|
Name |
Accession |
Description |
Interval |
E-value |
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
9-423 |
1.47e-155 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 446.13 E-value: 1.47e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 9 PSERLRGAQLDAVRHLLARVLTGNEFYRRKLGA--LAPASLRTFDDFVQLPFTTKAELIADQlerpPYGtNLSFPLDRYT 86
Cdd:COG1541 12 SREELEALQLERLRATVARAYENSPFYRRKFDEagVDPDDIKSLEDLAKLPFTTKEDLRDNY----PFG-LFAVPLEEIV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 87 RFHQTSGTTsGRPLHWLDTSETWDWLTGCWATNFALIGLRPTDRLFFPFSFGPFLGFWTAFEAAARCGFLVMPGGGLSST 166
Cdd:COG1541 87 RIHASSGTT-GKPTVVGYTRKDLDRWAELFARSLRAAGVRPGDRVQNAFGYGLFTGGLGLHYGAERLGATVIPAGGGNTE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 167 ARLRFLLDHRCTVLFATPTYALHLAEIASKEGIDLASSAVRALVVAGEPGGniPGTRQRLEAVWGARVFDHYGMTEIGP- 245
Cdd:COG1541 166 RQLRLMQDFGPTVLVGTPSYLLYLAEVAEEEGIDPRDLSLKKGIFGGEPWS--EEMRKEIEERWGIKAYDIYGLTEVGPg 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 246 VAVEAEGRPGeLYLLESDYLAEVVDPQTGRPVPDGDTGELVLTNLGRTGSPLIRYRTGDLIRMAPAPDPTGRTWRRLeGG 325
Cdd:COG1541 244 VAYECEAQDG-LHIWEDHFLVEIIDPETGEPVPEGEEGELVVTTLTKEAMPLIRYRTGDLTRLLPEPCPCGRTHPRI-GR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 326 VLGRADDMIHVRGNNVYPGALESIIRRFADVA-EYRIHVDRRNPLADLRLEIEPVAG-DGHALAEEVGRAVRDALCFRID 403
Cdd:COG1541 322 ILGRADDMLIIRGVNVFPSQIEEVLLRIPEVGpEYQIVVDREGGLDELTVRVELAPGaSLEALAEAIAAALKAVLGLRAE 401
|
410 420
....*....|....*....|
gi 497728519 404 VSAAPPGSLPRFEMKARRVV 423
Cdd:COG1541 402 VELVEPGSLPRSEGKAKRVI 421
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
9-423 |
1.09e-118 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 352.31 E-value: 1.09e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 9 PSERLRGAQLDAVRHLLARVLTGNEFYRRKLGA--LAPASLRTFDDFVQLPFTTKAELIADQlerpPYGTnLSFPLDRYT 86
Cdd:cd05913 7 SRDELDALQLARLKWTVRHAYENVPFYRRKFAAagIDPDDIKSLDDLRKLPFTTKEDLRDNY----PFGL-FAVPREKVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 87 RFHQTSGTTsGRPLHWLDTSETWDWLTGCWATNFALIGLRPTDRLFFPFSFGPFLGFWTAFEAAARCGFLVMPGGGLSST 166
Cdd:cd05913 82 RIHASSGTT-GKPTVVGYTKNDLDVWAELVARCLDAAGVTPGDRVQNAYGYGLFTGGLGFHYGAERLGALVIPAGGGNTE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 167 ARLRFLLDHRCTVLFATPTYALHLAEIASKEGIDLASSAVRALVVAGEPGGNIPgtRQRLEAVWGARVFDHYGMTEI-GP 245
Cdd:cd05913 161 RQLQLIKDFGPTVLCCTPSYALYLAEEAEEEGIDPRELSLKVGIFGAEPWTEEM--RKRIERRLGIKAYDIYGLTEIiGP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 246 -VAVEAEGRpGELYLLESDYLAEVVDPQTGRPVPDGDTGELVLTNLGRTGSPLIRYRTGDLIRMAPAPDPTGRTWRRLEg 324
Cdd:cd05913 239 gVAFECEEK-DGLHIWEDHFIPEIIDPETGEPVPPGEVGELVFTTLTKEAMPLIRYRTRDITRLLPGPCPCGRTHRRID- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 325 GVLGRADDMIHVRGNNVYPGALESIIRRFADV-AEYRIHVDRRNPLADLRLEIE--PVAGDGH---ALAEEVGRAVRDAL 398
Cdd:cd05913 317 RITGRSDDMLIIRGVNVFPSQIEDVLLKIPGLgPHYQLILTRQEHLDELTIKVEvrPEADDDEkleALKQRLERHIKSVL 396
|
410 420
....*....|....*....|....*
gi 497728519 399 CFRIDVSAAPPGSLPRFEMKARRVV 423
Cdd:cd05913 397 GVTVEVELVEPGSLPRSEGKAKRVI 421
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
91-358 |
2.81e-29 |
|
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: 118.76 E-value: 2.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 91 TSGTTsGRP---LHwldtseTWDWLTGCWATNFALIGLRPTDRLF--FPFS--FGPFLGFWTAFEAAARcgFLVMPGGGL 163
Cdd:COG0318 108 TSGTT-GRPkgvML------THRNLLANAAAIAAALGLTPGDVVLvaLPLFhvFGLTVGLLAPLLAGAT--LVLLPRFDP 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 164 SSTARLrfLLDHRCTVLFATPTYALHLAEIASKEGIDLasSAVRALVVAGEPggnIP-GTRQRLEAVWGARVFDHYGMTE 242
Cdd:COG0318 179 ERVLEL--IERERVTVLFGVPTMLARLLRHPEFARYDL--SSLRLVVSGGAP---LPpELLERFEERFGVRIVEGYGLTE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 243 IGPVAV-----EAEGRPGELYLLESDYLAEVVDPQtGRPVPDGDTGELV----------LTNLGRTGSPLIR--YRTGDL 305
Cdd:COG0318 252 TSPVVTvnpedPGERRPGSVGRPLPGVEVRIVDED-GRELPPGEVGEIVvrgpnvmkgyWNDPEATAEAFRDgwLRTGDL 330
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 497728519 306 IRMapapDPTGRTWrrleggVLGRADDMIHVRGNNVYPGALESIIRRFADVAE 358
Cdd:COG0318 331 GRL----DEDGYLY------IVGRKKDMIISGGENVYPAEVEEVLAAHPGVAE 373
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
91-358 |
5.02e-28 |
|
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: 113.15 E-value: 5.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 91 TSGTTsGRP---LHwldTSETWDWLtgcWATNFALIGLRPTDRLFFPFSFGPFLGFWTAFEAAARCGFLVMPGGGlSSTA 167
Cdd:cd04433 8 TSGTT-GKPkgvVL---SHRNLLAA---AAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKF-DPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 168 RLRFLLDHRCTVLFATPTYALHLAEIASKEGIDLASsaVRALVVAGEPGGniPGTRQRLEAVWGARVFDHYGMTEIGPV- 246
Cdd:cd04433 80 ALELIEREKVTILLGVPTLLARLLKAPESAGYDLSS--LRALVSGGAPLP--PELLERFEEAPGIKLVNGYGLTETGGTv 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 247 ----AVEAEGRPGELYLLESDYLAEVVDPQtGRPVPDGDTGELVLTN----LGRTGSPLIR--------YRTGDLIRMap 310
Cdd:cd04433 156 atgpPDDDARKPGSVGRPVPGVEVRIVDPD-GGELPPGEIGELVVRGpsvmKGYWNNPEATaavdedgwYRTGDLGRL-- 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 497728519 311 apDPTGRTWrrleggVLGRADDMIHVRGNNVYPGALESIIRRFADVAE 358
Cdd:cd04433 233 --DEDGYLY------IVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAE 272
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
91-337 |
1.12e-23 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 102.01 E-value: 1.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 91 TSGTTsGRP---------LHWLdtsetwdwLTGCWATNFALIGLRPTDRLFFP----FSFGPFLGFWTAFEAAARCGFlV 157
Cdd:pfam00501 163 TSGTT-GKPkgvmlthrnLVAN--------VLSIKRVRPRGFGLGPDDRVLSTlplfHDFGLSLGLLGPLLAGATVVL-P 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 158 MPGGGLSSTARLRFLLDHRCTVLFATPTYALHLAEIASKEGIDLASsaVRALVVAGEPGGniPGTRQRLEAVWGARVFDH 237
Cdd:pfam00501 233 PGFPALDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSS--LRLVLSGGAPLP--PELARRFRELFGGALVNG 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 238 YGMTEIGPVAVEAEGRPGELYLLES------DYLAEVVDPQTGRPVPDGDTGELV----------LTNLGRTGSPLIR-- 299
Cdd:pfam00501 309 YGLTETTGVVTTPLPLDEDLRSLGSvgrplpGTEVKIVDDETGEPVPPGEPGELCvrgpgvmkgyLNDPELTAEAFDEdg 388
|
250 260 270
....*....|....*....|....*....|....*....
gi 497728519 300 -YRTGDLIRMapapDPTGRTWrrleggVLGRADDMIHVR 337
Cdd:pfam00501 389 wYRTGDLGRR----DEDGYLE------IVGRKKDQIKLG 417
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
91-358 |
3.03e-23 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 102.11 E-value: 3.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 91 TSGTTsGRP---LHwlDTSetwdWLTGCWATNFALI-GLRPTDRLFF--PFSFGPFLGFWTAFEAAARCGFLVMPGGGLS 164
Cdd:COG0365 192 TSGTT-GKPkgvVH--THG----GYLVHAATTAKYVlDLKPGDVFWCtaDIGWATGHSYIVYGPLLNGATVVLYEGRPDF 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 165 STAR--LRFLLDHRCTVLFATPTY--ALHLAEIASKEGIDLasSAVRALVVAGEPggnI-PGTRQRLEAVWGARVFDHYG 239
Cdd:COG0365 265 PDPGrlWELIEKYGVTVFFTAPTAirALMKAGDEPLKKYDL--SSLRLLGSAGEP---LnPEVWEWWYEAVGVPIVDGWG 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 240 MTEIG----------PVaveaegRPGEL---YLLesdYLAEVVDPQtGRPVPDGDTGELVLTnLGRTGSPL------IR- 299
Cdd:COG0365 340 QTETGgifisnlpglPV------KPGSMgkpVPG---YDVAVVDED-GNPVPPGEEGELVIK-GPWPGMFRgywndpERy 408
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 300 -----------YRTGDLIRMapapDPTGRTWrrleggVLGRADDMIHVRGNNVYPGALESIIRRFADVAE 358
Cdd:COG0365 409 retyfgrfpgwYRTGDGARR----DEDGYFW------ILGRSDDVINVSGHRIGTAEIESALVSHPAVAE 468
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
91-358 |
1.69e-21 |
|
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: 96.06 E-value: 1.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 91 TSGTTsGRP----------LHWLDtsetWDWltgcwatnfALIGLRPTDRL--FFPFSFGPFLG-FWTAFEAAARCgfLV 157
Cdd:cd05930 101 TSGST-GKPkgvmvehrglVNLLL----WMQ---------EAYPLTPGDRVlqFTSFSFDVSVWeIFGALLAGATL--VV 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 158 MPGGGLSSTARL-RFLLDHRCTVLFATPTYALHLAEiaskEGIDLASSAVRALVVAGEPggnIPGT--RQRLEAVWGARV 234
Cdd:cd05930 165 LPEEVRKDPEALaDLLAEEGITVLHLTPSLLRLLLQ----ELELAALPSLRLVLVGGEA---LPPDlvRRWRELLPGARL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 235 FDHYGMTEIGPVAVEAEGRPGELYLLE-------SDYLAEVVDPQtGRPVPDGDTGELVLT----NLGRTGSP-LIR--- 299
Cdd:cd05930 238 VNLYGPTEATVDATYYRVPPDDEEDGRvpigrpiPNTRVYVLDEN-LRPVPPGVPGELYIGgaglARGYLNRPeLTAerf 316
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 300 -----------YRTGDLIRMapapDPTGRtwrrLEggVLGRADDMIHVRGNNVYPGALESIIRRFADVAE 358
Cdd:cd05930 317 vpnpfgpgermYRTGDLVRW----LPDGN----LE--FLGRIDDQVKIRGYRIELGEIEAALLAHPGVRE 376
|
|
| AMP-binding_C_2 |
pfam14535 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
338-423 |
1.35e-20 |
|
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: 434024 [Multi-domain] Cd Length: 96 Bit Score: 85.99 E-value: 1.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 338 GNNVYPGALESIIRRFADVA-EYRIHVDRRNPLADLRLEIE------PVAGDGHALAEEVGRAVRDALCFRIDVSAAPPG 410
Cdd:pfam14535 1 GVNVFPSQIEEVLLEIPGVGpEYQIIVTREGGLDELEVKVEvaegfsDEIKDLEALEKRIAKELKSVLGVSVKVELVEPG 80
|
90
....*....|...
