|
Name |
Accession |
Description |
Interval |
E-value |
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
1-354 |
0e+00 |
|
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: 698.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 1 MVIFFTSGTTGFPKMAKHSHGLALQPSFPGSRKLRSLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCTVFIHHLPQFDTK 80
Cdd:cd05928 177 MAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWIQGACVFVHHLPRFDPL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 81 VIIQTLLKYPINHFWGVSSIYRMILQQDFTSIRFPALEHCYTGGEVVLPKDQEEWKRRTGLLLYENYGQSETGLICATYW 160
Cdd:cd05928 257 VILKTLSSYPITTFCGAPTVYRMLVQQDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGLICANFK 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 161 GMKIKPGFMGKATPPYDVQVIDDKGSILPPNTEGNIGIRIKPVRPVSLFMCYEGDPEKTAKVECGDFYNTGDRGKMDEEG 240
Cdd:cd05928 337 GMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKPIRPFGLFSGYVDNPEKTAATIRGDFYLTGDRGIMDEDG 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 241 YICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFLSHDKDQLTKELQQHVKSV 320
Cdd:cd05928 417 YFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLSHDPEQLTKELQQHVKSV 496
|
330 340 350
....*....|....*....|....*....|....
gi 578828480 321 TAPYKYPRKVEFVSELPKTITGKIERKELRKKET 354
Cdd:cd05928 497 TAPYKYPRKVEFVQELPKTVTGKIQRNELRDKEW 530
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
3-351 |
5.66e-159 |
|
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: 452.18 E-value: 5.66e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPKMAKHSHGLALQpSFPGSRKLRSLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCTVFIHHLPQFDTKVI 82
Cdd:cd05972 86 IYFTSGTTGLPKGVLHTHSYPLG-HIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRFDAERI 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 83 IQTLLKYPINHFWGVSSIYRMILQQDFTSIRFPALEHCYTGGEVVLPKDQEEWKRRTGLLLYENYGQSETGLICATYWGM 162
Cdd:cd05972 165 LELLERYGVTSFCGPPTAYRMLIKQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDM 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 163 KIKPGFMGKATPPYDVQVIDDKGSILPPNTEGNIGIRIKpvrPVSLFMCYEGDPEKTAKVECGDFYNTGDRGKMDEEGYI 242
Cdd:cd05972 245 PVKPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKLP---PPGLFLGYVGDPEKTEASIRGDYYLTGDRAYRDEDGYF 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 243 CFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFLshDKDQLTKELQQHVKSVTA 322
Cdd:cd05972 322 WFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYE--PSEELAEELQGHVKKVLA 399
|
330 340
....*....|....*....|....*....
gi 578828480 323 PYKYPRKVEFVSELPKTITGKIERKELRK 351
Cdd:cd05972 400 PYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
1-356 |
2.23e-130 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 384.46 E-value: 2.23e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 1 MVIFFTSGTTGFPKMAKHSH-GLALQPSFPGSRKLRsLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCTVFIHH-LPQF- 77
Cdd:COG0365 187 LFILYTSGTTGKPKGVVHTHgGYLVHAATTAKYVLD-LKPGDVFWCTADIGWATGHSYIVYGPLLNGATVVLYEgRPDFp 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 78 DTKVIIQTLLKYPINHFWGVSSIYRMILQQDFTSIR---FPALEHCYTGGEVVLPKDQEEWKRRTGLLLYENYGQSETG- 153
Cdd:COG0365 266 DPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKkydLSSLRLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGg 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 154 LICATYWGMKIKPGFMGKATPPYDVQVIDDKGSILPPNTEGNIGIRiKPvRPvSLFMCYEGDPEKTAKV---ECGDFYNT 230
Cdd:COG0365 346 IFISNLPGLPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIK-GP-WP-GMFRGYWNDPERYRETyfgRFPGWYRT 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 231 GDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFlsHDKDQLT 310
Cdd:COG0365 423 GDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGV--EPSDELA 500
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 578828480 311 KELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKKETGQ 356
Cdd:COG0365 501 KELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEGR 546
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
2-353 |
8.32e-123 |
|
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: 364.12 E-value: 8.32e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 2 VIFFTSGTTGFPKMAKHSHGLALQPSFPGSRkLRSLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCTVFIHHLPQFDTKV 81
Cdd:cd05970 189 LVYFSSGTTGMPKMVEHDFTYPLGHIVTAKY-WQNVREGGLHLTVADTGWGKAVWGKIYGQWIAGAAVFVYDYDKFDPKA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 82 IIQTLLKYPINHFWGVSSIYRMILQQDFTSIRFPALEHCYTGGEVVLPKDQEEWKRRTGLLLYENYGQSETGLICATYWG 161
Cdd:cd05970 268 LLEKLSKYGVTTFCAPPTIYRFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTLTIATFPW 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 162 MKIKPGFMGKATPPYDVQVIDDKGSILPPNTEGNIGIRIKPVRPVSLFMCYEGDPEKTAKVECGDFYNTGDRGKMDEEGY 241
Cdd:cd05970 348 MEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSKGKPVGLFGGYYKDAEKTAEVWHDGYYHTGDAAWMDEDGY 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 242 ICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFlsHDKDQLTKELQQHVKSVT 321
Cdd:cd05970 428 LWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGY--EPSEELKKELQDHVKKVT 505
|
330 340 350
....*....|....*....|....*....|..
gi 578828480 322 APYKYPRKVEFVSELPKTITGKIERKELRKKE 353
Cdd:cd05970 506 APYKYPRIVEFVDELPKTISGKIRRVEIRERD 537
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
2-351 |
2.35e-101 |
|
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: 306.35 E-value: 2.35e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 2 VIFFTSGTTGFPKMAKHSHG------LALQPSFPGSRKLRSLktsdvsWCLS---DSGWIVATIWtlvePWTAGCTVFIh 72
Cdd:COG0318 104 LILYTSGTTGRPKGVMLTHRnllanaAAIAAALGLTPGDVVL------VALPlfhVFGLTVGLLA----PLLAGATLVL- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 73 hLPQFDTKVIIQTLLKYPINHFWGVSSIYRMILQQ-DFTSIRFPALEHCYTGGEVVLPKDQEEWKRRTGLLLYENYGQSE 151
Cdd:COG0318 173 -LPRFDPERVLELIERERVTVLFGVPTMLARLLRHpEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 152 TGLICATYWGMKI--KPGFMGKATPPYDVQVIDDKGSILPPNTEGNIGirikpVRPVSLFMCYEGDPEKTAKVECGDFYN 229
Cdd:COG0318 252 TSPVVTVNPEDPGerRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIV-----VRGPNVMKGYWNDPEATAEAFRDGWLR 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 230 TGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPqflshDKDQL 309
Cdd:COG0318 327 TGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRP-----GAELD 401
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 578828480 310 TKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRK 351
Cdd:COG0318 402 AEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRE 443
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
2-350 |
3.49e-99 |
|
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: 300.50 E-value: 3.49e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 2 VIFFTSGTTGFPKMAKHSHGLAL---------QPSFPgsrklrslKTSDVSWCLSDSGWIVATIWTLVEPWTAGCTVFIH 72
Cdd:cd05971 92 LIIYTSGTTGPPKGALHAHRVLLghlpgvqfpFNLFP--------RDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAH 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 73 HLPQFDTKVIIQTLLKYPINHFWGVSSIYRMILQQDFTSIRFP-ALEHCYTGGEvvlPKDQEE--WKRRT-GLLLYENYG 148
Cdd:cd05971 164 RMTKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQvKLRAIATGGE---SLGEELlgWAREQfGVEVNEFYG 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 149 QSETGLI---CATYwgMKIKPGFMGKATPPYDVQVIDDKGSILPPNTEGNIGIRikpvRPVSL-FMCYEGDPEKTAKVEC 224
Cdd:cd05971 241 QTECNLVignCSAL--FPIKPGSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVE----LPDPVaFLGYWNNPSATEKKMA 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 225 GDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFLsh 304
Cdd:cd05971 315 GDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGET-- 392
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 578828480 305 DKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELR 350
Cdd:cd05971 393 PSDALAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
2-344 |
1.05e-97 |
|
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: 293.04 E-value: 1.05e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 2 VIFFTSGTTGFPKMAKHSHGLALQpSFPGSRKLRSLKTSDVSWCLSDSGWIvATIWTLVEPWTAGCTVFIHhlPQFDTKV 81
Cdd:cd04433 4 LILYTSGTTGKPKGVVLSHRNLLA-AAAALAASGGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLL--PKFDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 82 IIQTLLKYPINHFWGVSSIYRMILQQD-FTSIRFPALEHCYTGGEVVLPKDQEEWKRRTGLLLYENYGQSETGLICATYW 160
Cdd:cd04433 80 ALELIEREKVTILLGVPTLLARLLKAPeSAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 161 G--MKIKPGFMGKATPPYDVQVIDDKGSILPPNTEGNIGIRIKpvrpvSLFMCYEGDPEKTAKVECGDFYNTGDRGKMDE 238
Cdd:cd04433 160 PddDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGP-----SVMKGYWNNPEATAAVDEDGWYRTGDLGRLDE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 239 EGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPqflshDKDQLTKELQQHVK 318
Cdd:cd04433 235 DGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRP-----GADLDAEELRAHVR 309
|
330 340
....*....|....*....|....*.
gi 578828480 319 SVTAPYKYPRKVEFVSELPKTITGKI 344
Cdd:cd04433 310 ERLAPYKVPRRVVFVDALPRTASGKI 335
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
3-353 |
3.31e-93 |
|
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: 285.17 E-value: 3.31e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPKMAKHSHGLALQPSFPGSRKLrSLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCTVFIHHlPQFDTKVI 82
Cdd:cd05969 94 LHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVL-DLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYE-GRFDAESW 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 83 IQTLLKYPINHFWGVSSIYRMIL--------QQDFTSIRFPAlehcyTGGEVVLPkDQEEWKRRT-GLLLYENYGQSETG 153
Cdd:cd05969 172 YGIIERVKVTVWYTAPTAIRMLMkegdelarKYDLSSLRFIH-----SVGEPLNP-EAIRWGMEVfGVPIHDTWWQTETG 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 154 LIC-ATYWGMKIKPGFMGKATPPYDVQVIDDKGSILPPNTEGNIGIriKPVRPvSLFMCYEGDPEKTAKVECGDFYNTGD 232
Cdd:cd05969 246 SIMiANYPCMPIKPGSMGKPLPGVKAAVVDENGNELPPGTKGILAL--KPGWP-SMFRGIWNDEERYKNSFIDGWYLTGD 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 233 RGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFLSHDKdqLTKE 312
Cdd:cd05969 323 LAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDE--LKEE 400
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 578828480 313 LQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKKE 353
Cdd:cd05969 401 IINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLKAKE 441
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1-353 |
4.71e-91 |
|
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: 279.45 E-value: 4.71e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 1 MVIFFTSGTTGFPKMAKHSHGlalqpSFP----GSRKLRSLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCTVFIHHLPQ 76
Cdd:cd05974 88 MLLYFTSGTTSKPKLVEHTHR-----SYPvghlSTMYWIGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYAR 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 77 FDTKVIIQTLLKYPINHFWGVSSIYRMILQQDFTSIRFPALEHCyTGGEVVLPKDQEEWKRRTGLLLYENYGQSETGLIC 156
Cdd:cd05974 163 FDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASFDVKLREVV-GAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALV 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 157 ATYWGMKIKPGFMGKATPPYDVQVIDDKGSilpPNTEGNIGIRIKPVRPVSLFMCYEGDPEKTAKVECGDFYNTGDRGKM 236
Cdd:cd05974 242 GNSPGQPVKAGSMGRPLPGYRVALLDPDGA---PATEGEVALDLGDTRPVGLMKGYAGDPDKTAHAMRGGYYRTGDIAMR 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 237 DEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQflSHDKDQLTKELQQH 316
Cdd:cd05974 319 DEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAG--YEPSPETALEIFRF 396
|
330 340 350
....*....|....*....|....*....|....*..
gi 578828480 317 VKSVTAPYKYPRKVEFVsELPKTITGKIERKELRKKE 353
Cdd:cd05974 397 SRERLAPYKRIRRLEFA-ELPKTISGKIRRVELRRRE 432
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
1-355 |
6.65e-86 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 270.23 E-value: 6.65e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 1 MVIFFTSGTTGFPKMAKHSHGLALQPSFPGSRKLrSLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCTVFIHHlPQFDTK 80
Cdd:PRK04319 208 AILHYTSGSTGKPKGVLHVHNAMLQHYQTGKYVL-DLHEDDVYWCTADPGWVTGTSYGIFAPWLNGATNVIDG-GRFSPE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 81 VIIQTLLKYPINHFWGVSSIYRMIL--------QQDFTSIRFPAlehcyTGGEvvlPKDQE--EWKRRT-GLLLYENYGQ 149
Cdd:PRK04319 286 RWYRILEDYKVTVWYTAPTAIRMLMgagddlvkKYDLSSLRHIL-----SVGE---PLNPEvvRWGMKVfGLPIHDNWWM 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 150 SETG--LICaTYWGMKIKPGFMGKATPPYDVQVIDDKGSILPPNTEGNIGIriKPVRPvSLFMCYEGDPEKTAKVECGDF 227
Cdd:PRK04319 358 TETGgiMIA-NYPAMDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAI--KKGWP-SMMRGIWNNPEKYESYFAGDW 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 228 YNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFlsHDKD 307
Cdd:PRK04319 434 YVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGY--EPSE 511
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 578828480 308 QLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKKETG 355
Cdd:PRK04319 512 ELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLKAWELG 559
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1-351 |
2.73e-84 |
|
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: 262.07 E-value: 2.73e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 1 MVIFFTSGTTGFPKMAKHShgLALQPSFPG-SRKLRSLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCTVFIHHLPqFDT 79
Cdd:cd05973 91 FVMMFTSGTTGLPKGVPVP--LRALAAFGAyLRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEGG-FSV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 80 KVIIQTLLKYPINHFWGVSSIYRMILQQDFTSIRFPA--LEHCYTGGEVVLPkDQEEWKR-RTGLLLYENYGQSETGLIC 156
Cdd:cd05973 168 ESTWRVIERLGVTNLAGSPTAYRLLMAAGAEVPARPKgrLRRVSSAGEPLTP-EVIRWFDaALGVPIHDHYGQTELGMVL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 157 ATYWGMK--IKPGFMGKATPPYDVQVIDDKGSILPPNTEGNIGIRIKPvRPVSLFMCYEGDPEKTAKvecGDFYNTGDRG 234
Cdd:cd05973 247 ANHHALEhpVHAGSAGRAMPGWRVAVLDDDGDELGPGEPGRLAIDIAN-SPLMWFRGYQLPDTPAID---GGYYLTGDTV 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 235 KMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFlsHDKDQLTKELQ 314
Cdd:cd05973 323 EFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGH--EGTPALADELQ 400
|
330 340 350
....*....|....*....|....*....|....*..
gi 578828480 315 QHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRK 351
Cdd:cd05973 401 LHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
2-350 |
1.74e-79 |
|
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: 250.56 E-value: 1.74e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 2 VIFFTSGTTGFPKMAKHSHG------LALQPSFPGSRKLRslktsDVSWC---LSDS-GWIVAtiwtLVEPWTAGCTVFI 71
Cdd:cd05936 129 VLQYTSGTTGVPKGAMLTHRnlvanaLQIKAWLEDLLEGD-----DVVLAalpLFHVfGLTVA----LLLPLALGATIVL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 72 hhLPQFDTKVIIQTLLKYPINHFWGVSSIYRMILQQ-DFTSIRFPALEHCYTGGEVVLPKDQEEWKRRTGLLLYENYGQS 150
Cdd:cd05936 200 --IPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLNApEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLT 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 151 ETG-LICATYWGMKIKPGFMGKATPPYDVQVIDDKGSILPPNTEGNIGIRiKPvrpvSLFMCYEGDPEKTAKVECGDFYN 229
Cdd:cd05936 278 ETSpVVAVNPLDGPRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVR-GP----QVMKGYWNRPEETAEAFVDGWLR 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 230 TGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLtpqflsHDKDQL 309
Cdd:cd05936 353 TGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVL------KEGASL 426
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 578828480 310 TK-ELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELR 350
Cdd:cd05936 427 TEeEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
5-350 |
6.45e-68 |
|
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: 220.04 E-value: 6.45e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 5 FTSGTTGFPKMAKHSHGLALQPSFPGSRKLRSLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCTVFIhhLPQFDTKVIIQ 84
Cdd:cd05958 104 FTSGTTGAPKATMHFHRDPLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVL--LEEATPDLLLS 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 85 TLLKYPINHFWGVSSIYRMIL------QQDFTSIRFpalehCYTGGEVVLPKDQEEWKRRTGLLLYENYGQSETGLICAT 158
Cdd:cd05958 182 AIARYKPTVLFTAPTAYRAMLahpdaaGPDLSSLRK-----CVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFIS 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 159 YWGMKIKPGFMGKATPPYDVQVIDDKGSILPPNTEGNIGIRikpvRPVSlfmcYEGDPEKTAKVECGDFYN-TGDRGKMD 237
Cdd:cd05958 257 ARPGDARPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVR----GPTG----CRYLADKRQRTYVQGGWNiTGDTYSRD 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 238 EEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFLShdKDQLTKELQQHV 317
Cdd:cd05958 329 PDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIP--GPVLARELQDHA 406
|
330 340 350
....*....|....*....|....*....|...
gi 578828480 318 KSVTAPYKYPRKVEFVSELPKTITGKIERKELR 350
Cdd:cd05958 407 KAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
1-344 |
9.27e-68 |
|
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: 219.40 E-value: 9.27e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 1 MVIFFTSGTTGFPKMAKHSHG------LALQPSFPGSRKLRSLKTSDVSWCLSDSGWIVATIWtlvepwtAGCTVFIhhL 74
Cdd:cd17631 101 ALLMYTSGTTGRPKGAMLTHRnllwnaVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLL-------RGGTVVI--L 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 75 PQFDTKVIIQTLLKYPINHFWGVSSIYRMILQQ-DFTSIRFPALEHCYTGGEVVLPKDQEEWKRRtGLLLYENYGQSETG 153
Cdd:cd17631 172 RKFDPETVLDLIERHRVTSFFLVPTMIQALLQHpRFATTDLSSLRAVIYGGAPMPERLLRALQAR-GVKFVQGYGMTETS 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 154 -LICATYWGMKI-KPGFMGKATPPYDVQVIDDKGSILPPNTEGNIGIRiKPvrpvSLFMCYEGDPEKTAKVECGDFYNTG 231
Cdd:cd17631 251 pGVTFLSPEDHRrKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVR-GP----HVMAGYWNRPEATAAAFRDGWFHTG 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 232 DRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPqflshdKDQLT- 310
Cdd:cd17631 326 DLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRP------GAELDe 399
|
330 340 350
....*....|....*....|....*....|....
gi 578828480 311 KELQQHVKSVTAPYKYPRKVEFVSELPKTITGKI 344
Cdd:cd17631 400 DELIAHCRERLARYKIPKSVEFVDALPRNATGKI 433
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
5-350 |
4.18e-67 |
|
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: 219.55 E-value: 4.18e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 5 FTSGTTGFPKMAKHSHGLALQPSFPGSRKLRSLKTSDVswCLSdsgwiVATIW-------TLVEPWTAGCTVFIhhLPQF 77
Cdd:cd05959 170 YSSGSTGRPKGVVHLHADIYWTAELYARNVLGIREDDV--CFS-----AAKLFfayglgnSLTFPLSVGATTVL--MPER 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 78 DT-KVIIQTLLKYPINHFWGVSSIYRMIL------QQDFTSIRFpalehCYTGGEVvLPKD-QEEWKRRTGLLLYENYGQ 149
Cdd:cd05959 241 PTpAAVFKRIRRYRPTVFFGVPTLYAAMLaapnlpSRDLSSLRL-----CVSAGEA-LPAEvGERWKARFGLDILDGIGS 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 150 SETGLICATYWGMKIKPGFMGKATPPYDVQVIDDKGSILPpntEGNIGIRIkpVRPVSLFMCYEGDPEKTAKVECGDFYN 229
Cdd:cd05959 315 TEMLHIFLSNRPGRVRYGTTGKPVPGYEVELRDEDGGDVA---DGEPGELY--VRGPSSATMYWNNRDKTRDTFQGEWTR 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 230 TGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFlsHDKDQL 309
Cdd:cd05959 390 TGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGY--EDSEAL 467
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 578828480 310 TKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELR 350
Cdd:cd05959 468 EEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
3-351 |
3.16e-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: 219.88 E-value: 3.16e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPKMAKHS---HGLALQPSFpgsRKLRSLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCT-VFIHHLPQF- 77
Cdd:cd05967 235 ILYTSGTTGKPKGVVRDnggHAVALNWSM---RNIYGIKPGDVWWAASDVGWVVGHSYIVYGPLLHGATtVLYEGKPVGt 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 78 -DTKVIIQTLLKYPINHFWGVSSIYRMILQQD--FTSIR---FPALEHCYTGGEVVLPKDQEEWKRRTGLLLYENYGQSE 151
Cdd:cd05967 312 pDPGAFWRVIEKYQVNALFTAPTAIRAIRKEDpdGKYIKkydLSSLRTLFLAGERLDPPTLEWAENTLGVPVIDHWWQTE 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 152 TG-LICATYWG---MKIKPGFMGKATPPYDVQVIDDKGSILPPNTEGNIGIRIkPVRPVSLFMCYeGDPEKTAKVECGDF 227
Cdd:cd05967 392 TGwPITANPVGlepLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKL-PLPPGCLLTLW-KNDERFKKLYLSKF 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 228 ---YNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQfLSH 304
Cdd:cd05967 470 pgyYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEG-VKI 548
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 578828480 305 DKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRK 351
Cdd:cd05967 549 TAEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRK 595
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
1-352 |
9.27e-66 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 216.59 E-value: 9.27e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 1 MVIFFTSGTTGFPKMAKHSH-GLALQPsfPGSRKLRSLKTSDVSwclsdsgwIVAT------IWTL-VEPWTAGCTVFIH 72
Cdd:PRK06187 170 AAMLYTSGTTGHPKGVVLSHrNLFLHS--LAVCAWLKLSRDDVY--------LVIVpmfhvhAWGLpYLALMAGAKQVIP 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 73 HlpQFDTKVIIQTLLKYPINHFWGVSSIYRMILQ------QDFTSIRfpalEHCYtGGEVVLPKDQEEWKRRTGLLLYEN 146
Cdd:PRK06187 240 R--RFDPENLLDLIETERVTFFFAVPTIWQMLLKaprayfVDFSSLR----LVIY-GGAALPPALLREFKEKFGIDLVQG 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 147 YGQSETG-LICATY--WGMKIKPGFMGKATPP---YDVQVIDDKGSILPPNtEGNIGIRIkpVRPVSLFMCYEGDPEKTA 220
Cdd:PRK06187 313 YGMTETSpVVSVLPpeDQLPGQWTKRRSAGRPlpgVEARIVDDDGDELPPD-GGEVGEII--VRGPWLMQGYWNRPEATA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 221 KVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLtpq 300
Cdd:PRK06187 390 ETIDGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVL--- 466
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 578828480 301 flsHDKDQLT-KELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKK 352
Cdd:PRK06187 467 ---KPGATLDaKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLREQ 516
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
3-350 |
1.24e-64 |
|
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: 211.00 E-value: 1.24e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPKMAKHSHglalqpsfpgsRKLRSLKTSDVSWCLSDSG----------WIVATIWTLVEPWTAGCTVFIh 72
Cdd:cd05934 86 ILYTSGTTGPPKGVVITH-----------ANLTFAGYYSARRFGLGEDdvyltvlplfHINAQAVSVLAALSVGATLVL- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 73 hLPQFDTKVIIQTLLKYPINHFWGVSSIYRMILQQdftsirfPALE----HCY--TGGEVVLPKDQEEWKRRTGLLLYEN 146
Cdd:cd05934 154 -LPRFSASRFWSDVRRYGATVTNYLGAMLSYLLAQ-------PPSPddraHRLraAYGAPNPPELHEEFEERFGVRLLEG 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 147 YGQSETGLICATYWGMKIKPGFMGKATPPYDVQVIDDKGSILPPNTEGNIGIRikPVRPVSLFMCYEGDPEKTAKVECGD 226
Cdd:cd05934 226 YGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIR--GLRGWGFFKGYYNMPEATAEAMRNG 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 227 FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTP-QFLSHD 305
Cdd:cd05934 304 WFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPgETLDPE 383
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 578828480 306 kdqltkELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELR 350
Cdd:cd05934 384 ------ELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
5-350 |
3.41e-63 |
|
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: 207.70 E-value: 3.41e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 5 FTSGTTGFPKMAKHSHGLALQPSFPGSRKLRSLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCTVFIHHLPQfDTKVIIQ 84
Cdd:cd05919 98 YSSGTTGPPKGVMHAHRDPLLFADAMAREALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWP-TAERVLA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 85 TLLKYPINHFWGVSSIY-RMILQQDFTSIRFPALEHCYTGGEVvLPKDQ-EEWKRRTGLLLYENYGQSETGLICATYWGM 162
Cdd:cd05919 177 TLARFRPTVLYGVPTFYaNLLDSCAGSPDALRSLRLCVSAGEA-LPRGLgERWMEHFGGPILDGIGATEVGHIFLSNRPG 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 163 KIKPGFMGKATPPYDVQVIDDKGSILPPNTEGNIGIRIKpvrpvSLFMCYEGDPEKTAKVECGDFYNTGDRGKMDEEGYI 242
Cdd:cd05919 256 AWRLGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGP-----SAAVGYWNNPEKSRATFNGGWYRTGDKFCRDADGWY 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 243 CFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFLSHDKdqLTKELQQHVKSVTA 322
Cdd:cd05919 331 THAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQES--LARDIHRHLLERLS 408
|
330 340
....*....|....*....|....*...
