|
Name |
Accession |
Description |
Interval |
E-value |
| PA_CoA_ligase |
TIGR02155 |
phenylacetate-CoA ligase; Phenylacetate-CoA ligase (PA-CoA ligase) catalyzes the first step in ... |
14-432 |
0e+00 |
|
phenylacetate-CoA ligase; Phenylacetate-CoA ligase (PA-CoA ligase) catalyzes the first step in aromatic catabolism of phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Often located in a conserved gene cluster with enzymes involved in phenylacetic acid activation (paaG/H/I/J), phenylacetate-CoA ligase has been found among the proteobacteria as well as in gram positive prokaryotes. In the B-subclass proteobacterium Azoarcus evansii, phenylacetate-CoA ligase has been shown to be induced under aerobic and anaerobic growth conditions. It remains unclear however, whether this induction is due to the same enzyme or to another isoenzyme restricted to specific anaerobic growth conditions. [Energy metabolism, Other]
Pssm-ID: 131210 [Multi-domain] Cd Length: 422 Bit Score: 710.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 14 ETASRDAVQALQLERLKRSLAHAYENVPAYRAKFDAAGVHPSDLSSLSDLAKFPFTTKGDLRENYPFGMFAVPQDRIARI 93
Cdd:TIGR02155 1 ETASLDELRALQTQRLKWTVKHAYENVPHYRKAFDAAGVHPDDLQSLSDLAKFPFTQKHDLRDNYPFGLFAVPREQVVRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 94 HASSGTTGKPTVVGYTLADIETWAGLVARSIRAAGARRGDKVHVSYGYGLFTGGLGAHYGAERAGLTVIPFGGGQTERQV 173
Cdd:TIGR02155 81 HASSGTTGKPTVVGYTQNDIDTWSSVVARSIRAAGGRPGDLIHNAYGYGLFTGGLGAHYGAEKLGCTVVPISGGQTEKQV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 174 QLIRDFEPQIIMVTPSYMLAIADEFERQGMDPAASSLQIGIFGAEPWTPEMRAAIEARMGLSAVDIYGLSEVMGPGVASE 253
Cdd:TIGR02155 161 QLIQDFKPDIIMVTPSYMLNLLEELKRMGIDPAQTSLQVGIFGAEPWTNAMRKEIEARLGMKATDIYGLSEVIGPGVAME 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 254 CAETKDGPTIWEDHFYPEIIDPNTGDVLPDGEFGELVFTSLTKEAMPVVRYRTRDLTRLLPGTARPgFRRMEKITGRCDD 333
Cdd:TIGR02155 241 CVETQDGLHIWEDHFYPEIIDPHTGEVLPDGEEGELVFTTLTKEALPVIRYRTRDLTRLLPGTART-MRRMDRITGRSDD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 334 MMIVRGVNVFPSQIEELILKHAALSPHYQCVLGKEGPLDTLTVRIEAALGAPADAAASASRQLA----HDIKSLIGVTAA 409
Cdd:TIGR02155 320 MLIIRGVNVFPTQLEEVILKMDELSPHYQLELTRNGHMDELTLKVELKPESYTLRLHEQASLLAgeiqHTIKQEVGVSMD 399
|
410 420
....*....|....*....|...
gi 1021858603 410 IEILAAGGIERSVGKARRVVDLR 432
Cdd:TIGR02155 400 VHLVEPGSLPRSEGKARRVVDLR 422
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
6-431 |
0e+00 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 673.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 6 TDLPLDPIETASRDAVQALQLERLKRSLAHAYENVPAYRAKFDAAGVHPSDLSSLSDLAKFPFTTKGDLRENYPFGMFAV 85
Cdd:COG1541 1 SEMYWNPIETLSREELEALQLERLRATVARAYENSPFYRRKFDEAGVDPDDIKSLEDLAKLPFTTKEDLRDNYPFGLFAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 86 PQDRIARIHASSGTTGKPTVVGYTLADIETWAGLVARSIRAAGARRGDKVHVSYGYGLFTGGLGAHYGAERAGLTVIPFG 165
Cdd:COG1541 81 PLEEIVRIHASSGTTGKPTVVGYTRKDLDRWAELFARSLRAAGVRPGDRVQNAFGYGLFTGGLGLHYGAERLGATVIPAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 166 GGQTERQVQLIRDFEPQIIMVTPSYMLAIADEFERQGMDPAASSLQIGIFGAEPWTPEMRAAIEARMGLSAVDIYGLSEv 245
Cdd:COG1541 161 GGNTERQLRLMQDFGPTVLVGTPSYLLYLAEVAEEEGIDPRDLSLKKGIFGGEPWSEEMRKEIEERWGIKAYDIYGLTE- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 246 MGPGVASECaETKDGPTIWEDHFYPEIIDPNTGDVLPDGEFGELVFTSLTKEAMPVVRYRTRDLTRLLPG---TARPgFR 322
Cdd:COG1541 240 VGPGVAYEC-EAQDGLHIWEDHFLVEIIDPETGEPVPEGEEGELVVTTLTKEAMPLIRYRTGDLTRLLPEpcpCGRT-HP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 323 RMEKITGRCDDMMIVRGVNVFPSQIEELILKHAALSPHYQCVLGKEGPLDTLTVRIEaalGAPADAAASASRQLAHDIKS 402
Cdd:COG1541 318 RIGRILGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYQIVVDREGGLDELTVRVE---LAPGASLEALAEAIAAALKA 394
|
410 420
....*....|....*....|....*....