gi 497728519 411 SLPRFEMKARRVV 423
Cdd:pfam14535 81 TLPRSEGKAKRVI 93
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
9-358 |
3.32e-18 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 85.78 E-value: 3.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 9 PSERLRgAQLDAVRhlLARVLTGNEFYRRKLGALAPASLRTFDDFVQLPfttkAELIADQLERPPYGTNLSfpldrYTRF 88
Cdd:TIGR01733 60 PAERLA-FILEDAG--ARLLLTDSALASRLAGLVLPVILLDPLELAALD----DAPAPPPPDAPSGPDDLA-----YVIY 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 89 hqTSGTTsGRP-----LHwLDTSETWDWLTGCWatnfaliGLRPTDRL--FFPFSFGPFLG--FWTAFEAAARCgfLVMP 159
Cdd:TIGR01733 128 --TSGST-GRPkgvvvTH-RSLVNLLAWLARRY-------GLDPDDRVlqFASLSFDASVEeiFGALLAGATLV--VPPE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 160 GGGLSSTARLRFLLDHR-CTVLFATPTYALHLAEiaskeGIDLASSAVRALVVAGEPGGniPGTRQRLEAVWG-ARVFDH 237
Cdd:TIGR01733 195 DEERDDAALLAALIAEHpVTVLNLTPSLLALLAA-----ALPPALASLRLVILGGEALT--PALVDRWRARGPgARLINL 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 238 YGMTE------IGPVAVEAE--------GRP---GELYLLESDylaevvdpqtGRPVPDGDTGELV-------------- 286
Cdd:TIGR01733 268 YGPTEttvwstATLVDPDDAprespvpiGRPlanTRLYVLDDD----------LRPVPVGVVGELYiggpgvargylnrp 337
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497728519 287 -------LTNLGRTGSPLIRYRTGDLIRMAPApdptgrtwRRLEggVLGRADDMIHVRGNNVYPGALESIIRRFADVAE 358
Cdd:TIGR01733 338 eltaerfVPDPFAGGDGARLYRTGDLVRYLPD--------GNLE--FLGRIDDQVKIRGYRIELGEIEAALLRHPGVRE 406
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
91-358 |
2.08e-16 |
|
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: 80.60 E-value: 2.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 91 TSGTTsGRP---LHWL-DTSETWDwltgCWATNfaLIGLRPTDR------LFFPFSFGPFLGFWTAFEAAarcgFLVMPG 160
Cdd:cd05958 105 TSGTT-GAPkatMHFHrDPLASAD----RYAVN--VLRLREDDRfvgsppLAFTFGLGGVLLFPFGVGAS----GVLLEE 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 161 gglsSTARLRFLL--DHRCTVLFATPTYALHLAEIASKEGIDLasSAVRALVVAGE--PggniPGTRQRLEAVWGARVFD 236
Cdd:cd05958 174 ----ATPDLLLSAiaRYKPTVLFTAPTAYRAMLAHPDAAGPDL--SSLRKCVSAGEalP----AALHRAWKEATGIPIID 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 237 HYGMTE---IGPVAVEAEGRPGELYLLESDYLAEVVDpQTGRPVPDGDTGELVLTnlGRTGSpliRYR------------ 301
Cdd:cd05958 244 GIGSTEmfhIFISARPGDARPGATGKPVPGYEAKVVD-DEGNPVPDGTIGRLAVR--GPTGC---RYLadkrqrtyvqgg 317
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 302 ---TGDLIRMapapDPTGRTWRRleggvlGRADDMIHVRGNNVYPGALESIIRRFADVAE 358
Cdd:cd05958 318 wniTGDTYSR----DPDGYFRHQ------GRSDDMIVSGGYNIAPPEVEDVLLQHPAVAE 367
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
91-398 |
3.17e-16 |
|
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: 80.47 E-value: 3.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 91 TSGTTsGRPLHWLDTSETWDWLTGcWATnfALIGLRPTDR--LFFPFSFGPFlgFWTAFEAAARCGFLVMPGG--GLSST 166
Cdd:cd17651 144 TSGST-GRPKGVVMPHRSLANLVA-WQA--RASSLGPGARtlQFAGLGFDVS--VQEIFSTLCAGATLVLPPEevRTDPP 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 167 ARLRFLLDHRCTVLFAtPTYALH-LAEIASKEGIDLAssAVRALVVAGEPGGNIPGTRQRLEAVWGARVFDHYGMTE--- 242
Cdd:cd17651 218 ALAAWLDEQRISRVFL-PTVALRaLAEHGRPLGVRLA--ALRYLLTGGEQLVLTEDLREFCAGLPGLRLHNHYGPTEthv 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 243 ----------IGPVAVEAEGRP---GELYLLESDylaevvdpqtGRPVPDGDTGELVLTN-------LGRTG-------- 294
Cdd:cd17651 295 vtalslpgdpAAWPAPPPIGRPidnTRVYVLDAA----------LRPVPPGVPGELYIGGaglargyLNRPEltaerfvp 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 295 ---SPLIR-YRTGDLIRMAPAPdptgrtwrRLEggVLGRADDMIHVRGNNVYPGALESIIRRFADVAEYRIhVDRRNPLA 370
Cdd:cd17651 365 dpfVPGARmYRTGDLARWLPDG--------ELE--FLGRADDQVKIRGFRIELGEIEAALARHPGVREAVV-LAREDRPG 433
|
330 340
....*....|....*....|....*....
gi 497728519 371 DLRLEIEPVAGDGHAL-AEEVGRAVRDAL 398
Cdd:cd17651 434 EKRLVAYVVGDPEAPVdAAELRAALATHL 462
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
91-398 |
4.83e-16 |
|
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: 79.43 E-value: 4.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 91 TSGTTsGRPLHWLDTSETWDWLTGCWATNfaLIGLRPTDR------LFFPFSFGPFLGFWTAFEAAArcgfLVMPGGgLS 164
Cdd:cd05919 99 SSGTT-GPPKGVMHAHRDPLLFADAMARE--ALGLTPGDRvfssakMFFGYGLGNSLWFPLAVGASA----VLNPGW-PT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 165 STARLRFLLDHRCTVLFATPTyaLHLAEIASKEGIDLASSAVRALVVAGEPggnIP-GTRQRLEAVWGARVFDHYGMTEI 243
Cdd:cd05919 171 AERVLATLARFRPTVLYGVPT--FYANLLDSCAGSPDALRSLRLCVSAGEA---LPrGLGERWMEHFGGPILDGIGATEV 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 244 GPVAVEA---EGRPGELYLLESDYLAEVVDPQtGRPVPDGDTGELVLTNLG-------RTGSPLIR-----YRTGDLIRM 308
Cdd:cd05919 246 GHIFLSNrpgAWRLGSTGRPVPGYEIRLVDEE-GHTIPPGEEGDLLVRGPSaavgywnNPEKSRATfnggwYRTGDKFCR 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 309 apapDPTGRTWRRleggvlGRADDMIHVRGNNVYPGALESIIRRFADVAEYR-IHVDRRNPLADLRLEI--EPVAGDGHA 385
Cdd:cd05919 325 ----DADGWYTHA------GRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAvVAVPESTGLSRLTAFVvlKSPAAPQES 394
|
330
....*....|...
gi 497728519 386 LAEEVGRAVRDAL 398
Cdd:cd05919 395 LARDIHRHLLERL 407
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
11-358 |
1.73e-15 |
|
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: 78.04 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 11 ERLRGAQLDAVRHLLARVLTGNEFYR-RKLGALAPASLRTFDD----------FVQLPFTTKAELIADQLERppygTNLS 79
Cdd:cd17631 19 RSLTYAELDERVNRLAHALRALGVAKgDRVAVLSKNSPEFLELlfaaarlgavFVPLNFRLTPPEVAYILAD----SGAK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 80 FPLDRYTRFHQTSGTTsGRPLHWLDTSETWDWLTgcwATNFALIGLRPTDRLF--FPFSFGPFLGFWTAFeAAARCGFLV 157
Cdd:cd17631 95 VLFDDLALLMYTSGTT-GRPKGAMLTHRNLLWNA---VNALAALDLGPDDVLLvvAPLFHIGGLGVFTLP-TLLRGGTVV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 158 MPGGgLSSTARLRFLLDHRCTVLFATPTYALHLAEIASKEGIDLASsaVRALVVAGEPggnipgTRQRLEAVW---GARV 234
Cdd:cd17631 170 ILRK-FDPETVLDLIERHRVTSFFLVPTMIQALLQHPRFATTDLSS--LRAVIYGGAP------MPERLLRALqarGVKF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 235 FDHYGMTEIGPVAV--EAE---------GRPgelyLLESDYlaEVVDPQtGRPVPDGDTGELVLTNLGRTGSPLIR---- 299
Cdd:cd17631 241 VQGYGMTETSPGVTflSPEdhrrklgsaGRP----VFFVEV--RIVDPD-GREVPPGEVGEIVVRGPHVMAGYWNRpeat 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497728519 300 --------YRTGDLIRMapapDPTGRTWrrleggVLGRADDMIHVRGNNVYPGALESIIRRFADVAE 358
Cdd:cd17631 314 aaafrdgwFHTGDLGRL----DEDGYLY------IVDRKKDMIISGGENVYPAEVEDVLYEHPAVAE 370
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
91-358 |
1.32e-14 |
|
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: 75.07 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 91 TSGTTsGRP---LHwldtseTWDWLTGCWATNFALIGLRPTDRLFFPFSFGPFLGFWTAFEA--AARCGFLVMPGGGLSS 165
Cdd:cd05972 89 TSGTT-GLPkgvLH------THSYPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGpwLLGATVFVYEGPRFDA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 166 TARLRFLLDHRCTVLFATPT-YALHLAEiaskegiDLAS---SAVRALVVAGEPGGniPGTRQRLEAVWGARVFDHYGMT 241
Cdd:cd05972 162 ERILELLERYGVTSFCGPPTaYRMLIKQ-------DLSSykfSHLRLVVSAGEPLN--PEVIEWWRAATGLPIRDGYGQT 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 242 EIG-PVAV--EAEGRPGELYLLESDYLAEVVDpQTGRPVPDGDTGELVLTN------LGRTGSPL-----IR---YRTGD 304
Cdd:cd05972 233 ETGlTVGNfpDMPVKPGSMGRPTPGYDVAIID-DDGRELPPGEEGDIAIKLpppglfLGYVGDPEkteasIRgdyYLTGD 311
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 497728519 305 LIRMapapDPTGRTWrrleggVLGRADDMIHVRGNNVYPGALESIIRRFADVAE 358
Cdd:cd05972 312 RAYR----DEDGYFW------FVGRADDIIKSSGYRIGPFEVESALLEHPAVAE 355
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
91-358 |
8.58e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 72.91 E-value: 8.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 91 TSGTTsGRP-----------LHwLDTSETWdwltgcwatnfalIGLRPTDR------LFFPFSFG-PFLgfwtAFEAAAR 152
Cdd:PRK06187 175 TSGTT-GHPkgvvlshrnlfLH-SLAVCAW-------------LKLSRDDVylvivpMFHVHAWGlPYL----ALMAGAK 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 153 cgfLVMPGGGLSSTArLRFLLDHRCTVLFATPT--YALHLAEIAskEGIDLASsaVRALVVAGEPggnIP-GTRQRLEAV 229
Cdd:PRK06187 236 ---QVIPRRFDPENL-LDLIETERVTFFFAVPTiwQMLLKAPRA--YFVDFSS--LRLVIYGGAA---LPpALLREFKEK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 230 WGARVFDHYGMTEIGPVAV---EAEGRPGELYLLES------DYLAEVVDPQtGRPVP--DGDTGELVLT---------N 289
Cdd:PRK06187 305 FGIDLVQGYGMTETSPVVSvlpPEDQLPGQWTKRRSagrplpGVEARIVDDD-GDELPpdGGEVGEIIVRgpwlmqgywN 383
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497728519 290 LGRTGSPLIR---YRTGDLIRMapapDPTGRTWrrleggVLGRADDMIHVRGNNVYPGALESIIRRFADVAE 358
Cdd:PRK06187 384 RPEATAETIDggwLHTGDVGYI----DEDGYLY------ITDRIKDVIISGGENIYPRELEDALYGHPAVAE 445
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
124-358 |
3.31e-13 |
|
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: 70.86 E-value: 3.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 124 GLRPTDRL--FFPFSFGPFLGFWTAFEAAARCgfLVMPGGGLSSTAR--LRFLLDHRCTVLFATPTYALHLAEIASKEGI 199
Cdd:cd17649 131 GLTPGDRElqFASFNFDGAHEQLLPPLICGAC--VVLRPDELWASADelAEMVRELGVTVLDLPPAYLQQLAEEADRTGD 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 200 DLASSaVRALVVAGEPggnIPGTRQRLEAVWGARVFDHYGMTEIGPVAVEAEGRPGELYLLES--------DYLAEVVDP 271
Cdd:cd17649 209 GRPPS-LRLYIFGGEA---LSPELLRRWLKAPVRLFNAYGPTEATVTPLVWKCEAGAARAGASmpigrplgGRSAYILDA 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 272 QtGRPVPDGDTGELVLTN-------LGRT------------GSPLIR-YRTGDLIRmapapdptgrtwRRLEGGV--LGR 329
Cdd:cd17649 285 D-LNPVPVGVTGELYIGGeglargyLGRPeltaerfvpdpfGAPGSRlYRTGDLAR------------WRDDGVIeyLGR 351
|
250 260
....*....|....*....|....*....