gi 578828480 323 PYKYPRKVEFVSELPKTITGKIERKELR 350
Cdd:cd05919 409 AHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
2-351 |
1.44e-61 |
|
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: 203.29 E-value: 1.44e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 2 VIFFTSGTTGFPKMAKHSHG-LALQpsfpgsrkLRSLkTSDVSWCLSDS-----------GWIVAtiwtLVEPWTAGCTV 69
Cdd:cd05941 93 LILYTSGTTGRPKGVVLTHAnLAAN--------VRAL-VDAWRWTEDDVllhvlplhhvhGLVNA----LLCPLFAGASV 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 70 fiHHLPQFDTKVIIQTLLKYPINHFWGVSSIYRMILQ---QDFTSIRFPALEHC-----YTGGEVVLPKD-QEEWKRRTG 140
Cdd:cd05941 160 --EFLPKFDPKEVAISRLMPSITVFMGVPTIYTRLLQyyeAHFTDPQFARAAAAerlrlMVSGSAALPVPtLEEWEAITG 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 141 LLLYENYGQSETGLICATYWGMKIKPGFMGKATPPYDVQVIDDKGS-ILPPNTEGNIGIRiKPvrpvSLFMCYEGDPEKT 219
Cdd:cd05941 238 HTLLERYGMTEIGMALSNPLDGERRPGTVGMPLPGVQARIVDEETGePLPRGEVGEIQVR-GP----SVFKEYWNKPEAT 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 220 AKVECGD-FYNTGDRGKMDEEGYICFLGR-SDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVL 297
Cdd:cd05941 313 KEEFTDDgWFKTGDLGVVDEDGYYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVL 392
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 578828480 298 TPQFLSHDKDqltkELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRK 351
Cdd:cd05941 393 RAGAAALSLE----ELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
3-356 |
2.53e-58 |
|
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: 198.94 E-value: 2.53e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPKMAKHSHG-------LALQPSFpgsrklrSLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCTVFIHH-- 73
Cdd:cd05966 236 ILYTSGSTGKPKGVVHTTGgyllyaaTTFKYVF-------DYHPDDIYWCTADIGWITGHSYIVYGPLANGATTVMFEgt 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 74 --LPQFDTKV-IIQtllKYPINHFWGVSSIYRMILQQ--------DFTSIRfpaleHCYTGGEvvlPKDQEEWKrrtglL 142
Cdd:cd05966 309 ptYPDPGRYWdIVE---KHKVTIFYTAPTAIRALMKFgdewvkkhDLSSLR-----VLGSVGE---PINPEAWM-----W 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 143 LYENYG-----------QSETGLICATYW--GMKIKPgfmGKATPP---YDVQVIDDKGSILPPNTEGNIGIRikpvRP- 205
Cdd:cd05966 373 YYEVIGkercpivdtwwQTETGGIMITPLpgATPLKP---GSATRPffgIEPAILDEEGNEVEGEVEGYLVIK----RPw 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 206 VSLFMCYEGDPE---KTAKVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGS 282
Cdd:cd05966 446 PGMARTIYGDHEryeDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGR 525
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578828480 283 PDPIRGEVVKAFIVLTPQFlsHDKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKKETGQ 356
Cdd:cd05966 526 PHDIKGEAIYAFVTLKDGE--EPSDELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKIAAGE 597
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
1-349 |
2.18e-56 |
|
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: 189.61 E-value: 2.18e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 1 MVIFFTSGTTGFPKMAKHSHGlALQPSFPGSRKLRSLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCTVFIhhLPQFDTK 80
Cdd:cd05935 87 ALIPYTSGTTGLPKGCMHTHF-SAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVL--MARWDRE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 81 VIIQTLLKYPINHFWGVSSIYRMIL------QQDFTSIRFPAlehcyTGGEVVLPKDQEEWKRRTGLLLYENYGQSETgl 154
Cdd:cd05935 164 TALELIEKYKVTFWTNIPTMLVDLLatpefkTRDLSSLKVLT-----GGGAPMPPAVAEKLLKLTGLRFVEGYGLTET-- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 155 ICATYWGMKIKPGFMGKATPPYDVQ--VID-DKGSILPPNTEGNIGIRiKPvrpvSLFMCYEGDPEKTAK--VECG--DF 227
Cdd:cd05935 237 MSQTHTNPPLRPKLQCLGIP*FGVDarVIDiETGRELPPNEVGEIVVR-GP----QIFKGYWNRPEETEEsfIEIKgrRF 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 228 YNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFLSHDKD 307
Cdd:cd05935 312 FRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGKVTE 391
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 578828480 308 QltkELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKEL 349
Cdd:cd05935 392 E---DIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
3-344 |
7.33e-55 |
|
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: 189.33 E-value: 7.33e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPKMAKHSHG---LALQPSFpgsRKLRSLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCTVFIHH-LPQF- 77
Cdd:cd17634 237 ILYTSGTTGKPKGVLHTTGgylVYAATTM---KYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLYEgVPNWp 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 78 DTKVIIQTLLKYPINHFWGVSSIYRMILQQDFTSIRFPALEHCYTGGEVVLPKDQEEWKRRTGLL------LYENYGQSE 151
Cdd:cd17634 314 TPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIEGTDRSSLRILGSVGEPINPEAYEWYWKKIgkekcpVVDTWWQTE 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 152 TGLICATYWGMKI--KPGFMGKATPPYDVQVIDDKGSILPPNTEGNI------------GIRIKPVRPVSLFMCYEGdpe 217
Cdd:cd17634 394 TGGFMITPLPGAIelKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLvitdpwpgqtrtLFGDHERFEQTYFSTFKG--- 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 218 ktakvecgdFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVL 297
Cdd:cd17634 471 ---------MYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVL 541
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 578828480 298 TPQFLshDKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKI 344
Cdd:cd17634 542 NHGVE--PSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
1-357 |
1.31e-54 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 187.47 E-value: 1.31e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 1 MVIFFTSGTTGFPKMAKHSHGlALQPSFPGSRKLRSLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCTVFIhhLPQFDTK 80
Cdd:PRK08314 193 AVLPYTSGTTGVPKGCMHTHR-TVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVL--MPRWDRE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 81 VIIQTLLKYPINHfWGvsSIYRMIL---------QQDFTSIRfpalehCYTGGEVVLPKD-QEEWKRRTGLLLYENYGQS 150
Cdd:PRK08314 270 AAARLIERYRVTH-WT--NIPTMVVdflaspglaERDLSSLR------YIGGGGAAMPEAvAERLKELTGLDYVEGYGLT 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 151 ETglICATYWG--MKIKPGFMGKATPPYDVQVID-DKGSILPPNTEGNIgirikPVRPVSLFMCYEGDPEKTAKV----E 223
Cdd:PRK08314 341 ET--MAQTHSNppDRPKLQCLGIPTFGVDARVIDpETLEELPPGEVGEI-----VVHGPQVFKGYWNRPEATAEAfieiD 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 224 CGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPqfls 303
Cdd:PRK08314 414 GKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRP---- 489
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 578828480 304 HDKDQLTKE-LQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKKETGQM 357
Cdd:PRK08314 490 EARGKTTEEeIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQLQEQEKARA 544
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
3-356 |
1.18e-52 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 184.19 E-value: 1.18e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPKMAKHSHG-------LALQPSFpgsrklrSLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCTVfihhlp 75
Cdd:PRK00174 250 ILYTSGSTGKPKGVLHTTGgylvyaaMTMKYVF-------DYKDGDVYWCTADVGWVTGHSYIVYGPLANGATT------ 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 76 qfdtkVIIQTLLKYPINH-FW------GVSSIY------RMILQQ--------DFTSIRfpaLEHcyTGGEvvlPKDQEE 134
Cdd:PRK00174 317 -----LMFEGVPNYPDPGrFWevidkhKVTIFYtaptaiRALMKEgdehpkkyDLSSLR---LLG--SVGE---PINPEA 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 135 WKrrtglLLYENYG-----------QSETG--LICATYWGMKIKPGfmgKATPPY---DVQVIDDKGSILPPNTEGNIGI 198
Cdd:PRK00174 384 WE-----WYYKVVGgercpivdtwwQTETGgiMITPLPGATPLKPG---SATRPLpgiQPAVVDEEGNPLEGGEGGNLVI 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 199 RiKP----VRPVslfmcYeGDPEKTAKV---ECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEH 271
Cdd:PRK00174 456 K-DPwpgmMRTI-----Y-GDHERFVKTyfsTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAH 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 272 PAVAESAVVGSPDPIRGEVVKAFIVL----TPQflshdkDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERK 347
Cdd:PRK00174 529 PKVAEAAVVGRPDDIKGQGIYAFVTLkggeEPS------DELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRR 602
|
....*....
gi 578828480 348 ELRKKETGQ 356
Cdd:PRK00174 603 ILRKIAEGE 611
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
5-351 |
2.31e-52 |
|
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: 180.80 E-value: 2.31e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 5 FTSGTTGFPKMAKHSHGLALQPSFPGSRKLRSLKTSDVswCLSDSGWIVATIW--TLVEPWTAGCT-VFIHHLPQFDTkv 81
Cdd:TIGR02262 168 YSSGSTGMPKGVVHTHSNPYWTAELYARNTLGIREDDV--CFSAAKLFFAYGLgnALTFPMSVGATtVLMGERPTPDA-- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 82 IIQTLLKYPINHFWGVSSIYR-MILQQDFTSIRFPALEHCYTGGEVvLPKD-QEEWKRRTGLLLYENYGQSETGLICATY 159
Cdd:TIGR02262 244 VFDRLRRHQPTIFYGVPTLYAaMLADPNLPSEDQVRLRLCTSAGEA-LPAEvGQRWQARFGVDIVDGIGSTEMLHIFLSN 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 160 WGMKIKPGFMGKATPPYDVQVIDDKGSILPPNTEGNIGIRikpvRPVSLFMcYEGDPEKTAKVECGDFYNTGDRGKMDEE 239
Cdd:TIGR02262 323 LPGDVRYGTSGKPVPGYRLRLVGDGGQDVADGEPGELLIS----GPSSATM-YWNNRAKSRDTFQGEWTRSGDKYVRNDD 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 240 GYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFlshdkDQLTKELQQHVKS 319
Cdd:TIGR02262 398 GSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPGQ-----TALETELKEHVKD 472
|
330 340 350
....*....|....*....|....*....|..
gi 578828480 320 VTAPYKYPRKVEFVSELPKTITGKIERKELRK 351
Cdd:TIGR02262 473 RLAPYKYPRWIVFVDDLPKTATGKIQRFKLRE 504
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
1-352 |
9.80e-52 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 179.33 E-value: 9.80e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 1 MVIFFTSGTTGFPKMAKHSHG------------LALQPsfpGSRKLRSLKTSDVsWCLSdSGWIVATIwtlvepwtAGCT 68
Cdd:PRK07656 169 ADILFTSGTTGRPKGAMLTHRqllsnaadwaeyLGLTE---GDRYLAANPFFHV-FGYK-AGVNAPLM--------RGAT 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 69 VFIHhlPQFDTKVIIQTLLKYPINHFWGVSSIYRMILQQ------DFTSIRFpalehCYTGGEVV----LPKDQEEWKRR 138
Cdd:PRK07656 236 ILPL--PVFDPDEVFRLIETERITVLPGPPTMYNSLLQHpdrsaeDLSSLRL-----AVTGAASMpvalLERFESELGVD 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 139 TGLllyENYGQSE-TGLICATYWG--MKIKPGFMGKATPPYDVQVIDDKGSILPPNTEGNIGIRIKPVrpvslfMC-YEG 214
Cdd:PRK07656 309 IVL---TGYGLSEaSGVTTFNRLDddRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNV------MKgYYD 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 215 DPEKTAKVECGD-FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKA 293
Cdd:PRK07656 380 DPEATAAAIDADgWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKA 459
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 294 FIVLTPqflshdKDQLTKE-LQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKK 352
Cdd:PRK07656 460 YVVLKP------GAELTEEeLIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALREK 513
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
1-344 |
1.70e-50 |
|
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: 175.48 E-value: 1.70e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 1 MVIFFTSGTTGFPKMAKHSH-GLALQPSFPGSRKLRSLKTSDVSWCLSDSGWIVATIWTLVEPWtAGCTVFIHhlPQFDT 79
Cdd:cd05911 149 AAILYSSGTTGLPKGVCLSHrNLIANLSQVQTFLYGNDGSNDVILGFLPLYHIYGLFTTLASLL-NGATVIIM--PKFDS 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 80 KVIIQTLLKYPINHFWGVSSIYRMILQQ-DFTSIRFPALEHCYTGGEVVLPKDQEEWKRRTGLL-LYENYGQSETGLICA 157
Cdd:cd05911 226 ELFLDLIEKYKITFLYLVPPIAAALAKSpLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNAtIKQGYGMTETGGILT 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 158 TYWGMKIKPGFMGKATPPYDVQVIDDKG-SILPPNTEGNIGIRIKpvrpvSLFMCYEGDPEKTAkvECGD---FYNTGDR 233
Cdd:cd05911 306 VNPDGDDKPGSVGRLLPNVEAKIVDDDGkDSLGPNEPGEICVRGP-----QVMKGYYNNPEATK--ETFDedgWLHTGDI 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 234 GKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQflshdkDQLT-KE 312
Cdd:cd05911 379 GYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPG------EKLTeKE 452
|
330 340 350
....*....|....*....|....*....|...
gi 578828480 313 LQQHVKSVTAPYKYPRK-VEFVSELPKTITGKI 344
Cdd:cd05911 453 VKDYVAKKVASYKQLRGgVVFVDEIPKSASGKI 485
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
3-349 |
2.05e-49 |
|
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: 171.56 E-value: 2.05e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPK--MAKHsHGLA-----LQPSFPGSRKLRSLKTSDVSWclsdsgwiVATIWTLVEPWTAGCTVfiHHLP 75
Cdd:cd05930 98 VIYTSGSTGKPKgvMVEH-RGLVnlllwMQEAYPLTPGDRVLQFTSFSF--------DVSVWEIFGALLAGATL--VVLP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 76 Q---FDTKVIIQTLLKYPINHFWGVSSIYRMILQQDFTSiRFPALEHCYTGGEVVLPKDQEEWKRR-TGLLLYENYGQSE 151
Cdd:cd05930 167 EevrKDPEALADLLAEEGITVLHLTPSLLRLLLQELELA-ALPSLRLVLVGGEALPPDLVRRWRELlPGARLVNLYGPTE 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 152 TGlICATYWgmKIKPGFMGKATPP-------YDVQVIDDKGSILPPNTEGNI---GirikpvrpVSLFMCYEGDPEKTAK 221
Cdd:cd05930 246 AT-VDATYY--RVPPDDEEDGRVPigrpipnTRVYVLDENLRPVPPGVPGELyigG--------AGLARGYLNRPELTAE 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 222 VECGD-------FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAF 294
Cdd:cd05930 315 RFVPNpfgpgerMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAY 394
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 578828480 295 IVltpqfLSHDKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKEL 349
Cdd:cd05930 395 VV-----PDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
2-253 |
2.62e-48 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 167.87 E-value: 2.62e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 2 VIFFTSGTTGFPKMAKHSHG----LALQpSFPGSRKLRSLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCT-VFIHHLPQ 76
Cdd:pfam00501 159 YIIYTSGTTGKPKGVMLTHRnlvaNVLS-IKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATvVLPPGFPA 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 77 FDTKVIIQTLLKYPINHFWGVSSIYRMILQQ-DFTSIRFPALEHCYTGGEVVLPKDQEEWKRRTGLLLYENYGQSETGLI 155
Cdd:pfam00501 238 LDPAALLELIERYKVTVLYGVPTLLNMLLEAgAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGV 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 156 CATYWGMKIK---PGFMGKATPPYDVQVIDDK-GSILPPNTEGNIGIRikpvRPvSLFMCYEGDPEKTAKV-ECGDFYNT 230
Cdd:pfam00501 318 VTTPLPLDEDlrsLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVR----GP-GVMKGYLNDPELTAEAfDEDGWYRT 392
|
250 260
....*....|....*....|...
gi 578828480 231 GDRGKMDEEGYICFLGRSDDIIN 253
Cdd:pfam00501 393 GDLGRRDEDGYLEIVGRKKDQIK 415
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
3-351 |
4.25e-48 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 169.03 E-value: 4.25e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPKMAKHSHG-LAlqpsfpgsrklRSLKTSDVSWCLSDS-------------GWIVATIWTLVepwTAGCT 68
Cdd:cd05926 154 ILHTSGTTGRPKGVPLTHRnLA-----------ASATNITNTYKLTPDdrtlvvmplfhvhGLVASLLSTLA---AGGSV 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 69 VFIhhlPQFDTKVIIQTLLKYPINHFWGVSSIYRMILQ--QDFTSIRFPALEHCYTGGEVVLPKDQEEWKRRTGLLLYEN 146
Cdd:cd05926 220 VLP---PRFSASTFWPDVRDYNATWYTAVPTIHQILLNrpEPNPESPPPKLRFIRSCSASLPPAVLEALEATFGAPVLEA 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 147 YGQSETG--LICATYWGMKIKPGFMGKATPPyDVQVIDDKGSILPPNTEGNIGIRIKPVrpvslFMCYEGDPEKTAKV-E 223
Cdd:cd05926 297 YGMTEAAhqMTSNPLPPGPRKPGSVGKPVGV-EVRILDEDGEILPPGVVGEICLRGPNV-----TRGYLNNPEANAEAaF 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 224 CGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFlS 303
Cdd:cd05926 371 KDGWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGA-S 449
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 578828480 304 HDKDQLTKELQQHVksvtAPYKYPRKVEFVSELPKTITGKIERKELRK 351
Cdd:cd05926 450 VTEEELRAFCRKHL----AAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
5-350 |
2.50e-47 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 168.28 E-value: 2.50e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 5 FTSGTTGFPKMAK--HSHGLA--------LQPSFPGSRKLRSLKTsdvswclsdsgwIVA---------TIWTLVEPWTA 65
Cdd:PRK07059 211 YTGGTTGVSKGATllHRNIVAnvlqmeawLQPAFEKKPRPDQLNF------------VCAlplyhifalTVCGLLGMRTG 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 66 GCTVFIHHlPQfDTKVIIQTLLKYPINHFWGVSSIYRMILQQ-DFTSIRFPALEHCYTGGEVVLPKDQEEWKRRTGLLLY 144
Cdd:PRK07059 279 GRNILIPN-PR-DIPGFIKELKKYQVHIFPAVNTLYNALLNNpDFDKLDFSKLIVANGGGMAVQRPVAERWLEMTGCPIT 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 145 ENYGQSETGlICATYWGMKIK--PGFMGKATPPYDVQVIDDKGSILPPNTEGNIGIRIKPVRPvslfmCYEGDPEKTAKV 222
Cdd:PRK07059 357 EGYGLSETS-PVATCNPVDATefSGTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIRGPQVMA-----GYWNRPDETAKV 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 223 ECGD-FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVltpqf 301
Cdd:PRK07059 431 MTADgFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVV----- 505
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 578828480 302 lshDKDQ-LT-KELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELR 350
Cdd:PRK07059 506 ---KKDPaLTeEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
3-349 |
4.39e-46 |
|
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: 162.80 E-value: 4.39e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPKMAKHSHGlALQ-------PSFPGSRKLRSLKTSDVSWCLSdsgwiVATIW-TLVepwTAGCTVFIHHL 74
Cdd:cd05945 102 IIFTSGSTGRPKGVQISHD-NLVsftnwmlSDFPLGPGDVFLNQAPFSFDLS-----VMDLYpALA---SGATLVPVPRD 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 75 PQFDTKVIIQTLLKYPINHFWGVSSIYRMILQ-QDFTSIRFPALEHCYTGGEVvLPKDQ-EEWKRRT-GLLLYENYGQSE 151
Cdd:cd05945 173 ATADPKQLFRFLAEHGITVWVSTPSFAAMCLLsPTFTPESLPSLRHFLFCGEV-LPHKTaRALQQRFpDARIYNTYGPTE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 152 TGLICATY-------WGMKIKPgfMGKATPPYDVQVIDDKGSILPPNTEGNIGIRikpvrPVSLFMCYEGDPEKTAKV-- 222
Cdd:cd05945 252 ATVAVTYIevtpevlDGYDRLP--IGYAKPGAKLVILDEDGRPVPPGEKGELVIS-----GPSVSKGYLNNPEKTAAAff 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 223 --ECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPq 300
Cdd:cd05945 325 pdEGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKP- 403
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 578828480 301 flsHDKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKEL 349
Cdd:cd05945 404 ---GAEAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
1-351 |
1.55e-45 |
|
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: 160.59 E-value: 1.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 1 MVIFFTSGTTGFPKMAKHSHGLALQpSFPGSrKLRSLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCTVFIHhlPQFDTK 80
Cdd:cd05912 80 ATIMYTSGTTGKPKGVQQTFGNHWW-SAIGS-ALNLGLTEDDNWLCALPLFHISGLSILMRSVIYGMTVYLV--DKFDAE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 81 VIIQTLLKYPINHFWGVSSIYRMILQQDFTsiRFPALEHCYTGGEVVLPKDQEEWKRRTGLLLYENYGQSETG--LICAT 158
Cdd:cd05912 156 QVLHLINSGKVTIISVVPTMLQRLLEILGE--GYPNNLRCILLGGGPAPKPLLEQCKEKGIPVYQSYGMTETCsqIVTLS 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 159 YWGMKIKPGFMGKATPPYDVQVIDDKGsilPPNTEGNIGIRIKPVRPvslfmCYEGDPEKTAKVECGDFYNTGDRGKMDE 238
Cdd:cd05912 234 PEDALNKIGSAGKPLFPVELKIEDDGQ---PPYEVGEILLKGPNVTK-----GYLNRPDATEESFENGWFKTGDIGYLDE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 239 EGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFlshDKDQLTKELQQHVk 318
Cdd:cd05912 306 EGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPI---SEEELIAYCSEKL- 381
|
330 340 350
....*....|....*....|....*....|...
gi 578828480 319 svtAPYKYPRKVEFVSELPKTITGKIERKELRK 351
Cdd:cd05912 382 ---AKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
5-356 |
5.00e-45 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 162.12 E-value: 5.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 5 FTSGTTGFPKMAKHSHglalqpsfpgsRKLRSLKTSDVSW---CLSDSGWIVATI-WTLVEPWTAGCTVFIHH------L 74
Cdd:PRK06710 213 YTGGTTGFPKGVMLTH-----------KNLVSNTLMGVQWlynCKEGEEVVLGVLpFFHVYGMTAVMNLSIMQgykmvlI 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 75 PQFDTKVIIQTLLKYPINHFWGVSSIYRMIL------QQDFTSIRfpaleHCYTGGEVVLPKDQEEWKRRTGLLLYENYG 148
Cdd:PRK06710 282 PKFDMKMVFEAIKKHKVTLFPGAPTIYIALLnspllkEYDISSIR-----ACISGSAPLPVEVQEKFETVTGGKLVEGYG 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 149 QSETGLICAT--YWGMKIkPGFMGKATPPYDVQVID-DKGSILPPNTEGNIgirikPVRPVSLFMCYEGDPEKTAKVECG 225
Cdd:PRK06710 357 LTESSPVTHSnfLWEKRV-PGSIGVPWPDTEAMIMSlETGEALPPGEIGEI-----VVKGPQIMKGYWNKPEETAAVLQD 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 226 DFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVltpqfLSHD 305
Cdd:PRK06710 431 GWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVV-----LKEG 505
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 578828480 306 KDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERK-----ELRKKETGQ 356
Cdd:PRK06710 506 TECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRvlieeEKRKNEDEQ 561
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
3-350 |
8.82e-45 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 162.43 E-value: 8.82e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPKMAKHS---HGLALQPS----FPGsrklrslKTSDVSWCLSDSGWIVATIWTLVEPWTAGC-TVFIHHL 74
Cdd:PRK10524 238 ILYTSGTTGKPKGVQRDtggYAVALATSmdtiFGG-------KAGETFFCASDIGWVVGHSYIVYAPLLAGMaTIMYEGL 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 75 P-QFDTKVIIQTLLKYPINHFWGVSSIYRMILQQDFTSIR---FPALEHCYTGGEvvlPKDQE--EWKRRT-GLLLYENY 147
Cdd:PRK10524 311 PtRPDAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDPALLRkhdLSSLRALFLAGE---PLDEPtaSWISEAlGVPVIDNY 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 148 GQSETGL----ICATYWGMKIKPGFMGKATPPYDVQVIDDK-GSILPPNTEGNIGIRiKPVRPVSLFMCYeGDPEKTAKV 222
Cdd:PRK10524 388 WQTETGWpilaIARGVEDRPTRLGSPGVPMYGYNVKLLNEVtGEPCGPNEKGVLVIE-GPLPPGCMQTVW-GDDDRFVKT 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 223 ECGDF----YNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLT 298
Cdd:PRK10524 466 YWSLFgrqvYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPK 545
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 578828480 299 PQFLSHDKDQ---LTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELR 350
Cdd:PRK10524 546 DSDSLADREArlaLEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQ 600
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
5-353 |
1.44e-44 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 160.99 E-value: 1.44e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 5 FTSGTTGFPKMAKHSHG--LA--LQPSFPGSRKLRSLKTsdvswclsdsgwIVATIWTL--VEPWTAGCTVFIH------ 72
Cdd:PRK08974 213 YTGGTTGVAKGAMLTHRnmLAnlEQAKAAYGPLLHPGKE------------LVVTALPLyhIFALTVNCLLFIElggqnl 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 73 ------HLPQFdtkviIQTLLKYPINHFWGVSSIYRMILQ-QDFTSIRFPALEHCYTGGEVVLPKDQEEWKRRTGLLLYE 145
Cdd:PRK08974 281 litnprDIPGF-----VKELKKYPFTAITGVNTLFNALLNnEEFQELDFSSLKLSVGGGMAVQQAVAERWVKLTGQYLLE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 146 NYGQSETG-LICATYWGMKIKPGFMGKATPPYDVQVIDDKGSILPPNTEGNIGIRIKPVrpvslFMCYEGDPEKTAKVEC 224
Cdd:PRK08974 356 GYGLTECSpLVSVNPYDLDYYSGSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVKGPQV-----MLGYWQRPEATDEVIK 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 225 GDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVltpqflsh 304
Cdd:PRK08974 431 DGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVV-------- 502
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 578828480 305 DKDQ-LTK-ELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKKE 353
Cdd:PRK08974 503 KKDPsLTEeELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEA 553
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
3-350 |
1.42e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 157.46 E-value: 1.42e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPKMAKHSHglalqpsfpgsrklRSLKTSDVsWCLSDSGWIVATIWTLVEPWT--AGCTV--------FIH 72
Cdd:PRK06188 173 LAYTGGTTGKPKGVMGTH--------------RSIATMAQ-IQLAEWEWPADPRFLMCTPLShaGGAFFlptllrggTVI 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 73 HLPQFDTKVIIQTLLKYPINHFWGVSS-IYRMILQQDFTSIRFPALEHCYTGGEVVLPKDQEEWKRRTGLLLYENYGQSE 151
Cdd:PRK06188 238 VLAKFDPAEVLRAIEEQRITATFLVPTmIYALLDHPDLRTRDLSSLETVYYGASPMSPVRLAEAIERFGPIFAQYYGQTE 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 152 TGlICATYWG----MKIKPGFM---GKATPPYDVQVIDDKGSILPPNTEGNIGIRiKPvrpvsLFMC-YEGDPEKTAKVE 223
Cdd:PRK06188 318 AP-MVITYLRkrdhDPDDPKRLtscGRPTPGLRVALLDEDGREVAQGEVGEICVR-GP-----LVMDgYWNRPEETAEAF 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 224 CGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPqfls 303
Cdd:PRK06188 391 RDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRP---- 466
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 578828480 304 hDKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELR 350
Cdd:PRK06188 467 -GAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALR 512
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
3-352 |
3.77e-43 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 156.19 E-value: 3.77e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPKMAKHSHG------LALQPSF---PGSRKLRSLKTSDVSwclsdsGWIVATIWTLVepwtAGCTVFIhh 73
Cdd:PRK07514 161 ILYTSGTTGRSKGAMLSHGnllsnaLTLVDYWrftPDDVLIHALPIFHTH------GLFVATNVALL----AGASMIF-- 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 74 LPQFDTKVIIQTLLKYPInhFWGVSSIYRMILQQdftsirfPAL--EHC------YTGGEVVLPKDQEEWKRRTGLLLYE 145
Cdd:PRK07514 229 LPKFDPDAVLALMPRATV--MMGVPTFYTRLLQE-------PRLtrEAAahmrlfISGSAPLLAETHREFQERTGHAILE 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 146 NYGQSETGLICAT-YWGMKIkPGFMGKATPPYDVQVID-DKGSILPPNTEGNIgirikPVRPVSLFMCYEGDPEKTAKVE 223
Cdd:PRK07514 300 RYGMTETNMNTSNpYDGERR-AGTVGFPLPGVSLRVTDpETGAELPPGEIGMI-----EVKGPNVFKGYWRMPEKTAEEF 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 224 CGD-FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFl 302
Cdd:PRK07514 374 RADgFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGA- 452
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 578828480 303 SHDKDQLTKELQQHVksvtAPYKYPRKVEFVSELPKTITGKIERKELRKK 352
Cdd:PRK07514 453 ALDEAAILAALKGRL----ARFKQPKRVFFVDELPRNTMGKVQKNLLREQ 498
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
2-351 |
3.95e-43 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 157.08 E-value: 3.95e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 2 VIFFTSGTTGFPKMAKHSHglalqpsfpgsRKLRSLKTSDVSWC--LSDSGWIV-----------ATIWTLVEPWTAGCT 68
Cdd:PRK05605 223 LILYTSGTTGKPKGAQLTH-----------RNLFANAAQGKAWVpgLGDGPERVlaalpmfhaygLTLCLTLAVSIGGEL 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 69 VFihhLPQFDTKVIIQTLLKYPINHFWGVSSIYRMILQQ------DFTSIRFpALEhcytgGEVVLPKDQ-EEWKRRTGL 141
Cdd:PRK05605 292 VL---LPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAaeergvDLSGVRN-AFS-----GAMALPVSTvELWEKLTGG 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 142 LLYENYGQSETG-LICATYWGMKIKPGFMGKATPPYDVQVID--DKGSILPPNTEGNIGIRIKPVrpvslFMCYEGDPEK 218
Cdd:PRK05605 363 LLVEGYGLTETSpIIVGNPMSDDRRPGYVGVPFPDTEVRIVDpeDPDETMPDGEEGELLVRGPQV-----FKGYWNRPEE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 219 TAKVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLT 298
Cdd:PRK05605 438 TAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLE 517
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 578828480 299 PQfLSHDKDqltkELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRK 351
Cdd:PRK05605 518 PG-AALDPE----GLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVRE 565
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
5-350 |
7.20e-43 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 156.19 E-value: 7.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 5 FTSGTTGFPKMAKHSHglalqpsfpgsRKLRSLKTSDVSWcLSDSGWIVA---TIWTLVEPW-----TAGCTVFI----- 71
Cdd:PRK08751 215 YTGGTTGVAKGAMLTH-----------RNLVANMQQAHQW-LAGTGKLEEgceVVITALPLYhifalTANGLVFMkiggc 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 72 HHL---PQfDTKVIIQTLLKYPINHFWGVSSIYRMILQQ-DFTSIRFPALEHCYTGGEVVLPKDQEEWKRRTGLLLYENY 147
Cdd:PRK08751 283 NHLisnPR-DMPGFVKELKKTRFTAFTGVNTLFNGLLNTpGFDQIDFSSLKMTLGGGMAVQRSVAERWKQVTGLTLVEAY 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 148 GQSETG-LICATYWGMKIKPGFMGKATPPYDVQVIDDKGSILPPNTEGNIGIRIKPVrpvslFMCYEGDPEKTAKVECGD 226
Cdd:PRK08751 362 GLTETSpAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQV-----MKGYWKRPEETAKVMDAD 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 227 -FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFLSHD 305
Cdd:PRK08751 437 gWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVKKDPALTAE 516
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 578828480 306 kdqltkELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELR 350
Cdd:PRK08751 517 ------DVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELR 555
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
74-346 |
1.22e-42 |
|
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: 150.88 E-value: 1.22e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 74 LPQFDTKVIIQTLLKYPINHFWGVSSIYRMILQQ-DFTSIRFPALEHCyTGGEVvlPKDQEEWKRRTGLLLYENYGQSET 152
Cdd:cd17637 72 MEKFDPAEALELIEEEKVTLMGSFPPILSNLLDAaEKSGVDLSSLRHV-LGLDA--PETIQRFEETTGATFWSLYGQTET 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 153 -GLIcaTYWGMKIKPGFMGKATPPYDVQVIDDKGSILPPNTEGNIGIRIKPVrpvslFMCYEGDPEKTAKVECGDFYNTG 231
Cdd:cd17637 149 sGLV--TLSPYRERPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLV-----FQGYWNLPELTAYTFRNGWHHTG 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 232 DRGKMDEEGYICFLGRS--DDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTP-QFLShdkdq 308
Cdd:cd17637 222 DLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPgATLT----- 296
|
250 260 270
....*....|....*....|....*....|....*...