gi 1021858603 403 LIGVTAAIEILAAGGIERSVGKARRVVDL 431
Cdd:COG1541 395 VLGLRAEVELVEPGSLPRSEGKAKRVIDR 423
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
11-432 |
0e+00 |
|
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: 662.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 11 DPIETASRDAVQALQLERLKRSLAHAYENVPAYRAKFDAAGVHPSDLSSLSDLAKFPFTTKGDLRENYPFGMFAVPQDRI 90
Cdd:cd05913 1 EEIETMSRDELDALQLARLKWTVRHAYENVPFYRRKFAAAGIDPDDIKSLDDLRKLPFTTKEDLRDNYPFGLFAVPREKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 91 ARIHASSGTTGKPTVVGYTLADIETWAGLVARSIRAAGARRGDKVHVSYGYGLFTGGLGAHYGAERAGLTVIPFGGGQTE 170
Cdd:cd05913 81 VRIHASSGTTGKPTVVGYTKNDLDVWAELVARCLDAAGVTPGDRVQNAYGYGLFTGGLGFHYGAERLGALVIPAGGGNTE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 171 RQVQLIRDFEPQIIMVTPSYMLAIADEFERQGMDPAASSLQIGIFGAEPWTPEMRAAIEARMGLSAVDIYGLSEVMGPGV 250
Cdd:cd05913 161 RQLQLIKDFGPTVLCCTPSYALYLAEEAEEEGIDPRELSLKVGIFGAEPWTEEMRKRIERRLGIKAYDIYGLTEIIGPGV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 251 ASECAEtKDGPTIWEDHFYPEIIDPNTGDVLPDGEFGELVFTSLTKEAMPVVRYRTRDLTRLLPGTARPG--FRRMEKIT 328
Cdd:cd05913 241 AFECEE-KDGLHIWEDHFIPEIIDPETGEPVPPGEVGELVFTTLTKEAMPLIRYRTRDITRLLPGPCPCGrtHRRIDRIT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 329 GRCDDMMIVRGVNVFPSQIEELILKHAALSPHYQCVLGKEGPLDTLTVRIEAALGAPADAAASASRQ-LAHDIKSLIGVT 407
Cdd:cd05913 320 GRSDDMLIIRGVNVFPSQIEDVLLKIPGLGPHYQLILTRQEHLDELTIKVEVRPEADDDEKLEALKQrLERHIKSVLGVT 399
|
410 420
....*....|....*....|....*
gi 1021858603 408 AAIEILAAGGIERSVGKARRVVDLR 432
Cdd:cd05913 400 VEVELVEPGSLPRSEGKAKRVIDKR 424
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
89-356 |
6.79e-40 |
|
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: 145.51 E-value: 6.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 89 RIARIHASSGTTGKPTVVGYTLADietWAGLVARSIRAAGARRGDKVHVSYGYGlFTGGLGAHYGAERAGLTVIPFGGGQ 168
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRN---LLAAAAALAASGGLTEGDVFLSTLPLF-HIGGLFGLLGALLAGGTVVLLPKFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 169 TERQVQLIRDFEPQIIMVTPSYMLAIADEFERQGMDpaASSLQIGIFGAEPWTPEMRAAIEARMGLSAVDIYGLSEVMGP 248
Cdd:cd04433 77 PEAALELIEREKVTILLGVPTLLARLLKAPESAGYD--LSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 249 gVASECAETKD--GPTIW--EDHFYPEIIDPNTGDvLPDGEFGELVFTSLT---------KEAMPVVR---YRTRDLTRL 312
Cdd:cd04433 155 -VATGPPDDDArkPGSVGrpVPGVEVRIVDPDGGE-LPPGEIGELVVRGPSvmkgywnnpEATAAVDEdgwYRTGDLGRL 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1021858603 313 LPGtarpGFRRmekITGRCDDMMIVRGVNVFPSQIEELILKHAA 356
Cdd:cd04433 233 DED----GYLY---IVGRLKDMIKSGGENVYPAEVEAVLLGHPG 269
|
|
| AMP-binding_C_2 |
pfam14535 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
339-432 |
2.10e-30 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 434024 [Multi-domain] Cd Length: 96 Bit Score: 112.57 E-value: 2.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 339 GVNVFPSQIEELILKHAALSPHYQCVLGKEGPLDTLTVRIEAALGAPADAAASAS--RQLAHDIKSLIGVTAAIEILAAG 416
Cdd:pfam14535 1 GVNVFPSQIEEVLLEIPGVGPEYQIIVTREGGLDELEVKVEVAEGFSDEIKDLEAleKRIAKELKSVLGVSVKVELVEPG 80
|
90
....*....|....*.
gi 1021858603 417 GIERSVGKARRVVDLR 432
Cdd:pfam14535 81 TLPRSEGKAKRVIDLR 96
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
96-356 |
1.58e-23 |
|
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: 102.20 E-value: 1.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 96 SSGTTGKPTVVGYTLAdieTWAGLVARSIRAAGARRGDKVHV----SYGYGLFTGGLGAHYgaerAGLTVIPFGGGQTER 171
Cdd:COG0318 108 TSGTTGRPKGVMLTHR---NLLANAAAIAAALGLTPGDVVLValplFHVFGLTVGLLAPLL----AGATLVLLPRFDPER 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 172 QVQLIRDFEPQIIMVTPSYMLAIADEFERQGMDPaaSSLQIGIFGAEPWTPEMRAAIEARMGLSAVDIYGLSEvMGPGVA 251
Cdd:COG0318 181 VLELIERERVTVLFGVPTMLARLLRHPEFARYDL--SSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTE-TSPVVT 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 252 SECAETKDGPTIWEDHFYP----EIIDPNtGDVLPDGEFGELVFTS------------LTKEAMPVVRYRTRDLTRLLPG 315
Cdd:COG0318 258 VNPEDPGERRPGSVGRPLPgvevRIVDED-GRELPPGEVGEIVVRGpnvmkgywndpeATAEAFRDGWLRTGDLGRLDED 336
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1021858603 316 tarpGFRRmekITGRCDDMMIVRGVNVFPSQIEELILKHAA 356
Cdd:COG0318 337 ----GYLY---IVGRKKDMIISGGENVYPAEVEEVLAAHPG 370
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
23-338 |
1.27e-16 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 81.20 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 23 ALQLERLKRSLAHA-------YENVPAYRAKFDAAGVHPSDLSSLSDLAKFPFTTKGDLRENYPFGMFAVPQ----DRIA 91
Cdd:pfam00501 79 RLPAEELAYILEDSgakvlitDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPppdpDDLA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 92 RIHASSGTTGKPT-VV---GYTLADIETWAGLVARSIRAAGARRGDKVH-VSYGYGLFTGGLGAHYgaerAGLTVIPFGG 166
Cdd:pfam00501 159 YIIYTSGTTGKPKgVMlthRNLVANVLSIKRVRPRGFGLGPDDRVLSTLpLFHDFGLSLGLLGPLL----AGATVVLPPG 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 167 GQT---ERQVQLIRDFEPQIIMVTPSYMLAIADEFERQGMDpaASSLQIGIFGAEPWTPEMRAAIEARMGLSAVDIYGLS 243
Cdd:pfam00501 235 FPAldpAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRAL--LSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLT 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 244 EvMGPGVASECAETKD-------GPTIWEDHFYpeIIDPNTGDVLPDGEFGELVFTS------------LTKEAMPVVR- 303
Cdd:pfam00501 313 E-TTGVVTTPLPLDEDlrslgsvGRPLPGTEVK--IVDDETGEPVPPGEPGELCVRGpgvmkgylndpeLTAEAFDEDGw 389
|
330 340 350
....*....|....*....|....*....|....*.