gi 497728519 330 ADDMIHVRGNNVYPGALESIIRRFADVAE 358
Cdd:cd17649 352 VDHQVKIRGFRIELGEIEAALLEHPGVRE 380
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
91-358 |
7.30e-13 |
|
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: 70.09 E-value: 7.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 91 TSGTTsGRPLHWLDTSETWDWLTGCWATNfaLIGLRPTDR------LFFPFSFGPFLGFWTAFEAAArcgfLVMPGgglS 164
Cdd:cd05959 171 SSGST-GRPKGVVHLHADIYWTAELYARN--VLGIREDDVcfsaakLFFAYGLGNSLTFPLSVGATT----VLMPE---R 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 165 STARLRF--LLDHRCTVLFATPTyaLHLAEIASKEGIDLASSAVRALVVAGEPggnIPGT-RQRLEAVWGARVFDHYGMT 241
Cdd:cd05959 241 PTPAAVFkrIRRYRPTVFFGVPT--LYAAMLAAPNLPSRDLSSLRLCVSAGEA---LPAEvGERWKARFGLDILDGIGST 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 242 EIGPVAV---EAEGRPGELYLLESDYLAEVVDPqTGRPVPDGDTGELVLtnlgRTGSPLIRY-------RT---GDLIRm 308
Cdd:cd05959 316 EMLHIFLsnrPGRVRYGTTGKPVPGYEVELRDE-DGGDVADGEPGELYV----RGPSSATMYwnnrdktRDtfqGEWTR- 389
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 497728519 309 apapdpTGRTWRRLEGGVL---GRADDMIHVRGNNVYPGALESIIRRFADVAE 358
Cdd:cd05959 390 ------TGDKYVRDDDGFYtyaGRADDMLKVSGIWVSPFEVESALVQHPAVLE 436
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
175-358 |
1.32e-12 |
|
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: 69.07 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 175 HRCTVLFATPTyalHL-AEIASKEGIDLASSAVRALVVAGepgGNIP-GTRQRLEAVWGARVFDHYGMTEI------GPV 246
Cdd:cd05923 240 ERVTSLFATPT---HLdALAAAAEFAGLKLSSLRHVTFAG---ATMPdAVLERVNQHLPGEKVNIYGTTEAmnslymRDA 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 247 AVEAEGRPGelyllesdYLAEV-VDPQTGRPV---PDGDTGELVLTNLGR------------TGSPLI--RYRTGDLIRM 308
Cdd:cd05923 314 RTGTEMRPG--------FFSEVrIVRIGGSPDealANGEEGELIVAAAADaaftgylnqpeaTAKKLQdgWYRTGDVGYV 385
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 497728519 309 apapDPTGRTWrrleggVLGRADDMIHVRGNNVYPGALESIIRRFADVAE 358
Cdd:cd05923 386 ----DPSGDVR------ILGRVDDMIISGGENIHPSEIERVLSRHPGVTE 425
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
123-409 |
1.38e-12 |
|
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: 69.89 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 123 IGLRPTDR--LFFPFSFGPFLG-FWTAFEAAARCgfLVMPGGGLSSTARL-RFLLDHRCTVLFATPTYALHLAEIASKeg 198
Cdd:COG1020 653 YGLGPGDRvlQFASLSFDASVWeIFGALLSGATL--VLAPPEARRDPAALaELLARHRVTVLNLTPSLLRALLDAAPE-- 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 199 idlASSAVRALVVAGEPggnIPGTRQR--LEAVWGARVFDHYGMTE---------IGPVAVEAE----GRP---GELYll 260
Cdd:COG1020 729 ---ALPSLRLVLVGGEA---LPPELVRrwRARLPGARLVNLYGPTEttvdstyyeVTPPDADGGsvpiGRPianTRVY-- 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 261 esdylaeVVDPQtGRPVPDGDTGELV---------------LTN-------LGRTGSPLirYRTGDLIRmapapdptgrt 318
Cdd:COG1020 801 -------VLDAH-LQPVPVGVPGELYiggaglargylnrpeLTAerfvadpFGFPGARL--YRTGDLAR----------- 859
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 319 wrRLEGGV---LGRADDMIHVRGNNVYPGALESIIRRFADVAEYRIHVdRRNPLADLRLEIEPVAGDGHALAEEVGRAVR 395
Cdd:COG1020 860 --WLPDGNlefLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVA-REDAPGDKRLVAYVVPEAGAAAAAALLRLAL 936
|
330
....*....|....
gi 497728519 396 DALCFRIDVSAAPP 409
Cdd:COG1020 937 ALLLPPYMVPAAVV 950
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
91-358 |
1.95e-12 |
|
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: 68.74 E-value: 1.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 91 TSGTTsGRP-----LH---WLDTSETWDWLTGcwatnfaliGLRPTDRLFFPFSFGPFLGFWTAFEAAARCGFLVMpggg 162
Cdd:cd05936 133 TSGTT-GVPkgamlTHrnlVANALQIKAWLED---------LLEGDDVVLAALPLFHVFGLTVALLLPLALGATIV---- 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 163 LSSTAR----LRFLLDHRCTVLFATPTYALHLAEIASKEGIDLasSAVRALVVAGEPggnIP-GTRQRLEAVWGARVFDH 237
Cdd:cd05936 199 LIPRFRpigvLKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDF--SSLRLCISGGAP---LPvEVAERFEELTGVPIVEG 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 238 YGMTEIGPVA----VEAEGRPGELYLLESDYLAEVVDPQtGRPVPDGDTGELVLT---------NLGRTGSPLIR---YR 301
Cdd:cd05936 274 YGLTETSPVVavnpLDGPRKPGSIGIPLPGTEVKIVDDD-GEELPPGEVGELWVRgpqvmkgywNRPEETAEAFVdgwLR 352
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 497728519 302 TGDLIRMapapDPTGRTWrrleggVLGRADDMIHVRGNNVYPGALESIIRRFADVAE 358
Cdd:cd05936 353 TGDIGYM----DEDGYFF------IVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAE 399
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
123-398 |
2.16e-12 |
|
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: 68.46 E-value: 2.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 123 IGLRPTDRLFF--PFSFGPFLG-FWTAFEAAARcgfLVM--PGGGLSSTARLRFLLDHRCTVLFATPTYALHLAEIASKE 197
Cdd:cd17646 174 YPLGPGDRVLQktPLSFDVSVWeLFWPLVAGAR---LVVarPGGHRDPAYLAALIREHGVTTCHFVPSMLRVFLAEPAAG 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 198 GIDlassAVRALVVAGE--PggniPGTRQRLEAVWGARVFDHYGMTE--IGPVAVEAE----------GRP---GELYLL 260
Cdd:cd17646 251 SCA----SLRRVFCSGEalP----PELAARFLALPGAELHNLYGPTEaaIDVTHWPVRgpaetpsvpiGRPvpnTRLYVL 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 261 ESDylaevvdpqtGRPVPDGDTGELVLTN-------LGR--------------TGSPLirYRTGDLIRmapapdptgrtw 319
Cdd:cd17646 323 DDA----------LRPVPVGVPGELYLGGvqlargyLGRpaltaerfvpdpfgPGSRM--YRTGDLAR------------ 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 320 rRLEGGV---LGRADDMIHVRGNNVYPGALESIIRRFADVAEYRIhVDRRNPLADLRL--EIEPVAGDGHALAEEVGRAV 394
Cdd:cd17646 379 -WRPDGAlefLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVV-VARAAPAGAARLvgYVVPAAGAAGPDTAALRAHL 456
|
....
gi 497728519 395 RDAL 398
Cdd:cd17646 457 AERL 460
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
89-358 |
5.59e-12 |
|
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: 67.14 E-value: 5.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 89 HQTSGTTsGRP---LHwLDTSETWDWLTGCWAtnfalIGLRPTDRLFFP----FSFGPFLGFWTAFEAAARcgfLVMPGG 161
Cdd:cd05969 95 HYTSGTT-GTPkgvLH-VHDAMIFYYFTGKYV-----LDLHPDDIYWCTadpgWVTGTVYGIWAPWLNGVT---NVVYEG 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 162 GLSSTARLRFLLDHRCTVLFATPTyALHLAEiasKEGIDLAS----SAVRALVVAGEPggnipgtrQRLEAV-WGARVF- 235
Cdd:cd05969 165 RFDAESWYGIIERVKVTVWYTAPT-AIRMLM---KEGDELARkydlSSLRFIHSVGEP--------LNPEAIrWGMEVFg 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 236 ----DHYGMTEIGPVAVE----AEGRPGELYLLESDYLAEVVDpQTGRPVPDGDTGELVLT------------NLGRTGS 295
Cdd:cd05969 233 vpihDTWWQTETGSIMIAnypcMPIKPGSMGKPLPGVKAAVVD-ENGNELPPGTKGILALKpgwpsmfrgiwnDEERYKN 311
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497728519 296 PLIR--YRTGDLIRMapapDPTGRTWrrleggVLGRADDMIHVRGNNVYPGALESIIRRFADVAE 358
Cdd:cd05969 312 SFIDgwYLTGDLAYR----DEDGYFW------FVGRADDIIKTSGHRVGPFEVESALMEHPAVAE 366
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
216-358 |
6.37e-12 |
|
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: 66.93 E-value: 6.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 216 GGNIPGTRQRLEAVWGARVFDHYGMTE-IGPVAVEAEG--RPGELYLLESDYLAEVVDPQtGRPVPDGDTGELVLTNLGR 292
Cdd:cd05934 204 APNPPELHEEFEERFGVRLLEGYGMTEtIVGVIGPRDEprRPGSIGRPAPGYEVRIVDDD-GQELPAGEPGELVIRGLRG 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 293 TGSPLIRY---------------RTGDLIRMAPapdptgrtwrrlEGGV--LGRADDMIHVRGNNVYPGALESIIRRFAD 355
Cdd:cd05934 283 WGFFKGYYnmpeataeamrngwfHTGDLGYRDA------------DGFFyfVDRKKDMIRRRGENISSAEVERAILRHPA 350
|
...
gi 497728519 356 VAE 358
Cdd:cd05934 351 VRE 353
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
116-398 |
6.80e-11 |
|
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: 63.87 E-value: 6.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 116 WATNFALiGLRPTDR--LFFPFSFGpfLGFWTAFEAAARCGFLVMPGGGLSSTAR--LRFLLDHRCTVLFATPTYALHLA 191
Cdd:cd17643 123 AATQRWF-GFNEDDVwtLFHSYAFD--FSVWEIWGALLHGGRLVVVPYEVARSPEdfARLLRDEGVTVLNQTPSAFYQLV 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 192 EIASKEGIDLasSAVRALVVAGEPGgnipgTRQRLEAvWGARVFDH-------YGMTE--------------IGPVAVEA 250
Cdd:cd17643 200 EAADRDGRDP--LALRYVIFGGEAL-----EAAMLRP-WAGRFGLDrpqlvnmYGITEttvhvtfrpldaadLPAAAASP 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 251 EGRPgelyllESDYLAEVVDpQTGRPVPDGDTGELVLTN-------LGR-------------TGSPLIRYRTGDLIRMAP 310
Cdd:cd17643 272 IGRP------LPGLRVYVLD-ADGRPVPPGVVGELYVSGagvargyLGRpeltaerfvanpfGGPGSRMYRTGDLARRLP 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 311 APDptgrtwrrLEggVLGRADDMIHVRGNNVYPGALESIIRRFADVAEyrIHVD-RRNPLADLRLEIEPVAGDGHA-LAE 388
Cdd:cd17643 345 DGE--------LE--YLGRADEQVKIRGFRIELGEIEAALATHPSVRD--AAVIvREDEPGDTRLVAYVVADDGAAaDIA 412
|
330
....*....|
gi 497728519 389 EVGRAVRDAL 398
Cdd:cd17643 413 ELRALLKELL 422
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
169-398 |
1.31e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 63.02 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 169 LRFLLDHRCTVLFATPTYALHLAEIASKEGIDLASSAVRALVVAGEPGGniPGTRQRLEAVWGARVFDHYGMTEigpVAV 248
Cdd:PRK07788 288 LEDIAKHKATALVVVPVMLSRILDLGPEVLAKYDTSSLKIIFVSGSALS--PELATRALEAFGPVLYNLYGSTE---VAF 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 249 EAEGRPGELyllesdylaeVVDPQT----------------GRPVPDGDTGELVLTNlgrtGSPLIRY------------ 300
Cdd:PRK07788 363 ATIATPEDL----------AEAPGTvgrppkgvtvkildenGNEVPRGVVGRIFVGN----GFPFEGYtdgrdkqiidgl 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 301 -RTGDLIRMapapDPTGRTWrrleggVLGRADDMIHVRGNNVYPGALESIIRRFADVAE-YRIHVDRRNPLADLRLEIep 378
Cdd:PRK07788 429 lSSGDVGYF----DEDGLLF------VDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEaAVIGVDDEEFGQRLRAFV-- 496
|
250 260
....*....|....*....|.
gi 497728519 379 VAGDGHAL-AEEVGRAVRDAL 398
Cdd:PRK07788 497 VKAPGAALdEDAIKDYVRDNL 517
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
108-358 |
1.35e-10 |
|
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: 63.00 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 108 TWDWLTGCWATNFALI-GLRptdRLFFP-FSFGPFLgfwtafeaaarcgflvmpggglsstarlRFLLDHRCTVLFATPT 185
Cdd:cd05911 197 PLYHIYGLFTTLASLLnGAT---VIIMPkFDSELFL----------------------------DLIEKYKITFLYLVPP 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 186 YALHLAEIASKEGIDLASsaVRALVVAGEPGGNipGTRQRLEAVWGARVFDH-YGMTEIGPVAVEAegrPGELYLLES-- 262
Cdd:cd05911 246 IAAALAKSPLLDKYDLSS--LRVILSGGAPLSK--ELQELLAKRFPNATIKQgYGMTETGGILTVN---PDGDDKPGSvg 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 263 ----DYLAEVVDPQTGRPVPDGDTGELVLtnlgRTGSPLIRY-----------------RTGDLIRMapapDPTGRTWrr 321
Cdd:cd05911 319 rllpNVEAKIVDDDGKDSLGPNEPGEICV----RGPQVMKGYynnpeatketfdedgwlHTGDIGYF----DEDGYLY-- 388
|
250 260 270
....*....|....*....|....*....|....*..