gi 578828480 309 lTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIER 346
Cdd:cd17637 297 -ADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
5-349 |
3.08e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 154.81 E-value: 3.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 5 FTSGTTGFPKMAKHSHG--LALQPSFPGSRKLRSlkTSDVSWCLSDSGWIVATIWTLVEPWTAGCTVFIhhLPQFDTKVI 82
Cdd:PRK06178 216 YTGGTTGMPKGCEHTQRdmVYTAAAAYAVAVVGG--EDSVFLSFLPEFWIAGENFGLLFPLFSGATLVL--LARWDAVAF 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 83 IQTLLKYPINHFWGVSSIYRMIL------QQDFTSIRFPaleHCYTGGEVVLPKDQEEWKRRTGLLLYE-NYGQSETGlI 155
Cdd:PRK06178 292 MAAVERYRVTRTVMLVDNAVELMdhprfaEYDLSSLRQV---RVVSFVKKLNPDYRQRWRALTGSVLAEaAWGMTETH-T 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 156 CATY-WGM-------KIKPGFMGKATPPYDVQVID-DKGSILPPNTEGNIgirikPVRPVSLFMCYEGDPEKTAKVECGD 226
Cdd:PRK06178 368 CDTFtAGFqdddfdlLSQPVFVGLPVPGTEFKICDfETGELLPLGAEGEI-----VVRTPSLLKGYWNKPEATAEALRDG 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 227 FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPqflshDK 306
Cdd:PRK06178 443 WLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKP-----GA 517
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 578828480 307 DQLTKELQQHVKSVTAPYKYPrKVEFVSELPKTITGKIERKEL 349
Cdd:PRK06178 518 DLTAAALQAWCRENMAVYKVP-EIRIVDALPMTATGKVRKQDL 559
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
3-350 |
1.68e-41 |
|
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: 148.19 E-value: 1.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPKMAKHSHGLALQPSFPGSRKLRSlkTSDVSWCLSD-----SGWIVATIWTLvepwTAGCT-VFIHhlPQ 76
Cdd:cd05917 7 IQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGL--TEQDRLCIPVplfhcFGSVLGVLACL----THGATmVFPS--PS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 77 FDTKVIIQTLLKYPINHFWGVSSIY-RMILQQDFTSIRFPALEHCYTGGEVV---LPKDQEEWKRRTGLLLyeNYGQSET 152
Cdd:cd05917 79 FDPLAVLEAIEKEKCTALHGVPTMFiAELEHPDFDKFDLSSLRTGIMAGAPCppeLMKRVIEVMNMKDVTI--AYGMTET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 153 GLICA---TYWGMKIKPGFMGKATPPYDVQVIDDKGSILPP-NTEGNIGIRikpvrPVSLFMCYEGDPEKTAKVECGD-F 227
Cdd:cd05917 157 SPVSTqtrTDDSIEKRVNTVGRIMPHTEAKIVDPEGGIVPPvGVPGELCIR-----GYSVMKGYWNDPEKTAEAIDGDgW 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 228 YNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLtpqflsHDKD 307
Cdd:cd05917 232 LHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRL------KEGA 305
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 578828480 308 QLTKE-LQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELR 350
Cdd:cd05917 306 ELTEEdIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
3-351 |
2.37e-41 |
|
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: 149.84 E-value: 2.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPKMAKHSHGLALQPSFPGSRKLrSLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCTVfiHHLPQFDTKVI 82
Cdd:cd05903 98 LLFTSGTTGEPKGVMHSHNTLSASIRQYAERL-GLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPV--VLQDIWDPDKA 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 83 IQTLLKYPINHFWGVSS-IYRMILQQDFTSIRFPALEHCYTGGEVVLPKDQEEWKRRTGLLLYENYGQSETGLICATywg 161
Cdd:cd05903 175 LALMREHGVTFMMGATPfLTDLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTS--- 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 162 mkIKPG----FM---GKATPPYDVQVIDDKGSILPPNTEGNIGIRikpvrPVSLFMCYEGDPEKTAKVECGDFYNTGDRG 234
Cdd:cd05903 252 --ITPApedrRLytdGRPLPGVEIKVVDDTGATLAPGVEGELLSR-----GPSVFLGYLDRPDLTADAAPEGWFRTGDLA 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 235 KMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVL-TPQFLSHDkdqltkEL 313
Cdd:cd05903 325 RLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTkSGALLTFD------EL 398
|
330 340 350
....*....|....*....|....*....|....*....
gi 578828480 314 QQHVKSV-TAPYKYPRKVEFVSELPKTITGKIERKELRK 351
Cdd:cd05903 399 VAYLDRQgVAKQYWPERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
2-352 |
6.25e-41 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 150.68 E-value: 6.25e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 2 VIFFTSGTTGFPKMAKHshglalqPSFPGSRKLRSLkTSDVSWCLSDSGWIVATI---WTLVEPWTAG---CTVFIHHlp 75
Cdd:PRK13382 200 VILLTSGTTGTPKGARR-------SGPGGIGTLKAI-LDRTPWRAEEPTVIVAPMfhaWGFSQLVLAAslaCTIVTRR-- 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 76 QFDTKVIIQTLLKYPINHFWGVSSIYRMILQ--------QDFTSIRFPAlehcyTGGEVVLPKDQEEWKRRTGLLLYENY 147
Cdd:PRK13382 270 RFDPEATLDLIDRHRATGLAVVPVMFDRIMDlpaevrnrYSGRSLRFAA-----ASGSRMRPDVVIAFMDQFGDVIYNNY 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 148 GQSETGLIC-ATYWGMKIKPGFMGKATPPYDVQVIDDKGSILPPNTEGNIGirikpVRPVSLFMCYEgdPEKTAKVECGd 226
Cdd:PRK13382 345 NATEAGMIAtATPADLRAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIF-----VRNDTQFDGYT--SGSTKDFHDG- 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 227 FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPqflshDK 306
Cdd:PRK13382 417 FMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKP-----GA 491
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 578828480 307 DQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKK 352
Cdd:PRK13382 492 SATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
2-350 |
1.75e-40 |
|
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: 147.97 E-value: 1.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 2 VIFFTSGTTGFPKMAKHSH-----GLALQPSFPGSRKL-RSLKTSDVSWCLsdsGWIVATIWTLVepwtaGCTVFIHHLP 75
Cdd:cd05922 121 LLLYTSGSTGSPKLVRLSHqnllaNARSIAEYLGITADdRALTVLPLSYDY---GLSVLNTHLLR-----GATLVLTNDG 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 76 QFDTKVIiQTLLKYPINHFWGVSSIYRMILQQDFTSIRFPALEH-CYTGGEvvLPkdQEEWKRRTGLL----LYENYGQS 150
Cdd:cd05922 193 VLDDAFW-EDLREHGATGLAGVPSTYAMLTRLGFDPAKLPSLRYlTQAGGR--LP--QETIARLRELLpgaqVYVMYGQT 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 151 ETGLICATYWGMKI--KPGFMGKATPPYDVQVIDDKGSILPPNTEGNIGIRikpvRPVSLFMCYEGDPEKTAKVECGDFY 228
Cdd:cd05922 268 EATRRMTYLPPERIleKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHR----GPNVMKGYWNDPPYRRKEGRGGGVL 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 229 NTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIrGEVVKAFIVLTPQFLSHDkdq 308
Cdd:cd05922 344 HTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPL-GEKLALFVTAPDKIDPKD--- 419
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 578828480 309 ltkeLQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELR 350
Cdd:cd05922 420 ----VLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
124-350 |
1.89e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 145.52 E-value: 1.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 124 GEVVLP-KDQEEWKRRTGLLLYENYGQSETGLICATYWGMKIKPGFMGKATPPYDVQVIDDKGSILPPNTEgNIGiRIKp 202
Cdd:PRK07787 249 GSAALPvPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRLVDEDGGPVPHDGE-TVG-ELQ- 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 203 VRPVSLFMCYEGDPEKTAKVECGD-FYNTGDRGKMDEEGYICFLGR-SDDIINASGYRIGPAEVESALVEHPAVAESAVV 280
Cdd:PRK07787 326 VRGPTLFDGYLNRPDATAAAFTADgWFRTGDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIETALLGHPGVREAAVV 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 281 GSPDPIRGEVVKAFIVltpqflSHDkDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELR 350
Cdd:PRK07787 406 GVPDDDLGQRIVAYVV------GAD-DVAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
88-350 |
2.14e-39 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 145.98 E-value: 2.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 88 KYPINHFWGVSSIYR--------MILQqdfTSIRFPALE----HCYTGGEVVLP-KDQEE--WKRRTGLLLYENYGQSET 152
Cdd:PRK08008 248 KYSARAFWGQVCKYRatitecipMMIR---TLMVQPPSAndrqHCLREVMFYLNlSDQEKdaFEERFGVRLLTSYGMTET 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 153 --GLICAT-----YWGMKIKPGFMgkatppYDVQVIDDKGSILPPNTEGNIgiRIKPVRPVSLFMCYEGDPEKTAKVECG 225
Cdd:PRK08008 325 ivGIIGDRpgdkrRWPSIGRPGFC------YEAEIRDDHNRPLPAGEIGEI--CIKGVPGKTIFKEYYLDPKATAKVLEA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 226 D-FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPqflsh 304
Cdd:PRK08008 397 DgWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNE----- 471
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 578828480 305 dKDQLTKE-LQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELR 350
Cdd:PRK08008 472 -GETLSEEeFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
1-356 |
6.32e-39 |
|
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: 146.10 E-value: 6.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 1 MVIFfTSGTTGFPKMAKHSH-GLALQPSFPGSRKLrSLKTSDVSWCLSDSGWIVATiWTLVEPWTAGCTVFIHH-LPQFD 78
Cdd:cd05968 240 MIIY-TSGTTGKPKGTVHVHaGFPLKAAQDMYFQF-DLKPGDLLTWFTDLGWMMGP-WLIFGGLILGATMVLYDgAPDHP 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 79 TKV-IIQTLLKYPINHFwGVS-SIYRMILQQDFTSIRFPALEHCYTGGEVVLPKDQEEWkrrtgLLLYENYGQSE----- 151
Cdd:cd05968 317 KADrLWRMVEDHEITHL-GLSpTLIRALKPRGDAPVNAHDLSSLRVLGSTGEPWNPEPW-----NWLFETVGKGRnpiin 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 152 -------TGLICATYWGMKIKPGFMGKATPPYDVQVIDDKGSILPPnTEGNIGIRiKPVrpVSLFMCYEGDPEKT----- 219
Cdd:cd05968 391 ysggteiSGGILGNVLIKPIKPSSFNGPVPGMKADVLDESGKPARP-EVGELVLL-APW--PGMTRGFWRDEDRYletyw 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 220 AKVEcgDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTP 299
Cdd:cd05968 467 SRFD--NVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKP 544
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 578828480 300 QFlsHDKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKKETGQ 356
Cdd:cd05968 545 GV--TPTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAAYLGK 599
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
4-352 |
7.39e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 144.80 E-value: 7.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 4 FFTSGTTGFPKMAKHSHG-LA------LQPSFPGSRKL-RSLKTSDVSwclsdSGwivATIWTLVEPWTAGCTVFihhLP 75
Cdd:PRK07470 169 FFTSGTTGRPKAAVLTHGqMAfvitnhLADLMPGTTEQdASLVVAPLS-----HG---AGIHQLCQVARGAATVL---LP 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 76 --QFDTKVIIQTLLKYPINHFWGVSSIYRMIL------QQDFTSIRfpaleHCYTGGEVVLPKDQEEWKRRTGLLLYENY 147
Cdd:PRK07470 238 seRFDPAEVWALVERHRVTNLFTVPTILKMLVehpavdRYDHSSLR-----YVIYAGAPMYRADQKRALAKLGKVLVQYF 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 148 GQSE-TGLIC-------ATYWGMKIKPGFMGKATPPYDVQVIDDKGSILPPNTEGNIGIRIKPVrpvslFMCYEGDPEKT 219
Cdd:PRK07470 313 GLGEvTGNITvlppalhDAEDGPDARIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAV-----FAGYYNNPEAN 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 220 AKVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTp 299
Cdd:PRK07470 388 AKAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVAR- 466
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 578828480 300 qflshDKDQLTK-ELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKK 352
Cdd:PRK07470 467 -----DGAPVDEaELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREE 515
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
78-357 |
7.85e-39 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 145.29 E-value: 7.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 78 DTKVIIQTLLKYPINHFWGVSSIYRMILQ-QDFTSIRFPALEHCYTGGEVVLPKDQEEWKRRTGLLLYENYGQSETGLIC 156
Cdd:PRK05677 288 DLPAMVKELGKWKFSGFVGLNTLFVALCNnEAFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVV 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 157 ATYWGMKIKPGFMGKATPPYDVQVIDDKGSILPPNTEGNIGIRIKPVrpvslFMCYEGDPEKTAKVECGD-FYNTGDRGK 235
Cdd:PRK05677 368 SVNPSQAIQVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQV-----MKGYWQRPEATDEILDSDgWLKTGDIAL 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 236 MDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPqflshdKDQLTKE-LQ 314
Cdd:PRK05677 443 IQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKP------GETLTKEqVM 516
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 578828480 315 QHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKKETGQM 357
Cdd:PRK05677 517 EHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRDEELKKA 559
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
3-350 |
1.05e-38 |
|
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: 143.67 E-value: 1.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPKMAKHSHGLALQPSFPGsrklrslktsdVSWCLSdSGWIVATIWTLVEP--------WT-----AGCTV 69
Cdd:cd05929 130 MLYSGGTTGRPKGIKRGLPGGPPDNDTL-----------MAAALG-FGPGADSVYLSPAPlyhaapfrWSmtalfMGGTL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 70 FIhhLPQFDTKVIIQTLLKYPINHFWGVSSIYRMILQ--------QDFTSIRfpalEHCYTGGeVVLPKDQEEWKRRTGL 141
Cdd:cd05929 198 VL--MEKFDPEEFLRLIERYRVTFAQFVPTMFVRLLKlpeavrnaYDLSSLK----RVIHAAA-PCPPWVKEQWIDWGGP 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 142 LLYENYGQSE-TGLIC--ATYWgmKIKPGFMGKATPPyDVQVIDDKGSILPPNTEGNIGIRIKPvrPVSlfmcYEGDPEK 218
Cdd:cd05929 271 IIWEYYGGTEgQGLTIinGEEW--LTHPGSVGRAVLG-KVHILDEDGNEVPPGEIGEVYFANGP--GFE----YTNDPEK 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 219 TA-KVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAfiVL 297
Cdd:cd05929 342 TAaARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHA--VV 419
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 578828480 298 TPQFLSHDKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELR 350
Cdd:cd05929 420 QPAPGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
2-350 |
1.13e-38 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 144.00 E-value: 1.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 2 VIFFTSGTTGFPKmakhshglALQPSFPG-------------SRKLRSLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCT 68
Cdd:PRK13390 152 VMLYSSGTTGFPK--------GIQPDLPGrdvdapgdpivaiARAFYDISESDIYYSSAPIYHAAPLRWCSMVHALGGTV 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 69 VFIHhlpQFDTKVIIQTLLKYPINHFWGVSSIYRMILQ--------QDFTSIRfpALEHCYTGGEVVLPKDQEEWkrrTG 140
Cdd:PRK13390 224 VLAK---RFDAQATLGHVERYRITVTQMVPTMFVRLLKldadvrtrYDVSSLR--AVIHAAAPCPVDVKHAMIDW---LG 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 141 LLLYENYGQSET-GLICATYWGMKIKPGFMGKATPPyDVQVIDDKGSILPPNTEGNIGIRiKPVRPVSlfmcYEGDPEKT 219
Cdd:PRK13390 296 PIVYEYYSSTEAhGMTFIDSPDWLAHPGSVGRSVLG-DLHICDDDGNELPAGRIGTVYFE-RDRLPFR----YLNDPEKT 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 220 AKVE--CGDFYNT-GDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIV 296
Cdd:PRK13390 370 AAAQhpAHPFWTTvGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQ 449
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 578828480 297 LTPQFlsHDKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELR 350
Cdd:PRK13390 450 LVEGI--RGSDELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
3-351 |
1.61e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 143.92 E-value: 1.61e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPKMAKHSHglalqpsfpgsrklRSLKTSDVSwCLSDSGWIVATIWTLVEPW--TAGCTVFIhhLPQF--- 77
Cdd:PRK08316 176 ILYTSGTESLPKGAMLTH--------------RALIAEYVS-CIVAGDMSADDIPLHALPLyhCAQLDVFL--GPYLyvg 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 78 ---------DTKVIIQTLLKYPINHFWGVSSIYRMILQQ-DFTSIRFPALEHCYTGGEV----VLpkdqEEWKRR-TGLL 142
Cdd:PRK08316 239 atnvildapDPELILRTIEAERITSFFAPPTVWISLLRHpDFDTRDLSSLRKGYYGASImpveVL----KELRERlPGLR 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 143 LYENYGQSETGLIcATYWGMK---IKPGFMGKATPPYDVQVIDDKGSILPPNTEGNIGIRikpvRPVSLFMcYEGDPEKT 219
Cdd:PRK08316 315 FYNCYGQTEIAPL-ATVLGPEehlRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHR----SPQLMLG-YWDDPEKT 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 220 AKVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTP 299
Cdd:PRK08316 389 AEAFRGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKA 468
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 578828480 300 qflshDKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRK 351
Cdd:PRK08316 469 -----GATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRE 515
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
5-351 |
2.23e-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: 142.82 E-value: 2.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 5 FTSGTTGFPKMAKHSHGLALqpsfpgsrkLRSLKTSdVSWCLSDSG---WIV----ATIWTLvePWT----AGCTVFihh 73
Cdd:cd12118 140 YTSGTTGRPKGVVYHHRGAY---------LNALANI-LEWEMKQHPvylWTLpmfhCNGWCF--PWTvaavGGTNVC--- 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 74 LPQFDTKVIIQTLLKYPINHFWGVSSIYRMILQ-QDFTSIRFPALEHCYTGG----EVVLPKDQEEwkrrtGLLLYENYG 148
Cdd:cd12118 205 LRKVDAKAIYDLIEKHKVTHFCGAPTVLNMLANaPPSDARPLPHRVHVMTAGapppAAVLAKMEEL-----GFDVTHVYG 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 149 QSET-GLICATYW-------------GMKIKPGFMGKATPPydVQVIDDKGSILPP---NTEGNIGIRIKPVrpvslfMC 211
Cdd:cd12118 280 LTETyGPATVCAWkpewdelpteeraRLKARQGVRYVGLEE--VDVLDPETMKPVPrdgKTIGEIVFRGNIV------MK 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 212 -YEGDPEKTAKVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEV 290
Cdd:cd12118 352 gYLKNPEATAEAFRGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEV 431
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578828480 291 VKAFIVLtpqflsHDKDQLT-KELQQHVKSVTAPYKYPRKVEFvSELPKTITGKIERKELRK 351
Cdd:cd12118 432 PCAFVEL------KEGAKVTeEEIIAFCREHLAGFMVPKTVVF-GELPKTSTGKIQKFVLRD 486
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
5-350 |
2.28e-38 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 143.30 E-value: 2.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 5 FTSGTTGFPKMAKHSHGLALQpsfpgsrklrslktsdvswcLSDSGWIVATIWTLVEPWTAGCTVFIHH----------- 73
Cdd:PRK12406 159 YTSGTTGHPKGVRRAAPTPEQ--------------------AAAAEQMRALIYGLKPGIRALLTGPLYHsapnayglrag 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 74 --------LPQFDTKVIIQTLLKYPINHFWGVSSIYRMILQ--------QDFTSIRFpalehcYTGGEVVLPKDQE---- 133
Cdd:PRK12406 219 rlggvlvlQPRFDPEELLQLIERHRITHMHMVPTMFIRLLKlpeevrakYDVSSLRH------VIHAAAPCPADVKrami 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 134 EWkrrTGLLLYENYGQSETGLIC-ATYWGMKIKPGFMGKATPPYDVQVIDDKGSILPPNTEGNIGIRIkPVRPvsLFMcY 212
Cdd:PRK12406 293 EW---WGPVIYEYYGSTESGAVTfATSEDALSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRI-AGNP--DFT-Y 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 213 EGDPEKTAKVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVK 292
Cdd:PRK12406 366 HNKPEKRAEIDRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALM 445
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578828480 293 AfiVLTPQ---FLSHDkdqltkELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELR 350
Cdd:PRK12406 446 A--VVEPQpgaTLDEA------DIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLR 498
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
140-352 |
3.16e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 142.74 E-value: 3.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 140 GLLLYENYGQSETGLIC-ATYWGMKIKPGFMGKATPPyDVQVIDDKGSILPPNTEGNIGIRiKPVRPVSlfmcYEGDPEK 218
Cdd:PRK08276 287 GPIIHEYYASSEGGGVTvITSEDWLAHPGSVGKAVLG-EVRILDEDGNELPPGEIGTVYFE-MDGYPFE----YHNDPEK 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 219 TAKVECG-DFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAfiVL 297
Cdd:PRK08276 361 TAAARNPhGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKA--VV 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 578828480 298 TPQFLSHDKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKK 352
Cdd:PRK08276 439 QPADGADAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDR 493
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
4-351 |
3.97e-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: 341266 [Multi-domain] Cd Length: 359 Bit Score: 139.54 E-value: 3.97e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 4 FFTSGTTGFPKMAKHSHGLALQPSFPGSRKLRSlKTSDVSWCLSDSGWIVATIWTLVEPWTAGCTVFIHHLPQFDTKVII 83
Cdd:cd05944 8 FHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLF-DPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAGPAGYRNPGLF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 84 QTLLK----YPINHFWGVSSIYRMILQ----QDFTSIRFPAlehcytGGEVVLPKD-QEEWKRRTGLLLYENYGQSE-TG 153
Cdd:cd05944 87 DNFWKlverYRITSLSTVPTVYAALLQvpvnADISSLRFAM------SGAAPLPVElRARFEDATGLPVVEGYGLTEaTC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 154 LICATYWGMKIKPGFMGKATPPYDVQ--VIDDKGSIL---PPNTEGNIGIRIKPVRPVSLFmcyeGDPEKTAKVECGdFY 228
Cdd:cd05944 161 LVAVNPPDGPKRPGSVGLRLPYARVRikVLDGVGRLLrdcAPDEVGEICVAGPGVFGGYLY----TEGNKNAFVADG-WL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 229 NTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPqflshDKDQ 308
Cdd:cd05944 236 NTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKP-----GAVV 310
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 578828480 309 LTKELQQHV-KSVTAPYKYPRKVEFVSELPKTITGKIERKELRK 351
Cdd:cd05944 311 EEEELLAWArDHVPERAAVPKHIEVLEELPVTAVGKVFKPALRA 354
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
127-355 |
1.14e-37 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 141.82 E-value: 1.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 127 VLPKDQEEWKRRTGLLLYENYGQSETGLICATYWGMKiKPGFMGKATPPYDVQVIDDKGSILPPNTEGNIGIRIKPvrPV 206
Cdd:PRK06155 304 VPAALHAAFRERFGVDLLDGYGSTETNFVIAVTHGSQ-RPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRADE--PF 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 207 SLFMCYEGDPEKTAKVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPI 286
Cdd:PRK06155 381 AFATGYFGMPEKTVEAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSEL 460
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 287 RGEVVKAFIVLTP-QFLSHDkdqltkELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRkkETG 355
Cdd:PRK06155 461 GEDEVMAAVVLRDgTALEPV------ALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLR--EQG 522
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
4-354 |
2.15e-37 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 142.02 E-value: 2.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 4 FFTSGTTGFPKMAKHSHGlalqpsfpgsrklrslktSDVSwclsdSGWIVATIWTLVEpwtaGCTVFiHHLPQFDTKVII 83
Cdd:PRK07529 219 FHTGGTTGMPKLAQHTHG------------------NEVA-----NAWLGALLLGLGP----GDTVF-CGLPLFHVNALL 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 84 QTLL-------------------------------KYPINHFWGVSSIYRMILQQ-----DFTSIRFPAlehcytGGEVV 127
Cdd:PRK07529 271 VTGLaplargahvvlatpqgyrgpgvianfwkiveRYRINFLSGVPTVYAALLQVpvdghDISSLRYAL------CGAAP 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 128 LPKD-QEEWKRRTGLLLYENYGQSE-TGLICATYWGMKIKPGFMGKATPPYDVQVI--DDKGSIL---PPNTEGNIGIRI 200
Cdd:PRK07529 345 LPVEvFRRFEAATGVRIVEGYGLTEaTCVSSVNPPDGERRIGSVGLRLPYQRVRVVilDDAGRYLrdcAVDEVGVLCIAG 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 201 KPVrpvslFMCY-EGDPEKTAKVEcGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAV 279
Cdd:PRK07529 425 PNV-----FSGYlEAAHNKGLWLE-DGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAA 498
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578828480 280 VGSPDPIRGEVVKAFIVLTPQfLSHDKDQLTKELQQHVKSVTApykYPRKVEFVSELPKTITGKIERKELRKKET 354
Cdd:PRK07529 499 VGRPDAHAGELPVAYVQLKPG-ASATEAELLAFARDHIAERAA---VPKHVRILDALPKTAVGKIFKPALRRDAI 569
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
3-349 |
5.20e-37 |
|
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: 139.29 E-value: 5.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPKMAKHSHG-----LALQPSFPGSRKLRSlktsDVSWCLSDSGWIVATIWTLVEPWTAGCTVFIhhLPQF 77
Cdd:cd05904 163 LLYSSGTTGRSKGVMLTHRnliamVAQFVAGEGSNSDSE----DVFLCVLPMFHIYGLSSFALGLLRLGATVVV--MPRF 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 78 DTKVIIQTLLKYPINHFWGVSSIYRMILQQDFT-SIRFPALEHCYTGGeVVLPKD-QEEWKRR-TGLLLYENYGQSETGL 154
Cdd:cd05904 237 DLEELLAAIERYKVTHLPVVPPIVLALVKSPIVdKYDLSSLRQIMSGA-APLGKElIEAFRAKfPNVDLGQGYGMTESTG 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 155 ICATYW---GMKIKPGFMGKATPPYDVQVID-DKGSILPPNTEGNIGIRiKPvrpvSLFMCYEGDPEKTAKVECGD-FYN 229
Cdd:cd05904 316 VVAMCFapeKDRAKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIR-GP----SIMKGYLNNPEATAATIDKEgWLH 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 230 TGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQ-FLSHDkdq 308
Cdd:cd05904 391 TGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGsSLTED--- 467
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 578828480 309 ltkELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKEL 349
Cdd:cd05904 468 ---EIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
3-351 |
7.85e-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: 138.92 E-value: 7.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPKMAKHSH--------GLALQPSFPgsrklrsLKTSDV-----------SWCLSDSGWIVATiwTLVEPw 63
Cdd:cd12119 168 ICYTSGTTGNPKGVVYSHrslvlhamAALLTDGLG-------LSESDVvlpvvpmfhvnAWGLPYAAAMVGA--KLVLP- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 64 taGctvfihhlPQFDTKVIIQTLLKYPINHFWGVSSIYRMILQ-QDFTSIRFPALEHCYTGGEVVLPKDQEEWKRRtGLL 142
Cdd:cd12119 238 --G--------PYLDPASLAELIEREGVTFAAGVPTVWQGLLDhLEANGRDLSSLRRVVIGGSAVPRSLIEAFEER-GVR 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 143 LYENYGQSET--------------GLICATYWGMKIKPGFmgkatPPYDVQ--VIDDKGSILP--PNTEGNIGIRiKPVR 204
Cdd:cd12119 307 VIHAWGMTETsplgtvarppsehsNLSEDEQLALRAKQGR-----PVPGVElrIVDDDGRELPwdGKAVGELQVR-GPWV 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 205 PVSlfmcYEGDPEKTAKVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPD 284
Cdd:cd12119 381 TKS----YYKNDEESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPH 456
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578828480 285 PIRGEVVKAFIVLTPqflshDKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRK 351
Cdd:cd12119 457 PKWGERPLAVVVLKE-----GATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
3-351 |
9.79e-37 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 139.11 E-value: 9.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPK--MAKHSHGLALQPSFPGSRKLRSLktsDVSWCLSDSGWIVATIWTLVEPWTAGCTVFIhhLPQFDTK 80
Cdd:PRK06087 192 VLFTSGTEGLPKgvMLTHNNILASERAYCARLNLTWQ---DVFMMPAPLGHATGFLHGVTAPFLIGARSVL--LDIFTPD 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 81 VIIQTLLKYPINHFWGVSS-IYRMI--LQQ---DFTSIRFpalehcYTGGEVVLPKDQEEWKRRTGLLLYENYGQSETG- 153
Cdd:PRK06087 267 ACLALLEQQRCTCMLGATPfIYDLLnlLEKqpaDLSALRF------FLCGGTTIPKKVARECQQRGIKLLSVYGSTESSp 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 154 -----LICATYWGMkikpGFMGKATPPYDVQVIDDKGSILPPNTEGNigiriKPVRPVSLFMCYEGDPEKTAKV--ECGD 226
Cdd:PRK06087 341 havvnLDDPLSRFM----HTDGYAAAGVEIKVVDEARKTLPPGCEGE-----EASRGPNVFMGYLDEPELTARAldEEGW 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 227 FYnTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFLSHDK 306
Cdd:PRK06087 412 YY-SGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPHHSLTL 490
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 578828480 307 DQLTKEL-QQHVksvtAPYKYPRKVEFVSELPKTITGKIERKELRK 351
Cdd:PRK06087 491 EEVVAFFsRKRV----AKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
108-342 |
4.24e-36 |
|
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: 133.58 E-value: 4.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 108 DFTSIRFPALEHcytGGEVVLPKDQEEWKRRTGLllyenYGQSE-TGLICATYWGMKIKpGFMGKATPPYDVQVIDDKGS 186
Cdd:cd17636 112 DLSSLRSSPAAP---EWNDMATVDTSPWGRKPGG-----YGQTEvMGLATFAALGGGAI-GGAGRPSPLVQVRILDEDGR 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 187 ILPPNTEGNIGIRIKPVrpvslfMC-YEGDPEKTAKVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVE 265
Cdd:cd17636 183 EVPDGEVGEIVARGPTV------MAgYWNRPEVNARRTRGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVE 256
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578828480 266 SALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTP-QFLSHDkdqltkELQQHVKSVTAPYKYPRKVEFVSELPKTITG 342
Cdd:cd17636 257 RCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPgASVTEA------ELIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
2-353 |
9.51e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 136.60 E-value: 9.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 2 VIFFTSGTTGFPKMAKHSHGLALQP------SFPGSRKLRSLKTSDV--SWclsdsGWIVATIwtlvePWTAGCTVFIHH 73
Cdd:PRK07788 211 IVILTSGTTGTPKGAPRPEPSPLAPlagllsRVPFRAGETTLLPAPMfhAT-----GWAHLTL-----AMALGSTVVLRR 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 74 lpQFDTKVIIQTLLKYPINHFWGVSSIYRMILQQ--------DFTSIRFPALEHCYTGGEVVlpkdqeewkRRT----GL 141
Cdd:PRK07788 281 --RFDPEATLEDIAKHKATALVVVPVMLSRILDLgpevlakyDTSSLKIIFVSGSALSPELA---------TRAleafGP 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 142 LLYENYGQSETGLicATYWGMK---IKPGFMGKATPPYDVQVIDDKGSILPPNTEGNIGirikpvrpVSLFMCYEGDPEK 218
Cdd:PRK07788 350 VLYNLYGSTEVAF--ATIATPEdlaEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIF--------VGNGFPFEGYTDG 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 219 TAKVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLT 298
Cdd:PRK07788 420 RDKQIIDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKA 499
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 578828480 299 PqflshDKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKKE 353
Cdd:PRK07788 500 P-----GAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREMD 549
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
5-350 |
9.83e-36 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 136.34 E-value: 9.83e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 5 FTSGTTGFPKMAKHSHGLALQPSFPGSRKLRsLKTSDV-------------------------SWCLSDSgWIVATIWTL 59
Cdd:PRK13295 204 YTSGTTGEPKGVMHTANTLMANIVPYAERLG-LGADDVilmaspmahqtgfmyglmmpvmlgaTAVLQDI-WDPARAAEL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 60 VE----PWTAGCTVFIHHLpqfdtkVIIQTLLKYPinhfwgVSSIYRMIlqqdftsirfpalehCytGGEVVLPKDQEEW 135
Cdd:PRK13295 282 IRtegvTFTMASTPFLTDL------TRAVKESGRP------VSSLRTFL---------------C--AGAPIPGALVERA 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 136 KRRTGLLLYENYGQSETGLICATYWGMKIKPGFM--GKATPPYDVQVIDDKGSILPPNTEGNIgirikPVRPVSLFMCYE 213
Cdd:PRK13295 333 RAALGAKIVSAWGMTENGAVTLTKLDDPDERASTtdGCPLPGVEVRVVDADGAPLPAGQIGRL-----QVRGCSNFGGYL 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 214 GDPEKTAKVECGdFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKA 293
Cdd:PRK13295 408 KRPQLNGTDADG-WFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACA 486
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 578828480 294 FIVLTPQfLSHDKDQLTKELQQHvkSVTAPYkYPRKVEFVSELPKTITGKIERKELR 350
Cdd:PRK13295 487 FVVPRPG-QSLDFEEMVEFLKAQ--KVAKQY-IPERLVVRDALPRTPSGKIQKFRLR 539
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
1-349 |
1.28e-35 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 135.37 E-value: 1.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 1 MVIFFTSGTTGFPKMAKHSHGLALQPSFPGSRKLrSLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCTVFIHHlpQFDTK 80
Cdd:PRK06839 152 FIICYTSGTTGKPKGAVLTQENMFWNALNNTFAI-DLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVPR--KFEPT 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 81 VIIQTLLKYPINHFWGVSSIYRMILQQ-DFTSIRFPALEHCYTGGEVVLPKDQEEWKRRtGLLLYENYGQSETG--LICA 157
Cdd:PRK06839 229 KALSMIEKHKVTVVMGVPTIHQALINCsKFETTNLQSVRWFYNGGAPCPEELMREFIDR-GFLFGQGFGMTETSptVFML 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 158 TYWGMKIKPGFMGKATPPYDVQVIDDKGSILPPNTEGNIGIRIKPVrpvslFMCYEGDPEKTAKVECGDFYNTGDRGKMD 237
Cdd:PRK06839 308 SEEDARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNV-----MKEYWNRPDATEETIQDGWLCTGDLARVD 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 238 EEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFLSHDKDqltkeLQQHV 317
Cdd:PRK06839 383 EDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKD-----VIEHC 457
|
330 340 350
....*....|....*....|....*....|..