gi 1021858603 304 YRTRDLTRLLP-GTARpgfrrmekITGRCDDMMIVR 338
Cdd:pfam00501 390 YRTGDLGRRDEdGYLE--------IVGRKKDQIKLG 417
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
88-356 |
7.28e-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: 76.11 E-value: 7.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 88 DRIARIHASSGTTGKPTvvGYTLADiETWAGLVARSIRAAGARRGDK-VHV---SYGYGLFTGGLGAHYgaerAGLTVIP 163
Cdd:cd17631 98 DDLALLMYTSGTTGRPK--GAMLTH-RNLLWNAVNALAALDLGPDDVlLVVaplFHIGGLGVFTLPTLL----RGGTVVI 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 164 FGGGQTERQVQLIRDFEPQIIMVTPSYMLAIADEFERQGMDPaaSSLQIGIFGAEPWTPEMRAAIEARmGLSAVDIYGLS 243
Cdd:cd17631 171 LRKFDPETVLDLIERHRVTSFFLVPTMIQALLQHPRFATTDL--SSLRAVIYGGAPMPERLLRALQAR-GVKFVQGYGMT 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 244 EvMGPGVA---SECAETKDGpTIWEDHFYPE--IIDPNTGDVlPDGEFGELVFTS------------LTKEAMPVVRYRT 306
Cdd:cd17631 248 E-TSPGVTflsPEDHRRKLG-SAGRPVFFVEvrIVDPDGREV-PPGEVGEIVVRGphvmagywnrpeATAAAFRDGWFHT 324
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1021858603 307 RDLTRLlpgtARPGFRRmekITGRCDDMMIVRGVNVFPSQIEELILKHAA 356
Cdd:cd17631 325 GDLGRL----DEDGYLY---IVDRKKDMIISGGENVYPAEVEDVLYEHPA 367
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
79-356 |
1.03e-11 |
|
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: 66.43 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 79 PFGMFAVPQDRIARIHASSGTTGKPTVVGYTLADIetWAGLVARSIRAAGARRGDKV--------HVsygYGLFTGGLga 150
Cdd:cd05936 116 LGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNL--VANALQIKAWLEDLLEGDDVvlaalplfHV---FGLTVALL-- 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 151 hYGAeRAGLTVIPFGGGQTERQVQLIRDFEPQIIMVTPSYMLAIADEFERQGMDPaaSSLQIGIFGAEPWTPEMRAAIEA 230
Cdd:cd05936 189 -LPL-ALGATIVLIPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDF--SSLRLCISGGAPLPVEVAERFEE 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 231 RMGLSAVDIYGLSEvMGPGVASECAETKD-----GPTIWedHFYPEIIDPNtGDVLPDGEFGEL------VFT------S 293
Cdd:cd05936 265 LTGVPIVEGYGLTE-TSPVVAVNPLDGPRkpgsiGIPLP--GTEVKIVDDD-GEELPPGEVGELwvrgpqVMKgywnrpE 340
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1021858603 294 LTKEAMPVVRYRTRDLTRLLPgtarPGFRRmekITGRCDDMMIVRGVNVFPSQIEELILKHAA 356
Cdd:cd05936 341 ETAEAFVDGWLRTGDIGYMDE----DGYFF---IVDRKKDMIIVGGFNVYPREVEEVLYEHPA 396
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
93-356 |
4.85e-10 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 61.28 E-value: 4.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 93 IHASSGTTGKP--TV--VGYTLADIETWAGLVarsiraAGARRGDkVHVSY---GyglFTGGLG-AHYGAERAGLTVIPF 164
Cdd:COG0365 189 ILYTSGTTGKPkgVVhtHGGYLVHAATTAKYV------LDLKPGD-VFWCTadiG---WATGHSyIVYGPLLNGATVVLY 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 165 GGGQT----ERQVQLIRDFEPQIIMVTPSYMLAiadeFERQGMDPAA----SSLQIgIFGA-EPWTPEMRAAIEARMGLS 235
Cdd:COG0365 259 EGRPDfpdpGRLWELIEKYGVTVFFTAPTAIRA----LMKAGDEPLKkydlSSLRL-LGSAgEPLNPEVWEWWYEAVGVP 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 236 AVDIYGLSEVMGP-GVASECAETKDG------PTIwedhfYPEIIDPNtGDVLPDGEFGELVFTsLTKEAMPVVRYRTRD 308
Cdd:COG0365 334 IVDGWGQTETGGIfISNLPGLPVKPGsmgkpvPGY-----DVAVVDED-GNPVPPGEEGELVIK-GPWPGMFRGYWNDPE 406
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1021858603 309 LTR-----LLPGTARPG--FRRMEK----ITGRCDDMMIVRGVNVFPSQIEELILKHAA 356
Cdd:COG0365 407 RYRetyfgRFPGWYRTGdgARRDEDgyfwILGRSDDVINVSGHRIGTAEIESALVSHPA 465
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
96-357 |
6.79e-10 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 60.77 E-value: 6.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 96 SSGTTGKPTVVGYTLADIeTWAGlvARSIRAAGARRGDKVHVS----YGYGLFTGGLGAHYGAerAGLTVIP-FGGGQTE 170