gi 497728519 322 leggVLGRADDMIHVRGNNVYPGALESIIRRFADVAE 358
Cdd:cd05911 389 ----IVDRKKELIKYKGFQVAPAELEAVLLEHPGVAD 421
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
91-398 |
1.42e-10 |
|
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: 62.66 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 91 TSGTTsGRPLHWLDTSETwdwLTGCWATNFALIGLRPTDRL--FFPFSF-GPFLGFWTAFEAAARcgfLVMPGGG--LSS 165
Cdd:cd17652 101 TSGST-GRPKGVVVTHRG---LANLAAAQIAAFDVGPGSRVlqFASPSFdASVWELLMALLAGAT---LVLAPAEelLPG 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 166 TARLRFLLDHRCTVLFATPTYalhLAEIASKEGIDLassavRALVVAGEPggnIPGTrqrLEAVW--GARVFDHYGMTEI 243
Cdd:cd17652 174 EPLADLLREHRITHVTLPPAA---LAALPPDDLPDL-----RTLVVAGEA---CPAE---LVDRWapGRRMINAYGPTET 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 244 GPVAVEAE----------GRPgelyllESDYLAEVVDPQTgRPVPDGDTGELVLTNLGRT-------------------G 294
Cdd:cd17652 240 TVCATMAGplpgggvppiGRP------VPGTRVYVLDARL-RPVPPGVPGELYIAGAGLArgylnrpgltaerfvadpfG 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 295 SPLIR-YRTGDLIRmapapdptgrtWR---RLEggVLGRADDMIHVRGNNVYPGALESIIRRFADVAEYRIHVdRRNPLA 370
Cdd:cd17652 313 APGSRmYRTGDLAR-----------WRadgQLE--FLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVV-RDDRPG 378
|
330 340
....*....|....*....|....*...
gi 497728519 371 DLRLEIEPVAGDGHALAEEvgrAVRDAL 398
Cdd:cd17652 379 DKRLVAYVVPAPGAAPTAA---ELRAHL 403
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
175-358 |
1.89e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 59.63 E-value: 1.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 175 HRCTVLFATPTYALHLAEIASKEGIDLAS-----SAVRALVVAgepggnipgTRQRLEAVWGARVFDHYGMTEIGPVAV- 248
Cdd:PRK05605 309 HPPTWLPGVPPLYEKIAEAAEERGVDLSGvrnafSGAMALPVS---------TVELWEKLTGGLLVEGYGLTETSPIIVg 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 249 ---EAEGRPGELYLLESDYLAEVVDPQT-GRPVPDGDTGELVLTNLGRTGSPLIR------------YRTGDLIRMapap 312
Cdd:PRK05605 380 npmSDDRRPGYVGVPFPDTEVRIVDPEDpDETMPDGEEGELLVRGPQVFKGYWNRpeetaksfldgwFRTGDVVVM---- 455
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 497728519 313 DPTGRTwrrlegGVLGRADDMIHVRGNNVYPGALESIIRRFADVAE 358
Cdd:PRK05605 456 EEDGFI------RIVDRIKELIITGGFNVYPAEVEEVLREHPGVED 495
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
169-414 |
3.33e-09 |
|
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: 58.79 E-value: 3.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 169 LRFLLDHRCTVLFAtPTYALHLA----EIASKEGIDLasSAVRALVVAGEPggnI-PGTRQRLEAVWGARVFDH------ 237
Cdd:cd05931 235 LRLISRYRATISAA-PNFAYDLCvrrvRDEDLEGLDL--SSWRVALNGAEP---VrPATLRRFAEAFAPFGFRPeafrps 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 238 YGMTE-------------------------IGPVAVEAEGRPGELYL----LESDYLAEVVDPQTGRPVPDGDTGELVL- 287
Cdd:cd05931 309 YGLAEatlfvsggppgtgpvvlrvdrdalaGRAVAVAADDPAARELVscgrPLPDQEVRIVDPETGRELPDGEVGEIWVr 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 288 -TNLGR---TGSPLIRYRTGDLirmapaPDPTGRTWRR-------LEGG--VLGRADDMIHVRGNNVYPGALESIIRRFA 354
Cdd:cd05931 389 gPSVASgywGRPEATAETFGAL------AATDEGGWLRtgdlgflHDGElyITGRLKDLIIVRGRNHYPQDIEATAEEAH 462
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497728519 355 D------VAEYRIHVDRRNPLAdlrLEIEPVAGDGHALAEEVGRAVRDALCFRIDVSAA-----PPGSLPR 414
Cdd:cd05931 463 PalrpgcVAAFSVPDDGEERLV---VVAEVERGADPADLAAIAAAIRAAVAREHGVAPAdvvlvRPGSIPR 530
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
91-358 |
3.44e-09 |
|
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: 58.55 E-value: 3.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 91 TSGTTsGRPLHWLDTSETWDWLTGCWATNfalIGLRPTDRLFFPFSFGPFLGFWTAFEAAARCGFLVMPGGGLSSTARLR 170
Cdd:cd05903 101 TSGTT-GEPKGVMHSHNTLSASIRQYAER---LGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 171 FLLDHRCTVLFATPTYALHLAEIASKEGIDLasSAVRALVVAGEPggnIPGT-RQRLEAVWGARVFDHYGMTEIGPVAVE 249
Cdd:cd05903 177 LMREHGVTFMMGATPFLTDLLNAVEEAGEPL--SRLRTFVCGGAT---VPRSlARRAAELLGAKVCSAYGSTECPGAVTS 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 250 AEGRPGELYLLESDYLAEVVD----PQTGRPVPDGDTGELVL----TNLGRTGSPLIR--------YRTGDLIRMapapD 313
Cdd:cd05903 252 ITPAPEDRRLYTDGRPLPGVEikvvDDTGATLAPGVEGELLSrgpsVFLGYLDRPDLTadaapegwFRTGDLARL----D 327
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 497728519 314 PTGrtWRRLEGgvlgRADDMIHVRGNNVYPGALESIIRRFADVAE 358
Cdd:cd05903 328 EDG--YLRITG----RSKDIIIRGGENIPVLEVEDLLLGHPGVIE 366
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
174-350 |
5.35e-09 |
|
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: 58.11 E-value: 5.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 174 DHRCTVLFATPTYALHLAEIASKEgiDLASsaVRaLVVAGEPGGNiPGTRQRLEAVWGARVFDHYGMTEIGPVA----VE 249
Cdd:cd05909 235 DKKATILLGTPTFLRGYARAAHPE--DFSS--LR-LVVAGAEKLK-DTLRQEFQEKFGIRILEGYGTTECSPVIsvntPQ 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 250 AEGRPGELYLLESDYLAEVVDPQTGRPVPDGDTGELVLTN----LGRTGSPLIR--------YRTGDLIRMAPAPDPTgr 317
Cdd:cd05909 309 SPNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRGpnvmLGYLNEPELTsfafgdgwYDTGDIGKIDGEGFLT-- 386
|
170 180 190
....*....|....*....|....*....|...
gi 497728519 318 twrrleggVLGRADDMIHVRGNNVYPGALESII 350
Cdd:cd05909 387 --------ITGRLSRFAKIAGEMVSLEAIEDIL 411
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
91-358 |
5.72e-09 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 57.95 E-value: 5.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 91 TSGTTsGRPLHWLDTSETWDWLTgcwATNFALIGLRPTDR------LFFPFSFGPFlgfwtAFEAAARCGFLVMPGGgLS 164
Cdd:PRK06839 157 TSGTT-GKPKGAVLTQENMFWNA---LNNTFAIDLTMHDRsivllpLFHIGGIGLF-----AFPTLFAGGVIIVPRK-FE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 165 STARLRFLLDHRCTVLFATPTYALHLAEIASKEGIDLASsaVRALVVAGEPGgNIPGTRQRLEAvwGARVFDHYGMTEIG 244
Cdd:PRK06839 227 PTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQS--VRWFYNGGAPC-PEELMREFIDR--GFLFGQGFGMTETS 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 245 PVAV-----EAEGRPGEL--YLLESDYlaEVVDPQTGRpVPDGDTGELVLT---------NLGRTGSPLIR---YRTGDL 305
Cdd:PRK06839 302 PTVFmlseeDARRKVGSIgkPVLFCDY--ELIDENKNK-VEVGEVGELLIRgpnvmkeywNRPDATEETIQdgwLCTGDL 378
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 497728519 306 IRMapapDPTGRTWrrleggVLGRADDMIHVRGNNVYPGALESIIRRFADVAE 358
Cdd:PRK06839 379 ARV----DEDGFVY------IVGRKKEMIISGGENIYPLEVEQVINKLSDVYE 421
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
169-358 |
7.17e-09 |
|
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: 56.89 E-value: 7.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 169 LRFLLDHRCTVLFATPTYALHLAEIASKEGIDLASsaVRALvvagePGGNIPGTRQRLEAVWGARVFDHYGMTEI-GPVA 247
Cdd:cd17637 81 LELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSS--LRHV-----LGLDAPETIQRFEETTGATFWSLYGQTETsGLVT 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 248 VE-------AEGRPGELYLLEsdylaeVVDpQTGRPVPDGDTGELVLT---------NLGRTGSPLIR---YRTGDLIRM 308
Cdd:cd17637 154 LSpyrerpgSAGRPGPLVRVR------IVD-DNDRPVPAGETGEIVVRgplvfqgywNLPELTAYTFRngwHHTGDLGRF 226
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 497728519 309 apapDPTGRTWRRleggvlGR--ADDMIHVRGNNVYPGALESIIRRFADVAE 358
Cdd:cd17637 227 ----DEDGYLWYA------GRkpEKELIKPGGENVYPAEVEKVILEHPAIAE 268
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
204-358 |
7.58e-09 |
|
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: 57.33 E-value: 7.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 204 SAVRALVVAGEPggnIPGTR-QRLEA-VWGARVFDHYGMTE---------IGPVAVEAE--GRPgelyllESDYLAEVVD 270
Cdd:cd12115 213 ASVRVVNLAGEP---LPRDLvQRLYArLQVERVVNLYGPSEdttystvapVPPGASGEVsiGRP------LANTQAYVLD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 271 pQTGRPVPDGDTGELVLTNLG-------------------RTGSPLIRYRTGDLIRMapapDPTGRtwrrLEggVLGRAD 331
Cdd:cd12115 284 -RALQPVPLGVPGELYIGGAGvargylgrpgltaerflpdPFGPGARLYRTGDLVRW----RPDGL----LE--FLGRAD 352
|
170 180
....*....|....*....|....*..
gi 497728519 332 DMIHVRGNNVYPGALESIIRRFADVAE 358
Cdd:cd12115 353 NQVKVRGFRIELGEIEAALRSIPGVRE 379
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
138-358 |
1.24e-08 |
|
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: 56.53 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 138 GPFLGFWTAFEAAARCGFLvmpgGGLSSTARLRFLLDHRCTVLFATPT--------YALHLAEI-----ASKEGIDLASS 204
Cdd:cd05941 144 GLVNALLCPLFAGASVEFL----PKFDPKEVAISRLMPSITVFMGVPTiytrllqyYEAHFTDPqfaraAAAERLRLMVS 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 205 AVRALVVAgepggnipgTRQRLEAVWGARVFDHYGMTEIG---PVAVEAEGRPGELYLLESDYLAEVVDPQTGRPVPDGD 281
Cdd:cd05941 220 GSAALPVP---------TLEEWEAITGHTLLERYGMTEIGmalSNPLDGERRPGTVGMPLPGVQARIVDEETGEPLPRGE 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 282 TGELVLtnlgRTGSPLIRY-----------------RTGDLIRMapapDPTGRTWrrleggVLGR-ADDMIHVRGNNVYP 343
Cdd:cd05941 291 VGEIQV----RGPSVFKEYwnkpeatkeeftddgwfKTGDLGVV----DEDGYYW------ILGRsSVDIIKSGGYKVSA 356
|
250
....*....|....*
gi 497728519 344 GALESIIRRFADVAE 358
Cdd:cd05941 357 LEIERVLLAHPGVSE 371
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
123-398 |
1.31e-08 |
|
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: 56.83 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 123 IGLRPTDRLFF--PFSFGPF-LGFWTAFEAAARCgfLVMPGGGLSSTARLR-FLLDHRCTVLFATPTYALHLAEIASKeg 198
Cdd:cd12117 171 VTLGPDDRVLQtsPLAFDAStFEIWGALLNGARL--VLAPKGTLLDPDALGaLIAEEGVTVLWLTAALFNQLADEDPE-- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 199 idlASSAVRALVVAGEPGgNIPGTRQRLEAVWGARVFDHYGMTE---------IGPVAVEAE----GRP---GELYLLES 262
Cdd:cd12117 247 ---CFAGLRELLTGGEVV-SPPHVRRVLAACPGLRLVNGYGPTEnttfttshvVTELDEVAGsipiGRPianTRVYVLDE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 263 DylaevvdpqtGRPVPDGDTGELVLTN-------LGR--------------TGSPLirYRTGDLIRmapapdptgrtwrR 321
Cdd:cd12117 323 D----------GRPVPPGVPGELYVGGdglalgyLNRpaltaerfvadpfgPGERL--YRTGDLAR-------------W 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 322 LEGGVL---GRADDMIHVRGNNVYPGALESIIRRFADVAEYRIHVDRRNPlADLRLeIEPVAGDGHALAEEVGRAVRDAL 398
Cdd:cd12117 378 LPDGRLeflGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAG-GDKRL-VAYVVAEGALDAAELRAFLRERL 455
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
91-358 |
1.34e-08 |
|
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: 56.55 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 91 TSGTTsGRP----------LHWLDTSEtwdwltgcwatnfALIGLRPTDR--LFFPFSFGPFLgfWTAFEAAARCGFLVM 158
Cdd:cd17653 113 TSGST-GIPkgvmvphrgvLNYVSQPP-------------ARLDVGPGSRvaQVLSIAFDACI--GEIFSTLCNGGTLVL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 159 --PGGGLSSTARlrflldhRCTVLFATPTyalhlaeIASKegIDLAS-SAVRALVVAGEPggnIPgtrQRLEAVW--GAR 233
Cdd:cd17653 177 adPSDPFAHVAR-------TVDALMSTPS-------ILST--LSPQDfPNLKTIFLGGEA---VP---PSLLDRWspGRR 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 234 VFDHYGMTEIGPVAVEAEGRPGE------------LYLLESDylaevvdpqtGRPVPDGDTGELVLTNLGRT-------- 293
Cdd:cd17653 235 LYNAYGPTECTISSTMTELLPGQpvtigkpipnstCYILDAD----------LQPVPEGVVGEICISGVQVArgylgnpa 304
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497728519 294 -----------GSPLIRYRTGDLIRmapapdptgrtWRRlEGGV--LGRADDMIHVRGNNVYPGALESIIRRFADVAE 358
Cdd:cd17653 305 ltaskfvpdpfWPGSRMYRTGDYGR-----------WTE-DGGLefLGREDNQVKVRGFRINLEEIEEVVLQSQPEVT 370
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
124-358 |
1.77e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 57.09 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 124 GLRPTDRL--FFPFSFGpfLGFWTAFEAAARCGFLVM--PGGGLSSTARLRFLLDHRCTVLFATPTYALHLAEIASKEGI 199
Cdd:PRK12467 693 QLAADDSMlmVSTFAFD--LGVTELFGALASGATLHLlpPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALP 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 200 dlasSAVRALVVAGEpGGNIPGTRQRLEAVWGARVFDHYGMTE---------------------IG-------------- 244
Cdd:PRK12467 771 ----RPQRALVCGGE-ALQVDLLARVRALGPGARLINHYGPTEttvgvstyelsdeerdfgnvpIGqplanlglyildhy 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 245 --PVAVeaeGRPGELYL----LESDYLaevvdpqtGRPvpdGDTGELVLTN-LGRTGSPLirYRTGDLIRmapapdptgr 317
Cdd:PRK12467 846 lnPVPV---GVVGELYIggagLARGYH--------RRP---ALTAERFVPDpFGADGGRL--YRTGDLAR---------- 899
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 497728519 318 twRRLEGGV--LGRADDMIHVRGNNVYPGALESIIRRFADVAE 358
Cdd:PRK12467 900 --YRADGVIeyLGRMDHQVKIRGFRIELGEIEARLLAQPGVRE 940
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
123-358 |
2.11e-08 |
|
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: 55.75 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 123 IGLRPTDRLFFPF----SFGPFLGFwtaFEAAARCGFLVMPGGGLSSTARLRFLLDHRCTVLFATPTyaLHLAEIASKEG 198
Cdd:cd05917 38 LGLTEQDRLCIPVplfhCFGSVLGV---LACLTHGATMVFPSPSFDPLAVLEAIEKEKCTALHGVPT--MFIAELEHPDF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 199 IDLASSAVRALVVAGEPggnIPGT--RQRLEAVWGARVFDHYGMTEIGPVA------------VEAEGRPGElyLLEsdy 264
Cdd:cd05917 113 DKFDLSSLRTGIMAGAP---CPPElmKRVIEVMNMKDVTIAYGMTETSPVStqtrtddsiekrVNTVGRIMP--HTE--- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 265 lAEVVDPQTGRPVPDGDTGELV----LTNLGRTGSPLIR---------YRTGDLIRMapapDPTGRtwrrleGGVLGRAD 331
Cdd:cd05917 185 -AKIVDPEGGIVPPVGVPGELCirgySVMKGYWNDPEKTaeaidgdgwLHTGDLAVM----DEDGY------CRIVGRIK 253
|
250 260
....*....|....*....|....*...