gi 578828480 318 KSVTAPYKYPRKVEFVSELPKTITGKIERKEL 349
Cdd:PRK06839 458 RLFLAKYKIPKEIVFLKELPKNATGKIQKAQL 489
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
66-356 |
2.40e-35 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 134.32 E-value: 2.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 66 GCTVFIHhlPQFDTKVIIQTLLKYPINhfwgVSSIYRMILQQ---DFTSIRFPALEHCYT--GGEVVLPKdQEEWKRRtG 140
Cdd:PRK03640 207 GMRVVLV--EKFDAEKINKLLQTGGVT----IISVVSTMLQRlleRLGEGTYPSSFRCMLlgGGPAPKPL-LEQCKEK-G 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 141 LLLYENYGQSET-GLICA---TYWGMKIkpGFMGKatPPYDVQV-IDDKGSILPPNTEGNIGIRIKPVRPvslfmCYEGD 215
Cdd:PRK03640 279 IPVYQSYGMTETaSQIVTlspEDALTKL--GSAGK--PLFPCELkIEKDGVVVPPFEEGEIVVKGPNVTK-----GYLNR 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 216 PEKTAKVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFI 295
Cdd:PRK03640 350 EDATRETFQDGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFV 429
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578828480 296 VLTPQFlshDKDqltkELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKKETGQ 356
Cdd:PRK03640 430 VKSGEV---TEE----ELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQLVEEM 483
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
2-350 |
3.10e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 134.16 E-value: 3.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 2 VIFFTSGTTGFPKMAKHSHGLALQPSFPGSRKLRSLKTSdVSWCLSDSGWIVATIwTLVEPWTA-GCTVFIHhlPQFDTK 80
Cdd:PRK09088 139 LILFTSGTSGQPKGVMLSERNLQQTAHNFGVLGRVDAHS-SFLCDAPMFHIIGLI-TSVRPVLAvGGSILVS--NGFEPK 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 81 VIIQTL--LKYPINHFWGVSSIYRMILQQ-DFTSIRFPALEHCYTGGEVVLPKDQEEWKRRtGLLLYENYGQSETGlica 157
Cdd:PRK09088 215 RTLGRLgdPALGITHYFCVPQMAQAFRAQpGFDAAALRHLTALFTGGAPHAAEDILGWLDD-GIPMVDGFGMSEAG---- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 158 TYWGMKI-------KPGFMGKATPPYDVQVIDDKGSILPPNTEGNIGIRiKPvrpvSLFMCYEGDPEKTAKVECGD-FYN 229
Cdd:PRK09088 290 TVFGMSVdcdviraKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLR-GP----NLSPGYWRRPQATARAFTGDgWFR 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 230 TGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQflshdKDQL 309
Cdd:PRK09088 365 TGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADG-----APLD 439
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 578828480 310 TKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELR 350
Cdd:PRK09088 440 LERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLR 480
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
2-352 |
3.20e-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: 130.91 E-value: 3.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 2 VIFFTSGTTGFPKMAKHSHgLALQPSFPGSRKLRSLKTSDVSWCLSDSGWI--VATIWTLVepWTAGCTVFIHHLPQFdt 79
Cdd:cd17630 4 TVILTSGSTGTPKAVVHTA-ANLLASAAGLHSRLGFGGGDSWLLSLPLYHVggLAILVRSL--LAGAELVLLERNQAL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 80 kviIQTLLKYPINHFWGVSSIYRMILQQDFTSIRFPALEHCYTGGEVVLPKDQEEWKRRtGLLLYENYGQSETGLICATY 159
Cdd:cd17630 79 ---AEDLAPPGVTHVSLVPTQLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLERAADR-GIPLYTTYGMTETASQVATK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 160 WGMKIKPGFMGKATPpyDVQV-IDDKGSILppntegnigirikpVRPVSLFMCYEGDPEKTAKVECGDFYnTGDRGKMDE 238
Cdd:cd17630 155 RPDGFGRGGVGVLLP--GRELrIVEDGEIW--------------VGGASLAMGYLRGQLVPEFNEDGWFT-TKDLGELHA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 239 EGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLtpqflshDKDQLTKELQQHVK 318
Cdd:cd17630 218 DGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVG-------RGPADPAELRAWLK 290
|
330 340 350
....*....|....*....|....*....|....
gi 578828480 319 SVTAPYKYPRKVEFVSELPKTITGKIERKELRKK 352
Cdd:cd17630 291 DKLARFKLPKRIYPVPELPRTGGGKVDRRALRAW 324
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
83-350 |
5.36e-35 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 134.56 E-value: 5.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 83 IQTLLKYPINHFWGVSSIYRMILQQ-DFTSIRFPALEHCYTGGEVVLPKDQEEWKRRTGLLLYENYGQSETG-LICATYW 160
Cdd:PRK12492 300 IKELGKWRFSALLGLNTLFVALMDHpGFKDLDFSALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTETSpVASTNPY 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 161 GMKIKPGFMGKATPPYDVQVIDDKGSILPPNTEGNIGIRIKPVrpvslFMCYEGDPEKTAKV-ECGDFYNTGDRGKMDEE 239
Cdd:PRK12492 380 GELARLGTVGIPVPGTALKVIDDDGNELPLGERGELCIKGPQV-----MKGYWQQPEATAEAlDAEGWFKTGDIAVIDPD 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 240 GYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFLSHDkdqltkELQQHVKS 319
Cdd:PRK12492 455 GFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDPGLSVE------ELKAYCKE 528
|
250 260 270
....*....|....*....|....*....|.
gi 578828480 320 VTAPYKYPRKVEFVSELPKTITGKIERKELR 350
Cdd:PRK12492 529 NFTGYKVPKHIVLRDSLPMTPVGKILRRELR 559
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
1-357 |
6.14e-35 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 135.03 E-value: 6.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 1 MVIFFTSGTTGFPKMAKHSHGLALQPSFPGSRKLRSLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCTVFIHH-LPQF-D 78
Cdd:PLN02654 278 LFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTDVYWCTADCGWITGHSYVTYGPMLNGATVLVFEgAPNYpD 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 79 TKVIIQTLLKYPINHFWGVSSIYRMILQQDFTSIRFPALEHCYTGGEVVLPKDQEEWKrrtglLLYENYGQSETGlICAT 158
Cdd:PLN02654 358 SGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKSLRVLGSVGEPINPSAWR-----WFFNVVGDSRCP-ISDT 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 159 YWGMKIKpGFM------------GKATPPY-DVQ--VIDDKGSILPPNTEGNIGIriKPVRPvSLFMCYEGDPEK---TA 220
Cdd:PLN02654 432 WWQTETG-GFMitplpgawpqkpGSATFPFfGVQpvIVDEKGKEIEGECSGYLCV--KKSWP-GAFRTLYGDHERyetTY 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 221 KVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQ 300
Cdd:PLN02654 508 FKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEG 587
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 578828480 301 FLShdKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKKETGQM 357
Cdd:PLN02654 588 VPY--SEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIASRQL 642
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
3-350 |
2.96e-34 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 132.59 E-value: 2.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPKMAKHSHGLALQPSFPGSRKLRsLKTSDV-------SWCLsdsGWIVATIWTLvepwTAGCTVFIhhlP 75
Cdd:PRK12583 206 IQYTSGTTGFPKGATLSHHNILNNGYFVAESLG-LTEHDRlcvpvplYHCF---GMVLANLGCM----TVGACLVY---P 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 76 Q--FDTKVIIQTLLKYPINHFWGVSSIYRMILQQ-DFTSIRFPALEHCYTGGEVVLPkdqEEWKRRTGLL----LYENYG 148
Cdd:PRK12583 275 NeaFDPLATLQAVEEERCTALYGVPTMFIAELDHpQRGNFDLSSLRTGIMAGAPCPI---EVMRRVMDEMhmaeVQIAYG 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 149 QSETG---LICATYWGMKIKPGFMGKATPPYDVQVIDDKGSILPPNTEGNIGirikpVRPVSLFMCYEGDPEKTAKVECG 225
Cdd:PRK12583 352 MTETSpvsLQTTAADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELC-----TRGYSVMKGYWNNPEATAESIDE 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 226 D-FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPqflsh 304
Cdd:PRK12583 427 DgWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHP----- 501
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 578828480 305 DKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELR 350
Cdd:PRK12583 502 GHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMR 547
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
3-346 |
5.11e-34 |
|
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: 128.00 E-value: 5.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPK--MAKHSHGLALQPSFPGSRKLRSlktSDVSWCLS--------DSGWIVATIwtlvepwtAGCTVFIH 72
Cdd:cd17638 5 IMFTSGTTGRSKgvMCAHRQTLRAAAAWADCADLTE---DDRYLIINpffhtfgyKAGIVACLL--------TGATVVPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 73 HLpqFDTKVIIQTLLKYPINHFWGVSSIYRMILQQ------DFTSIRFPAlehcyTGGEVVLPkdqEEWKRRTGLLLYEN 146
Cdd:cd17638 74 AV--FDVDAILEAIERERITVLPGPPTLFQSLLDHpgrkkfDLSSLRAAV-----TGAATVPV---ELVRRMRSELGFET 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 147 ----YGQSETGliCATYwgmkIKPG--------FMGKATPPYDVQVIDDkGSILppntegnigirikpVRPVSLFMCYEG 214
Cdd:cd17638 144 vltaYGLTEAG--VATM----CRPGddaetvatTCGRACPGFEVRIADD-GEVL--------------VRGYNVMQGYLD 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 215 DPEKTAK-VECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKA 293
Cdd:cd17638 203 DPEATAEaIDADGWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKA 282
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 578828480 294 FIVLTPQfLSHDKDQLTKELQQHVksvtAPYKYPRKVEFVSELPKTITGKIER 346
Cdd:cd17638 283 FVVARPG-VTLTEEDVIAWCRERL----ANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
5-349 |
1.94e-33 |
|
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: 129.32 E-value: 1.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 5 FTSGTTGFPK--MAKHsHGLA-----LQPSFPGSRKLRSL-KTS---DVSwclsdsgwivatIWTLVEPWTAGCTVFI-- 71
Cdd:cd17646 145 YTSGSTGRPKgvMVTH-AGIVnrllwMQDEYPLGPGDRVLqKTPlsfDVS------------VWELFWPLVAGARLVVar 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 72 -------HHLPQFDTKVIIQTLlkypinHFwgVSSIYRMILQQDfTSIRFPALEHCYTGGEVvLPKDQ-EEWKRRTGLLL 143
Cdd:cd17646 212 pgghrdpAYLAALIREHGVTTC------HF--VPSMLRVFLAEP-AAGSCASLRRVFCSGEA-LPPELaARFLALPGAEL 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 144 YENYGQSETGlICATYW---GMKIKPGF-MGKATPPYDVQVIDDKGSILPPNTEGNIGIRikpvrPVSLFMCYEGDPEKT 219
Cdd:cd17646 282 HNLYGPTEAA-IDVTHWpvrGPAETPSVpIGRPVPNTRLYVLDDALRPVPVGVPGELYLG-----GVQLARGYLGRPALT 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 220 AKVECGD-------FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVK 292
Cdd:cd17646 356 AERFVPDpfgpgsrMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLV 435
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 578828480 293 AFIVLTPQFLSHDkdqlTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKEL 349
Cdd:cd17646 436 GYVVPAAGAAGPD----TAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
2-351 |
2.78e-33 |
|
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: 129.57 E-value: 2.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 2 VIFFTSGTTGFPK---------MAKHSHglALQPSF-----PGSRKLRSLKTSDVSWCLSDSGWIVatiwtlvepwtagC 67
Cdd:cd17642 188 LIMNSSGSTGLPKgvqlthkniVARFSH--ARDPIFgnqiiPDTAILTVIPFHHGFGMFTTLGYLI-------------C 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 68 TVFIHHLPQFDTKVIIQTLLKYPINHFWGVSSIY------RMILQQDFTSIrfpaleHCYTGGEVVLPKDQEEW-KRRTG 140
Cdd:cd17642 253 GFRVVLMYKFEEELFLRSLQDYKVQSALLVPTLFaffaksTLVDKYDLSNL------HEIASGGAPLSKEVGEAvAKRFK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 141 L-LLYENYGQSETGLICATYWGMKIKPGFMGKATPPYDVQVID-DKGSILPPNTEGNIGirikpVRPVSLFMCYEGDPEK 218
Cdd:cd17642 327 LpGIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDlDTGKTLGPNERGELC-----VKGPMIMKGYVNNPEA 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 219 TAKVECGD-FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVl 297
Cdd:cd17642 402 TKALIDKDgWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVV- 480
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 578828480 298 tpqfLSHDKDQLTKELQQHVKSVTAPYKYPR-KVEFVSELPKTITGKIERKELRK 351
Cdd:cd17642 481 ----LEAGKTMTEKEVMDYVASQVSTAKRLRgGVKFVDEVPKGLTGKIDRRKIRE 531
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
1-355 |
6.73e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 128.08 E-value: 6.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 1 MVIFFTSGTTGFPKMAKHSHGLALQPSFPGSRKLrSLKTSD---VSWCLSDSGWI----VATIWTlvepwtaGCTVFIHH 73
Cdd:PRK06145 152 VRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIAL-GLTASErllVVGPLYHVGAFdlpgIAVLWV-------GGTLRIHR 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 74 lpQFDTKVIIQTLLKYPINHFWGVSSIYRMIL------QQDFTSIRFpalehCYTGGEVVLPKDQEEWKRR-TGLLLYEN 146
Cdd:PRK06145 224 --EFDPEAVLAAIERHRLTCAWMAPVMLSRVLtvpdrdRFDLDSLAW-----CIGGGEKTPESRIRDFTRVfTRARYIDA 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 147 YGQSETgliCATYWGMKI-----KPGFMGKATPPYDVQVIDDKGSILPPNTEGNIGIRIKPVRpvslfMCYEGDPEKTAK 221
Cdd:PRK06145 297 YGLTET---CSGDTLMEAgreieKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVT-----KGYWKDPEKTAE 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 222 VECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTP-Q 300
Cdd:PRK06145 369 AFYGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPgA 448
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 578828480 301 FLSHDkdqltkELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKKETG 355
Cdd:PRK06145 449 TLTLE------ALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDELNG 497
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
2-279 |
9.90e-33 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 126.23 E-value: 9.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 2 VIFfTSGTTGFPKMAKHSHG------LALQPSFPGSRKLRSLKTSDVSWCLSdsgwiVATIWTlvePWTAGCTVFI--HH 73
Cdd:TIGR01733 125 VIY-TSGSTGRPKGVVVTHRslvnllAWLARRYGLDPDDRVLQFASLSFDAS-----VEEIFG---ALLAGATLVVppED 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 74 LPQFDTKVIIQTLLKYPINHFWGVSSIYRMILQQDFTSirFPALEHCYTGGEVVLPKDQEEWKRRTG-LLLYENYGQSET 152
Cdd:TIGR01733 196 EERDDAALLAALIAEHPVTVLNLTPSLLALLAAALPPA--LASLRLVILGGEALTPALVDRWRARGPgARLINLYGPTET 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 153 GLICATY-------WGMKIKPgfMGKATPPYDVQVIDDKGSILPPNTEGNIGIRikpvrPVSLFMCYEGDPEKTAKV--- 222
Cdd:TIGR01733 274 TVWSTATlvdpddaPRESPVP--IGRPLANTRLYVLDDDLRPVPVGVVGELYIG-----GPGVARGYLNRPELTAERfvp 346
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578828480 223 ------ECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAV 279
Cdd:TIGR01733 347 dpfaggDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
2-350 |
1.25e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 127.55 E-value: 1.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 2 VIFFTSGTTGFPKMAKHS------HGLALQPSF---PGSRKLRSLKTSDVsWCLSdsgwivatiwTLVEPWTAGCTVfiH 72
Cdd:PRK06164 185 LLFTTSGTTSGPKLVLHRqatllrHARAIARAYgydPGAVLLAALPFCGV-FGFS----------TLLGALAGGAPL--V 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 73 HLPQFDTKVIIQTLLKYPINHFWGVSSIYRMILQQDFTSIRFPALEHCytGGEVVLPKDQE--EWKRRTGLLLYENYGQS 150
Cdd:PRK06164 252 CEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERADFPSARLF--GFASFAPALGElaALARARGVPLTGLYGSS 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 151 E-----TGLICATYWGMKIKPGfmGK-ATPPYDVQVID-DKGSILPPNTEGNIGIRiKPvrpvSLFMCYEGDPEKTAKVE 223
Cdd:PRK06164 330 EvqalvALQPATDPVSVRIEGG--GRpASPEARVRARDpQDGALLPDGESGEIEIR-AP----SLMRGYLDNPDATARAL 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 224 CGD-FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSpdPIRGE-VVKAFIVLTPqf 301
Cdd:PRK06164 403 TDDgYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA--TRDGKtVPVAFVIPTD-- 478
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 578828480 302 lSHDKDQltKELQQHVKSVTAPYKYPRKVEFVSELPKTITG---KIERKELR 350
Cdd:PRK06164 479 -GASPDE--AGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLR 527
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
1-350 |
1.35e-32 |
|
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: 127.07 E-value: 1.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 1 MVIFfTSGTTGFPKMAKHSHG------LALQPSFPGSRKLRSLKTSDVSWCLSdsgwiVATIW-TLVepwTAGCTVFI-- 71
Cdd:cd17651 140 YVIY-TSGSTGRPKGVVMPHRslanlvAWQARASSLGPGARTLQFAGLGFDVS-----VQEIFsTLC---AGATLVLPpe 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 72 -------HHLPQFDTKVIIQTLLKYPINHFWgvssiyrmILQQDFTSIRFPALEHCYTGGE-VVLPKDQEEW-KRRTGLL 142
Cdd:cd17651 211 evrtdppALAAWLDEQRISRVFLPTVALRAL--------AEHGRPLGVRLAALRYLLTGGEqLVLTEDLREFcAGLPGLR 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 143 LYENYGQSETGLicATYWGMKIKPGFMGKATP---PYD---VQVIDDKGSILPPNTEG--NIGirikpvrPVSLFMCYEG 214
Cdd:cd17651 283 LHNHYGPTETHV--VTALSLPGDPAAWPAPPPigrPIDntrVYVLDAALRPVPPGVPGelYIG-------GAGLARGYLN 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 215 DPEKTAK-------VECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIR 287
Cdd:cd17651 354 RPELTAErfvpdpfVPGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPG 433
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578828480 288 GEVVKAFIVLTPqflshDKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELR 350
Cdd:cd17651 434 EKRLVAYVVGDP-----EAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
3-349 |
4.38e-32 |
|
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: 125.39 E-value: 4.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPK--MAKHSH--GLALQPSFpgsrklRSLKTSDVSWCLSDSGWIVAT--IWTlvePWTAGCTVFI---HH 73
Cdd:cd12117 141 VMYTSGSTGRPKgvAVTHRGvvRLVKNTNY------VTLGPDDRVLQTSPLAFDASTfeIWG---ALLNGARLVLapkGT 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 74 LpqFDTKVIIQTLLKYPINHFWGVSSIYRMILQQD---FTSIRfpaleHCYTGGEVVLPKDQEEWKRRT-GLLLYENYGQ 149
Cdd:cd12117 212 L--LDPDALGALIAEEGVTVLWLTAALFNQLADEDpecFAGLR-----ELLTGGEVVSPPHVRRVLAACpGLRLVNGYGP 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 150 SETGLiCATYWgmKIKPGFM-------GKATPPYDVQVIDDKGSILPPNTEGNI-----GirikpvrpVSLfmCYEGDPE 217
Cdd:cd12117 285 TENTT-FTTSH--VVTELDEvagsipiGRPIANTRVYVLDEDGRPVPPGVPGELyvggdG--------LAL--GYLNRPA 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 218 KTAK--VEC-----GDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAV-VGSPDPIRGE 289
Cdd:cd12117 352 LTAErfVADpfgpgERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVvVREDAGGDKR 431
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 290 VVkAFIVLTPQfLSHDkdqltkELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKEL 349
Cdd:cd12117 432 LV-AYVVAEGA-LDAA------ELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
170-351 |
5.26e-32 |
|
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: 125.64 E-value: 5.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 170 GKATPPYD-VQVIDDKGSILPPNTEGNI---G---IRikpvrpvslfmCYEGDPEKTAKVECGD-FYNTGDRGKMDEEGY 241
Cdd:COG1021 356 GRPISPDDeVRIVDEDGNPVPPGEVGELltrGpytIR-----------GYYRAPEHNARAFTPDgFYRTGDLVRRTPDGY 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 242 ICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFLShdkdqlTKELQQHVKSV- 320
Cdd:COG1021 425 LVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPRGEPLT------LAELRRFLRERg 498
|
170 180 190
....*....|....*....|....*....|.
