI 688
|
250 260 270
....*....|....*....|....*....|.
gi 492822008 270 DFVAELPKTPSGKIQrFLLRKAEVEKQQQQN 300
Cdd:PRK08043 689 RYLKQLPLLGSGKPD-FVTLKSMVDEPEQHD 718
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
40-290 |
8.03e-07 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 50.26 E-value: 8.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 40 TAF-------RLLMAAgPESAARVKGRLRVASSAGepLNPEVirW--FDACLGAP-IHDHYGQTE--LGMV-VNNhhgle 106
Cdd:PRK08279 290 TAFqyigelcRYLLNQ-PPKPTDRDHRLRLMIGNG--LRPDI--WdeFQQRFGIPrILEFYAASEgnVGFInVFN----- 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 107 hpvRQGSAG----YAMPGYRI---------AVLDEAG--KEVGPNEPGvLAID--IDNSPllwFTGY------------- 156
Cdd:PRK08279 360 ---FDGTVGrvplWLAHPYAIvkydvdtgePVRDADGrcIKVKPGEVG-LLIGriTDRGP---FDGYtdpeasekkilrd 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 157 -YKK-DTpsisggYYRTGDTVEFEPDGSISFIGRADD--------VITSsgyrigpfDVESALLEHPAVNEAAVVGVPDP 226
Cdd:PRK08279 433 vFKKgDA------WFNTGDLMRDDGFGHAQFVDRLGDtfrwkgenVATT--------EVENALSGFPGVEEAVVYGVEVP 498
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492822008 227 qRTE-------IVkafVILAPGFEGTpelaeELALHVKKQLSAHAYPRQIDFVAELPKTPSGKIQRFLLRK 290
Cdd:PRK08279 499 -GTDgragmaaIV---LADGAEFDLA-----ALAAHLYERLPAYAVPLFVRLVPELETTGTFKYRKVDLRK 560
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
58-188 |
5.98e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 47.66 E-value: 5.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 58 GRLRVASSAGEPLNPEVIRWFDACLGaPIHDHYGQTElgMVVNNHHGLEHPVRQGSAGYAMPGYRIAVLD-EAGKEVGPN 136
Cdd:PTZ00216 428 GRVRAMLSGGGPLSAATQEFVNVVFG-MVIQGWGLTE--TVCCGGIQRTGDLEPNAVGQLLKGVEMKLLDtEEYKHTDTP 504
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 492822008 137 EP-GVLAIdidNSPLLwFTGYYKKDTPS----ISGGYYRTGDTVEFEPDGSISFIGR 188
Cdd:PTZ00216 505 EPrGEILL---RGPFL-FKGYYKQEELTrevlDEDGWFHTGDVGSIAANGTLRIIGR 557
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
58-216 |
1.06e-05 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 46.65 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 58 GRLRVASSAGEPLNPEVIRWFDACLGAPIHDHYGQTELgmvvnnhhglehpvrqgSAGYAMPGYRiavlDEAGKEVGPNE 137
Cdd:PLN02387 420 GRIRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTET-----------------CAGATFSEWD----DTSVGRVGPPL 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 138 PGVLAIDIDnspllWFTGYYK-KDTP-----------SISGGYYR--------------------TGDTVEFEPDGSISF 185
Cdd:PLN02387 479 PCCYVKLVS-----WEEGGYLiSDKPmprgeiviggpSVTLGYFKnqektdevykvdergmrwfyTGDIGQFHPDGCLEI 553
|
170 180 190
....*....|....*....|....*....|..