gi 497728519 332 DMIhVRG-NNVYPGALESIIRRFADVAE 358
Cdd:cd05917 254 DMI-IRGgENIYPREIEEFLHTHPKVSD 280
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
174-358 |
2.22e-08 |
|
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: 56.05 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 174 DHRCTVLFATPTY--ALHLAEIASKEGIDLASsaVRALVVAGEPGgNIPGTRQRLEAVWGAR--VFDHYGMTEIG----- 244
Cdd:cd17634 324 KHGVNILYTAPTAirALMAAGDDAIEGTDRSS--LRILGSVGEPI-NPEAYEWYWKKIGKEKcpVVDTWWQTETGgfmit 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 245 PVAVEAEGRPGELYLLESDYLAEVVDPQtGRPVPDGDTGELVLT------NLGRTGSPLIRYRTgdLIRMAPAPDPTGRT 318
Cdd:cd17634 401 PLPGAIELKAGSATRPVFGVQPAVVDNE-GHPQPGGTEGNLVITdpwpgqTRTLFGDHERFEQT--YFSTFKGMYFSGDG 477
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 497728519 319 WRRLEGG---VLGRADDMIHVRGNNVYPGALESIIRRFADVAE 358
Cdd:cd17634 478 ARRDEDGyywITGRSDDVINVAGHRLGTAEIESVLVAHPKVAE 520
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
161-398 |
3.82e-08 |
|
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: 55.22 E-value: 3.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 161 GGLSSTARLRFLLDHRCTVLFATPT-YALHLAeiASKEGIDLASSAVRALVVAGEPGGniPGTRQRLEAVWGARVFDHYG 239
Cdd:cd05973 163 GGFSVESTWRVIERLGVTNLAGSPTaYRLLMA--AGAEVPARPKGRLRRVSSAGEPLT--PEVIRWFDAALGVPIHDHYG 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 240 MTEIGPV-----AVEAEGRPGELYLLESDYLAEVVDPQTGRPVPdgdtGELVLTNLGRTGSPLIRYRTgdlIRMAPAPDP 314
Cdd:cd05973 239 QTELGMVlanhhALEHPVHAGSAGRAMPGWRVAVLDDDGDELGP----GEPGRLAIDIANSPLMWFRG---YQLPDTPAI 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 315 TGRTWRRLEGGVL---------GRADDMIHVRGNNVYPGALESIIRRFADVAEYRIhVDRRNPLADLRLEIEPVAGDGH- 384
Cdd:cd05973 312 DGGYYLTGDTVEFdpdgsfsfiGRADDVITMSGYRIGPFDVESALIEHPAVAEAAV-IGVPDPERTEVVKAFVVLRGGHe 390
|
250
....*....|....*..
gi 497728519 385 ---ALAEEVGRAVRDAL 398
Cdd:cd05973 391 gtpALADELQLHVKKRL 407
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
170-358 |
6.65e-08 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 54.56 E-value: 6.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 170 RFLLDHRCTVLFATPTyalhLAEIASKEGIDLASS--AVRALVVAGEPGGNiPGTRQRLEAVWGARVFDHYGMTE----- 242
Cdd:cd05945 182 RFLAEHGITVWVSTPS----FAAMCLLSPTFTPESlpSLRHFLFCGEVLPH-KTARALQQRFPDARIYNTYGPTEatvav 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 243 ----IGPVAVEAEGR-------PG-ELYLLESDylaevvdpqtGRPVPDGDTGELVLT----------NLGRTGSPLIR- 299
Cdd:cd05945 257 tyieVTPEVLDGYDRlpigyakPGaKLVILDED----------GRPVPPGEKGELVISgpsvskgylnNPEKTAAAFFPd 326
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497728519 300 -----YRTGDLIRMAPapdptgrtwrrleGGVL---GRADDMIHVRGNNVYPGALESIIRRFADVAE 358
Cdd:cd05945 327 egqraYRTGDLVRLEA-------------DGLLfyrGRLDFQVKLNGYRIELEEIEAALRQVPGVKE 380
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
134-358 |
1.65e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 53.81 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 134 PFSFGpfLGFWTAFEAAARCGFLVM-PGGGLSSTARLRFLLD-HRCTVLFATPTyalHLAEIASKEGIDLASSaVRALVV 211
Cdd:PRK12316 704 PFSFD--VSVWEFFWPLMSGARLVVaAPGDHRDPAKLVELINrEGVDTLHFVPS---MLQAFLQDEDVASCTS-LRRIVC 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 212 AGEPggnIPGT-RQRLEA-VWGARVFDHYGMTE--IGPV---AVEAEGRPGELYLLESDYLAEVVDPQtGRPVPDGDTGE 284
Cdd:PRK12316 778 SGEA---LPADaQEQVFAkLPQAGLYNLYGPTEaaIDVThwtCVEEGGDSVPIGRPIANLACYILDAN-LEPVPVGVLGE 853
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 285 LVLTN-------LGRTG--------SPLI----RYRTGDLIRMapapdptgrtwrRLEGGV--LGRADDMIHVRGNNVYP 343
Cdd:PRK12316 854 LYLAGrglargyHGRPGltaerfvpSPFVagerMYRTGDLARY------------RADGVIeyAGRIDHQVKLRGLRIEL 921
|
250
....*....|....*
gi 497728519 344 GALESIIRRFADVAE 358
Cdd:PRK12316 922 GEIEARLLEHPWVRE 936
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
175-358 |
3.16e-07 |
|
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: 52.46 E-value: 3.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 175 HRCTVLFATPTYALHLAEIASKEGIDLASsaVRALVVAGEPGGniPGTRQRLEAVWGARVFDHYGMTEiGPV-------- 246
Cdd:COG1021 273 ERVTVTALVPPLALLWLDAAERSRYDLSS--LRVLQVGGAKLS--PELARRVRPALGCTLQQVFGMAE-GLVnytrlddp 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 247 ---AVEAEGRPgelylLESDYLAEVVDPQtGRPVPDGDTGELvLTnlgRtGSPLIR------------------YRTGDL 305
Cdd:COG1021 348 eevILTTQGRP-----ISPDDEVRIVDED-GNPVPPGEVGEL-LT---R-GPYTIRgyyrapehnaraftpdgfYRTGDL 416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 497728519 306 IRMapapDPTGRTWrrleggVLGRADDMIHVRGNNVYPGALESIIRRFADVAE 358
Cdd:COG1021 417 VRR----TPDGYLV------VEGRAKDQINRGGEKIAAEEVENLLLAHPAVHD 459
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
149-285 |
3.19e-07 |
|
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: 52.24 E-value: 3.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 149 AAARCG--FLVMPGGGLSSTarLRFLLDHRCTVLFATPTYALHLAEIASKEGIDLasSAVRALVVAGEPGGN--IPGTRQ 224
Cdd:cd05904 222 GLLRLGatVVVMPRFDLEEL--LAAIERYKVTHLPVVPPIVLALVKSPIVDKYDL--SSLRQIMSGAAPLGKelIEAFRA 297
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497728519 225 RLEAVwgaRVFDHYGMTEIGPVAV------EAEGRPGELYLLESDYLAEVVDPQTGRPVPDGDTGEL 285
Cdd:cd05904 298 KFPNV---DLGQGYGMTESTGVVAmcfapeKDRAKYGSVGRLVPNVEAKIVDPETGESLPPNQTGEL 361
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
164-374 |
3.78e-07 |
|
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: 52.05 E-value: 3.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 164 SSTARLRFLLDHRCTVLFATPTYALHLAEIASKEGIDLASSaVRALVVAGEpgGNIPGTRQRLEAVWGARV--FDHYGMT 241
Cdd:cd17644 185 SLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLPSS-LRLVIVGGE--AVQPELVRQWQKNVGNFIqlINVYGPT 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 242 EiGPVAVEaegrpgeLYLLESDYLAEVVDPQTGRP---------------VPDGDTGELVL--TNLGR------------ 292
Cdd:cd17644 262 E-ATIAAT-------VCRLTQLTERNITSVPIGRPiantqvyildenlqpVPVGVPGELHIggVGLARgylnrpeltaek 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 293 ------TGSPLIR-YRTGDLIRMAPapdptgrtwrrlEGGV--LGRADDMIHVRGNNVYPGALESIIRRFADVAEYRIhV 363
Cdd:cd17644 334 fishpfNSSESERlYKTGDLARYLP------------DGNIeyLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVV-I 400
|
250
....*....|.