gi 578828480 321 TAPYKYPRKVEFVSELPKTITGKIERKELRK 351
Cdd:COG1021 499 LAAFKLPDRLEFVDALPLTAVGKIDKKALRA 529
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
5-346 |
2.50e-31 |
|
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: 120.59 E-value: 2.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 5 FTSGTTGFPKMAKHSHGLALQpSFPGSRKLRSLKTSD---VSWCLSDSGWIVATIWTLvepWTAGCtvfIHHLPQFDTKV 81
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIE-SFVCNEDLFNISGEDailAPGPLSHSLFLYGAISAL---YLGGT---FIGQRKFNPKS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 82 IIQTLLKYPINHFWGVSSIYRMILQQDFTSIrfpALEHCYTGGEVvLPKDQEEWKRR--TGLLLYENYGQSETGLICATY 159
Cdd:cd17633 80 WIRKINQYNATVIYLVPTMLQALARTLEPES---KIKSIFSSGQK-LFESTKKKLKNifPKANLIEFYGTSELSFITYNF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 160 WGMKIKPGFMGKATPPYDVQVIDDKGsilppnteGNIGiRIKpVRPVSLFMCYEGDPEKTAkvecGDFYNTGDRGKMDEE 239
Cdd:cd17633 156 NQESRPPNSVGRPFPNVEIEIRNADG--------GEIG-KIF-VKSEMVFSGYVRGGFSNP----DGWMSVGDIGYVDEE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 240 GYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVltpqflshdKDQLT-KELQQHVK 318
Cdd:cd17633 222 GYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYS---------GDKLTyKQLKRFLK 292
|
330 340
....*....|....*....|....*...
gi 578828480 319 SVTAPYKYPRKVEFVSELPKTITGKIER 346
Cdd:cd17633 293 QKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
3-346 |
1.12e-30 |
|
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: 119.29 E-value: 1.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPKMAKHSHGLALQPSFPGSRKLRSLKTSDVSWCLSDSGWIVATIWTLVEPWTAG-CTVF----------- 70
Cdd:cd17635 6 VIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGlCVTGgenttykslfk 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 71 IHHLPQFDTKVIIQTLLKYpinhfwgVSSIYRMILQQdftsirFPALEHCYTGGEVVLPKDQE--EWKRRTGLLLYenYG 148
Cdd:cd17635 86 ILTTNAVTTTCLVPTLLSK-------LVSELKSANAT------VPSLRLIGYGGSRAIAADVRfiEATGLTNTAQV--YG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 149 QSETGLICATYWGMKIKP-GFMGKATPPYDVQVIDDKGSILPPNTEGNIGIRIKpvrpvSLFMCYEGDPEKTAKVECGDF 227
Cdd:cd17635 151 LSETGTALCLPTDDDSIEiNAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSP-----ANMLGYWNNPERTAEVLIDGW 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 228 YNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVltpqfLSHDKD 307
Cdd:cd17635 226 VNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVV-----ASAELD 300
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 578828480 308 QLTKELQQH-VKSVTAPYKYPRKVEFVSELPKTITGKIER 346
Cdd:cd17635 301 ENAIRALKHtIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
2-349 |
1.82e-30 |
|
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: 120.39 E-value: 1.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 2 VIFFTSGTTGFPKMAKHSHGLALQPSFPGSRKLRSLKTsDVSWCLSDSGWIVATIWTLVEPWTAGCTvfIHHLPqfDTKV 81
Cdd:cd05907 91 TIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEG-DRHLSFLPLAHVFERRAGLYVPLLAGAR--IYFAS--SAET 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 82 IIQTLLKYPINHFWGVSSIYRMI------------LQQDFTSIRFPALEHCYTGGeVVLPKDQEEWKRRTGLLLYENYGQ 149
Cdd:cd05907 166 LLDDLSEVRPTVFLAVPRVWEKVyaaikvkavpglKRKLFDLAVGGRLRFAASGG-APLPAELLHFFRALGIPVYEGYGL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 150 SET-GLICATYWGmKIKPGFMGKATPPYDVQvIDDKGSILppntegnigirikpVRPVSLFMCYEGDPEKTAKVECGD-F 227
Cdd:cd05907 245 TETsAVVTLNPPG-DNRIGTVGKPLPGVEVR-IADDGEIL--------------VRGPNVMLGYYKNPEATAEALDADgW 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 228 YNTGDRGKMDEEGYICFLGRSDD-IINASGYRIGPAEVESALVEHPAVAESAVVGSPDPirgeVVKAFIVLTPQFLSHDK 306
Cdd:cd05907 309 LHTGDLGEIDEDGFLHITGRKKDlIITSGGKNISPEPIENALKASPLISQAVVIGDGRP----FLVALIVPDPEALEAWA 384
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578828480 307 DQ----------------LTKELQQHVKSVTA---PYKYPRKVEFVSElPKTI-------TGKIERKEL 349
Cdd:cd05907 385 EEhgiaytdvaelaanpaVRAEIEAAVEAANArlsRYEQIKKFLLLPE-PFTIengeltpTLKLKRPVI 452
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
3-352 |
2.36e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 121.42 E-value: 2.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPKMAKHSHGLALQPSFPGSRKLRSLKTSDVSWCLSDSgWIVATIWTLVEPWTAGCTVFIHHLPQFDTKVI 82
Cdd:PRK07786 179 IMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVGFVGVPL-FHIAGIGSMLPGLLLGAPTVIYPLGAFDPGQL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 83 IQTLLKYPINHFWGVSSIYRMILQQDFTSIRFPALEHCYTGG----EVVLPKDQEEWKrrtGLLLYENYGQSETGLICAT 158
Cdd:PRK07786 258 LDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDLALRVLSWGAapasDTLLRQMAATFP---EAQILAAFGQTEMSPVTCM 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 159 YWGMKI--KPGFMGKATPPYDVQVIDDKGSILPPNTEGNIGIRiKPvrpvSLFMCYEGDPEKTAKVECGDFYNTGDRGKM 236
Cdd:PRK07786 335 LLGEDAirKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYR-AP----TLMSGYWNNPEATAEAFAGGWFHSGDLVRQ 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 237 DEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPqflshDKDQLT-KELQQ 315
Cdd:PRK07786 410 DEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRN-----DDAALTlEDLAE 484
|
330 340 350
....*....|....*....|....*....|....*..
gi 578828480 316 HVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKK 352
Cdd:PRK07786 485 FLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRER 521
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
170-352 |
2.97e-30 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 121.07 E-value: 2.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 170 GKATPPYDVQVID-DKGSILPPNTEGNIGIRIKPVrpvslfM-CYEGDPEKTAKVECGD-FYNTGDRGKMDEEGYICFLG 246
Cdd:PRK08315 374 GRALPHLEVKIVDpETGETVPRGEQGELCTRGYSV------MkGYWNDPEKTAEAIDADgWMHTGDLAVMDEEGYVNIVG 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 247 RSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLtpqflsHDKDQLTKE-LQQHVKSVTAPYK 325
Cdd:PRK08315 448 RIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIIL------RPGATLTEEdVRDFCRGKIAHYK 521
|
170 180
....*....|....*....|....*..
gi 578828480 326 YPRKVEFVSELPKTITGKIERKELRKK 352
Cdd:PRK08315 522 IPRYIRFVDEFPMTVTGKIQKFKMREM 548
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
5-350 |
5.34e-30 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 120.91 E-value: 5.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 5 FTSGTTGFPKMAKHSHGLALQPSFPGSRKLRSLKTSDVSWC---------LSDSGWIvatiwtlvePWTAGCTVFIHHLP 75
Cdd:PRK06060 152 YTSGTTGPPKAAIHRHADPLTFVDAMCRKALRLTPEDTGLCsarmyfaygLGNSVWF---------PLATGGSAVINSAP 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 76 qFDTKVIIQTLLKYPINHFWGVSSIYRMILQ----QDFTSIRfpalehCY-TGGEVVLPKDQEewkRRT----GLLLYEN 146
Cdd:PRK06060 223 -VTPEAAAILSARFGPSVLYGVPNFFARVIDscspDSFRSLR------CVvSAGEALELGLAE---RLMeffgGIPILDG 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 147 YGQSETGLICATYWGMKIKPGFMGKATPPYDVQVIDDKGSILPPNTEGNIGirikpVRPVSLFMCYEGDPEKTakVECGD 226
Cdd:PRK06060 293 IGSTEVGQTFVSNRVDEWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLW-----VRGPAIAKGYWNRPDSP--VANEG 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 227 FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVltPQFLSHDK 306
Cdd:PRK06060 366 WLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLV--ATSGATID 443
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 578828480 307 DQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELR 350
Cdd:PRK06060 444 GSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
263-343 |
7.54e-30 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 109.17 E-value: 7.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 263 EVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPqflshDKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITG 342
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKP-----GVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSG 75
|
.
gi 578828480 343 K 343
Cdd:pfam13193 76 K 76
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
147-349 |
7.58e-30 |
|
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: 119.35 E-value: 7.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 147 YGQSEtGLICATYWG--MKIKPGFMGKATPPYD-VQVIDDKGSILPPNTEGNIGIRikpvRPVSlFMCYEGDPEKTAKVE 223
Cdd:cd05920 287 FGMAE-GLLNYTRLDdpDEVIIHTQGRPMSPDDeIRVVDEEGNPVPPGEEGELLTR----GPYT-IRGYYRAPEHNARAF 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 224 CGD-FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFL 302
Cdd:cd05920 361 TPDgFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRDPPP 440
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 578828480 303 ShdkdqlTKELQQHVKSV-TAPYKYPRKVEFVSELPKTITGKIERKEL 349
Cdd:cd05920 441 S------AAQLRRFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
3-343 |
1.51e-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: 116.71 E-value: 1.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPKMAKHSHGLALQPSFPGSRKLRSLKTSDvSWCLSDSGWIVATIWTLVEP-------WTA------GCTV 69
Cdd:cd05924 8 ILYTGGTTGMPKGVMWRQEDIFRMLMGGADFGTGEFTPS-EDAHKAAAAAAGTVMFPAPPlmhgtgsWTAfggllgGQTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 70 FIHHlPQFDTKVIIQTLLKYPINHFWGVSSIYRMILQQ--------DFTSIRFPAlehcyTGGEVVLPKDQEEWKRRT-G 140
Cdd:cd05924 87 VLPD-DRFDPEEVWRTIEKHKVTSMTIVGDAMARPLIDalrdagpyDLSSLFAIS-----SGGALLSPEVKQGLLELVpN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 141 LLLYENYGQSETGLicatywGMKIKPGFMGKATPPY-----DVQVIDDKGSILPPNTEGNIGIRIKPVRPVSlfmcYEGD 215
Cdd:cd05924 161 ITLVDAFGSSETGF------TGSGHSAGSGPETGPFtranpDTVVLDDDGRVVPPGSGGVGWIARRGHIPLG----YYGD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 216 PEKTAK--VECGD--FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVV 291
Cdd:cd05924 231 EAKTAEtfPEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEV 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 578828480 292 KAFIVLTPqflSHDKDQltKELQQHVKSVTAPYKYPRKVEFVSELPKTITGK 343
Cdd:cd05924 311 VAVVQLRE---GAGVDL--EELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
2-351 |
1.56e-29 |
|
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: 118.20 E-value: 1.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 2 VIFFTSGTTGFPKMAKHSHGlALQPSFPGSRKLRSLKTSDV---------SWCLSDSGWIvatiwtlvePWTAGCTVFIH 72
Cdd:cd05909 151 VILFTSGSEGLPKGVVLSHK-NLLANVEQITAIFDPNPEDVvfgalpffhSFGLTGCLWL---------PLLSGIKVVFH 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 73 HLPqFDTKVIIQTLLKYPINHFWGVSSIYRMILQ----QDFTSIRFpalehCYTGGEVVLPKDQEEWKRRTGLLLYENYG 148
Cdd:cd05909 221 PNP-LDYKKIPELIYDKKATILLGTPTFLRGYARaahpEDFSSLRL-----VVAGAEKLKDTLRQEFQEKFGIRILEGYG 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 149 QSETG-LICATYWGMKIKPGFMGKATPPYDVQVIDDKGSILPPNTEGNigiRIKpVRPVSLFMCYEGDPEKTAKVECGDF 227
Cdd:cd05909 295 TTECSpVISVNTPQSPNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGG---LLL-VRGPNVMLGYLNEPELTSFAFGDGW 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 228 YNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEH-PAVAESAVVGSPDPIRGEVVKAFivLTPQFLSHDk 306
Cdd:cd05909 371 YDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLL--TTTTDTDPS- 447
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 578828480 307 dqltkELQQHVKSVTAPYKY-PRKVEFVSELPKTITGKIERKELRK 351
Cdd:cd05909 448 -----SLNDILKNAGISNLAkPSYIHQVEEIPLLGTGKPDYVTLKA 488
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
3-350 |
1.79e-29 |
|
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: 117.85 E-value: 1.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPKMAKHSHGLALQPSFPGSRKLRsLKTSDVSWCLSDSGWIVAtIWTLVEPWTAGCTVFIHHLPQFDTKVI 82
Cdd:cd17649 99 VIYTSGSTGTPKGVAVSHGPLAAHCQATAERYG-LTPGDRELQFASFNFDGA-HEQLLPPLICGACVVLRPDELWASADE 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 83 IQTLL-KYPINhfwgVSSIYRMILQQ------DFTSIRFPALEHCYTGGEVVLPKDQEEWkRRTGLLLYENYGQSETgLI 155
Cdd:cd17649 177 LAEMVrELGVT----VLDLPPAYLQQlaeeadRTGDGRPPSLRLYIFGGEALSPELLRRW-LKAPVRLFNAYGPTEA-TV 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 156 CATYWgmKIKPGF--------MGKATPPYDVQVIDDKGSILPPNTEGNIGIRikpvrPVSLFMCYEGDPEKTAK------ 221
Cdd:cd17649 251 TPLVW--KCEAGAaragasmpIGRPLGGRSAYILDADLNPVPVGVTGELYIG-----GEGLARGYLGRPELTAErfvpdp 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 222 --VECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVkAFIVL-T 298
Cdd:cd17649 324 fgAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQLV-AYVVLrA 402
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 578828480 299 PQFLSHDKDQltkeLQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELR 350
Cdd:cd17649 403 AAAQPELRAQ----LRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
1-351 |
3.39e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 117.86 E-value: 3.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 1 MVIFfTSGTTGFPKMAKHSHG-LAlqpsFPGSR--KLRSLKTSDVSWC---LSDS-----GWIVATiwtlvepwTAGCTV 69
Cdd:PRK07867 156 MLIF-TSGTSGDPKAVRCTHRkVA----SAGVMlaQRFGLGPDDVCYVsmpLFHSnavmaGWAVAL--------AAGASI 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 70 FIHhlPQFDTKVIIQTLLKYPINHFWGVSSIYRMIL-------QQDFTsirfpaLEHCYtGGEVVlPKDQEEWKRRTGLL 142
Cdd:PRK07867 223 ALR--RKFSASGFLPDVRRYGATYANYVGKPLSYVLatperpdDADNP------LRIVY-GNEGA-PGDIARFARRFGCV 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 143 LYENYGQSETGLicATYWGMKIKPGFMGKATPpyDVQVID-DKGSILPP---------NTEGNIGIRIKPVRPvSLFMCY 212
Cdd:PRK07867 293 VVDGFGSTEGGV--AITRTPDTPPGALGPLPP--GVAIVDpDTGTECPPaedadgrllNADEAIGELVNTAGP-GGFEGY 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 213 EGDPEKTAKVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVK 292
Cdd:PRK07867 368 YNDPEADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVM 447
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 578828480 293 AFIVLTPQfLSHDKDQLTKELqqHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRK 351
Cdd:PRK07867 448 AALVLAPG-AKFDPDAFAEFL--AAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
2-356 |
1.47e-28 |
|
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: 117.27 E-value: 1.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 2 VIFfTSGTTGFPKMAKHSHG------LALQPSFPGSRKLRSL-KTS---DVSwclsdsgwiVATIWTlvePWTAGCTVFI 71
Cdd:COG1020 622 VIY-TSGSTGRPKGVMVEHRalvnllAWMQRRYGLGPGDRVLqFASlsfDAS---------VWEIFG---ALLSGATLVL 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 72 hhLPQ---FDTKVIIQTLLKYPINHFWGVSSIYRMILQQDFTsiRFPALEHCYTGGEVVLPKDQEEWKRRT-GLLLYENY 147
Cdd:COG1020 689 --APPearRDPAALAELLARHRVTVLNLTPSLLRALLDAAPE--ALPSLRLVLVGGEALPPELVRRWRARLpGARLVNLY 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 148 GQSETGlICATYWgmKIKPGFMGKATPPY-------DVQVIDDKGSILPPNTEGNI---GirikpvrpVSLFMCYEGDPE 217
Cdd:COG1020 765 GPTETT-VDSTYY--EVTPPDADGGSVPIgrpiantRVYVLDAHLQPVPVGVPGELyigG--------AGLARGYLNRPE 833
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 218 KTAK--VEC-----GD-FYNTGDRGKMDEEGYICFLGRSDD---IinaSGYRIGPAEVESALVEHPAVAESAVVGSPDPI 286
Cdd:COG1020 834 LTAErfVADpfgfpGArLYRTGDLARWLPDGNLEFLGRADDqvkI---RGFRIELGEIEAALLQHPGVREAVVVAREDAP 910
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 287 RGEVVKAFIVLTPqflshDKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKKETGQ 356
Cdd:COG1020 911 GDKRLVAYVVPEA-----GAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAA 975
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
1-351 |
2.44e-28 |
|
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: 114.95 E-value: 2.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 1 MVIFFTSGTTGFPKMAKHSHG------LALQPSFPGSRKLRSLK----TSDVSwclsdsgwiVATIWTlvePWTAGCTVF 70
Cdd:cd05918 109 AYVIFTSGSTGKPKGVVIEHRalstsaLAHGRALGLTSESRVLQfasyTFDVS---------ILEIFT---TLAAGGCLC 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 71 I-------HHLPQFdtkviIQtllKYPINHFWGVSSIYRMILQQDFtsirfPALEHCYTGGEVVLPKDQEEWKRRTGLLl 143
Cdd:cd05918 177 IpseedrlNDLAGF-----IN---RLRVTWAFLTPSVARLLDPEDV-----PSLRTLVLGGEALTQSDVDTWADRVRLI- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 144 yeN-YGQSETGlICATY--WGMKIKPGFMGkatPPYDVQ--VID--DKGSILPPNT------EGNIgirikpvrpvsLFM 210
Cdd:cd05918 243 --NaYGPAECT-IAATVspVVPSTDPRNIG---RPLGATcwVVDpdNHDRLVPIGAvgelliEGPI-----------LAR 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 211 CYEGDPEKTAKV---------ECGD-----FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAE 276
Cdd:cd05918 306 GYLNDPEKTAAAfiedpawlkQEGSgrgrrLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAK 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 277 SAVVGSPDPIRGEVVK---AFIVLTPQFLSHDKDQ------------LTKELQQHVKSVTAPYKYPRKVEFVSELPKTIT 341
Cdd:cd05918 386 EVVVEVVKPKDGSSSPqlvAFVVLDGSSSGSGDGDslflepsdefraLVAELRSKLRQRLPSYMVPSVFLPLSHLPLTAS 465
|
410
....*....|
gi 578828480 342 GKIERKELRK 351
Cdd:cd05918 466 GKIDRRALRE 475
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
143-357 |
5.65e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 114.11 E-value: 5.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 143 LYENYGQSETGLICA-TYWGMKIKPGFMGKATPPYDVQVIDDKGSILPPNTEGNIGirikpVRPVSLFMCYEGDPEKTAK 221
Cdd:PRK07638 282 LYEFYGASELSFVTAlVDEESERRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVY-----VKSPQFFMGYIIGGVLARE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 222 VECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIvltpqf 301
Cdd:PRK07638 357 LNADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII------ 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 578828480 302 lshDKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKKETGQM 357
Cdd:PRK07638 431 ---KGSATKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWIENQE 483
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
212-352 |
5.81e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 114.27 E-value: 5.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 212 YEGDPEKTAKVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVV 291
Cdd:PRK08162 402 YLKNPKATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVP 481
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578828480 292 KAFIVLtpqflshdKDQLT---KELQQHVKSVTAPYKYPRKVEFvSELPKTITGKIERKELRKK 352
Cdd:PRK08162 482 CAFVEL--------KDGASateEEIIAHCREHLAGFKVPKAVVF-GELPKTSTGKIQKFVLREQ 536
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
140-352 |
7.19e-28 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 114.02 E-value: 7.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 140 GLLLYENYGQSETGLICAT---YWgmKIKPGFMGKATPPyDVQVIDDKGSILPPNTEGNIgiRIKPVRPVSlfmcYEGDP 216
Cdd:PRK13391 300 GPIIHEYYAATEGLGFTACdseEW--LAHPGTVGRAMFG-DLHILDDDGAELPPGEPGTI--WFEGGRPFE----YLNDP 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 217 EKT--AKVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAF 294
Cdd:PRK13391 371 AKTaeARHPDGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAV 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 578828480 295 IVLTPQflSHDKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKK 352
Cdd:PRK13391 451 VQPVDG--VDPGPALAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRDR 506
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
2-349 |
1.87e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 112.78 E-value: 1.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 2 VIFFTSGTTGFPK----MAKHSHGLALQPSFPGSRKLRSLKTSDVSWCLSDS---GWIVATIwtlvepwTAGCTVFIHHl 74
Cdd:PRK13383 178 IVLLTSGTTGKPKgvprAPQLRSAVGVWVTILDRTRLRTGSRISVAMPMFHGlglGMLMLTI-------ALGGTVLTHR- 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 75 pQFDTKVIIQTLLKYPINHFWGVSSIYRMILQ-QDFTSIR--FPALEHCYTGGEVVLPKDQEEWKRRTGLLLYENYGQSE 151
Cdd:PRK13383 250 -HFDAEAALAQASLHRADAFTAVPVVLARILElPPRVRARnpLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 152 TGL-ICATYWGMKIKPGFMGKATPPYDVQVIDDKGSILPPNTEGNIGirikpvrpVSLFMCYEGDPEKTAKVECGDFYNT 230
Cdd:PRK13383 329 VGIgALATPADLRDAPETVGKPVAGCPVRILDRNNRPVGPRVTGRIF--------VGGELAGTRYTDGGGKAVVDGMTST 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 231 GDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQfLSHDKDQlt 310
Cdd:PRK13383 401 GDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPG-SGVDAAQ-- 477
|
330 340 350
....*....|....*....|....*....|....*....
gi 578828480 311 keLQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKEL 349
Cdd:PRK13383 478 --LRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
5-352 |
3.20e-27 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 112.38 E-value: 3.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 5 FTSGTTGFPK--MAKHshglalqpsfpgsrklRSLKTS-----------------DVSWCLSDSGWIVATIWTLVEPWTA 65
Cdd:PLN02246 186 YSSGTTGLPKgvMLTH----------------KGLVTSvaqqvdgenpnlyfhsdDVILCVLPMFHIYSLNSVLLCGLRV 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 66 GCTVFIhhLPQFDTKVIIQTLLKY---------PInhfwgVSSIYR--MILQQDFTSIRFpalehcYTGGEVVLPKDQEE 134
Cdd:PLN02246 250 GAAILI--MPKFEIGALLELIQRHkvtiapfvpPI-----VLAIAKspVVEKYDLSSIRM------VLSGAAPLGKELED 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 135 WKRRT--GLLLYENYGQSETGLICATYWG-----MKIKPGFMGKATPPYDVQVID-DKGSILPPNTEGNIGIRIKPVrpv 206
Cdd:PLN02246 317 AFRAKlpNAVLGQGYGMTEAGPVLAMCLAfakepFPVKSGSCGTVVRNAELKIVDpETGASLPRNQPGEICIRGPQI--- 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 207 slfM-CYEGDPEKTAK-VECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPD 284
Cdd:PLN02246 394 ---MkGYLNDPEATANtIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKD 470
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578828480 285 PIRGEVVKAFIVLTPQF-LSHDkdqltkELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKK 352
Cdd:PLN02246 471 EVAGEVPVAFVVRSNGSeITED------EIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRAK 533
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
136-352 |
3.80e-27 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 111.99 E-value: 3.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 136 KRRTGLLLYENYGQSETGLICATYW----GMKI-KPGFMGKATPPYDVQVID-DKGSILPPNTEGNIGIRIKPVrpvslF 209
Cdd:PLN02330 325 AKFPGVQVQEAYGLTEHSCITLTHGdpekGHGIaKKNSVGFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQCV-----M 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 210 MCYEGDPEKTAK-VECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRG 288
Cdd:PLN02330 400 QGYYNNKEETDRtIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAG 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578828480 289 EVVKAFIVLTPQFLSHDKDQLtkelqQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKK 352
Cdd:PLN02330 480 EIPAACVVINPKAKESEEDIL-----NFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEK 538
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
161-349 |
7.59e-27 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 110.68 E-value: 7.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 161 GMKIKPGFMGKatppydVQVIDDKGS---ILPPNTEGNIgirIKPVRPVSLFMCYEGDPEKTAKVECGDFYNTGDRGKMD 237
Cdd:cd05923 316 GTEMRPGFFSE------VRIVRIGGSpdeALANGEEGEL---IVAAAADAAFTGYLNQPEATAKKLQDGWYRTGDVGYVD 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 238 EEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFLSHDkdqltkELQQHV 317
Cdd:cd05923 387 PSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLSAD------ELDQFC 460
|
170 180 190
....*....|....*....|....*....|...