Cdd:cd05934 89 TSGTTGPPKGVVITHANL-TFAG--YYSARRFGLGEDDVYLTVlplfHINAQAVSVLAALSVG--ATLVLLPrFSASRFW 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 171 RQVQLIRDFEPQIIMVTPSYMLAIADEferqgMDPAASSLQIgIFGAEPwTPEMRAAIEARMGLSAVDIYGLSEVmGPGV 250
Cdd:cd05934 164 SDVRRYGATVTNYLGAMLSYLLAQPPS-----PDDRAHRLRA-AYGAPN-PPELHEEFEERFGVRLLEGYGMTET-IVGV 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 251 ASEcaetKDGPTIW------EDHFYPEIIDPNTGDVlPDGEFGELVFTSL---------------TKEAMPVVRYRTRDL 309
Cdd:cd05934 236 IGP----RDEPRRPgsigrpAPGYEVRIVDDDGQEL-PAGEPGELVIRGLrgwgffkgyynmpeaTAEAMRNGWFHTGDL 310
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1021858603 310 TRLLPGtarpGFRRMekiTGRCDDMMIVRGVNVFPSQIEELILKHAAL 357
Cdd:cd05934 311 GYRDAD----GFFYF---VDRKKDMIRRRGENISSAEVERAILRHPAV 351
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
208-358 |
1.33e-09 |
|
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: 59.21 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 208 SSLQIGIFGAEPWTPEMRAAIEARMGLSAVDI-YGLSEVmGPGvaSECAETKDGP-----TIWE--DHFYPEIIDPNTGD 279
Cdd:cd05917 118 SSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIaYGMTET-SPV--STQTRTDDSIekrvnTVGRimPHTEAKIVDPEGGI 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 280 VLPDGEFGELVFT------------SLTKEAMPVVR-YRTRDLTRLLP-GTARpgfrrmekITGRCDDMMIVRGVNVFPS 345
Cdd:cd05917 195 VPPVGVPGELCIRgysvmkgywndpEKTAEAIDGDGwLHTGDLAVMDEdGYCR--------IVGRIKDMIIRGGENIYPR 266
|
170
....*....|...
gi 1021858603 346 QIEELILKHAALS 358
Cdd:cd05917 267 EIEEFLHTHPKVS 279
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
68-356 |
3.65e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 58.38 E-value: 3.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 68 FTTKGDLRENYPfgmfAVPQDRIARIHASSGTTGKPTVV----GYTLADIETWAGLvarsiraAGARRGDKV-------H 136
Cdd:PRK07656 150 FLAAGDPAERAP----EVDPDDVADILFTSGTTGRPKGAmlthRQLLSNAADWAEY-------LGLTEGDRYlaanpffH 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 137 VsYGYglfTGGLGAhygAERAGLTVIPFGGGQTERQVQLIRDFEPQIIMVTPS---YMLAIADeferqGMDPAASSLQIG 213
Cdd:PRK07656 219 V-FGY---KAGVNA---PLMRGATILPLPVFDPDEVFRLIETERITVLPGPPTmynSLLQHPD-----RSAEDLSSLRLA 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 214 IFGAEPWTPEMRAAIEARMGLSAV-DIYGLSEVMG------PGVASECAETKDGPTIWedHFYPEIIDPNtGDVLPDGEF 286
Cdd:PRK07656 287 VTGAASMPVALLERFESELGVDIVlTGYGLSEASGvttfnrLDDDRKTVAGTIGTAIA--GVENKIVNEL-GEEVPVGEV 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 287 GELV---------FTSLTKEAMPVVRY----RTRDLTRLlpgTARPGFRrmekITGRCDDMMIVRGVNVFPSQIEELILK 353
Cdd:PRK07656 364 GELLvrgpnvmkgYYDDPEATAAAIDAdgwlHTGDLGRL---DEEGYLY----IVDRKKDMFIVGGFNVYPAEVEEVLYE 436
|
...
gi 1021858603 354 HAA 356
Cdd:PRK07656 437 HPA 439
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
51-356 |
7.15e-09 |
|
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: 57.61 E-value: 7.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 51 GVHPSDLSSLSDLAKFPFTTkgdlRENYPFGMFAVPQDRIARIHASSGTTGKPTVVGYTLADIETWAGLVARSIRAAgAR 130
Cdd:cd05911 113 DDKPDGVLSIEDLLSPTLGE----EDEDLPPPLKDGKDDTAAILYSSGTTGLPKGVCLSHRNLIANLSQVQTFLYGN-DG 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 131 RGDKV-HVS---YGYGLFTgglgAHYGAERaGLTVIPFGGGQTERQVQLIRDFEPQIIMVTPSYMLAIADEFERQGMDpa 206
Cdd:cd05911 188 SNDVIlGFLplyHIYGLFT----TLASLLN-GATVIIMPKFDSELFLDLIEKYKITFLYLVPPIAAALAKSPLLDKYD-- 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 207 ASSLQIGIFGAEPWTPEMRAAIEARMGLSAV-DIYGLSEVMGPgvaseCAETKDGptiweDHFYP-----------EIID 274
Cdd:cd05911 261 LSSLRVILSGGAPLSKELQELLAKRFPNATIkQGYGMTETGGI-----LTVNPDG-----DDKPGsvgrllpnveaKIVD 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 275 PNTGDVLPDGEFGELVFTSLTK--------EAMPVVR-----YRTRDLtrllpgtarpGFRRMEK---ITGRCDDMMIVR 338
Cdd:cd05911 331 DDGKDSLGPNEPGEICVRGPQVmkgyynnpEATKETFdedgwLHTGDI----------GYFDEDGylyIVDRKKELIKYK 400
|
330
....*....|....*...