gi 492822008 186 IGRADDVIT-SSGYRIGPFDVESALLEHPAVN 216
Cdd:PLN02387 554 IDRKKDIVKlQHGEYVSLGKVEAALSVSPYVD 585
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
4-285 |
1.41e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 46.70 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 4 PLLLGVPTILNEGGFTAENT---YDIIERLGVTSLAGSPTAFRLLMAAGPESA-ARVK-GRLRVASSAGEPLNPEVIRWF 78
Cdd:PRK05691 231 PIFSGVPCVLMSPAYFLERPlrwLEAISEYGGTISGGPDFAYRLCSERVSESAlERLDlSRWRVAYSGSEPIRQDSLERF 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 79 ----DACLGAP--IHDHYGQTELGMVVN-------------NHHGLEHPVR---QGSA----GYAMPGYRIAVLDEA-GK 131
Cdd:PRK05691 311 aekfAACGFDPdsFFASYGLAEATLFVSggrrgqgipalelDAEALARNRAepgTGSVlmscGRSQPGHAVLIVDPQsLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 132 EVGPNEPGVLaididnspllWFTGyykkdtPSISGGYY-------------------RTGDtVEFEPDGSISFIGRADDV 192
Cdd:PRK05691 391 VLGDNRVGEI----------WASG------PSIAHGYWrnpeasaktfvehdgrtwlRTGD-LGFLRDGELFVTGRLKDM 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 193 ITSSGYRIGPFDVESALLEhpavnEAAVVgvpdpqRTEIVKAFVILAPGFEGTPeLAEELALHVKKQLSAHAYPRQI-DF 271
Cdd:PRK05691 454 LIVRGHNLYPQDIEKTVER-----EVEVV------RKGRVAAFAVNHQGEEGIG-IAAEISRSVQKILPPQALIKSIrQA 521
|
330 340 350
....*....|....*....|....*....|
gi 492822008 272 VAE----------------LPKTPSGKIQR 285
Cdd:PRK05691 522 VAEacqeapsvvlllnpgaLPKTSSGKLQR 551
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
167-300 |
6.22e-05 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 44.09 E-value: 6.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 167 GYYRTGDTVEFEpDGSISFIGRADDVITSSGYRIGPFDVESALLEHPAVNEAAVVGVPDP---QRTEIVKAFVilapgfe 243
Cdd:PRK09029 332 GWFATRDRGEWQ-NGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAefgQRPVAVVESD------- 403
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492822008 244 gTPELAEELALHVKKQLSAHAYPrqidfVA--ELPKT-PSG--KIQRFLLrKAEVEKQQQQN 300
Cdd:PRK09029 404 -SEAAVVNLAEWLQDKLARFQQP-----VAyyLLPPElKNGgiKISRQAL-KEWVAQQLGNN 458
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
59-222 |
8.67e-05 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) 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. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It 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: 341256 [Multi-domain] Cd Length: 596 Bit Score: 43.89 E-value: 8.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 59 RLRVASSAGEPLNPEVIRWFDAcLGAPIHDHYGQTElgmvVNNHHGLEHP--VRQGSAGYAMPGYRIavldeagKEVGPN 136
Cdd:cd05933 321 RCQKFFTGAAPISRETLEFFLS-LNIPIMELYGMSE----TSGPHTISNPqaYRLLSCGKALPGCKT-------KIHNPD 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 137 EPGVLAIdidnspLLW----FTGYY---KKDTPSI-SGGYYRTGDTVEFEPDGSISFIGRADDVI-TSSGYRIGPFDVES 207
Cdd:cd05933 389 ADGIGEI------CFWgrhvFMGYLnmeDKTEEAIdEDGWLHSGDLGKLDEDGFLYITGRIKELIiTAGGENVPPVPIED 462
|
170
....*....|....*.