gi 578828480 318 K-SVTAPYKYPRKVEFVSELPKTITGKIERKEL 349
Cdd:cd05923 461 RaSELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
2-347 |
2.48e-26 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 109.59 E-value: 2.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 2 VIFFTSGTTGFPKMAKHSHGlalqpSFPGSrkLRSLKTSdvsWCLSDSGWIVAT---------IWTLVEPWTAGCTVFIH 72
Cdd:PRK05852 180 MIMFTGGTTGLPKMVPWTHA-----NIASS--VRAIITG---YRLSPRDATVAVmplyhghglIAALLATLASGGAVLLP 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 73 HLPQFDTKVIIQTLLKYPINHFWGVSSIYRMILQ----QDFTSIRfPALEHCYTGGEVVLPKDQEEWKRRTGLLLYENYG 148
Cdd:PRK05852 250 ARGRFSAHTFWDDIKAVGATWYTAVPTIHQILLEraatEPSGRKP-AALRFIRSCSAPLTAETAQALQTEFAAPVVCAFG 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 149 QSETGLICAT---YWGMK-----IKPGFMGKATPPyDVQVIDDKGSILPPNTEGNIGIRIKPVrpvslFMCYEGDPEKTA 220
Cdd:PRK05852 329 MTEATHQVTTtqiEGIGQtenpvVSTGLVGRSTGA-QIRIVGSDGLPLPAGAVGEVWLRGTTV-----VRGYLGDPTITA 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 221 KVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVltPQ 300
Cdd:PRK05852 403 ANFTDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIV--PR 480
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 578828480 301 FLSHDKDQltkELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERK 347
Cdd:PRK05852 481 ESAPPTAE---ELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRR 524
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
3-349 |
2.94e-26 |
|
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: 108.56 E-value: 2.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPKMAKHSHGLA---LQ---PSFPGSRKLRSLKTSDVSWCLSdsgwivatIWTLVEPWTAGCTVFI----H 72
Cdd:cd12115 110 VIYTSGSTGRPKGVAIEHRNAaafLQwaaAAFSAEELAGVLASTSICFDLS--------VFELFGPLATGGKVVLadnvL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 73 HLPQFDTKVIIqTLlkypINhfwGVSSIYRMILQQDF--TSIRFPALehcytGGEVvLPKD--QEEWKRRTGLLLYENYG 148
Cdd:cd12115 182 ALPDLPAAAEV-TL----IN---TVPSAAAELLRHDAlpASVRVVNL-----AGEP-LPRDlvQRLYARLQVERVVNLYG 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 149 QSETglicATY-WGMKIKPGF-----MGKATPPYDVQVIDDKGSILPPNTEGNIGIRIKpvrpvSLFMCYEGDPEKTAKV 222
Cdd:cd12115 248 PSED----TTYsTVAPVPPGAsgevsIGRPLANTQAYVLDRALQPVPLGVPGELYIGGA-----GVARGYLGRPGLTAER 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 223 ECGD-------FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFI 295
Cdd:cd12115 319 FLPDpfgpgarLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYI 398
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 578828480 296 VLTPQFLShdkdqLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKEL 349
Cdd:cd12115 399 VAEPGAAG-----LVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
141-343 |
3.97e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 108.82 E-value: 3.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 141 LLLYENYGQSETGLICATYWGMKIKPGFMGKATPPYDVQVIDDKGSILPPNtEGNIG-IRIKPVRPVSlfmcYEGDPEKT 219
Cdd:PRK07798 323 VVLTDSIGSSETGFGGSGTVAKGAVHTGGPRFTIGPRTVVLDEDGNPVEPG-SGEIGwIARRGHIPLG----YYKDPEKT 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 220 AK----VEcGDFYN-TGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAF 294
Cdd:PRK07798 398 AEtfptID-GVRYAiPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAV 476
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 578828480 295 IVLTPQfLSHDKDqltkELQQHVKSVTAPYKYPRKVEFVSELPKTITGK 343
Cdd:PRK07798 477 VQLREG-ARPDLA----ELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
3-349 |
5.20e-26 |
|
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: 108.18 E-value: 5.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPK--MAKHsHGL-----ALQPSFPGSRKLRSLKTSDVSWclsDsgwivATIWTLVEPWTAGCTVFIH-HL 74
Cdd:cd17655 142 VIYTSGSTGKPKgvMIEH-RGVvnlveWANKVIYQGEHLRVALFASISF---D-----ASVTEIFASLLSGNTLYIVrKE 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 75 PQFDTKVIIQTLLKYPINHFWGVSSIYRMILQQDFTSirFPALEHCYTGGEVVLPKDQEEWKRRTGL--LLYENYGQSET 152
Cdd:cd17655 213 TVLDGQALTQYIRQNRITIIDLTPAHLKLLDAADDSE--GLSLKHLIVGGEALSTELAKKIIELFGTnpTITNAYGPTET 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 153 gLICATYW---GMKIKPGF--MGKATPPYDVQVIDDKGSILPPNTEGNigirikpvrpvslfMCYEGD---------PEK 218
Cdd:cd17655 291 -TVDASIYqyePETDQQVSvpIGKPLGNTRIYILDQYGRPQPVGVAGE--------------LYIGGEgvargylnrPEL 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 219 TAK-------VECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVV 291
Cdd:cd17655 356 TAEkfvddpfVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYL 435
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 578828480 292 KAFIVltpqflsHDKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKEL 349
Cdd:cd17655 436 CAYIV-------SEKELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
5-351 |
1.46e-25 |
|
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: 107.13 E-value: 1.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 5 FTSGTTGFPKMAKHSH-GLALQPSFPGSRKLRSLKTSDVSWCLSD----SGWivATIWTLvepwTAGCTVFIHHLPQFDT 79
Cdd:cd05915 160 YTTGTTGLPKGVVYSHrALVLHSLAASLVDGTALSEKDVVLPVVPmfhvNAW--CLPYAA----TLVGAKQVLPGPRLDP 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 80 KVIIQTLLKYPINHFWGVSSIYRMILQ-QDFTSIRFPALEHCYTGGEVVlPKDQEEWKRRTGLLLYENYGQSET-GLICA 157
Cdd:cd05915 234 ASLVELFDGEGVTFTAGVPTVWLALADyLESTGHRLKTLRRLVVGGSAA-PRSLIARFERMGVEVRQGYGLTETsPVVVQ 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 158 TYW-------------GMKIKPGFMGKATPpydVQVIDDKGSILPPNTEGnigIRIKPVRPVSLFMCYEGDPEKT-AKVE 223
Cdd:cd05915 313 NFVkshleslseeeklTLKAKTGLPIPLVR---LRVADEEGRPVPKDGKA---LGEVQLKGPWITGGYYGNEEATrSALT 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 224 CGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTpqfls 303
Cdd:cd05915 387 PDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPR----- 461
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 578828480 304 hDKDQLTKELQQHVKSVTAPYKY-PRKVEFVSELPKTITGKIERKELRK 351
Cdd:cd05915 462 -GEKPTPEELNEHLLKAGFAKWQlPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
177-351 |
1.54e-25 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 107.38 E-value: 1.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 177 DVQVIDDKGSILPPNTEGNIGIRikpvRPVSlFMCYEGDPEKTAKVECGD-FYNTGDRGKMDEEGYICFLGRSDDIINAS 255
Cdd:PRK10946 364 EVWVADADGNPLPQGEVGRLMTR----GPYT-FRGYYKSPQHNASAFDANgFYCSGDLVSIDPDGYITVVGREKDQINRG 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 256 GYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLtpqflshdKDQL-TKELQQHVKSV-TAPYKYPRKVEFV 333
Cdd:PRK10946 439 GEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVV--------KEPLkAVQLRRFLREQgIAEFKLPDRVECV 510
|
170
....*....|....*...
gi 578828480 334 SELPKTITGKIERKELRK 351
Cdd:PRK10946 511 DSLPLTAVGKVDKKQLRQ 528
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
3-355 |
2.76e-25 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 106.52 E-value: 2.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPKMAKHSH--------------GLALQPSF----PGSRKLrslktSDVSW--CLSDSGwivaTIWTLVEP 62
Cdd:PRK04813 148 IIFTSGTTGKPKGVQISHdnlvsftnwmledfALPEGPQFlnqaPYSFDL-----SVMDLypTLASGG----TLVALPKD 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 63 WTAgctvfihhlpqfDTKVIIQTLLKYPINhFWgVS--SIYRM-ILQQDFTSIRFPALEHCYTGGEVVLPKDQEEWKRR- 138
Cdd:PRK04813 219 MTA------------NFKQLFETLPQLPIN-VW-VStpSFADMcLLDPSFNEEHLPNLTHFLFCGEELPHKTAKKLLERf 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 139 TGLLLYENYGQSE----------TGLICATYWGMKIkpgfmGKATPPYDVQVIDDKGSILPPNTEGNIGIrikpVRP-VS 207
Cdd:PRK04813 285 PSATIYNTYGPTEatvavtsieiTDEMLDQYKRLPI-----GYAKPDSPLLIIDEEGTKLPDGEQGEIVI----SGPsVS 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 208 LfmCYEGDPEKTAKVecgdF--------YNTGDRGKMDEeGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAV 279
Cdd:PRK04813 356 K--GYLNNPEKTAEA----FftfdgqpaYHTGDAGYLED-GLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVV 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 280 VgspdPI-RGEVVK---AFIVLTPQflSHDKD-QLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKKET 354
Cdd:PRK04813 429 V----PYnKDHKVQyliAYVVPKEE--DFEREfELTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKALIEEVN 502
|
.
gi 578828480 355 G 355
Cdd:PRK04813 503 K 503
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
229-354 |
4.40e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 105.12 E-value: 4.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 229 NTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAfivltpQFLSH---D 305
Cdd:PRK08308 294 FTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKA------KVISHeeiD 367
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 578828480 306 KDQLTKELQQHVksvtAPYKYPRKVEFVSELPKTITGKIERKELRKKET 354
Cdd:PRK08308 368 PVQLREWCIQHL----APYQVPHEIESVTEIPKNANGKVSRKLLELGEV 412
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
5-352 |
5.89e-25 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 105.70 E-value: 5.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 5 FTSGTTGFPKMAKHSHGLALqpsfpgsrkLRSLKTSDVsWCLSDSGwivATIWTL--------VEPWT--AGCTVFIHhL 74
Cdd:PLN02479 202 YTSGTTASPKGVVLHHRGAY---------LMALSNALI-WGMNEGA---VYLWTLpmfhcngwCFTWTlaALCGTNIC-L 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 75 PQFDTKVIIQTLLKYPINHFWGVSSIYRMILQ--QDFTSIRFPALEHCYTGGEVVLPKDQEEWKRRtGLLLYENYGQSET 152
Cdd:PLN02479 268 RQVTAKAIYSAIANYGVTHFCAAPVVLNTIVNapKSETILPLPRVVHVMTAGAAPPPSVLFAMSEK-GFRVTHTYGLSET 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 153 ---GLICAtyWgmkiKPGFmgKATPPYDVQVIDDKGSILPPNTEGNIGIRIKPVRPV---------------SLFMCYEG 214
Cdd:PLN02479 347 ygpSTVCA--W----KPEW--DSLPPEEQARLNARQGVRYIGLEGLDVVDTKTMKPVpadgktmgeivmrgnMVMKGYLK 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 215 DPEKTAKVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAF 294
Cdd:PLN02479 419 NPKANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAF 498
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 578828480 295 IVLTPQFLSHDKDQLTKELQQHVKSVTAPYKYPRKVEFvSELPKTITGKIERKELRKK 352
Cdd:PLN02479 499 VTLKPGVDKSDEAALAEDIMKFCRERLPAYWVPKSVVF-GPLPKTATGKIQKHVLRAK 555
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
3-349 |
7.17e-25 |
|
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: 104.64 E-value: 7.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPK--MAKHSHGLALQPSF-------PGSRKLRSLKTS-DVSwclsdsgwivatIWTLVEPWTAGCTVFIh 72
Cdd:cd17652 98 VIYTSGSTGRPKgvVVTHRGLANLAAAQiaafdvgPGSRVLQFASPSfDAS------------VWELLMALLAGATLVL- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 73 hLPQFDTKV---IIQTLLKYPINHFWGVSSIYRMIlqqdfTSIRFPALEHCYTGGEVVLPKDQEEWKRrtGLLLYENYGQ 149
Cdd:cd17652 165 -APAEELLPgepLADLLREHRITHVTLPPAALAAL-----PPDDLPDLRTLVVAGEACPAELVDRWAP--GRRMINAYGP 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 150 SETgLICATYW----GMKIKPgfMGKATPPYDVQVIDDKGSILPPNTEGNIGIRikpvrPVSLFMCYEGDPEKTAK--VE 223
Cdd:cd17652 237 TET-TVCATMAgplpGGGVPP--IGRPVPGTRVYVLDARLRPVPPGVPGELYIA-----GAGLARGYLNRPGLTAErfVA 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 224 C------GDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVL 297
Cdd:cd17652 309 DpfgapgSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVP 388
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 578828480 298 TPqflshDKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKEL 349
Cdd:cd17652 389 AP-----GAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
2-351 |
7.53e-24 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 102.57 E-value: 7.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 2 VIFFTSGTTGFPKMAKHSHgLALqpsfpgsrKLRSL-KTSDVSWCLSDS----------GWIVATIWTLVepwTAGCTVF 70
Cdd:PLN02860 176 LICFTSGTTGRPKGVTISH-SAL--------IVQSLaKIAIVGYGEDDVylhtaplchiGGLSSALAMLM---VGACHVL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 71 IhhlPQFDTKVIIQTLLKYPINHFWGVSSIYRMILQQDFTSIR---FPALEHCYTGGEVV---LPKDQEEWKRRTGLLly 144
Cdd:PLN02860 244 L---PKFDAKAALQAIKQHNVTSMITVPAMMADLISLTRKSMTwkvFPSVRKILNGGGSLssrLLPDAKKLFPNAKLF-- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 145 ENYGQSETgliCATYWGMKIKPGFMgkATPPYDVQVIDDKGSILPPNTEG--------NIGIRIKP----------VRPV 206
Cdd:PLN02860 319 SAYGMTEA---CSSLTFMTLHDPTL--ESPKQTLQTVNQTKSSSVHQPQGvcvgkpapHVELKIGLdessrvgrilTRGP 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 207 SLFMCYEGDPEKTAKVECGDFY-NTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDP 285
Cdd:PLN02860 394 HVMLGYWGQNSETASVLSNDGWlDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDS 473
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578828480 286 IRGEVVKAFIVLTPQFLSHDKD--------QLTKE-LQQHV--KSVTApYKYPRK-VEFVSELPKTITGKIERKELRK 351
Cdd:PLN02860 474 RLTEMVVACVRLRDGWIWSDNEkenakknlTLSSEtLRHHCreKNLSR-FKIPKLfVQWRKPFPLTTTGKIRRDEVRR 550
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
180-349 |
1.37e-23 |
|
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: 101.19 E-value: 1.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 180 VIDDKGSILPPNTEGNIGIRikpvrPVSLFMCYEGDPEKTAK--VECGD---FYNTGDRGKMDEEGYICFLGRSDDIINA 254
Cdd:cd12114 313 VLDPRGRDCPDWVPGELWIG-----GRGVALGYLGDPELTAArfVTHPDgerLYRTGDLGRYRPDGTLEFLGRRDGQVKV 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 255 SGYRIGPAEVESALVEHPAVAESAVVGSPDPiRGEVVKAFIVLTPQFLSHDKDQLTKELQQHVKSvtapYKYPRKVEFVS 334
Cdd:cd12114 388 RGYRIELGEIEAALQAHPGVARAVVVVLGDP-GGKRLAAFVVPDNDGTPIAPDALRAFLAQTLPA----YMIPSRVIALE 462
|
170
....*....|....*
gi 578828480 335 ELPKTITGKIERKEL 349
Cdd:cd12114 463 ALPLTANGKVDRAAL 477
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
3-357 |
1.69e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 102.34 E-value: 1.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPKMAKHSHG------LALQPSFPGSRKLRSLKTSDVSWCLSDSGWIvatiwtlvEPWTAGCTVFIHHLPQ 76
Cdd:PRK12316 4699 VIYTSGSTGRPKGVAVSHGslvnhlHATGERYELTPDDRVLQFMSFSFDGSHEGLY--------HPLINGASVVIRDDSL 4770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 77 FDTKVIIQTLLKYPINHFWGVSSIYRMILQQDFTSIRFPALEHCYTGGEVVLPKDQEE-WKRRTGLLLYENYGQSETgLI 155
Cdd:PRK12316 4771 WDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDGEPPSLRVYCFGGEAVAQASYDLaWRALKPVYLFNGYGPTET-TV 4849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 156 CATYWgmKIKPGFM--------GKATPPYDVQVIDDKGSILPPNTEGNIGIRIKpvrpvSLFMCYEGDPEKTAK------ 221
Cdd:PRK12316 4850 TVLLW--KARDGDAcgaaympiGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGE-----GVARGYLERPALTAErfvpdp 4922
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 222 --VECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTP 299
Cdd:PRK12316 4923 fgAPGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVGYVVPQDP 5002
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 300 QFLSHDKDQ--LTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKKETGQM 357
Cdd:PRK12316 5003 ALADADEAQaeLRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDASLL 5062
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
3-351 |
1.84e-23 |
|
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: 100.46 E-value: 1.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPKMAKHSHG----LALQPSF-----PGSRKLRSLKTS-DVSW-----CLSDSGwivatiwTLV-----EP 62
Cdd:cd17653 110 IIFTSGSTGIPKGVMVPHRgvlnYVSQPPArldvgPGSRVAQVLSIAfDACIgeifsTLCNGG-------TLVladpsDP 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 63 WTA---GCTVFIHhlpqfdTKVIIQTLlkypinhfwgvssiyrmilqqdfTSIRFPALEHCYTGGEVVLPKDQEEWK-RR 138
Cdd:cd17653 183 FAHvarTVDALMS------TPSILSTL-----------------------SPQDFPNLKTIFLGGEAVPPSLLDRWSpGR 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 139 TgllLYENYGQSETGLICATYWGMKIKPGFMGKATPPYDVQVIDDKGSILPPNTEGNIGIRikpvrPVSLFMCYEGDPEK 218
Cdd:cd17653 234 R---LYNAYGPTECTISSTMTELLPGQPVTIGKPIPNSTCYILDADLQPVPEGVVGEICIS-----GVQVARGYLGNPAL 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 219 TAK--VECGD-----FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIG-PAEVESALVEHPAVAESAVVGSpdpirGEV 290
Cdd:cd17653 306 TASkfVPDPFwpgsrMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINlEEIEEVVLQSQPEVTQAAAIVV-----NGR 380
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578828480 291 VKAFIvlTPQflSHDKDQLTKELQQHVKSvtapYKYPRKVEFVSELPKTITGKIERKELRK 351
Cdd:cd17653 381 LVAFV--TPE--TVDVDGLRSELAKHLPS----YAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
1-350 |
1.91e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 101.26 E-value: 1.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 1 MVIFFTSGTTGFPKMAKHSHGLALQPSFPGSRKlRSLKTSDVSWC---LSDS-----GWIVATiwtlvepwTAGCTVFIH 72
Cdd:PRK13388 153 FMLIFTSGTTGAPKAVRCSHGRLAFAGRALTER-FGLTRDDVCYVsmpLFHSnavmaGWAPAV--------ASGAAVALP 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 73 hlPQFDTKVIIQTLLKYPINHFWGVSSIYRMILQQ-------DFTsirfpaLEHCYtGGEVVlPKDQEEWKRRTGLLLYE 145
Cdd:PRK13388 224 --AKFSASGFLDDVRRYGATYFNYVGKPLAYILATperpddaDNP------LRVAF-GNEAS-PRDIAEFSRRFGCQVED 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 146 NYGQSETGLICATYWGMKikPGFMGKATPP---YD--------VQVIDDKGSILppNTEGNIGiRIKPVRPVSLFMCYEG 214
Cdd:PRK13388 294 GYGSSEGAVIVVREPGTP--PGSIGRGAPGvaiYNpetltecaVARFDAHGALL--NADEAIG-ELVNTAGAGFFEGYYN 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 215 DPEKTAKVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAF 294
Cdd:PRK13388 369 NPEATAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAA 448
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578828480 295 IVLTP----------QFLSHDKDQLTKelqqhvksvtapyKYPRKVEFVSELPKTITGKIERKELR 350
Cdd:PRK13388 449 LVLRDgatfdpdafaAFLAAQPDLGTK-------------AWPRYVRIAADLPSTATNKVLKRELI 501
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
3-349 |
2.31e-23 |
|
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: 100.46 E-value: 2.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPK--MAKHSHGLALqpsFPGSRKLRSLKTSDV-----SWCLSDSGWivaTIW---------TLVEPWTAG 66
Cdd:cd17643 98 VIYTSGSTGRPKgvVVSHANVLAL---FAATQRWFGFNEDDVwtlfhSYAFDFSVW---EIWgallhggrlVVVPYEVAR 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 67 CTVFIHHLPQfDTKVII--QTllkyPinhfwgvSSIYRMILQQDFTSIRFPALEHCYTGGEVVLPKDQEEWKRRTGL--- 141
Cdd:cd17643 172 SPEDFARLLR-DEGVTVlnQT----P-------SAFYQLVEAADRDGRDPLALRYVIFGGEALEAAMLRPWAGRFGLdrp 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 142 LLYENYGQSETgLICATYWGMK---IKPGFM---GKATPPYDVQVIDDKGSILPPNTEGNIGIRIKPVRPvslfmCYEGD 215
Cdd:cd17643 240 QLVNMYGITET-TVHVTFRPLDaadLPAAAAspiGRPLPGLRVYVLDADGRPVPPGVVGELYVSGAGVAR-----GYLGR 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 216 PEKTAKVECGD--------FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIR 287
Cdd:cd17643 314 PELTAERFVANpfggpgsrMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPG 393
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578828480 288 GEVVKAFIVLTPQflshdKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKEL 349
Cdd:cd17643 394 DTRLVAYVVADDG-----AAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
3-349 |
2.51e-23 |
|
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: 100.32 E-value: 2.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPK--MAKHSHGLAL----QPSFPGSRKLRSLKTSDVSWclsdsgwiVATIWTLVEPWTAGCTVfiHHLPQ 76
Cdd:cd17645 109 VIYTSGSTGLPKgvMIEHHNLVNLcewhRPYFGVTPADKSLVYASFSF--------DASAWEIFPHLTAGAAL--HVVPS 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 77 fDTKVIIQTLLKYPINHFWGVSSIYRMILQQdFTSIRFPALEHCYTGGEVVlpkdqeEWKRRTGLLLYENYGQSETGLIC 156
Cdd:cd17645 179 -ERRLDLDALNDYFNQEGITISFLPTGAAEQ-FMQLDNQSLRVLLTGGDKL------KKIERKGYKLVNNYGPTENTVVA 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 157 ATYwgmKIKPGF----MGKATPPYDVQVIDDKGSILPPNTEGNIGIRIKpvrpvSLFMCYEGDPEKTAKVECGD------ 226
Cdd:cd17645 251 TSF---EIDKPYanipIGKPIDNTRVYILDEALQLQPIGVAGELCIAGE-----GLARGYLNRPELTAEKFIVHpfvpge 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 227 -FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVlTPQFLSHD 305
Cdd:cd17645 323 rMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVT-APEEIPHE 401
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 578828480 306 kdqltkELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKEL 349
Cdd:cd17645 402 ------ELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
169-350 |
2.97e-23 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 100.69 E-value: 2.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 169 MGKATPPYDVQVID-DKGSILPPNTEGNIGIRIKPVrpvslFMCYEGDPEKTAKVECGD-FYNTGDRGKMDEEGYICFLG 246
Cdd:PLN02574 376 VGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGV-----MKGYLNNPKATQSTIDKDgWLRTGDIAYFDEDGYLYIVD 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 247 RSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQflshdkDQLTKE-LQQHVKSVTAPYK 325
Cdd:PLN02574 451 RLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQG------STLSQEaVINYVAKQVAPYK 524
|
170 180
....*....|....*....|....*
gi 578828480 326 YPRKVEFVSELPKTITGKIERKELR 350
Cdd:PLN02574 525 KVRKVVFVQSIPKSPAGKILRRELK 549
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
1-322 |
3.24e-23 |
|
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: 100.24 E-value: 3.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 1 MVIFFTSGTTGFPKMAKHSHGlalQPSFPGSRKLRSLKTSDVSWCLS-------------DSGWI--------VATIWTL 59
Cdd:cd05932 140 ATLIYTSGTTGQPKGVMLTFG---SFAWAAQAGIEHIGTEENDRMLSylplahvtervfvEGGSLyggvlvafAESLDTF 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 60 VEPWT-AGCTVFIHhLPQ----FDTKVI-------IQTLLKYPInhfwgVSSIYRMILQQDFtsirfpALEHC--YTGGE 125
Cdd:cd05932 217 VEDVQrARPTLFFS-VPRlwtkFQQGVQdkipqqkLNLLLKIPV-----VNSLVKRKVLKGL------GLDQCrlAGCGS 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 126 VVLPKDQEEWKRRTGLLLYENYGQSETGLICATYWGMKIKPGFMGKATPpyDVQV-IDDKGSILppntegnigirikpVR 204
Cdd:cd05932 285 APVPPALLEWYRSLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGP--GVEVrISEDGEIL--------------VR 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 205 PVSLFMCYEGDPEKTAKVECGD-FYNTGDRGKMDEEGYICFLGRSDDIINAS-GYRIGPAEVESALVEHPAVAESAVVGS 282
Cdd:cd05932 349 SPALMMGYYKDPEATAEAFTADgFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIGS 428
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 578828480 283 --PDPIRGEVVKAFIVltPQFLSHDKDQLTKELQQHVKSVTA 322
Cdd:cd05932 429 glPAPLALVVLSEEAR--LRADAFARAELEASLRAHLARVNS 468
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
1-346 |
3.82e-23 |
|
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: 99.82 E-value: 3.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 1 MVIFFTSGTTGFPK--MAKHSHglaLQPSFPGSRKLRSLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCTV-FIHHLP-- 75
Cdd:cd05914 92 ALINYTSGTTGNSKgvMLTYRN---IVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVvFLDKIPsa 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 76 ------QFDTKVIIQTLLKYPINHF------------WGVSSIYRMILQQDFTSIRFPALEHCYTG-------GEVVLPK 130
Cdd:cd05914 169 kiialaFAQVTPTLGVPVPLVIEKIfkmdiipkltlkKFKFKLAKKINNRKIRKLAFKKVHEAFGGnikefviGGAKINP 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 131 DQEEWKRRTGLLLYENYGQSETG-LICATYWGmKIKPGFMGKATPPYDVQvIDDKGsilPPNTEGNIGIRIKPVrpvslF 209
Cdd:cd05914 249 DVEEFLRTIGFPYTIGYGMTETApIISYSPPN-RIRLGSAGKVIDGVEVR-IDSPD---PATGEGEIIVRGPNV-----M 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 210 MCYEGDPEKTAKV--ECGDFYnTGDRGKMDEEGYICFLGRSDD-IINASGYRIGPAEVESALVEHPAVAESAVVgspdpI 286
Cdd:cd05914 319 KGYYKNPEATAEAfdKDGWFH-TGDLGKIDAEGYLYIRGRKKEmIVLSSGKNIYPEEIEAKINNMPFVLESLVV-----V 392
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578828480 287 RGEVVKAFIVLTPQFL-------SHDKDQLTKELQQHVKSVTAPYKYPRKVEFV-SELPKTITGKIER 346
Cdd:cd05914 393 QEKKLVALAYIDPDFLdvkalkqRNIIDAIKWEVRDKVNQKVPNYKKISKVKIVkEEFEKTPKGKIKR 460
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
117-352 |
7.59e-23 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 99.79 E-value: 7.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 117 LEHCYTGGEVvLPKDQEEWKRRTGLLLYENYGQSET-GLICATYWGmKIKPGFMGKATPpyDVQV-IDDKGSILppnteg 194
Cdd:COG1022 349 LRFAVSGGAA-LGPELARFFRALGIPVLEGYGLTETsPVITVNRPG-DNRIGTVGPPLP--GVEVkIAEDGEIL------ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 195 nigirikpVRPVSLFMCYEGDPEKTAKVECGD-FYNTGDRGKMDEEGYICFLGRSDDII-NASGYRIGPAEVESALVEHP 272
Cdd:COG1022 419 --------VRGPNVMKGYYKNPEATAEAFDADgWLHTGDIGELDEDGFLRITGRKKDLIvTSGGKNVAPQPIENALKASP 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 273 AVAESAVVGSPDPirgeVVKAFIVLTPQFLSH----------------DKDQLTKELQQHVKSVT---APYKYPRKVEFv 333
Cdd:COG1022 491 LIEQAVVVGDGRP----FLAALIVPDFEALGEwaeenglpytsyaelaQDPEVRALIQEEVDRANaglSRAEQIKRFRL- 565
|
250 260
....*....|....*....|....*...