gi 1021858603 339 GVNVFPSQIEELILKHAA 356
Cdd:cd05911 401 GFQVAPAELEAVLLEHPG 418
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
97-356 |
8.75e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 57.50 E-value: 8.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 97 SGTTGKPTVVGYTLADIetwAGLVARSIRAAGARRGDKV-------HVsygyglftGGLGAHYGAERAGLT-VIP--Fgg 166
Cdd:PRK06187 176 SGTTGHPKGVVLSHRNL---FLHSLAVCAWLKLSRDDVYlvivpmfHV--------HAWGLPYLALMAGAKqVIPrrF-- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 167 gQTERQVQLIRDFEPQIIMVTPSYMLAIADEFERQGMDpaASSLQIGIFGAEPWTPE-MRAAIEaRMGLSAVDIYGLSEv 245
Cdd:PRK06187 243 -DPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVD--FSSLRLVIYGGAALPPAlLREFKE-KFGIDLVQGYGMTE- 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 246 MGPgVASECAETKDGPTIWEDH-----FYP----EIIDPNtGDVLP--DGEFGELVFTS------------LTKEAMPVV 302
Cdd:PRK06187 318 TSP-VVSVLPPEDQLPGQWTKRrsagrPLPgveaRIVDDD-GDELPpdGGEVGEIIVRGpwlmqgywnrpeATAETIDGG 395
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1021858603 303 RYRTRDLTRLLPGtarpGFRRmekITGRCDDMMIVRGVNVFPSQIEELILKHAA 356
Cdd:PRK06187 396 WLHTGDVGYIDED----GYLY---ITDRIKDVIISGGENIYPRELEDALYGHPA 442
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
87-358 |
8.99e-09 |
|
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: 57.09 E-value: 8.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 87 QDRIARIHASSGTTGKPTVVGYTLADIETWAGLVARSIraAGARRGDKVHVS----YGYGLFTGGLGAHYgaerAGLTVI 162
Cdd:cd05919 90 ADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREA--LGLTPGDRVFSSakmfFGYGLGNSLWFPLA----VGASAV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 163 PFGGGQT-ERQVQLIRDFEPQIIMVTPSYMLAIADE--FERQGMdpaaSSLQIGIFGAEPWTPEMRAAIEARMGLSAVDI 239
Cdd:cd05919 164 LNPGWPTaERVLATLARFRPTVLYGVPTFYANLLDScaGSPDAL----RSLRLCVSAGEALPRGLGERWMEHFGGPILDG 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 240 YGLSEVMGPGVASECAETKDGPTIWEDHFYP-EIIDPNtGDVLPDGEFGELVFTSltkEAMPVVRYRTRDLTR--LLPGT 316
Cdd:cd05919 240 IGATEVGHIFLSNRPGAWRLGSTGRPVPGYEiRLVDEE-GHTIPPGEEGDLLVRG---PSAAVGYWNNPEKSRatFNGGW 315
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1021858603 317 ARPG--FRRME----KITGRCDDMMIVRGVNVFPSQIEELILKHAALS 358
Cdd:cd05919 316 YRTGdkFCRDAdgwyTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVA 363
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
96-356 |
1.24e-08 |
|
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: 56.99 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 96 SSGTTGKPTVVGYTLADIETWAGLVARSIraaGARRGDKVHVSYGYGLFTGGLG-AHYGAERAGLTVIPFGGGQTERQV- 173
Cdd:cd05959 171 SSGSTGRPKGVVHLHADIYWTAELYARNV---LGIREDDVCFSAAKLFFAYGLGnSLTFPLSVGATTVLMPERPTPAAVf 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 174 QLIRDFEPQIIMVTPSY---MLAIADEFERQGmdpaaSSLQIGIFGAEPWTPEMRAAIEARMGLSAVDIYGLSEVMGPGV 250
Cdd:cd05959 248 KRIRRYRPTVFFGVPTLyaaMLAAPNLPSRDL-----SSLRLCVSAGEALPAEVGERWKARFGLDILDGIGSTEMLHIFL 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 251 ASECAETKDGPTIWEDHFYP-EIIDPNTGDVlPDGEFGELVftsLTKEAMPVVRYRTRDLTR--LLPGTARPG--FRRME 325
Cdd:cd05959 323 SNRPGRVRYGTTGKPVPGYEvELRDEDGGDV-ADGEPGELY---VRGPSSATMYWNNRDKTRdtFQGEWTRTGdkYVRDD 398
|
250 260 270
....*....|....*....|....*....|....*
gi 1021858603 326 KIT----GRCDDMMIVRGVNVFPSQIEELILKHAA 356
Cdd:cd05959 399 DGFytyaGRADDMLKVSGIWVSPFEVESALVQHPA 433
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
97-364 |
6.78e-08 |
|
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: 54.46 E-value: 6.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 97 SGTTGKP-TVVGytladieTWAGLVAR---SIRAAGARRGDKV--HVSYGyglFTGGLGAHYGAERAGLTVIPFGGGQT- 169
Cdd:cd05930 102 SGSTGKPkGVMV-------EHRGLVNLllwMQEAYPLTPGDRVlqFTSFS---FDVSVWEIFGALLAGATLVVLPEEVRk 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 170 --ERQVQLIRDFEPQIIMVTPSYMLAIADEferqGMDPAASSLQIGIFGAEPWTPE-MRAAIEARMGLSAVDIYGLSEVM 246
Cdd:cd05930 172 dpEALADLLAEEGITVLHLTPSLLRLLLQE----LELAALPSLRLVLVGGEALPPDlVRRWRELLPGARLVNLYGPTEAT 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 247 GPGVASECAETKDGPT-------IWEDHFYpeIIDPNtGDVLPDGEFGELVFT------------SLTKEA------MPV 301
Cdd:cd05930 248 VDATYYRVPPDDEEDGrvpigrpIPNTRVY--VLDEN-LRPVPPGVPGELYIGgaglargylnrpELTAERfvpnpfGPG 324