gi 497728519 364 DRRNPLADLRL 374
Cdd:cd17644 401 VREDQPGNKRL 411
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
124-358 |
6.30e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 51.88 E-value: 6.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 124 GLRPTDRL--FFPFSF-GPFLGFWTAFEAAARcgfLVMPGGGLSSTARLRFLL-DHRCTVLFATPTYALHLAEIASKEGi 199
Cdd:PRK12316 4731 ELTPDDRVlqFMSFSFdGSHEGLYHPLINGAS---VVIRDDSLWDPERLYAEIhEHRVTVLVFPPVYLQQLAEHAERDG- 4806
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 200 DLASsaVRALVVAGEPggnIPGTRQRLeaVWGA----RVFDHYGMTEIGPVAVEAEGRPGELYLLESDYL--------AE 267
Cdd:PRK12316 4807 EPPS--LRVYCFGGEA---VAQASYDL--AWRAlkpvYLFNGYGPTETTVTVLLWKARDGDACGAAYMPIgtplgnrsGY 4879
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 268 VVDPQTGrPVPDGDTGELVLTN----------------------LGRTGSPLirYRTGDLIRmapapdptgrtwRRLEGG 325
Cdd:PRK12316 4880 VLDGQLN-PLPVGVAGELYLGGegvargylerpaltaerfvpdpFGAPGGRL--YRTGDLAR------------YRADGV 4944
|
250 260 270
....*....|....*....|....*....|....*
gi 497728519 326 V--LGRADDMIHVRGNNVYPGALESIIRRFADVAE 358
Cdd:PRK12316 4945 IdyLGRVDHQVKIRGFRIELGEIEARLREHPAVRE 4979
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
175-356 |
7.84e-07 |
|
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: 51.17 E-value: 7.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 175 HRCTVLFATPTYALHLAEIASKEGIDLASsaVRALVVAGEPGGniPGTRQRLEAVWGARVFDHYGMTE----------IG 244
Cdd:cd05920 228 EGVTVTALVPALVSLWLDAAASRRADLSS--LRLLQVGGARLS--PALARRVPPVLGCTLQQVFGMAEgllnytrlddPD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 245 PVAVEAEGRPgelylLESDYLAEVVDPQtGRPVPDGDTGELVL----TNLG---------RTGSPLIRYRTGDLIRMAPA 311
Cdd:cd05920 304 EVIIHTQGRP-----MSPDDEIRVVDEE-GNPVPPGEEGELLTrgpyTIRGyyrapehnaRAFTPDGFYRTGDLVRRTPD 377
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 497728519 312 PDPTgrtwrrleggVLGRADDMIHVRGNNVYPGALESIIRRFADV 356
Cdd:cd05920 378 GYLV----------VEGRIKDQINRGGEKIAAEEVENLLLRHPAV 412
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
91-358 |
1.13e-06 |
|
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: 50.64 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 91 TSGTTSgRPLHWLDTSETWDwlTGCWATNFaLIGLRPTDRLFFPFSFGPFLGFWTAFEA---AARCGFLVMPGGgLSSTA 167
Cdd:cd05974 93 TSGTTS-KPKLVEHTHRSYP--VGHLSTMY-WIGLKPGDVHWNISSPGWAKHAWSCFFApwnAGATVFLFNYAR-FDAKR 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 168 RLRFLLDHRCTVLFATPT-YALHLAEiaskegiDLASSAV--RALVVAGEPGGniPGTRQRLEAVWGARVFDHYGMTEIG 244
Cdd:cd05974 168 VLAALVRYGVTTLCAPPTvWRMLIQQ-------DLASFDVklREVVGAGEPLN--PEVIEQVRRAWGLTIRDGYGQTETT 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 245 PVAVEAEGRP---GELYLLESDYLAEVVDPqTGRPVPDGDTGeLVLTNLGRTGspLIRYRTGDLIRMAPAPD----PTGR 317
Cdd:cd05974 239 ALVGNSPGQPvkaGSMGRPLPGYRVALLDP-DGAPATEGEVA-LDLGDTRPVG--LMKGYAGDPDKTAHAMRggyyRTGD 314
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 497728519 318 TWRRLEGGVL---GRADDMIHVRGNNVYPGALESIIRRFADVAE 358
Cdd:cd05974 315 IAMRDEDGYLtyvGRADDVFKSSDYRISPFELESVLIEHPAVAE 358
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
91-358 |
2.54e-06 |
|
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: 49.35 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 91 TSGTTsGRPlhwldtsetwdwlTGCWATNFALIGLRPTDRlfFPFSFGPFLG--FWTAFEAAARCGFLV---------MP 159
Cdd:cd05971 96 TSGTT-GPP-------------KGALHAHRVLLGHLPGVQ--FPFNLFPRDGdlYWTPADWAWIGGLLDvllpslyfgVP 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 160 -----GGGLSSTARLRFLLDHRCTVLFATPTyALHLAEiASKEGIDLASSAVRALVVAGEPGGnipgtrqRLEAVWGARV 234
Cdd:cd05971 160 vlahrMTKFDPKAALDLMSRYGVTTAFLPPT-ALKMMR-QQGEQLKHAQVKLRAIATGGESLG-------EELLGWAREQ 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 235 F-----DHYGMTE----IGPVAVEAEGRPGELYLLESDYLAEVVDpQTGRPVPDGDTGELVL------------TNLGRT 293
Cdd:cd05971 231 FgvevnEFYGQTEcnlvIGNCSALFPIKPGSMGKPIPGHRVAIVD-DNGTPLPPGEVGEIAVelpdpvaflgywNNPSAT 309
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497728519 294 GSPLIR--YRTGDLIRMapapDPTGRTWrrleggVLGRADDMIHVRGNNVYPGALESIIRRFADVAE 358
Cdd:cd05971 310 EKKMAGdwLLTGDLGRK----DSDGYFW------YVGRDDDVITSSGYRIGPAEIEECLLKHPAVLM 366
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
175-358 |
3.13e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 49.26 E-value: 3.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 175 HRCTVLFATPTyaLHLAEIASKEGIDLASSAVRALVVAGEPggnIP-GTRQRLEAVWGARVFDHYGMTEIGPVAVEA--- 250
Cdd:PRK06710 296 HKVTLFPGAPT--IYIALLNSPLLKEYDISSIRACISGSAP---LPvEVQEKFETVTGGKLVEGYGLTESSPVTHSNflw 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 251 EGR-PGELYLLESDYLAEVVDPQTGRPVPDGDTGELVLT---------NLGRTGSPLIR---YRTGDLIRMapapDPTGR 317
Cdd:PRK06710 371 EKRvPGSIGVPWPDTEAMIMSLETGEALPPGEIGEIVVKgpqimkgywNKPEETAAVLQdgwLHTGDVGYM----DEDGF 446
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 497728519 318 TWrrleggVLGRADDMIHVRGNNVYPGALESIIRRFADVAE 358
Cdd:PRK06710 447 FY------VKDRKKDMIVASGFNVYPREVEEVLYEHEKVQE 481
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
7-358 |
3.13e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 49.96 E-value: 3.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 7 NTPSERL-------RGAQLDAVRHLLARVLTgnefyrrklgalaPASLRTfddfvqLPFTTKAELIADQLERPP---YGT 76
Cdd:PRK12316 2086 NYPAERLaymledsGAALLLTQRHLLERLPL-------------PAGVAR------LPLDRDAEWADYPDTAPAvqlAGE 2146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 77 NLSFPLdrytrfhQTSGTTsGRPlhwldtsetwdwlTGCWATNFALI----------GLRPTDRL--FFPFSF-GPFLGF 143
Cdd:PRK12316 2147 NLAYVI-------YTSGST-GLP-------------KGVAVSHGALVahcqaageryELSPADCElqFMSFSFdGAHEQW 2205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 144 WTAFEAAARcgfLVMPGGGLSSTARL-RFLLDHRCTVLFATPTYALHLAEIASKEGIDLassAVRALVVAGEpGGNIPGT 222
Cdd:PRK12316 2206 FHPLLNGAR---VLIRDDELWDPEQLyDEMERHGVTILDFPPVYLQQLAEHAERDGRPP---AVRVYCFGGE-AVPAASL 2278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 223 RQRLEAVWGARVFDHYGMTE--IGPVA-----VEAEGRPG----------ELYLLESDYlaevvdpqtgRPVPDGDTGEL 285
Cdd:PRK12316 2279 RLAWEALRPVYLFNGYGPTEavVTPLLwkcrpQDPCGAAYvpigralgnrRAYILDADL----------NLLAPGMAGEL 2348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 286 VLTN-------LGRTGSPLIR-------------YRTGDLIRmapapdptgrtwRRLEGGV--LGRADDMIHVRGNNVYP 343
Cdd:PRK12316 2349 YLGGeglargyLNRPGLTAERfvpdpfsasgerlYRTGDLAR------------YRADGVVeyLGRIDHQVKIRGFRIEL 2416
|
410
....*....|....*
gi 497728519 344 GALESIIRRFADVAE 358
Cdd:PRK12316 2417 GEIEARLQAHPAVRE 2431
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
123-358 |
3.22e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 49.39 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 123 IGLRPTDRLFFPFSFGPFLGFWTAFEAAARCG-FLVMPGGGLSSTARLRFLLDHRCTVLFATPTyaLHLAEIASKEGIDL 201
Cdd:PRK12583 237 LGLTEHDRLCVPVPLYHCFGMVLANLGCMTVGaCLVYPNEAFDPLATLQAVEEERCTALYGVPT--MFIAELDHPQRGNF 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 202 ASSAVRALVVAGEPgGNIPGTRQRLEAVWGARVFDHYGMTEIGPVA------------VEAEGRpgELYLLESdylaEVV 269
Cdd:PRK12583 315 DLSSLRTGIMAGAP-CPIEVMRRVMDEMHMAEVQIAYGMTETSPVSlqttaaddlerrVETVGR--TQPHLEV----KVV 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 270 DPQtGRPVPDGDTGELV----LTNLGRTGSPLIR---------YRTGDLIRMapapDPTGRTwrrlegGVLGRADDMIHV 336
Cdd:PRK12583 388 DPD-GATVPRGEIGELCtrgySVMKGYWNNPEATaesidedgwMHTGDLATM----DEQGYV------RIVGRSKDMIIR 456
|
250 260
....*....|....*....|..
gi 497728519 337 RGNNVYPGALESIIRRFADVAE 358
Cdd:PRK12583 457 GGENIYPREIEEFLFTHPAVAD 478
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
167-358 |
3.43e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 49.19 E-value: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 167 ARLRFLLDHRCTVLFATPTYALHLAEIASKEGIDLASsavraLVVAGEPGGNIP-GTRQRLEAVWGARVFDHYGMTE-IG 244
Cdd:PRK08314 270 AAARLIERYRVTHWTNIPTMVVDFLASPGLAERDLSS-----LRYIGGGGAAMPeAVAERLKELTGLDYVEGYGLTEtMA 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 245 PVAVEAEGRPGELYL----LESDylAEVVDPQTGRPVPDGDTGELVLTN----LGRTGSP------LI-----RY-RTGD 304
Cdd:PRK08314 345 QTHSNPPDRPKLQCLgiptFGVD--ARVIDPETLEELPPGEVGEIVVHGpqvfKGYWNRPeataeaFIeidgkRFfRTGD 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 497728519 305 LIRMapapDPTGRTWrrleggVLGRADDMIHVRGNNVYPGALESIIRRFADVAE 358
Cdd:PRK08314 423 LGRM----DEEGYFF------ITDRLKRMINASGFKVWPAEVENLLYKHPAIQE 466
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
174-358 |
4.21e-06 |
|
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: 48.63 E-value: 4.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 174 DHRCTVLFATPTYALHLAEIASKEGIDLASsavraLVVAGEPGGNIP-GTRQRLEAVWGARVFDHYGMTE-IGPVAVEAE 251
Cdd:cd05935 171 KYKVTFWTNIPTMLVDLLATPEFKTRDLSS-----LKVLTGGGAPMPpAVAEKLLKLTGLRFVEGYGLTEtMSQTHTNPP 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 252 GRPGE--LYLLESDYLAEVVDPQTGRPVPDGDTGELVLtnlgrTGSPLIR---------------------YRTGDLIRM 308
Cdd:cd05935 246 LRPKLqcLGIP*FGVDARVIDIETGRELPPNEVGEIVV-----RGPQIFKgywnrpeeteesfieikgrrfFRTGDLGYM 320
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 497728519 309 apapDPTGRTWrrleggVLGRADDMIHVRGNNVYPGALESIIRRFADVAE 358
Cdd:cd05935 321 ----DEEGYFF------FVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*E 360
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
143-362 |
5.67e-06 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 48.89 E-value: 5.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 143 FWTAFEAAARcgfLVM--PGGGLSSTARLRFLLDHRCTVLFATPTY-ALHLAEIASkEGIDLASSAVRALVVAGEPggnI 219
Cdd:PRK10252 657 FFWPFIAGAK---LVMaePEAHRDPLAMQQFFAEYGVTTTHFVPSMlAAFVASLTP-EGARQSCASLRQVFCSGEA---L 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 220 P-GTRQRLEAVWGARVFDHYGMTEigpVAVEAEGRPG---ELYLLESDYLA----------EVVDPQtGRPVPDGDTGEL 285
Cdd:PRK10252 730 PaDLCREWQQLTGAPLHNLYGPTE---AAVDVSWYPAfgeELAAVRGSSVPigypvwntglRILDAR-MRPVPPGVAGDL 805
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 286 VLTN-------LGR---TGSPLIR---------YRTGDLIRmapapdptgrtWRRlEGGV--LGRADDMIHVRGNNVYPG 344
Cdd:PRK10252 806 YLTGiqlaqgyLGRpdlTASRFIAdpfapgermYRTGDVAR-----------WLD-DGAVeyLGRSDDQLKIRGQRIELG 873
|
250
....*....|....*...
gi 497728519 345 ALESIIRRFADVAEYRIH 362
Cdd:PRK10252 874 EIDRAMQALPDVEQAVTH 891
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
115-358 |
6.42e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 48.62 E-value: 6.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 115 CWATnfALIGLRPTDR--LFFPFSFGPFLgfWTAFEAAARCGFLVMPGGGLSSTARLRFLLD-HRCTVLFATPTYALHLA 191
Cdd:PRK12467 3267 CWIA--EAYELDANDRvlLFMSFSFDGAQ--ERFLWTLICGGCLVVRDNDLWDPEELWQAIHaHRISIACFPPAYLQQFA 3342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 192 EIAskEGIDLASsaVRALVVAGE--PGGNIPGTRQRLEAVWgarVFDHYGMTE--IGPV--AVEAEGRPGELYLLESDYL 265
Cdd:PRK12467 3343 EDA--GGADCAS--LDIYVFGGEavPPAAFEQVKRKLKPRG---LTNGYGPTEavVTVTlwKCGGDAVCEAPYAPIGRPV 3415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 266 AE---VVDPQTGRPVPDGDTGELVLTNLG-------RTGSPLIR-------------YRTGDLIRMapapdptgrtwrRL 322
Cdd:PRK12467 3416 AGrsiYVLDGQLNPVPVGVAGELYIGGVGlargyhqRPSLTAERfvadpfsgsggrlYRTGDLARY------------RA 3483
|
250 260 270
....*....|....*....|....*....|....*...