gi 578828480 334 seLPK---------TITGKIERKELRKK 352
Cdd:COG1022 566 --LPKeftiengelTPTLKLKRKVILEK 591
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
5-350 |
2.08e-22 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 98.17 E-value: 2.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 5 FTSGTTGFPKMAKHSHglalqpsfpgsrklRSLKTSDVSWCLsdsGWIVAT----IWTL--------VEPWT----AGCT 68
Cdd:PLN03102 193 YTSGTTADPKGVVISH--------------RGAYLSTLSAII---GWEMGTcpvyLWTLpmfhcngwTFTWGtaarGGTS 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 69 VFIHHL--PQfdtkvIIQTLLKYPINHFWGVSSIYRMILQQDFT--SIRFPALeHCYTGGE---VVLPKDQEewkrRTGL 141
Cdd:PLN03102 256 VCMRHVtaPE-----IYKNIEMHNVTHMCCVPTVFNILLKGNSLdlSPRSGPV-HVLTGGSpppAALVKKVQ----RLGF 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 142 LLYENYGQSE-TGLICATYWG-------------MKIKPGFMGKATPPYDVQVIDDKGSIlPPN--TEGNIGIRikpvrP 205
Cdd:PLN03102 326 QVMHAYGLTEaTGPVLFCEWQdewnrlpenqqmeLKARQGVSILGLADVDVKNKETQESV-PRDgkTMGEIVIK-----G 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 206 VSLFMCYEGDPEKTAKVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDP 285
Cdd:PLN03102 400 SSIMKGYLKNPKATSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHP 479
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 286 IRGEVVKAFIVL--TPQFLSHDKDQL-TKE--LQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELR 350
Cdd:PLN03102 480 TWGETPCAFVVLekGETTKEDRVDKLvTRErdLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLR 549
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
3-353 |
2.76e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 98.69 E-value: 2.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPKMAKHSHGlALQpSFPGSRKLRSLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCTVfiHHLPQ---FDT 79
Cdd:PRK12467 661 VIYTSGSTGQPKGVAISHG-ALA-NYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATL--HLLPPdcaRDA 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 80 KVIIQTLLKYPINHFWGVSSIYRMILQQDFTSIRFPaLEHCYTGGEVVLPKDQEEWKR-RTGLLLYENYGQSETGlICAT 158
Cdd:PRK12467 737 EAFAALMADQGVTVLKIVPSHLQALLQASRVALPRP-QRALVCGGEALQVDLLARVRAlGPGARLINHYGPTETT-VGVS 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 159 YWGMK-----IKPGFMGKATPPYDVQVIDDKGSILPPNTEGNIGIRikpvrPVSLFMCYEGDPEKTAK--------VECG 225
Cdd:PRK12467 815 TYELSdeerdFGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIG-----GAGLARGYHRRPALTAErfvpdpfgADGG 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 226 DFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVkAFIVLTPQFLSHD 305
Cdd:PRK12467 890 RLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLV-AYLVPAAVADGAE 968
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 578828480 306 KDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKKE 353
Cdd:PRK12467 969 HQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPD 1016
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
3-351 |
3.60e-22 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 97.89 E-value: 3.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPKMAKHSHG-----LALQPSFPGSRK--LRSLKTSDVSWcLSDSGWIVATI---WTLVEpWTAGCTVFIH 72
Cdd:PTZ00237 259 ILYTSGTTGNSKAVVRSNGphlvgLKYYWRSIIEKDipTVVFSHSSIGW-VSFHGFLYGSLslgNTFVM-FEGGIIKNKH 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 73 HLPQFdtkviIQTLLKYPINHFWGVSSIYRMILQQD--FTSIR----FPALEHCYTGGEVVLPKDQEEWKRRTGLLLYEN 146
Cdd:PTZ00237 337 IEDDL-----WNTIEKHKVTHTLTLPKTIRYLIKTDpeATIIRskydLSNLKEIWCGGEVIEESIPEYIENKLKIKSSRG 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 147 YGQSETG---LICatYWGMKIKPGFMGKATPPYDVQVIDDKGSILPPNTEGNIGIRIkPVRPVSLFMCYEGDpEKTAKV- 222
Cdd:PTZ00237 412 YGQTEIGityLYC--YGHINIPYNATGVPSIFIKPSILSEDGKELNVNEIGEVAFKL-PMPPSFATTFYKND-EKFKQLf 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 223 -ECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQF 301
Cdd:PTZ00237 488 sKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQ 567
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 578828480 302 LSH--DKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRK 351
Cdd:PTZ00237 568 SNQsiDLNKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISK 619
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
3-356 |
2.04e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 96.18 E-value: 2.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPKMAKHSHGlALQPSFPGSRKLRSLKTSDVSWCLSDSGWIVAtIWTLVEPWTAGCTVFIHHLPQF-DTKV 81
Cdd:PRK12316 3201 VIYTSGSTGKPKGVGIRHS-ALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVF-VEELFWPLMSGARVVLAGPEDWrDPAL 3278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 82 IIQTLLKYPINHFWGVSSIYRMILQqDFTSIRFPALEHCYTGGEVVLPKDQEEWKrrTGLLLYENYGQSETGLICATYWG 161
Cdd:PRK12316 3279 LVELINSEGVDVLHAYPSMLQAFLE-EEDAHRCTSLKRIVCGGEALPADLQQQVF--AGLPLYNLYGPTEATITVTHWQC 3355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 162 MKIKPG--FMGKATPPYDVQVIDDKGSILPPNTEGNIGIRikpvrPVSLFMCYEGDPEKTAK-------VECGDFYNTGD 232
Cdd:PRK12316 3356 VEEGKDavPIGRPIANRACYILDGSLEPVPVGALGELYLG-----GEGLARGYHNRPGLTAErfvpdpfVPGERLYRTGD 3430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 233 RGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGspdpIRGEVVKAFIVLTPQflshdKDQLTKE 312
Cdd:PRK12316 3431 LARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLA----VDGRQLVAYVVPEDE-----AGDLREA 3501
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 578828480 313 LQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKKETGQ 356
Cdd:PRK12316 3502 LKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAAL 3545
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
3-357 |
5.37e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 94.84 E-value: 5.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPKMAKHSHGlALQPSFPGSRKLRSLKTSDvSWCLSDSGWIVATIWTLVEPWTAGCTVFI-----HHLPQF 77
Cdd:PRK12467 1723 VIYTSGSTGRPKGAGNRHG-ALVNRLCATQEAYQLSAAD-VVLQFTSFAFDVSVWELFWPLINGARLVIappgaHRDPEQ 1800
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 78 dtkvIIQTLLKYPIN--HFwgVSSIYRMILQQDFTSIRFPALEHCYTGGEVVLPKDQEEWKRRTG-LLLYENYGQSETGl 154
Cdd:PRK12467 1801 ----LIQLIERQQVTtlHF--VPSMLQQLLQMDEQVEHPLSLRRVVCGGEALEVEALRPWLERLPdTGLFNLYGPTETA- 1873
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 155 ICATYWGMKIKPgFMGKATPPYDVQVIDDKGSIL-------PPNTEGNIgirikPVRPVSLFMCYEGDPEKTAK------ 221
Cdd:PRK12467 1874 VDVTHWTCRRKD-LEGRDSVPIGQPIANLSTYILdaslnpvPIGVAGEL-----YLGGVGLARGYLNRPALTAErfvadp 1947
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 222 --VECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSpDPIRGEVVKAFIV-LT 298
Cdd:PRK12467 1948 fgTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQ-DGANGKQLVAYVVpTD 2026
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578828480 299 PQFLSHDKDQLT--KELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKKETGQM 357
Cdd:PRK12467 2027 PGLVDDDEAQVAlrAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDASEL 2087
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
185-351 |
8.18e-21 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 93.14 E-value: 8.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 185 GSILP-------PNTEGNIGIRIKpvrpvSLFMCYEgdPEKTAKVECgdfYNTGDRGKMDEEGYICFLGRSDDIINASGY 257
Cdd:PRK07445 286 GQVLPhaqitipANQTGNITIQAQ-----SLALGYY--PQILDSQGI---FETDDLGYLDAQGYLHILGRNSQKIITGGE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 258 RIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFLSHDkdqltkELQQHVKSVTAPYKYPRKVEFVSELP 337
Cdd:PRK07445 356 NVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSISLE------ELKTAIKDQLSPFKQPKHWIPVPQLP 429
|
170
....*....|....
gi 578828480 338 KTITGKIERKELRK 351
Cdd:PRK07445 430 RNPQGKINRQQLQQ 443
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
3-349 |
5.45e-20 |
|
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: 90.57 E-value: 5.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPK--MAKHS----HGLALQPSFPGSRKLRSLKTSDVSWCLSdsgwiVATIWTLvepWTAGCTVFIH-HLP 75
Cdd:cd17644 111 VIYTSGSTGKPKgvMIEHQslvnLSHGLIKEYGITSSDRVLQFASIAFDVA-----AEEIYVT---LLSGATLVLRpEEM 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 76 QFDTKVIIQTLLKYPINhFWGVSSIYRMILQQDFTSIRFPALEH---CYTGGEVVLPKDQEEWKRRTGLL--LYENYGQS 150
Cdd:cd17644 183 RSSLEDFVQYIQQWQLT-VLSLPPAYWHLLVLELLLSTIDLPSSlrlVIVGGEAVQPELVRQWQKNVGNFiqLINVYGPT 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 151 EtGLICAT------YWGMKIKPGFMGKATPPYDVQVIDDKGSILPPNTEGNIGIRikpvrPVSLFMCYEGDPEKTAK--- 221
Cdd:cd17644 262 E-ATIAATvcrltqLTERNITSVPIGRPIANTQVYILDENLQPVPVGVPGELHIG-----GVGLARGYLNRPELTAEkfi 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 222 ------VECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFI 295
Cdd:cd17644 336 shpfnsSESERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYI 415
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 578828480 296 VltPQFlshDKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKEL 349
Cdd:cd17644 416 V--PHY---EESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
5-352 |
2.38e-19 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 89.04 E-value: 2.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 5 FTSGTTGFPKMAKHSHG-------LALQPSFPGsrklrsLKTSDV-----------SWCLSDSGWIVATiwTLVEPwtaG 66
Cdd:PRK06018 184 YTSGTTGDPKGVLYSHRsnvlhalMANNGDALG------TSAADTmlpvvplfhanSWGIAFSAPSMGT--KLVMP---G 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 67 CtvfihhlpQFDTKVIIQTLLKYPINHFWGVSSIYRMILQQ-DFTSIRFPALEHCYTGGEVvLPKDQEEWKRRTGLLLYE 145
Cdd:PRK06018 253 A--------KLDGASVYELLDTEKVTFTAGVPTVWLMLLQYmEKEGLKLPHLKMVVCGGSA-MPRSMIKAFEDMGVEVRH 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 146 NYGQSET---GLICAtywgmkIKPGFMG------------KATPPYDVQ--VIDDKGSILPpnTEGNIGIRIKPVRPVSL 208
Cdd:PRK06018 324 AWGMTEMsplGTLAA------LKPPFSKlpgdarldvlqkQGYPPFGVEmkITDDAGKELP--WDGKTFGRLKVRGPAVA 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 209 FMCYEGDPEKtakVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRG 288
Cdd:PRK06018 396 AAYYRVDGEI---LDDDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWD 472
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578828480 289 EVVKAFIVLTPqflshDKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKK 352
Cdd:PRK06018 473 ERPLLIVQLKP-----GETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQ 531
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
3-356 |
3.82e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 89.25 E-value: 3.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPKMAKHSHGlALQPSFPGSRKLRSLKTSDVSWCLSDSGWIVaTIWTLVEPWTAGCTvfIHHLPQ---FDT 79
Cdd:PRK12316 660 VIYTSGSTGKPKGAGNRHR-ALSNRLCWMQQAYGLGVGDTVLQKTPFSFDV-SVWEFFWPLMSGAR--LVVAAPgdhRDP 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 80 KVIIQTLLKYPINHFWGVSSIYRMILQ----QDFTSIRFPALehcytGGEVvLPKDQEE--WKRRTGLLLYENYGQSETG 153
Cdd:PRK12316 736 AKLVELINREGVDTLHFVPSMLQAFLQdedvASCTSLRRIVC-----SGEA-LPADAQEqvFAKLPQAGLYNLYGPTEAA 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 154 lICATYWGMKIKpgfmGKATPPYDVQVIDDKGSILPPNTEgnigirikPVrPVS-----------LFMCYEGDPEKTAK- 221
Cdd:PRK12316 810 -IDVTHWTCVEE----GGDSVPIGRPIANLACYILDANLE--------PV-PVGvlgelylagrgLARGYHGRPGLTAEr 875
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 222 ------VECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGspdpIRGEVVKAFI 295
Cdd:PRK12316 876 fvpspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDGKQLVGYV 951
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578828480 296 VLTpqflshDKDQLTKE-LQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKKETGQ 356
Cdd:PRK12316 952 VLE------SEGGDWREaLKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASV 1007
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
3-349 |
4.57e-19 |
|
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: 88.12 E-value: 4.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPK--MAKHS------HGLALQPSF-PGSRKLrSLKTS--DVSwclsdsgwivatIWTLVEPWTAGCTVFI 71
Cdd:cd12116 131 VIYTSGSTGRPKgvVVSHRnlvnflHSMRERLGLgPGDRLL-AVTTYafDIS------------LLELLLPLLAGARVVI 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 72 hhLP---QFDTKVIIQTLLKYPINHFWGVSSIYRMILQQDFTSIR-FPALehCytGGEVvLPKDQEEWKRRTGLLLYENY 147
Cdd:cd12116 198 --APretQRDPEALARLIEAHSITVMQATPATWRMLLDAGWQGRAgLTAL--C--GGEA-LPPDLAARLLSRVGSLWNLY 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 148 GQSETglicaTYWG--MKIKPGF----MGKATPPYDVQVIDDKGSILPPNTEGNIGIRikpvrPVSLFMCYEGDPEKTAK 221
Cdd:cd12116 271 GPTET-----TIWStaARVTAAAgpipIGRPLANTQVYVLDAALRPVPPGVPGELYIG-----GDGVAQGYLGRPALTAE 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 222 V--------ECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVkA 293
Cdd:cd12116 341 RfvpdpfagPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLV-A 419
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 578828480 294 FIVLtPQFLSHDKDQLTKELQQHVKSvtapYKYPRKVEFVSELPKTITGKIERKEL 349
Cdd:cd12116 420 YVVL-KAGAAPDAAALRAHLRATLPA----YMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
212-356 |
8.29e-19 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 86.25 E-value: 8.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 212 YEGDPEKTAKVECGDFyNTGDRGKMDEeGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVV 291
Cdd:PRK07824 221 YRNPVDPDPFAEPGWF-RTDDLGALDD-GVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRV 298
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578828480 292 KAFIVLTPqflsHDKDQLTkELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKKETGQ 356
Cdd:PRK07824 299 VAAVVGDG----GPAPTLE-ALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRRFAGE 358
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
3-349 |
1.22e-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: 83.68 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPK--MAKHSHGLAL-QPSFPGSRKLRSLKTSDVSWCLSDSGW--IVATiwtlvepWTAGCTVFI-HHLPQ 76
Cdd:cd17656 133 IIYTSGTTGKPKgvQLEHKNMVNLlHFEREKTNINFSDKVLQFATCSFDVCYqeIFST-------LLSGGTLYIiREETK 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 77 FDTKVIIQTLLKYPINHFWGVSSIYRMILQQDFTSIRFP-ALEHCYTGGE-VVLPKDQEEWKRRTGLLLYENYGQSETGL 154
Cdd:cd17656 206 RDVEQLFDLVKRHNIEVVFLPVAFLKFIFSEREFINRFPtCVKHIITAGEqLVITNEFKEMLHEHNVHLHNHYGPSETHV 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 155 IcATYwgmKIKPGFMGKATPPY-------DVQVIDDKGSILPPNTEGNIGIrikpvRPVSLFMCYEGDPEKTAKVECGD- 226
Cdd:cd17656 286 V-TTY---TINPEAEIPELPPIgkpisntWIYILDQEQQLQPQGIVGELYI-----SGASVARGYLNRQELTAEKFFPDp 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 227 ------FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTpQ 300
Cdd:cd17656 357 fdpnerMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVME-Q 435
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 578828480 301 FLShdkdqlTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKEL 349
Cdd:cd17656 436 ELN------ISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
3-349 |
1.90e-17 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 82.90 E-value: 1.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPK--MAKHSH------------GLALQPsfpgsrkLRSLKTSDVSWCLSDSGWIVATiwtlvepwTAGCT 68
Cdd:cd17650 98 VIYTSGTTGKPKgvMVEHRNvahaahawrreyELDSFP-------VRLLQMASFSFDVFAGDFARSL--------LNGGT 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 69 VFIhhLPQ---FDTKVIIQTLLKYPINHFWGVSSIYRMILQQ-DFTSIRFPALEHCYTGGEVVLPKDQEEWKRRTG--LL 142
Cdd:cd17650 163 LVI--CPDevkLDPAALYDLILKSRITLMESTPALIRPVMAYvYRNGLDLSAMRLLIVGSDGCKAQDFKTLAARFGqgMR 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 143 LYENYGQSETgLICATYW----GMKIKPGF--MGKATPPYDVQVIDDKGSILPPNTEGNIGIRIKPVRpvslfMCYEGDP 216
Cdd:cd17650 241 IINSYGVTEA-TIDSTYYeegrDPLGDSANvpIGRPLPNTAMYVLDERLQPQPVGVAGELYIGGAGVA-----RGYLNRP 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 217 EKTAK-------VECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPiRGE 289
Cdd:cd17650 315 ELTAErfvenpfAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDK-GGE 393
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578828480 290 V-VKAFIVltpqfLSHDKDqlTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKEL 349
Cdd:cd17650 394 ArLCAYVV-----AAATLN--TAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
1-349 |
7.61e-17 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 81.59 E-value: 7.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 1 MVIFFTSGTTGFPKMAKhshgLALQPSFPGSRKLRSLKTSDVSWCLSDSGW--IVAT----IWTLVEPWTAG--CTVFIH 72
Cdd:PRK05857 172 LAMIFTSGTTGEPKAVL----LANRTFFAVPDILQKEGLNWVTWVVGETTYspLPAThiggLWWILTCLMHGglCVTGGE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 73 HlpqfdTKVIIQTLLKYPINHFWGVSSIY-RMILQQDFTSIRFPALEHCYTGGEVVLPKDQEeWKRRTGLLLYENYGQSE 151
Cdd:PRK05857 248 N-----TTSLLEILTTNAVATTCLVPTLLsKLVSELKSANATVPSLRLVGYGGSRAIAADVR-FIEATGVRTAQVYGLSE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 152 TG---LICATYWG--MKIKPGFMGKATPPYDVQVIDDKGSilPPNTE--------GNIGIRikpvRPVSLfMCYEGDPEK 218
Cdd:PRK05857 322 TGctaLCLPTDDGsiVKIEAGAVGRPYPGVDVYLAATDGI--GPTAPgagpsasfGTLWIK----SPANM-LGYWNNPER 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 219 TAKVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLT 298
Cdd:PRK05857 395 TAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVAS 474
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 578828480 299 PQFLSHDKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKEL 349
Cdd:PRK05857 475 AELDESAARALKHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
5-350 |
7.66e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 81.68 E-value: 7.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 5 FTSGTTGFPKMAKHSH--------GLALQPSFpgsrklrSLKTSDV-----------SWCLSDSGWIVATiwTLVEPWta 65
Cdd:PRK07008 183 YTSGTTGNPKGALYSHrstvlhayGAALPDAM-------GLSARDAvlpvvpmfhvnAWGLPYSAPLTGA--KLVLPG-- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 66 gctvfihhlPQFDTKVIIQTLLKYPINHFWGVSSIYRMILQQ-DFTSIRFPALEHCYTGGEVVLPKDQEEWKRRTGLLLY 144
Cdd:PRK07008 252 ---------PDLDGKSLYELIEAERVTFSAGVPTVWLGLLNHmREAGLRFSTLRRTVIGGSACPPAMIRTFEDEYGVEVI 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 145 ENYGQSET---GLICATYWG---------MKIKPGfMGKATPPYDVQVIDDKGSILPPN--TEGNIGIRIKPVrpVSLFM 210
Cdd:PRK07008 323 HAWGMTEMsplGTLCKLKWKhsqlpldeqRKLLEK-QGRVIYGVDMKIVGDDGRELPWDgkAFGDLQVRGPWV--IDRYF 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 211 CYEGDPEKTakvecgDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEV 290
Cdd:PRK07008 400 RGDASPLVD------GWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDER 473
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578828480 291 VKAFIVLTPQFlshdkdQLTK-ELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELR 350
Cdd:PRK07008 474 PLLVVVKRPGA------EVTReELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLR 528
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
3-355 |
1.48e-16 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 81.24 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPK--MAKH----SHGLALQPSFPGSRKLRSL-KTS---DVSwclsdsgwivatIWTLVEPWTAGCTVFI- 71
Cdd:PRK10252 603 IIFTSGSTGRPKgvMVGQtaivNRLLWMQNHYPLTADDVVLqKTPcsfDVS------------VWEFFWPFIAGAKLVMa 670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 72 ----HHLPQFDTKVI----IQTLlkypinHFwgVSSIYRMILQQ---DFTSIRFPALEHCYTGGEVvLPKDQ-EEWKRRT 139
Cdd:PRK10252 671 epeaHRDPLAMQQFFaeygVTTT------HF--VPSMLAAFVASltpEGARQSCASLRQVFCSGEA-LPADLcREWQQLT 741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 140 GLLLYENYGQSETGlICATYW-----------GMKIKPGFmgkatPPYDVQ--VIDDKGSILPPNTEGNIGIRikpvrPV 206
Cdd:PRK10252 742 GAPLHNLYGPTEAA-VDVSWYpafgeelaavrGSSVPIGY-----PVWNTGlrILDARMRPVPPGVAGDLYLT-----GI 810
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 207 SLFMCYEGDPEKTAK-------VECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHP----AVA 275
Cdd:PRK10252 811 QLAQGYLGRPDLTASrfiadpfAPGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPdveqAVT 890
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 276 ESAVVGSPDPIRGEVVKAFIVLTPQF-LSHDKDQltkeLQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKKET 354
Cdd:PRK10252 891 HACVINQAAATGGDARQLVGYLVSQSgLPLDTSA----LQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKALPLPEL 966
|
.
gi 578828480 355 G 355
Cdd:PRK10252 967 K 967
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
3-351 |
3.11e-16 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 79.83 E-value: 3.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPKMAKHSH-GLALQPsfpgsrklRSLKTSD-------------------VSWCLSDSGWIVATiwTLVEP 62
Cdd:PRK05620 186 ICYSTGTTGAPKGVVYSHrSLYLQS--------LSLRTTDslavthgesflccvpiyhvLSWGVPLAAFMSGT--PLVFP 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 63 wtaGCTVFIHHLpqfdTKVIIQTLLKypINHfwGVSSIY-RMILQQDFTSIRFPALEHCYTGGEVVLPKDQEEWKRRTGL 141
Cdd:PRK05620 256 ---GPDLSAPTL----AKIIATAMPR--VAH--GVPTLWiQLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEERYGV 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 142 LLYENYGQSETGLIcatywGMKIKP--GFMGKATPPYDV-----------QVIDDkGSILPPN--TEGNIGIRIKPVR-- 204
Cdd:PRK05620 325 DVVHVWGMTETSPV-----GTVARPpsGVSGEARWAYRVsqgrfpasleyRIVND-GQVMESTdrNEGEIQVRGNWVTas 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 205 -----------PVSLFMCYEGDPEKTAKVECGdFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPA 273
Cdd:PRK05620 399 yyhspteegggAASTFRGEDVEDANDRFTADG-WLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPE 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 274 VAESAVVGSPDPIRGEVVKAFIVLTP--QFLSHDKDQLTKELQQHVKSVTAPYKYprkvEFVSELPKTITGKIERKELRK 351
Cdd:PRK05620 478 VVECAVIGYPDDKWGERPLAVTVLAPgiEPTRETAERLRDQLRDRLPNWMLPEYW----TFVDEIDKTSVGKFDKKDLRQ 553
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
3-354 |
3.33e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 80.21 E-value: 3.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPKMAKHSHGlALQPSFPGSRKLRSLKTSD-----VSWCLSDSGWIVatIWTLVepwTAGCtvfihhlpqf 77
Cdd:PRK12467 3242 VIYTSGSTGKPKGVGVRHG-ALANHLCWIAEAYELDANDrvllfMSFSFDGAQERF--LWTLI---CGGC---------- 3305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 78 dtkVIIQTllkypiNHFWGVSSIYRMILQQDFTSIRFP-----------------ALEHCYTGGEVVLPKDQEEWKRRTG 140
Cdd:PRK12467 3306 ---LVVRD------NDLWDPEELWQAIHAHRISIACFPpaylqqfaedaggadcaSLDIYVFGGEAVPPAAFEQVKRKLK 3376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 141 -LLLYENYGQSETgLICATYW--GMKIKPGF----MGKATPPYDVQVIDDKGSILPPNTEGNIGIRikpvrPVSLFMCYE 213
Cdd:PRK12467 3377 pRGLTNGYGPTEA-VVTVTLWkcGGDAVCEApyapIGRPVAGRSIYVLDGQLNPVPVGVAGELYIG-----GVGLARGYH 3450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 214 GDPEKTAK-------VECGD-FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSpDP 285
Cdd:PRK12467 3451 QRPSLTAErfvadpfSGSGGrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DG 3529
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578828480 286 IRGEVVKAFIVltPQFLSHDkdqLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKKET 354
Cdd:PRK12467 3530 AGGKQLVAYVV--PADPQGD---WRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDA 3593
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
3-349 |
4.84e-16 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 79.83 E-value: 4.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPKMAKHSHGlALQPSFPGSRKLRSLKTSDVSWCLSDSGWIVaTIWTLVEPWTAGCTVFI-----HHLPQF 77
Cdd:PRK05691 1278 VIYTSGSTGQPKGVGNTHA-ALAERLQWMQATYALDDSDVLMQKAPISFDV-SVWECFWPLITGCRLVLagpgeHRDPQR 1355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 78 DTKVIIQ---TLLkypinHFwgVSSIYRMILQQdftsirfPALEHC------YTGGEVVLPkdqeEWKRRT-----GLLL 143
Cdd:PRK05691 1356 IAELVQQygvTTL-----HF--VPPLLQLFIDE-------PLAAACtslrrlFSGGEALPA----ELRNRVlqrlpQVQL 1417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 144 YENYGQSETGlICATYWGMKIKPGF---MGKATPPYDVQVIDDKGSILPPNTEGNIGIRikpvrPVSLFMCYEGDPEKTA 220
Cdd:PRK05691 1418 HNRYGPTETA-INVTHWQCQAEDGErspIGRPLGNVLCRVLDAELNLLPPGVAGELCIG-----GAGLARGYLGRPALTA 1491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 221 KVECGD--------FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVgspdpIRGEVVK 292
Cdd:PRK05691 1492 ERFVPDplgedgarLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVL-----VREGAAG 1566
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 578828480 293 AFIVltpQFLSHDK--DQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKEL 349
Cdd:PRK05691 1567 AQLV---GYYTGEAgqEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
2-351 |
1.16e-15 |
|
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: 78.09 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 2 VIFFTSGTTGFPKMAKHSHGlALQPSFPGSRKLRSLKTSDVSwcLSdsgWI----VATIwtlvepwtagctVFIHHLP-- 75
Cdd:cd05906 171 LLMLTSGSTGFPKAVPLTHR-NILARSAGKIQHNGLTPQDVF--LN---WVpldhVGGL------------VELHLRAvy 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 76 ----QFDTK---VIIQTLL------KYPINHFWGVSSIYRMILQQ---------DFTSIRFpalehCYTGGEVVLPKDQE 133
Cdd:cd05906 233 lgcqQVHVPteeILADPLRwldlidRYRVTITWAPNFAFALLNDLleeiedgtwDLSSLRY-----LVNAGEAVVAKTIR 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 134 ewkRRTGLL----LYEN-----YGQSET--GLI----CATYwGMKIKPGFM--GKATPPYDVQVIDDKGSILPPNTEGNI 196
Cdd:cd05906 308 ---RLLRLLepygLPPDairpaFGMTETcsGVIysrsFPTY-DHSQALEFVslGRPIPGVSMRIVDDEGQLLPEGEVGRL 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 197 GIRIKPVrpvslFMCYEGDPEKTAKVECGD-FYNTGDRGKMDEeGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVA 275
Cdd:cd05906 384 QVRGPVV-----TKGYYNNPEANAEAFTEDgWFRTGDLGFLDN-GNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 276 ES--AVVGSPDPIRGEVVKAFIVLTPQFLSHDKDQLTKELQQHVK---SVTAPYKYPRKVEfvsELPKTITGKIERKELR 350
Cdd:cd05906 458 PSftAAFAVRDPGAETEELAIFFVPEYDLQDALSETLRAIRSVVSrevGVSPAYLIPLPKE---EIPKTSLGKIQRSKLK 534
|
.
gi 578828480 351 K 351
Cdd:cd05906 535 A 535
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
3-357 |
3.46e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 77.30 E-value: 3.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPKMAKHSHGlALQPSFPGSRKLRSLKTSDVSWCLSDSGWIVAtIWTLVEPWTAGCTVFIHHLPQFDTKVI 82
Cdd:PRK12316 2151 VIYTSGSTGLPKGVAVSHG-ALVAHCQAAGERYELSPADCELQFMSFSFDGA-HEQWFHPLLNGARVLIRDDELWDPEQL 2228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 83 IQTLLKYPINHFWGVSSIYRMILQQDFTSIRFPALEHCYTGGEVVLPKDQEEWKRRT-GLLLYENYGQSETgLICATYW- 160
Cdd:PRK12316 2229 YDEMERHGVTILDFPPVYLQQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLAWEALrPVYLFNGYGPTEA-VVTPLLWk 2307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 161 -------GMKIKPgfMGKATPPYDVQVIDDKGSILPPNTEGNIGIRikpvrPVSLFMCYEGDPEKTAKVECGD------- 226
Cdd:PRK12316 2308 crpqdpcGAAYVP--IGRALGNRRAYILDADLNLLAPGMAGELYLG-----GEGLARGYLNRPGLTAERFVPDpfsasge 2380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 227 -FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSpDPIRGEVVKAFIVltPQFLSHD 305
Cdd:PRK12316 2381 rLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVV--PDDAAED 2457
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 578828480 306 kdqLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKKETGQM 357
Cdd:PRK12316 2458 ---LLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQL 2506
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
3-344 |
5.25e-15 |
|
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: 76.16 E-value: 5.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPKMAKHSHG---------LALQpsfpgsrklRSLKTSDVSWCLSDSGWIvatIWT-LVEPWTAGCTVFIH 72
Cdd:cd05943 254 ILYSSGTTGLPKCIVHGAGgtllqhlkeHILH---------CDLRPGDRLFYYTTCGWM---MWNwLVSGLAVGATIVLY 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 73 HLPQF--DTKVIIQTLLKYPINHFwGVSSIYRMILQQ-DFTsirfPALEHCYTGGEVV------LPKDQEEW---KRRTG 140
Cdd:cd05943 322 DGSPFypDTNALWDLADEEGITVF-GTSAKYLDALEKaGLK----PAETHDLSSLRTIlstgspLKPESFDYvydHIKPD 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 141 LLLYENYGQSEtglICATYWGM-KIKPGFMGKATPPY---DVQVIDDKGSILPpnteGNIG----IRIKPVRPVSLFmcy 212
Cdd:cd05943 397 VLLASISGGTD---IISCFVGGnPLLPVYRGEIQCRGlgmAVEAFDEEGKPVW----GEKGelvcTKPFPSMPVGFW--- 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 213 eGDPEKtAKVECGDF------YNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPI 286
Cdd:cd05943 467 -NDPDG-SRYRAAYFakypgvWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKD 544
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578828480 287 RGEVVKAFIVLTPQFlshdkdQLTKELQQHVKSVTA----PYKYPRKVEFVSELPKTITGKI 344
Cdd:cd05943 545 GDERVILFVKLREGV------ELDDELRKRIRSTIRsalsPRHVPAKIIAVPDIPRTLSGKK 600
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
212-357 |
1.52e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 75.20 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 212 YEGDPEKTAKV-------ECGD-FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAEsAVVGSP 283
Cdd:PRK05691 4080 YVGDPLRTALAfvphpfgAPGErLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVRE-AAVAVQ 4158
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578828480 284 DPIRGEVVKAFIVLTPQFLSHdkDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKKETGQM 357
Cdd:PRK05691 4159 EGVNGKHLVGYLVPHQTVLAQ--GALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQL 4230
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
108-351 |
4.30e-14 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 73.46 E-value: 4.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 108 DFTSIRFpalehCYTGGEVVLPKDQEEWKRRTGLLLYENYGQSETGLICATYWGMKIKPGFMGKATPPYD-----VQVID 182
Cdd:PRK06814 905 DFRSLRY-----VFAGAEKVKEETRQTWMEKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEyrlepVPGID 979
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 183 DKG--SILPPN-------TEGNiGIrIKPvrpvslfmcyegdPEktakvecGDFYNTGDRGKMDEEGYICFLGRSDDIIN 253
Cdd:PRK06814 980 EGGrlFVRGPNvmlgylrAENP-GV-LEP-------------PA-------DGWYDTGDIVTIDEEGFITIKGRAKRFAK 1037
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 254 ASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVkafIVLTPQflshdKDQLTKELQQHVKSVTAPYKY-PRKVEF 332
Cdd:PRK06814 1038 IAGEMISLAAVEELAAELWPDALHAAVSIPDARKGERI---ILLTTA-----SDATRAAFLAHAKAAGASELMvPAEIIT 1109
|
250
....*....|....*....