gi 492822008 208 AL-LEHPAVNEAAVVG 222
Cdd:cd05933 463 AVkKELPIISNAMLIG 478
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
54-234 |
1.83e-04 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 42.78 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 54 ARVKGRLRVASSAGEPLNPEVIRWFDACLGAPIHDHYGQTELGMVVNNHHglEHPVRQGSAGYAMPGYRIAVLD----EA 129
Cdd:PLN02736 372 AKLGGRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISGMD--EGDNLSGHVGSPNPACEVKLVDvpemNY 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 130 GKEVGPNEPGVLAIdidNSPLLwFTGYYKKD--TPSI--SGGYYRTGDTVEFEPDGSISFIGRADDVIT-SSGYRIGPFD 204
Cdd:PLN02736 450 TSEDQPYPRGEICV---RGPII-FKGYYKDEvqTREVidEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKlAQGEYIAPEK 525
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 492822008 205 VESALLEHPAVNEAAVVG-----------VPDPqrtEIVKA 234
Cdd:PLN02736 526 IENVYAKCKFVAQCFVYGdslnsslvavvVVDP---EVLKA 563
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
114-296 |
6.38e-04 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 41.18 E-value: 6.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 114 AGYAMPGYRIAVLDEAGKEV-GPNEPGVLAIDIDNSPLLWFTGYYK-----KDTPSISGG-------YYRTGD------- 173
Cdd:cd05905 363 SGKVLPGAQVAIVNPETKGLcKDGEIGEIWVNSPANASGYFLLDGEtndtfKVFPSTRLStgitnnsYARTGLlgflrpt 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 174 ---TVEFEPDGSISFIGRADDVITSSGYRIGPFDVE-SALLEHPAVNEAAVVgvpdpQRTEIVkafVILAPGFEGT-PEL 248
Cdd:cd05905 443 kctDLNVEEHDLLFVVGSIDETLEVRGLRHHPSDIEaTVMRVHPYRGRCAVF-----SITGLV---VVVAEQPPGSeEEA 514
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 492822008 249 AEELALHVKKQLSAHayprQI--DFVA-----ELPKTPSGKIQRFLLRKAEVEKQ 296
Cdd:cd05905 515 LDLVPLVLNAILEEH----QVivDCVAlvppgSLPKNPLGEKQRMEIRQAFLAGK 565
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
8-222 |
3.16e-03 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 38.85 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 8 GVPTILNEGGFTAENTYDII-------ERLGVTSLAGSPTAFRLLMAAGPESaarVKGRLRVASSAGEPLNPEVIRWFDA 80
Cdd:PLN02614 332 GLQKKLSDGGFLKKFVFDSAfsykfgnMKKGQSHVEASPLCDKLVFNKVKQG---LGGNVRIILSGAAPLASHVESFLRV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 81 CLGAPIHDHYGQTE------------LGMVvnnhhglehpvrqGSAGYAMPGYRIAVldEAGKEVGPNEPGVLA---IDI 145
Cdd:PLN02614 409 VACCHVLQGYGLTEscagtfvslpdeLDML-------------GTVGPPVPNVDIRL--ESVPEMEYDALASTPrgeICI 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 146 DNSPLlwFTGYYKKDTPS---ISGGYYRTGDTVEFEPDGSISFIGRADDVIT-SSGYRIGPFDVESALLEHPAVNEAAVV 221
Cdd:PLN02614 474 RGKTL--FSGYYKREDLTkevLIDGWLHTGDVGEWQPNGSMKIIDRKKNIFKlSQGEYVAVENIENIYGEVQAVDSVWVY 551
|
.
gi 492822008 222 G 222
Cdd:PLN02614 552 G 552
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
153-230 |
4.40e-03 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 38.67 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 153 FTGYYKKDTPS---ISGGYYRTGDTVEFEPDGSISFIGRADDVIT-SSGYRIGPFDVESALLEHPAVNEAAVVG------ 222
Cdd:PLN02861 476 FSGYHKRQDLTeevLIDGWFHTGDIGEWQPNGAMKIIDRKKNIFKlSQGEYVAVENLENTYSRCPLIASIWVYGnsfesf 555
|
90
....*....|...
gi 492822008 223 -----VPDPQRTE 230
Cdd:PLN02861 556 lvavvVPDRQALE 568
|
|
| PRK09188 |
PRK09188 |
serine/threonine protein kinase; Provisional |
208-289 |
6.61e-03 |
|
serine/threonine protein kinase; Provisional
Pssm-ID: 236400 [Multi-domain] Cd Length: 365 Bit Score: 37.82 E-value: 6.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492822008 208 ALLEHPAVNEAAVVGVPDPQRTEIVKAFVILAPgfegtPELAEELALHVKKQLSAHAyPRQIDFVAELPKTPSGKIQRFL 287
Cdd:PRK09188 248 ALKSDPAVSDVAIALFSLPAKGVGLYAFVEAEL-----PADEKSLRARLAGAKPPKP-PEHIQPVAALPRDADGTVRDDI 321
|
..
gi 492822008 288 LR 289
Cdd:PRK09188 322 LR 323
|
|
| |