gi 497728519 323 EGGV--LGRADDMIHVRGNNVYPGALESIIRRFADVAE 358
Cdd:PRK12467 3484 DGVIeyLGRIDHQVKIRGFRIELGEIEARLLQHPSVRE 3521
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
220-358 |
6.96e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 48.14 E-value: 6.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 220 PGTRQRLEAVWGARVFDHYGMTEiGPVAVEAE--GRPGELYLLESDylAEVVDPQTGRPVP------------DGDTGEL 285
Cdd:PRK07867 279 PGDIARFARRFGCVVVDGFGSTE-GGVAITRTpdTPPGALGPLPPG--VAIVDPDTGTECPpaedadgrllnaDEAIGEL 355
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497728519 286 VLTNLGRTGSPLIRYRTGDLIRMAPAPDPTGRTWRRLEGGVL---GRADDMIHVRGNNVYPGALESIIRRFADVAE 358
Cdd:PRK07867 356 VNTAGPGGFEGYYNDPEADAERMRGGVYWSGDLAYRDADGYAyfaGRLGDWMRVDGENLGTAPIERILLRYPDATE 431
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
124-358 |
8.31e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 48.62 E-value: 8.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 124 GLRPTDR--LFFPFSFGpfLGFWTAFEAAARCGFLVM--PGGGLSSTARLRFLLDHRCTVLFATPTYALHLAEIASKEGi 199
Cdd:PRK12467 1755 QLSAADVvlQFTSFAFD--VSVWELFWPLINGARLVIapPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVE- 1831
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 200 dlASSAVRALVVAGEpGGNIPGTRQRLEAVWGARVFDHYGMTEigpVAVEAEGRPGELYLLESDYLAEVVDPQTGR---- 275
Cdd:PRK12467 1832 --HPLSLRRVVCGGE-ALEVEALRPWLERLPDTGLFNLYGPTE---TAVDVTHWTCRRKDLEGRDSVPIGQPIANLstyi 1905
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 276 ------PVPDGDTGELVLTNLG----------------------RTGSPLirYRTGDLIRmapapdptgrtWRrlEGGV- 326
Cdd:PRK12467 1906 ldaslnPVPIGVAGELYLGGVGlargylnrpaltaerfvadpfgTVGSRL--YRTGDLAR-----------YR--ADGVi 1970
|
250 260 270
....*....|....*....|....*....|....
gi 497728519 327 --LGRADDMIHVRGNNVYPGALESIIRRFADVAE 358
Cdd:PRK12467 1971 eyLGRIDHQVKIRGFRIELGEIEARLREQGGVRE 2004
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
156-360 |
1.30e-05 |
|
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: 47.39 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 156 LVMPGGGLSSTARL-RFLLDHRCTVLFATPTYALHlaeiaskegIDLAS-SAVRALVVAGEPGgnipgTRQRLEAV---W 230
Cdd:cd17648 166 VVPPDEMRFDPDRFyAYINREKVTYLSGTPSVLQQ---------YDLARlPHLKRVDAAGEEF-----TAPVFEKLrsrF 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 231 GARVFDHYGMTEIGPVAVEAEGRPGE--------------LYLLESDYlaevvdpqtgRPVPDGDTGELVLTNLG----- 291
Cdd:cd17648 232 AGLIINAYGPTETTVTNHKRFFPGDQrfdkslgrpvrntkCYVLNDAM----------KRVPVGAVGELYLGGDGvargy 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 292 ----------------------RTGSPLIRYRTGDLIRMAPAPDptgrtwrrLEggVLGRADDMIHVRGNNVYPGALESI 349
Cdd:cd17648 302 lnrpeltaerflpnpfqteqerARGRNARLYKTGDLVRWLPSGE--------LE--YLGRNDFQVKIRGQRIEPGEVEAA 371
|
250
....*....|....*..
gi 497728519 350 ------IRRFADVAEYR 360
Cdd:cd17648 372 lasypgVRECAVVAKED 388
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
169-358 |
2.18e-05 |
|
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: 46.14 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 169 LRFLLDHRCTVLFATPTYALHLAEIASKEGIDLasSAVRALVVAGEPGGNIPGTRQRleavWGARVFDhYGMTEI----- 243
Cdd:cd17636 81 LELIEAERCTHAFLLPPTIDQIVELNADGLYDL--SSLRSSPAAPEWNDMATVDTSP----WGRKPGG-YGQTEVmglat 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 244 ----GPVAVEAEGRPGELYLLEsdylaeVVDPQtGRPVPDGDTGELV----LTNLGRTGSPLIR--------YRTGDLir 307
Cdd:cd17636 154 faalGGGAIGGAGRPSPLVQVR------ILDED-GREVPDGEVGEIVargpTVMAGYWNRPEVNarrtrggwHHTNDL-- 224
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 497728519 308 mapapdptGrtwRRLEGGVL---GRADDMIHVRGNNVYPGALESIIRRFADVAE 358
Cdd:cd17636 225 --------G---RREPDGSLsfvGPKTRMIKSGAENIYPAEVERCLRQHPAVAD 267
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
122-332 |
2.70e-05 |
|
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: 46.30 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 122 LIGLRPTDRL---FFPFS-FGPFLGFWTA-----FEAAARCgflvmpggglSSTARLRFLLDHRCTVLFATPTYALHLAE 192
Cdd:cd05910 120 LYGIRPGEVDlatFPLFAlFGPALGLTSVipdmdPTRPARA----------DPQKLVGAIRQYGVSIVFGSPALLERVAR 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 193 IASKEGIDLASsaVRALVVAGEPGGniPGTRQRLEAVW--GARVFDHYGMTEIGPVA------VEAE------------- 251
Cdd:cd05910 190 YCAQHGITLPS--LRRVLSAGAPVP--IALAARLRKMLsdEAEILTPYGATEALPVSsigsreLLATttaatsggagtcv 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 252 GRP---GELYLLESDYlAEVVDPQTGRPVPDGDTGELVLTnlGRTGSPLIRYRTgDLIRMAPAPDPTGRTWRRLegGVLG 328
Cdd:cd05910 266 GRPipgVRVRIIEIDD-EPIAEWDDTLELPRGEIGEITVT--GPTVTPTYVNRP-VATALAKIDDNSEGFWHRM--GDLG 339
|
....
gi 497728519 329 RADD 332
Cdd:cd05910 340 YLDD 343
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
91-358 |
4.44e-05 |
|
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: 45.18 E-value: 4.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 91 TSGTTsGRPLHWLDTSETWDWLTGCWAtnfALIGLRPTDRLFFPFSFGPFLGFWTAFEAAARCGFLVMPGGGLSSTARLR 170
Cdd:cd17638 8 TSGTT-GRSKGVMCAHRQTLRAAAAWA---DCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVFDVDAILE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 171 FLLDHRCTVLFATPTYALHLAEIASKEGIDLASSAVRALVVAGEPGGNIPGTRQRL--EAVWGArvfdhYGMTEIGPVAV 248
Cdd:cd17638 84 AIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELgfETVLTA-----YGLTEAGVATM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 249 eaeGRPGElyllesdyLAEVVDPQTGRPVPD-----GDTGELVLtnlgRTGSPLIRYrTGDLIRMAPAPDP-----TGRT 318
Cdd:cd17638 159 ---CRPGD--------DAETVATTCGRACPGfevriADDGEVLV----RGYNVMQGY-LDDPEATAEAIDAdgwlhTGDV 222
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 497728519 319 WRRLEGGVL---GRADDMIHVRGNNVYPGALESIIRRFADVAE 358
Cdd:cd17638 223 GELDERGYLritDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQ 265
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
175-358 |
8.44e-05 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 44.75 E-value: 8.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 175 HRCTVlfatpTYAL-HLAEI--ASKEGIDLASSAVRALVVAGEPGGNIPGTRQRleavWGARVFDHYGMTEIGPV--AVE 249
Cdd:PRK06155 267 HGATV-----TYLLgAMVSIllSQPARESDRAHRVRVALGPGVPAALHAAFRER----FGVDLLDGYGSTETNFViaVTH 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 250 AEGRPGELYLLESDYLAEVVDpQTGRPVPDGDTGELVLtnlgRTGSPLiRYRTGdLIRMapaPDPTGRTWRRL------- 322
Cdd:PRK06155 338 GSQRPGSMGRLAPGFEARVVD-EHDQELPDGEPGELLL----RADEPF-AFATG-YFGM---PEKTVEAWRNLwfhtgdr 407
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 497728519 323 -----EGGV--LGRADDMIHVRGNNVYPGALESIIRRFADVAE 358
Cdd:PRK06155 408 vvrdaDGWFrfVDRIKDAIRRRGENISSFEVEQVLLSHPAVAA 450
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
175-353 |
9.96e-05 |
|
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: 44.39 E-value: 9.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 175 HRCTVLFATPTYALHLAEIASKEGIDLASSAVRALVVAGE--PGGNIPGTRQRLEAvwGARVFDHYGMTEIG------PV 246
Cdd:cd17654 209 HRITVLQATPTLFRRFGSQSIKSTVLSATSSLRVLALGGEpfPSLVILSSWRGKGN--RTRIFNIYGITEVScwalayKV 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 247 AVEAEGRPGELYLLESdyLAEVVDpQTGRPVpdgdTGELVLTNLGRTGsPLIRYRTGDLIRMApapdPTGRTWRRLEGGV 326
Cdd:cd17654 287 PEEDSPVQLGSPLLGT--VIEVRD-QNGSEG----TGQVFLGGLNRVC-ILDDEVTVPKGTMR----ATGDFVTVKDGEL 354
|
170 180
....*....|....*....|....*....
gi 497728519 327 --LGRADDMIHVRGNNVYPGALESIIRRF 353
Cdd:cd17654 355 ffLGRKDSQIKRRGKRINLDLIQQVIESC 383
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
268-398 |
9.97e-05 |
|
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: 44.59 E-value: 9.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 268 VVDPQtGRPVPDGDTGEL---------------VLTN-------LGRTGSPLirYRTGDLIRMapapdptgRTWRRLEgg 325
Cdd:cd12116 304 VLDAA-LRPVPPGVPGELyiggdgvaqgylgrpALTAerfvpdpFAGPGSRL--YRTGDLVRR--------RADGRLE-- 370
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497728519 326 VLGRADDMIHVRGNNVYPGALESIIRRFADVAEYRIHVdrRNPLADLRLEIEPVAGDGHAL-AEEVGRAVRDAL 398
Cdd:cd12116 371 YLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVV--REDGGDRRLVAYVVLKAGAAPdAAALRAHLRATL 442
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
174-358 |
1.05e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 44.77 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 174 DHRCTVLFATPTYALHLAEIASKEGidlASSAVRALVVAGEpgGNIPGTRQRLEAVWG-ARVFDHYGMTE--IGPVAVEA 250
Cdd:PRK05691 2421 EQQVSILGFTPSYGSQLAQWLAGQG---EQLPVRMCITGGE--ALTGEHLQRIRQAFApQLFFNAYGPTEtvVMPLACLA 2495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 251 EGRPGE---------------LYLLESDyLAevvdpqtgrPVPDGDTGELVLTNLG-------RTGSPLIR--------- 299
Cdd:PRK05691 2496 PEQLEEgaasvpigrvvgarvAYILDAD-LA---------LVPQGATGELYVGGAGlaqgyhdRPGLTAERfvadpfaad 2565
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497728519 300 ----YRTGDLIRMapapdptgrtwrRLEGGV--LGRADDMIHVRGNNVYPGALESIIRRFADVAE 358
Cdd:PRK05691 2566 ggrlYRTGDLVRL------------RADGLVeyVGRIDHQVKIRGFRIELGEIESRLLEHPAVRE 2618
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
124-399 |
1.09e-04 |
|
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: 44.18 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 124 GLRPTDRLFF--PFSFGpfLGFWTAFEAAARCGFLVMPGGGLSSTAR--LRFLLDHRCTVLFATPTYALHLAEIASKEGI 199
Cdd:cd12114 163 AVGPDDRVLAlsSLSFD--LSVYDIFGALSAGATLVLPDEARRRDPAhwAELIERHGVTLWNSVPALLEMLLDVLEAAQA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 200 DLASsaVRALVVAGE-PGGNIPGTRQRLEAvwGARVFDHYGMTEIG------PVA-VEAE------GRPgelylLESDYl 265
Cdd:cd12114 241 LLPS--LRLVLLSGDwIPLDLPARLRALAP--DARLISLGGATEASiwsiyhPIDeVPPDwrsipyGRP-----LANQR- 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 266 AEVVDPQtGRPVPDGDTGELVLTNLG----------RTGSPLIR-------YRTGDLirmapapdptGRTWrrlEGGV-- 326
Cdd:cd12114 311 YRVLDPR-GRDCPDWVPGELWIGGRGvalgylgdpeLTAARFVThpdgerlYRTGDL----------GRYR---PDGTle 376
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497728519 327 -LGRADDMIHVRGNNVYPGALESIIRRFADVAEYRIHVDRRNPLADLRLEIEPVAGDGHALAEEVGRAVRDALC 399
Cdd:cd12114 377 fLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRLAAFVVPDNDGTPIAPDALRAFLAQTLP 450
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
169-358 |
1.23e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 44.15 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 169 LRFLLDHRCTVLFATPTYALHLAEIASKEGIDLASsavralVVAGEPGGNI-PGT-----RQRLEavwGARVFDHYGMTE 242
Cdd:PRK08316 253 LRTIEAERITSFFAPPTVWISLLRHPDFDTRDLSS------LRKGYYGASImPVEvlkelRERLP---GLRFYNCYGQTE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 243 IGPVAV-----EAEGRPGE----LYLLESdylaEVVDPQtGRPVPDGDTGELVltnlGRTGSPLIRY------------- 300
Cdd:PRK08316 324 IAPLATvlgpeEHLRRPGSagrpVLNVET----RVVDDD-GNDVAPGEVGEIV----HRSPQLMLGYwddpektaeafrg 394
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497728519 301 ---RTGDLIRMapapDPTGRTWrrleggVLGRADDMIHVRGNNVYPGALESIIRRFADVAE 358
Cdd:PRK08316 395 gwfHSGDLGVM----DEEGYIT------VVDRKKDMIKTGGENVASREVEEALYTHPAVAE 445
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
266-414 |
1.44e-04 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 43.96 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 266 AEVVDPQTGRPVPDGDTGELVL--TNLGRT--GSP---------LIRYRTGDLIRMAPAPDptGRTWRR-------LEGG 325
Cdd:PRK12476 413 AVIVDPDTGAELPDGEVGEIWLhgDNIGRGywGRPeetertfgaKLQSRLAEGSHADGAAD--DGTWLRtgdlgvyLDGE 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 326 --VLGRADDMIHVRGNNVYPGALE------SIIRRFADVAEYRIHVDRRNPLAdlrLEIEPVAGDGHALAEEVGRAVRDA 397
Cdd:PRK12476 491 lyITGRIADLIVIDGRNHYPQDIEatvaeaSPMVRRGYVTAFTVPAEDNERLV---IVAERAAGTSRADPAPAIDAIRAA 567
|
170 180
....*....|....*....|..