gi 578828480 333 VSELPKTITGKIERKELRK 351
Cdd:PRK06814 1110 IDEIPLLGTGKIDYVAVTK 1128
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
108-351 |
5.26e-14 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 73.42 E-value: 5.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 108 DFTSIRFpalehCYTGGEVVLPKDQEEWKRRTGLLLYENYGQSETG---------LICATYWGMK-IKPGFMGKATPPYD 177
Cdd:PRK08633 896 MFASLRL-----VVAGAEKLKPEVADAFEEKFGIRILEGYGATETSpvasvnlpdVLAADFKRQTgSKEGSVGMPLPGVA 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 178 VQVID-DKGSILPPNTEGNIGIRIKPVrpvslfMC-YEGDPEKTAKV----ECGDFYNTGDRGKMDEEGYICFLGRSDDI 251
Cdd:PRK08633 971 VRIVDpETFEELPPGEDGLILIGGPQV------MKgYLGDPEKTAEVikdiDGIGWYVTGDKGHLDEDGFLTITDRYSRF 1044
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 252 INASGYRIGPAEVESALveHPAVAES----AVVGSPDPIRGEVVkafIVLTPQflshdKDQLTKELQQHVKSVTAP--YK 325
Cdd:PRK08633 1045 AKIGGEMVPLGAVEEEL--AKALGGEevvfAVTAVPDEKKGEKL---VVLHTC-----GAEDVEELKRAIKESGLPnlWK 1114
|
250 260
....*....|....*....|....*.
gi 578828480 326 yPRKVEFVSELPKTITGKIERKELRK 351
Cdd:PRK08633 1115 -PSRYFKVEALPLLGSGKLDLKGLKE 1139
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
3-352 |
3.42e-13 |
|
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: 70.47 E-value: 3.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPK--MAKH-------SHGLALQPSFPGSRKLRSLKtsdvswclsdsgwivatIW----TLVEPWTAGCTV 69
Cdd:cd17640 93 IIYTSGTTGNPKgvMLTHanllhqiRSLSDIVPPQPGDRFLSILP-----------------IWhsyeRSAEYFIFACGC 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 70 FIHhlpqFDT-KVIIQTLLKYPINHFWGV----SSIYRMILQQDFTSIRF-PALEHCY-TGGEVV--------LPKDQEE 134
Cdd:cd17640 156 SQA----YTSiRTLKDDLKRVKPHYIVSVprlwESLYSGIQKQVSKSSPIkQFLFLFFlSGGIFKfgisgggaLPPHVDT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 135 WKRRTGLLLYENYGQSETGLI--CATYWGMKIkpGFMGKATPPYDVQVID-DKGSILPPNTEGNIGIRIKPVrpvslFMC 211
Cdd:cd17640 232 FFEAIGIEVLNGYGLTETSPVvsARRLKCNVR--GSVGRPLPGTEIKIVDpEGNVVLPPGEKGIVWVRGPQV-----MKG 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 212 YEGDPEKTAKVECGD-FYNTGDRGKMDEEGYICFLGRSDDIINAS-GYRIGPAEVESALVEHPAVAESAVVGSPDPIRGe 289
Cdd:cd17640 305 YYKNPEATSKVLDSDgWFNTGDLGWLTCGGELVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIMVVGQDQKRLG- 383
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578828480 290 vvkAFIVltPqflshDKDQLTKELQQhvksvtapykypRKVEFVSELPKTITGKIERKELRKK 352
Cdd:cd17640 384 ---ALIV--P-----NFEELEKWAKE------------SGVKLANDRSQLLASKKVLKLYKNE 424
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
3-349 |
4.64e-13 |
|
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: 69.81 E-value: 4.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 3 IFFTSGTTGFPKMAKHSHGlALQPSFPGSRK-----------LRSLKTSDVSwclsdsgwIVATIWTLvepwTAGCTVFI 71
Cdd:cd17654 123 VIHTSGTTGTPKIVAVPHK-CILPNIQHFRSlfnitsedilfLTSPLTFDPS--------VVEIFLSL----SSGATLLI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 72 ---------HHLPQ-FDTKVIIQTLLKYP--INHFwGVSSIYRMILQQDfTSIRFPALehcytGGEVvLPKDQEEWKRRT 139
Cdd:cd17654 190 vptsvkvlpSKLADiLFKRHRITVLQATPtlFRRF-GSQSIKSTVLSAT-SSLRVLAL-----GGEP-FPSLVILSSWRG 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 140 GLL---LYENYGQSETGlICATYWGMKIKPGFMGKATPPYD--VQVIDDKGSILPPNTEGNIGIRIkpvrpvslfmCYEG 214
Cdd:cd17654 262 KGNrtrIFNIYGITEVS-CWALAYKVPEEDSPVQLGSPLLGtvIEVRDQNGSEGTGQVFLGGLNRV----------CILD 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 215 DPEKTAKvecGDFYNTGDRGKMdEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDpirgEVVKAF 294
Cdd:cd17654 331 DEVTVPK---GTMRATGDFVTV-KDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQ----QRLIAF 402
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 578828480 295 IVLTPQflshdKDQLTKELQQHVKSvtaPYKYPRKVEFVSELPKTITGKIERKEL 349
Cdd:cd17654 403 IVGESS-----SSRIHKELQLTLLS---SHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
231-344 |
6.23e-13 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 69.82 E-value: 6.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 231 GDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTP-QFLShdkDQL 309
Cdd:PRK03584 503 GDWIEITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLAEgVTLD---DAL 579
|
90 100 110
....*....|....*....|....*....|....*
gi 578828480 310 TKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKI 344
Cdd:PRK03584 580 RARIRTTIRTNLSPRHVPDKIIAVPDIPRTLSGKK 614
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
5-349 |
1.62e-12 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 69.04 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 5 FTSGTTGFPKMAKHSHG------LALQPSFpgsrklrSLKTSDVSWCLSDSGWIVATIWTLVePWTAGCTVFIHHLPQFD 78
Cdd:PRK05691 2340 YTSGSTGKPKGVVVSHGeiamhcQAVIERF-------GMRADDCELHFYSINFDAASERLLV-PLLCGARVVLRAQGQWG 2411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 79 TKVIIQTLLKYPINhFWGVSSIY------RMILQQDFTSIRFpalehCYTGGEVVLPkdqEEWKR-RTGL---LLYENYG 148
Cdd:PRK05691 2412 AEEICQLIREQQVS-ILGFTPSYgsqlaqWLAGQGEQLPVRM-----CITGGEALTG---EHLQRiRQAFapqLFFNAYG 2482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 149 QSETGLI-CATYWGMKIKPGF----MGKATPPYDVQVIDDKGSILPPNTEGNIgirikPVRPVSLFMCYEGDPEKTAK-- 221
Cdd:PRK05691 2483 PTETVVMpLACLAPEQLEEGAasvpIGRVVGARVAYILDADLALVPQGATGEL-----YVGGAGLAQGYHDRPGLTAErf 2557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 222 ------VECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFI 295
Cdd:PRK05691 2558 vadpfaADGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPSGKQLAGYLV 2637
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 578828480 296 VLTPQFLSHDKDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKEL 349
Cdd:PRK05691 2638 SAVAGQDDEAQAALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
228-349 |
1.70e-12 |
|
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: 68.20 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 228 YNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVV------GSPDPIRGEVVkAFIVLTPQF 301
Cdd:cd17648 332 YKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVakedasQAQSRIQKYLV-GYYLPEPGH 410
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 578828480 302 LSHdkdqltKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKEL 349
Cdd:cd17648 411 VPE------SDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
188-352 |
2.30e-12 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 67.84 E-value: 2.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 188 LPPNTEGNIGIRIkPVRPVSLFMCYEGDPEKTAK------VECGD-FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIG 260
Cdd:cd05937 294 APVGEPGEMLGRV-PFKNREAFQGYLHNEDATESklvrdvFRKGDiYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVS 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 261 PAEVESALVEHPAVAESAVVGSPDP-IRGEVVKAFIVLTPQflSHDKDQLTK-ELQQHVKSVTAPYKYPRKVEFVSELPK 338
Cdd:cd05937 373 TTEVADVLGAHPDIAEANVYGVKVPgHDGRAGCAAITLEES--SAVPTEFTKsLLASLARKNLPSYAVPLFLRLTEEVAT 450
|
170
....*....|....
gi 578828480 339 TITGKIERKELRKK 352
Cdd:cd05937 451 TDNHKQQKGVLRDE 464
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
169-352 |
5.42e-11 |
|
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: 63.66 E-value: 5.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 169 MGKATPPYDVQVIDDKGSILPPNTEGNIGIRIKPVRPvslfmCYEGDPEKTAKVECGD-FYNTGDRGKM-DEEGYIcfLG 246
Cdd:cd05908 316 VGKPIDETDIRICDEDNKILPDGYIGHIQIRGKNVTP-----GYYNNPEATAKVFTDDgWLKTGDLGFIrNGRLVI--TG 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 247 RSDDIINASGYRIGPAEVESALVEHPAV--AESAVVGSPDP-IRGEVVKAFIVltpqflsHDKD-----QLTKELQQHVK 318
Cdd:cd05908 389 REKDIIFVNGQNVYPHDIERIAEELEGVelGRVVACGVNNSnTRNEEIFCFIE-------HRKSeddfyPLGKKIKKHLN 461
|
170 180 190
....*....|....*....|....*....|....
gi 578828480 319 SVTApyKYPRKVEFVSELPKTITGKIERKELRKK 352
Cdd:cd05908 462 KRGG--WQINEVLPIRRIPKTTSGKVKRYELAQR 493
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
169-346 |
4.37e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 60.78 E-value: 4.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 169 MGKATPPYDVQVIDDKGSILPPNTEGNIGIRIKPVRPVSLFMcyegDPEKTAKVECGdFYNTGDRGKMDEEGYICFLGRS 248
Cdd:PRK07768 362 LGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGYLTM----DGFIPAQDADG-WLDTGDLGYLTEEGEVVVCGRV 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 249 DDIINASGYRIGPAEVESALVEHPAV-AESAV-VGSPDPIRGEvvkAFIVLTPQFLSHDKDQLTKELQQHVKSVTAPYKY 326
Cdd:PRK07768 437 KDVIIMAGRNIYPTDIERAAARVEGVrPGNAVaVRLDAGHSRE---GFAVAVESNAFEDPAEVRRIRHQVAHEVVAEVGV 513
|
170 180
....*....|....*....|...
gi 578828480 327 -PRKVEFVS--ELPKTITGKIER 346
Cdd:PRK07768 514 rPRNVVVLGpgSIPKTPSGKLRR 536
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
170-351 |
1.03e-09 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 59.63 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 170 GKATPPYDVQVIDDKGSILPPNTEGNIGIRiKPvrpvSLFMCYEGDPEKTAKVECGDFYNTGDRGKMdEEGYICFLGRSD 249
Cdd:PRK09192 388 GKALPGHEIEIRNEAGMPLPERVVGHICVR-GP----SLMSGYFRDEESQDVLAADGWLDTGDLGYL-LDGYLYITGRAK 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 250 DIINASGYRIGPAEVESALVEHPAV--AESAVVGSPDPIRGEVVkafiVLTPQFLS--HDKDQLTKELQQHVKSVTApyk 325
Cdd:PRK09192 462 DLIIINGRNIWPQDIEWIAEQEPELrsGDAAAFSIAQENGEKIV----LLVQCRISdeERRGQLIHALAALVRSEFG--- 534
|
170 180
....*....|....*....|....*...
gi 578828480 326 YPRKVEFVS--ELPKTITGKIERKELRK 351
Cdd:PRK09192 535 VEAAVELVPphSLPRTSSGKLSRAKAKK 562
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
5-351 |
1.35e-09 |
|
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: 59.29 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 5 FTSGTTGFPKMAKHSHGLALQPSFPGSRKLRSLKTSDVSWCLS---DSGWIVATIWTLVepwtAGCTVFIHHlpQFDTKV 81
Cdd:cd05940 88 YTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSDVLYTCLPlyhSTALIVGWSACLA----SGATLVIRK--KFSASN 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 82 IIQTLLKYPINHFWGVSSIYRMILQQdftsirfPALE----HCYTG--GEVVLPKDQEEWKRRTGLL-LYENYGQSEtGL 154
Cdd:cd05940 162 FWDDIRKYQATIFQYIGELCRYLLNQ-------PPKPterkHKVRMifGNGLRPDIWEEFKERFGVPrIAEFYAATE-GN 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 155 IcaTYWGMKIKPGFMGKATP------PYD-VQVIDDKGSILPPNT-------EGNIGIRIKPVRPVSLFMCYEGDPEKTA 220
Cdd:cd05940 234 S--GFINFFGKPGAIGRNPSllrkvaPLAlVKYDLESGEPIRDAEgrcikvpRGEPGLLISRINPLEPFDGYTDPAATEK 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 221 KV-----ECGD-FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDP-IRGEVVKA 293
Cdd:cd05940 312 KIlrdvfKKGDaWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPgTDGRAGMA 391
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 578828480 294 FIVLTPqflSHDKDqlTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRK 351
Cdd:cd05940 392 AIVLQP---NEEFD--LSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRN 444
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
231-354 |
3.09e-09 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 58.29 E-value: 3.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 231 GDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVE-HPAVAESAVVGSPDPIRGE----VVKAFIVLTPQFLSHD 305
Cdd:PLN03051 362 GDIMKRTPGGYFCVQGRADDTMNLGGIKTSSVEIERACDRaVAGIAETAAVGVAPPDGGPellvIFLVLGEEKKGFDQAR 441
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 578828480 306 KDQLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELR---KKET 354
Cdd:PLN03051 442 PEALQKKFQEAIQTNLNPLFKVSRVKIVPELPRNASNKLLRRVLRdqlKKEL 493
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
5-343 |
4.07e-09 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 57.69 E-value: 4.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 5 FTSGTTGFPKMAKHSHGLALQPSFPGSrkLRSLKTSDVSW-CLS---DSGWIV---------ATIwTLVEPWTAGCtvFI 71
Cdd:cd05938 151 YTSGTTGLPKAARISHLRVLQCSGFLS--LCGVTADDVIYiTLPlyhSSGFLLgiggcielgATC-VLKPKFSASQ--FW 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 72 HHLPQFDTKVI--IQTLLKYPINhfwgvssiyrmILQQDFT---SIRFPAlehcytgGEVVLPKDQEEWKRRTG-LLLYE 145
Cdd:cd05938 226 DDCRKHNVTVIqyIGELLRYLCN-----------QPQSPNDrdhKVRLAI-------GNGLRADVWREFLRRFGpIRIRE 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 146 NYGQSETGLICATYWGmkiKPGFMGKA-------TP----PYDVQ----VIDDKGSILPPNTeGNIGIRIKPVRPVSLFM 210
Cdd:cd05938 288 FYGSTEGNIGFFNYTG---KIGAVGRVsylykllFPfeliKFDVEkeepVRDAQGFCIPVAK-GEPGLLVAKITQQSPFL 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 211 CYEGDPEKTAK------VECGD-FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSP 283
Cdd:cd05938 364 GYAGDKEQTEKkllrdvFKKGDvYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVT 443
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578828480 284 DP-IRGEVVKAFIVLTPqflSHDKDQltKELQQHVKSVTAPYKYPRKVEFVSELPKTITGK 343
Cdd:cd05938 444 VPgHEGRIGMAAVKLKP---GHEFDG--KKLYQHVREYLPAYARPRFLRIQDSLEITGTFK 499
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
203-351 |
7.49e-09 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 57.08 E-value: 7.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 203 VRPVSLFMCYEGDpektAKVECGDFYNTGDRGKM-DEEGYICflGRSDDIINASGYRIGPAEVESALVEHPAVAESAVV- 280
Cdd:PRK05851 377 IRGASMMSGYLGQ----APIDPDDWFPTGDLGYLvDGGLVVC--GRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVa 450
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578828480 281 -GSPDpirgEVVKAFIVLTPQFLSHDKDQLTKELQQHVKSVTApyKYPRKVEFVS--ELPKTITGKIERKELRK 351
Cdd:PRK05851 451 vGTGE----GSARPGLVIAAEFRGPDEAGARSEVVQRVASECG--VVPSDVVFVApgSLPRTSSGKLRRLAVKR 518
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
170-316 |
1.19e-08 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 56.45 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 170 GKATPPYDVQVID---------DKGSILPPnteGNIG-IRIK-PVrpVSlfMCYEGDPEKT--AKVE--CGDFYN-TGDR 233
Cdd:PRK09274 355 GRPVDGVEVRIIAisdapipewDDALRLAT---GEIGeIVVAgPM--VT--RSYYNRPEATrlAKIPdgQGDVWHrMGDL 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 234 GKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPirGEVVKAFIVLTPQFLSHDKDQLTKEL 313
Cdd:PRK09274 428 GYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGVGVP--GAQRPVLCVELEPGVACSKSALYQEL 505
|
...
gi 578828480 314 QQH 316
Cdd:PRK09274 506 RAL 508
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
169-351 |
2.60e-08 |
|
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: 55.32 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 169 MGKATPPYDVQVIDDKGSI-LPPNTEGNIGIRIKPVRPvslfmCYEGDPEKTAKVEC-------GDFYNTGDRGKM-DEE 239
Cdd:cd05931 357 CGRPLPDQEVRIVDPETGReLPDGEVGEIWVRGPSVAS-----GYWGRPEATAETFGalaatdeGGWLRTGDLGFLhDGE 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 240 GYICflGRSDDIINASGYRIGPAEVESALVE-HPAVAES--AVVGSPDPIRGEVVkAFIVLTPQFLSHDKDQLTKELQQH 316
Cdd:cd05931 432 LYIT--GRLKDLIIVRGRNHYPQDIEATAEEaHPALRPGcvAAFSVPDDGEERLV-VVAEVERGADPADLAAIAAAIRAA 508
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 578828480 317 VKS---VTapykyPRKVEFVS--ELPKTITGKIERKELRK 351
Cdd:cd05931 509 VARehgVA-----PADVVLVRpgSIPRTSSGKIQRRACRA 543
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
5-351 |
9.25e-08 |
|
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: 53.58 E-value: 9.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 5 FTSGTTGFPKMA--KHSHGLALQPsfpGSRKLRSLKTSDVSW-CLsdsgwivatiwtlvePW--TAGCTVFIHHLPQFDT 79
Cdd:cd05939 111 YTSGTTGLPKAAviVHSRYYRIAA---GAYYAFGMRPEDVVYdCL---------------PLyhSAGGIMGVGQALLHGS 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 80 KVIIQTllKYPINHFWG------------VSSIYRMILQQdftSIRFPALEHC--YTGGEVVLPKDQEEWKRRTGLL-LY 144
Cdd:cd05939 173 TVVIRK--KFSASNFWDdcvkynctivqyIGEICRYLLAQ---PPSEEEQKHNvrLAVGNGLRPQIWEQFVRRFGIPqIG 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 145 ENYGQSETGLICATYWGMKIKPGFMGKATPP-YDVQVI-----------DDKGSILP--PNTEGNIGIRIKPVRPVSLFM 210
Cdd:cd05939 248 EFYGATEGNSSLVNIDNHVGACGFNSRILPSvYPIRLIkvdedtgelirDSDGLCIPcqPGEPGLLVGKIIQNDPLRRFD 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 211 CY--EGDPEKtaKV-----ECGD-FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGS 282
Cdd:cd05939 328 GYvnEGATNK--KIardvfKKGDsAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGV 405
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 283 PDP-IRGEVVKAFIVLTPQFLshDKDQLTKELQqhvkSVTAPYKYPRKVEFVSELPKTITGKIERKELRK 351
Cdd:cd05939 406 EVPgVEGRAGMAAIVDPERKV--DLDRFSAVLA----KSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQK 469
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
101-281 |
8.83e-07 |
|
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: 50.43 E-value: 8.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 101 YRMILQQDFTSIR-FPALEHC---YTGGeVVLPKDQEEWKRRTGLLLYENYGQSET-GL--ICATYwgmKIKPGFMGKAT 173
Cdd:cd05933 302 YRLAKKLVFKKVRkALGLDRCqkfFTGA-APISRETLEFFLSLNIPIMELYGMSETsGPhtISNPQ---AYRLLSCGKAL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 174 PPYDVQVI--DDKGSilppnteGNIGIRIKPVrpvslFMCYEGDPEKTA-KVECGDFYNTGDRGKMDEEGYICFLGRSDD 250
Cdd:cd05933 378 PGCKTKIHnpDADGI-------GEICFWGRHV-----FMGYLNMEDKTEeAIDEDGWLHSGDLGKLDEDGFLYITGRIKE 445
|
170 180 190
....*....|....*....|....*....|...
gi 578828480 251 -IINASGYRIGPAEVESAL-VEHPAVAESAVVG 281
Cdd:cd05933 446 lIITAGGENVPPVPIEDAVkKELPIISNAMLIG 478
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1-281 |
2.13e-06 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 49.38 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 1 MVIFFTSGTTGFPKMAKHSHGL------ALQPSF---PGSRKLRSLKTsdvsWCLSDSGWIVATIWTLVEPwTAGCTVfi 71
Cdd:cd05910 88 AAILFTSGSTGTPKGVVYRHGTfaaqidALRQLYgirPGEVDLATFPL----FALFGPALGLTSVIPDMDP-TRPARA-- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 72 hhlpqfDTKVIIQTLLKYPINHFWGVSSIYRMI----LQQDftsIRFPALEHCYTGGEVVLPKDQEEWKR--RTGLLLYE 145
Cdd:cd05910 161 ------DPQKLVGAIRQYGVSIVFGSPALLERVarycAQHG---ITLPSLRRVLSAGAPVPIALAARLRKmlSDEAEILT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 146 NYGQSETGLICA----------TYWGMKIKPGFMGKATPPYDVQVID-DKGSI--------LPPNTEGNIGIRIKPVRPV 206
Cdd:cd05910 232 PYGATEALPVSSigsrellattTAATSGGAGTCVGRPIPGVRVRIIEiDDEPIaewddtleLPRGEIGEITVTGPTVTPT 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 207 slfmcYEGDPEKTA--KVECGD---FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVG 281
Cdd:cd05910 312 -----YVNRPVATAlaKIDDNSegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVG 386
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
240-352 |
7.53e-06 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 47.77 E-value: 7.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 240 GYICFLGRSDDIINASGYRIGPAEVE----SAlveHPAVAESAVVGSPDPIRG--EVVKAFIVLTPQFLSHDKDQLTKEL 313
Cdd:PLN03052 603 GYYRAHGRADDTMNLGGIKVSSVEIErvcnAA---DESVLETAAIGVPPPGGGpeQLVIAAVLKDPPGSNPDLNELKKIF 679
|
90 100 110
....*....|....*....|....*....|....*....
gi 578828480 314 QQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRKK 352
Cdd:PLN03052 680 NSAIQKKLNPLFKVSAVVIVPSFPRTASNKVMRRVLRQQ 718
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
214-349 |
1.50e-05 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 46.74 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 214 GDPEKTAKVECGD-FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGSPDPIRGEVVK 292
Cdd:cd17647 359 NEPWRQFWLGPRDrLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLV 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 293 AFIVltPQFLSHDKD------------------------QLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKE 348
Cdd:cd17647 439 SYIV--PRFDKPDDEsfaqedvpkevstdpivkgligyrKLIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPK 516
|
.
gi 578828480 349 L 349
Cdd:cd17647 517 L 517
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
114-351 |
2.11e-05 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 46.24 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 114 FPALEHCYTGGEVVLPKDQEEWKRRTGLLLYENYGQSETGLICATYWGMKIKPGFMGKATPPYD-----VQVIDDKG--S 186
Cdd:PRK08043 478 FARLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDarllsVPGIEQGGrlQ 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 187 ILPPNTEgNIGIRIKpvRPVSLFMCYEGDPEktAKVECGdFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVES 266
Cdd:PRK08043 558 LKGPNIM-NGYLRVE--KPGVLEVPTAENAR--GEMERG-WYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQ 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 267 ALVEHPAVAESAVVGSPDPIRGEvvkAFIVLTPqflshDKdQLTKE-LQQHVKSVTAP-YKYPRKVEFVSELPKTITGKI 344
Cdd:PRK08043 632 LALGVSPDKQHATAIKSDASKGE---ALVLFTT-----DS-ELTREkLQQYAREHGVPeLAVPRDIRYLKQLPLLGSGKP 702
|
....*..
gi 578828480 345 ERKELRK 351
Cdd:PRK08043 703 DFVTLKS 709
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
212-351 |
2.91e-05 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 46.02 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 212 YEG--DPEKTAKV------ECGD-FYNTGDRGKMDEEGYICFLGRSDDIINASGYRIGPAEVESALVEHPAVAESAVVGS 282
Cdd:PRK08279 416 FDGytDPEASEKKilrdvfKKGDaWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVYGV 495
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578828480 283 PDP-IRGEVVKAFIVLtpqflsHDKDQLT-KELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIERKELRK 351
Cdd:PRK08279 496 EVPgTDGRAGMAAIVL------ADGAEFDlAALAAHLYERLPAYAVPLFVRLVPELETTGTFKYRKVDLRK 560
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
140-357 |
4.33e-05 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 45.28 E-value: 4.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 140 GLLLYENYGQSETGLICATYWGMKIKPGFMGKATPPYDVQVID--DKG-SILPPNTEGNIGIRIKpvrpvSLFMCYEGDP 216
Cdd:cd05927 299 GCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDvpEMNyDAKDPNPRGEVCIRGP-----NVFSGYYKDP 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 217 EKTAKVECGD-FYNTGDRGKMDEEGYICFLGRSDDIIN-ASGYRIGPAEVESALVEHPAVAESAVVGspDPIRGEVVkAF 294
Cdd:cd05927 374 EKTAEALDEDgWLHTGDIGEWLPNGTLKIIDRKKNIFKlSQGEYVAPEKIENIYARSPFVAQIFVYG--DSLKSFLV-AI 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578828480 295 IVLTPQFL----------SHDKDQLTK--ELQQHV---------KSVTAPYKYPRKVEFVSELPK------TITGKIERK 347
Cdd:cd05927 451 VVPDPDVLkewaaskgggTGSFEELCKnpEVKKAIledlvrlgkENGLKGFEQVKAIHLEPEPFSvengllTPTFKLKRP 530
|
250
....*....|
gi 578828480 348 ELRKKETGQM 357
Cdd:cd05927 531 QLKKYYKKQI 540
|
|
| |