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1021858603 302 VR-YRTRDLTRLLP-GTarpgfrrMEKItGRCDDMMIVRGVNVFPSQIEELILKHAALSphyQCV 364
Cdd:cd05930 325 ERmYRTGDLVRWLPdGN-------LEFL-GRIDDQVKIRGYRIELGEIEAALLAHPGVR---EAA 378
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
88-357 |
2.21e-07 |
|
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: 52.77 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 88 DRIARIHASSGTTGKPTVVGYTLadiETWAGLVARSIRAAGARRGDKVHVSYGYGLFTGGLGAHYGAERAGLTVIPFGGG 167
Cdd:cd05903 93 DAVALLLFTSGTTGEPKGVMHSH---NTLSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIW 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 168 QTERQVQLIRDFEPQIIMVTPSYMLAIADEFERQGmdPAASSLQIGIFGAEPWTPEMRAAIEARMGLSAVDIYGLSEVmg 247
Cdd:cd05903 170 DPDKALALMREHGVTFMMGATPFLTDLLNAVEEAG--EPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTEC-- 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 248 PGVASECAETKDGPTIWEDHfYP----EI-IDPNTGDVLPDGEFGELVFTS------------LTKEAMPVVRYRTRDLT 310
Cdd:cd05903 246 PGAVTSITPAPEDRRLYTDG-RPlpgvEIkVVDDTGATLAPGVEGELLSRGpsvflgyldrpdLTADAAPEGWFRTGDLA 324
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1021858603 311 RLLPGtarpGFRRmekITGRCDDMMIVRGVNVFPSQIEELILKHAAL 357
Cdd:cd05903 325 RLDED----GYLR---ITGRSKDIIIRGGENIPVLEVEDLLLGHPGV 364
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
85-289 |
2.23e-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: 53.01 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 85 VPQDRIARIHASSGTTGKPTVVgytladIETWAGLVA-----RSIRAAGARRGDKV-------HVsYGYGLFTgglgahY 152
Cdd:cd05904 155 IKQDDVAALLYSSGTTGRSKGV------MLTHRNLIAmvaqfVAGEGSNSDSEDVFlcvlpmfHI-YGLSSFA------L 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 153 GAERAGLTVIPFGGGQTERQVQLIRDFEPQIIMVTPSYMLAIADEFERQGMDpaASSLQIGIFGAEPWTPEMRAAIEARm 232
Cdd:cd05904 222 GLLRLGATVVVMPRFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYD--LSSLRQIMSGAAPLGKELIEAFRAK- 298
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1021858603 233 gLSAVDI---YGLSEvMGPGVASECAETKDGPTI---------WEdhfyPEIIDPNTGDVLPDGEFGEL 289
Cdd:cd05904 299 -FPNVDLgqgYGMTE-STGVVAMCFAPEKDRAKYgsvgrlvpnVE----AKIVDPETGESLPPNQTGEL 361
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
272-427 |
2.78e-07 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 52.63 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 272 IIDPNTGDVLPDGEFGELVFTS-------LTKEAMpvvryrTRDLTRLLPGTARPGFRRMEK----------ITGRCDDM 334
Cdd:cd05931 368 IVDPETGRELPDGEVGEIWVRGpsvasgyWGRPEA------TAETFGALAATDEGGWLRTGDlgflhdgelyITGRLKDL 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 335 MIVRGVNVFPSQIEELI-LKHAALSPHYQCVLG-KEGPLDTLTVRIEAALGAPADAAASASRQLAHDIKSLIGVT-AAIE 411
Cdd:cd05931 442 IIVRGRNHYPQDIEATAeEAHPALRPGCVAAFSvPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVAREHGVApADVV 521
|
170
....*....|....*..
gi 1021858603 412 ILAAGGIER-SVGKARR 427
Cdd:cd05931 522 LVRPGSIPRtSSGKIQR 538
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
87-367 |
5.50e-07 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 51.71 E-value: 5.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 87 QDRIARIHASSGTTGKPTVVGYTLADIetWAGlVARSIRAAGARRGDKVHVSYGYGLFTGGLGAHYGAERAGLTVIPFGG 166
Cdd:cd05935 83 LDDLALIPYTSGTTGLPKGCMHTHFSA--AAN-ALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMAR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 167 GQTERQVQLIRDFEPQIIMVTPSYMLAIADEFERQGMDpaASSLQIGIFGAEPWTPEMRAAIEARMGLSAVDIYGLSEVM 246
Cdd:cd05935 160 WDRETALELIEKYKVTFWTNIPTMLVDLLATPEFKTRD--LSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETM 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 247 GP--------------GVASECAETKdgptiwedhfypeIIDPNTGDVLPDGEFGELVFT------------SLTKEAMP 300
Cdd:cd05935 238 SQthtnpplrpklqclGIP*FGVDAR-------------VIDIETGRELPPNEVGEIVVRgpqifkgywnrpEETEESFI 304
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1021858603 301 VVR----YRTRDLtrllpgtarpGFRRMEK---ITGRCDDMMIVRGVNVFPSQIEELILKHAALSPhyQCVLGK 367
Cdd:cd05935 305 EIKgrrfFRTGDL----------GYMDEEGyffFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*E--VCVISV 366
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
88-357 |
5.65e-07 |
|
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: 51.71 E-value: 5.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 88 DRIARIHASSGTTGKPTVVGYTLADIETWAGLVARSIraAGARRGD------KVHVSYGYG---LFTGGLGAhygaerag 158