gi 497728519 398 LCFR-----IDVSAAPPGSLPR 414
Cdd:PRK12476 568 VSRRhglavADVRLVPAGAIPR 589
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
233-370 |
2.08e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 43.49 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 233 RVFDHYGMTEIGPVAVEAEGR-PGELyllesdylaevvdpqtGRPVP---------DGDTGELVLTNLGRTgsplirYRT 302
Cdd:PRK08308 238 YMMQQYGCSEAGCVSICPDMKsHLDL----------------GNPLPhvsvsagsdENAPEEIVVKMGDKE------IFT 295
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497728519 303 GDLirmapapdptgrTWRRLEGGV--LGRADDMIHVRGNNVYPGALESIIRRFADVAE---YRihvdRRNPLA 370
Cdd:PRK08308 296 KDL------------GYKSERGTLhfMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEavvYR----GKDPVA 352
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
220-358 |
2.25e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 43.45 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 220 PGTRQRLEAVWGARVFDHYGMTEIGpvaVEAEGRPGELylleSDYLAEVVDPQTGRPV--------PDGDT--------G 283
Cdd:PRK13383 306 PTLGQRFMDTYGDILYNGYGSTEVG---IGALATPADL----RDAPETVGKPVAGCPVrildrnnrPVGPRvtgrifvgG 378
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497728519 284 ELVLTNLGRTGSPLI---RYRTGDLIRMapapDPTGRTWrrleggVLGRADDMIHVRGNNVYPGALESIIRRFADVAE 358
Cdd:PRK13383 379 ELAGTRYTDGGGKAVvdgMTSTGDMGYL----DNAGRLF------IVGREDDMIISGGENVYPRAVENALAAHPAVAD 446
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
268-398 |
3.15e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 43.23 E-value: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 268 VVDPQTGRPVPDGDTGELVLTN----LGRTGSPLIRYRTgdLIRMApapdptGRTW---------RRLEGGVLGRADDMI 334
Cdd:PRK05691 383 IVDPQSLEVLGDNRVGEIWASGpsiaHGYWRNPEASAKT--FVEHD------GRTWlrtgdlgflRDGELFVTGRLKDML 454
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497728519 335 HVRGNNVYPGALESIIRRFADVAeyrihvdRRNPLADLRLEIEPVAGDGhaLAEEVGRAVRDAL 398
Cdd:PRK05691 455 IVRGHNLYPQDIEKTVEREVEVV-------RKGRVAAFAVNHQGEEGIG--IAAEISRSVQKIL 509
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
175-358 |
3.28e-04 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 42.76 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 175 HRCTVLFATPTYALHLAEI--ASKEGIDLasSAVRALVVAGEPGGniPGTRQRLEAVWGARVFDHYGMTEIGPVAV---- 248
Cdd:PRK12406 242 HRITHMHMVPTMFIRLLKLpeEVRAKYDV--SSLRHVIHAAAPCP--ADVKRAMIEWWGPVIYEYYGSTESGAVTFatse 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 249 EAEGRPGELYLLESDYLAEVVDpQTGRPVPDGDTGELVltnlgrtgspliryrtgdlIRMAPAPDPT--GRTWRRLEGGV 326
Cdd:PRK12406 318 DALSHPGTVGKAAPGAELRFVD-EDGRPLPQGEIGEIY-------------------SRIAGNPDFTyhNKPEKRAEIDR 377
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 497728519 327 LG--------------------RADDMIHVRGNNVYPGALESIIRRFADVAE 358
Cdd:PRK12406 378 GGfitsgdvgyldadgylflcdRKRDMVISGGVNIYPAEIEAVLHAVPGVHD 429
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
171-358 |
5.69e-04 |
|
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: 42.08 E-value: 5.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 171 FLLDHRCTVLFaTPTYALHLaeIAS-KEGIDLASSAVRALVVAGEPGgNIPGTRQRLEAVWGARVFDHYGMTEIGPVAV- 248
Cdd:cd17656 214 LVKRHNIEVVF-LPVAFLKF--IFSeREFINRFPTCVKHIITAGEQL-VITNEFKEMLHEHNVHLHNHYGPSETHVVTTy 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 249 ----EAE-------GRP---GELYLLEsdylaevvdpQTGRPVPDGDTGELVLT--NLGR-------------TGSPL-- 297
Cdd:cd17656 290 tinpEAEipelppiGKPisnTWIYILD----------QEQQLQPQGIVGELYISgaSVARgylnrqeltaekfFPDPFdp 359
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497728519 298 --IRYRTGDLIRmapapdptgrtwrRLEGG---VLGRADDMIHVRGNNVYPGALESIIRRFADVAE 358
Cdd:cd17656 360 neRMYRTGDLAR-------------YLPDGnieFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSE 412
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
220-357 |
5.89e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 41.95 E-value: 5.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 220 PGTRQRLEAVWGARVFD-HYGMTEIGPVAVEAEGRPGELYLLESDYL----------AEVVDPQTGRPVPDGDTGELVLT 288
Cdd:PRK06178 341 PDYRQRWRALTGSVLAEaAWGMTETHTCDTFTAGFQDDDFDLLSQPVfvglpvpgteFKICDFETGELLPLGAEGEIVVR 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 289 ---------NLGRTGSPLIR---YRTGDLIRMAPapdptgrtwrrlEGGV--LGRADDMIHVRGNNVYPGALESIIRRFA 354
Cdd:PRK06178 421 tpsllkgywNKPEATAEALRdgwLHTGDIGKIDE------------QGFLhyLGRRKEMLKVNGMSVFPSEVEALLGQHP 488
|
...
gi 497728519 355 DVA 357
Cdd:PRK06178 489 AVL 491
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
174-286 |
7.18e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 41.86 E-value: 7.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 174 DHRCTVLFATPTY--ALHLAEIASKEGIDlasSAVRALVV-AGEPGGNIPGTRQRleavwGARVFDHYGMTEI-GPVAVE 249
Cdd:PRK08162 268 EHGVTHYCGAPIVlsALINAPAEWRAGID---HPVHAMVAgAAPPAAVIAKMEEI-----GFDLTHVYGLTETyGPATVC 339
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 497728519 250 AE----------------GRPGELYLLESDylAEVVDPQTGRPVP-DGDT-GELV 286
Cdd:PRK08162 340 AWqpewdalplderaqlkARQGVRYPLQEG--VTVLDPDTMQPVPaDGETiGEIM 392
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
200-358 |
1.56e-03 |
|
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: 40.53 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 200 DLASSAVRAL---VVAGEPggNIPGTRQRLEAVWGARVFDHYGMTEIGPVAVEAEG---RPGELYLLESDYLAEVVDpQT 273
Cdd:cd05928 284 DLSSYKFPSLqhcVTGGEP--LNPEVLEKWKAQTGLDIYEGYGQTETGLICANFKGmkiKPGSMGKASPPYDVQIID-DN 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 274 GRPVPDGDTGELVLT---------------NLGRTGSPLIR--YRTGDLIRMapapDPTGRTWrrleggVLGRADDMIHV 336
Cdd:cd05928 361 GNVLPPGTEGDIGIRvkpirpfglfsgyvdNPEKTAATIRGdfYLTGDRGIM----DEDGYFW------FMGRADDVINS 430
|
170 180
....*....|....*....|..
gi 497728519 337 RGNNVYPGALESIIRRFADVAE 358
Cdd:cd05928 431 SGYRIGPFEVESALIEHPAVVE 452
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
174-287 |
1.75e-03 |
|
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: 40.36 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 174 DHRCTVLFATPTYALHLAEiASKEGIDLASSAVRALVVAGEPGgniPGTRQRLEAVwGARVFDHYGMTEI-GPVAV---- 248
Cdd:cd12118 219 KHKVTHFCGAPTVLNMLAN-APPSDARPLPHRVHVMTAGAPPP---AAVLAKMEEL-GFDVTHVYGLTETyGPATVcawk 293
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 497728519 249 -EAEGRPGEL-YLLES----DYLA----EVVDPQTGRPVP-DGDT-GELVL 287
Cdd:cd12118 294 pEWDELPTEErARLKArqgvRYVGleevDVLDPETMKPVPrDGKTiGEIVF 344
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
227-357 |
2.02e-03 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 40.44 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 227 EAVWGARVFDHYGMTE-----IGPVAVEAE-----GRPGelylleSDYLAEVVDPQtGRPVPDGDTGELVLTNL-GRTgs 295
Cdd:PRK08008 308 EERFGVRLLTSYGMTEtivgiIGDRPGDKRrwpsiGRPG------FCYEAEIRDDH-NRPLPAGEIGEICIKGVpGKT-- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 296 pLIRYRTGDlirmapaPDPTGRTWRR---LEGGVLGRADD------------MIHVRGNNVYPGALESIIR---RFADVA 357
Cdd:PRK08008 379 -IFKEYYLD-------PKATAKVLEAdgwLHTGDTGYVDEegffyfvdrrcnMIKRGGENVSCVELENIIAthpKIQDIV 450
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
238-363 |
4.19e-03 |
|
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: 39.35 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 238 YGMTEIGPVAveAEGRPGELYLLESDYLAEVVDPQTGRPVPDGDTGELVL----------TNLGRTGSPLIR---YRTGD 304
Cdd:cd05914 265 YGMTETAPII--SYSPPNRIRLGSAGKVIDGVEVRIDSPDPATGEGEIIVrgpnvmkgyyKNPEATAEAFDKdgwFHTGD 342
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 305 LIRMapapDPTGRTWrrleggVLGRADDMIHV-RGNNVYPGALESIIRRFADVAEYRIHV 363
Cdd:cd05914 343 LGKI----DAEGYLY------IRGRKKEMIVLsSGKNIYPEEIEAKINNMPFVLESLVVV 392
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
200-409 |
5.13e-03 |
|
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: 38.90 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 200 DLASsaVRALVVAGEPGGniPGTRQRLEAVWGARVFDHYGMTE-IGPVAVEAE---------GRP--GELYLLESDylae 267
Cdd:cd05929 242 DLSS--LKRVIHAAAPCP--PWVKEQWIDWGGPIIWEYYGGTEgQGLTIINGEewlthpgsvGRAvlGKVHILDED---- 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 268 vvdpqtGRPVPDGDTGELVLTNlgrtgSPLIRYrTGDLIRMAPAPDPTGrtWRRLegGVLGRAD------------DMIH 335
Cdd:cd05929 314 ------GNEVPPGEIGEVYFAN-----GPGFEY-TNDPEKTAAARNEGG--WSTL--GDVGYLDedgylyltdrrsDMII 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 336 VRGNNVYPGALESIIRRFADVAEYRI----HVDR-RNPLAdlRLEIEPVAGDGHALAEEVGRAVRDAL----CFR-IDVS 405
Cdd:cd05929 378 SGGVNIYPQEIENALIAHPKVLDAAVvgvpDEELgQRVHA--VVQPAPGADAGTALAEELIAFLRDRLsrykCPRsIEFV 455
|
....
gi 497728519 406 AAPP 409
Cdd:cd05929 456 AELP 459
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
221-414 |
6.23e-03 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 38.97 E-value: 6.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 221 GTRQRLEAV------WGARVFDHYGMTEIGPVAV----------EAEGRPGELYLLEsdylaeVVDPQtGRPVPDGDTGE 284
Cdd:PRK13382 321 GSRMRPDVViafmdqFGDVIYNNYNATEAGMIATatpadlraapDTAGRPAEGTEIR------ILDQD-FREVPTGEVGT 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 285 LVLTNL----GRTGSPLIRYR-----TGDLIRMapapDPTGRTWrrleggVLGRADDMIHVRGNNVYPGALESIIRRFAD 355
Cdd:PRK13382 394 IFVRNDtqfdGYTSGSTKDFHdgfmaSGDVGYL----DENGRLF------VVGRDDEMIVSGGENVYPIEVEKTLATHPD 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497728519 356 VAEYR-IHVDrrNPLADLRLEIEPV-AGDGHALAEEVGRAVRDALC-FRIDVSAAPPGSLPR 414
Cdd:PRK13382 464 VAEAAvIGVD--DEQYGQRLAAFVVlKPGASATPETLKQHVRDNLAnYKVPRDIVVLDELPR 523
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
238-358 |
7.89e-03 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 38.64 E-value: 7.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497728519 238 YGMTEIGPVA------------VEAEGR--PGelylLEsdylAEVVDPQTGRPVPDGDTGELvltnLGRTGSPLIRY--- 300
Cdd:PRK08315 348 YGMTETSPVStqtrtddplekrVTTVGRalPH----LE----VKIVDPETGETVPRGEQGEL----CTRGYSVMKGYwnd 415
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497728519 301 --------------RTGDLIRMapapDPtgrtwrrlEGGV--LGRADDMIhVR-GNNVYPGALESIIRRFADVAE 358
Cdd:PRK08315 416 pektaeaidadgwmHTGDLAVM----DE--------EGYVniVGRIKDMI-IRgGENIYPREIEEFLYTHPKIQD 477
|
|
| |