Cdd:cd05958 97 DDICILAFTSGTTGAPKATMHFHRDPLASADRYAVNV--LRLREDDrfvgspPLAFTFGLGgvlLFPFGVGA-------- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 159 lTVIPFGGGQTERQVQLIRDFEPQIIMVTPSYMLAIADEFERQGMDpaASSLQIGIFGAEPWTPEMRAAIEARMGLSAVD 238
Cdd:cd05958 167 -SGVLLEEATPDLLLSAIARYKPTVLFTAPTAYRAMLAHPDAAGPD--LSSLRKCVSAGEALPAALHRAWKEATGIPIID 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 239 IYGLSEVM------GPGVASECAETKDGPTiwedhFYPEIIDpNTGDVLPDGEFGELVFTSLTKeampvvrYRTRDLTRl 312
Cdd:cd05958 244 GIGSTEMFhifisaRPGDARPGATGKPVPG-----YEAKVVD-DEGNPVPDGTIGRLAVRGPTG-------CRYLADKR- 309
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 313 lpgtARPGFRRMEKITG---------------RCDDMMIVRGVNVFPSQIEELILKHAAL 357
Cdd:cd05958 310 ----QRTYVQGGWNITGdtysrdpdgyfrhqgRSDDMIVSGGYNIAPPEVEDVLLQHPAV 365
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
86-358 |
7.12e-07 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 51.31 E-value: 7.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 86 PQDrIARIHASSGTTGKPTVVGYTLADIE----TWA---GLVARSIRAAGArrgdkvhVSYGYGLFTGGLGAhygAERAG 158
Cdd:cd17650 92 PED-LAYVIYTSGTTGKPKGVMVEHRNVAhaahAWRreyELDSFPVRLLQM-------ASFSFDVFAGDFAR---SLLNG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 159 LTVIPFGGG---QTERQVQLIRDFEPQIIMVTPSYMLAIADEFERQGMDPaaSSLQIGIFGAEPWTPEMRAAIEARMGLS 235
Cdd:cd17650 161 GTLVICPDEvklDPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDL--SAMRLLIVGSDGCKAQDFKTLAARFGQG 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 236 AVDI--YGLSEVMgpgVASECAETKDGPTIWED-----------HFYpeIIDPnTGDVLPDGEFGELVF----------- 291
Cdd:cd17650 239 MRIInsYGVTEAT---IDSTYYEEGRDPLGDSAnvpigrplpntAMY--VLDE-RLQPQPVGVAGELYIggagvargyln 312
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1021858603 292 -TSLTKEAM------PVVR-YRTRDLTRLLP-GTARpgfrrmekITGRCDDMMIVRGVNVFPSQIEELILKHAALS 358
Cdd:cd17650 313 rPELTAERFvenpfaPGERmYRTGDLARWRAdGNVE--------LLGRVDHQVKIRGFRIELGEIESQLARHPAID 380
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
188-357 |
8.82e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 50.93 E-value: 8.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 188 PSYMLAIADEFERQGMDpaASSLQIGIFGAEPWTPEMRAAIEARMGLSAVDI-YGLSEVmGPgVASECAETKDGPTIWED 266
Cdd:PRK12583 299 PTMFIAELDHPQRGNFD--LSSLRTGIMAGAPCPIEVMRRVMDEMHMAEVQIaYGMTET-SP-VSLQTTAADDLERRVET 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 267 ------HFYPEIIDPNtGDVLPDGEFGELVFTSL------------TKEAMPVVRY-RTRDLTRLlpgtARPGFRRmekI 327
Cdd:PRK12583 375 vgrtqpHLEVKVVDPD-GATVPRGEIGELCTRGYsvmkgywnnpeaTAESIDEDGWmHTGDLATM----DEQGYVR---I 446
|
170 180 190
....*....|....*....|....*....|
gi 1021858603 328 TGRCDDMMIVRGVNVFPSQIEELILKHAAL 357
Cdd:PRK12583 447 VGRSKDMIIRGGENIYPREIEEFLFTHPAV 476
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
84-354 |
2.38e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 49.61 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 84 AVPQDRIARIHASSGTTGKPTvvgytladietWAGLVARSIRAAGAR-------RGDKVHVSYG-------YGL-FTGGL 148
Cdd:PRK05605 215 RPTPDDVALILYTSGTTGKPK-----------GAQLTHRNLFANAAQgkawvpgLGDGPERVLAalpmfhaYGLtLCLTL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 149 GAHYGAEragltvipfgggqterqVQLIRDFEPQIIMV-----TPSYMLA-------IADEFERQGMDpaASSLQIGIFG 216
Cdd:PRK05605 284 AVSIGGE-----------------LVLLPAPDIDLILDamkkhPPTWLPGvpplyekIAEAAEERGVD--LSGVRNAFSG 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 217 AEPWTPEMRAAIEARMGLSAVDIYGLSEVMGPGVASECAETKDGPTIWEDhfYPE----IIDPNTGDV-LPDGEFGEL-- 289
Cdd:PRK05605 345 AMALPVSTVELWEKLTGGLLVEGYGLTETSPIIVGNPMSDDRRPGYVGVP--FPDtevrIVDPEDPDEtMPDGEEGELlv 422
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1021858603 290 ----VFT------SLTKEAMPVVRYRTRDLTRLLPGtarpGFRRmekITGRCDDMMIVRGVNVFPSQIEELILKH 354
Cdd:PRK05605 423 rgpqVFKgywnrpEETAKSFLDGWFRTGDVVVMEED----GFIR---IVDRIKELIITGGFNVYPAEVEEVLREH 490
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
87-356 |
3.08e-06 |
|
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: 49.26 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 87 QDRIARIHASSGTTGKPTVV----GYTLADIETWAGLVarsiraaGARRGDKVHVSYGYGLFTGGLGAHYGAERAGLTVI 162
Cdd:cd05972 80 AEDPALIYFTSGTTGLPKGVlhthSYPLGHIPTAAYWL-------GLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVF 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 163 PFGGGQ--TERQVQLIRDFEPQIIMVTPS-YMLAIADEFERQgmdpAASSLQIGIFGAEPWTPEMRAAIEARMGLSAVDI 239
Cdd:cd05972 153 VYEGPRfdAERILELLERYGVTSFCGPPTaYRMLIKQDLSSY----KFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDG 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 240 YGLSEVMGPGVASECAETKDG----PTiweDHFYPEIIDPNtGDVLPDGEFGELV-----------FTSLTKEAMPVVR- 303
Cdd:cd05972 229 YGQTETGLTVGNFPDMPVKPGsmgrPT---PGYDVAIIDDD-GRELPPGEEGDIAiklpppglflgYVGDPEKTEASIRg 304
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1021858603 304 --YRTRDLTRLLPgtarPGFRRMEkitGRCDDMMIVRGVNVFPSQIEELILKHAA 356
Cdd:cd05972 305 dyYLTGDRAYRDE----DGYFWFV---GRADDIIKSSGYRIGPFEVESALLEHPA 352
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
73-357 |
5.11e-06 |
|
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: 48.66 E-value: 5.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 73 DLRENYPFG-MFAVPQDRI---ARIHASSGTTGKPTVVGYTLADIETWAGLVARSiraAGARRGDK---------VHVSY 139
Cdd:cd05923 131 GLGEPESAGpLIEDPPREPeqpAFVFYTSGTTGLPKGAVIPQRAAESRVLFMSTQ---AGLRHGRHnvvlglmplYHVIG 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 140 GYGLFTGGLGAhygaeraGLTVIPFGGGQTERQVQLIRDFEPQIIMVTPSYMLAIADEFERQGMDpaASSLQIGIFGAEP 219
Cdd:cd05923 208 FFAVLVAALAL-------DGTYVVVEEFDPADALKLIEQERVTSLFATPTHLDALAAAAEFAGLK--LSSLRHVTFAGAT 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 220 WTPEMRAAIEARMGLSAVDIYGLSEVMGPGV---ASECAETKDGptiwedhFYPEI----IDPNTGDVLPDGEFGELVFT 292
Cdd:cd05923 279 MPDAVLERVNQHLPGEKVNIYGTTEAMNSLYmrdARTGTEMRPG-------FFSEVrivrIGGSPDEALANGEEGELIVA 351
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1021858603 293 SLTKEAMpvVRYRTR---DLTRLLPG---TARPGFRRME---KITGRCDDMMIVRGVNVFPSQIEELILKHAAL 357
Cdd:cd05923 352 AAADAAF--TGYLNQpeaTAKKLQDGwyrTGDVGYVDPSgdvRILGRVDDMIISGGENIHPSEIERVLSRHPGV 423
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
204-366 |
6.46e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 48.50 E-value: 6.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 204 DPAA-----SSLQIGIFGAEPWTPEMRAAIEARMGLSAVDIYGLSEVMG------PGVASEcaetKDGPtiwEDHF---- 268
Cdd:PRK07470 271 HPAVdrydhSSLRYVIYAGAPMYRADQKRALAKLGKVLVQYFGLGEVTGnitvlpPALHDA----EDGP---DARIgtcg 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 269 YP------EIIDPNtGDVLPDGEFGEL------VFTSL------TKEAMPVVRYRTRDLTRLlpgTARpGFRRmekITGR 330
Cdd:PRK07470 344 FErtgmevQIQDDE-GRELPPGETGEIcvigpaVFAGYynnpeaNAKAFRDGWFRTGDLGHL---DAR-GFLY---ITGR 415
|
170 180 190
....*....|....*....|....*....|....*.
gi 1021858603 331 CDDMMIVRGVNVFPSQIEELILKHAALSPhyQCVLG 366
Cdd:PRK07470 416 ASDMYISGGSNVYPREIEEKLLTHPAVSE--VAVLG 449
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
96-358 |
8.13e-06 |
|
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: 47.96 E-value: 8.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 96 SSGTTGKPTVVGYTLADIETWAGLVARSIRAAGArrGDKVHVSYGYGLFTGGLGAHYGAERAGLTVIPFGGG----QTER 171
Cdd:cd17634 240 TSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGP--GDIYWCTADVGWVTGHSYLLYGPLACGATTLLYEGVpnwpTPAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 172 QVQLIRDFEPQIIMVTPSYMLAIA----DEFERQGMdpaaSSLQIgIFGA-EPWTPEMRAAIEARMGLS---AVDIYGLS 243
Cdd:cd17634 318 MWQVVDKHGVNILYTAPTAIRALMaagdDAIEGTDR----SSLRI-LGSVgEPINPEAYEWYWKKIGKEkcpVVDTWWQT 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 244 EVMG------PGVASECAETKDGPTIwedHFYPEIIDpNTGDVLPDGEFGELVftsltkeampvvryrtrdLTRLLPGTA 317
Cdd:cd17634 393 ETGGfmitplPGAIELKAGSATRPVF---GVQPAVVD-NEGHPQPGGTEGNLV------------------ITDPWPGQT 450
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1021858603 318 RPGFRRMEK----------------------------ITGRCDDMMIVRGVNVFPSQIEELILKHAALS 358
Cdd:cd17634 451 RTLFGDHERfeqtyfstfkgmyfsgdgarrdedgyywITGRSDDVINVAGHRLGTAEIESVLVAHPKVA 519
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
208-354 |
3.37e-05 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 45.96 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 208 SSLQIGIFGAEPwTPE--MRAAIEaRMGLSAVDI-YGLSE---VMgpgvaseCAETKDGP------TIWEDHFYPE--II 273
Cdd:PRK08315 315 SSLRTGIMAGSP-CPIevMKRVID-KMHMSEVTIaYGMTEtspVS-------TQTRTDDPlekrvtTVGRALPHLEvkIV 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 274 DPNTGDVLPDGEFGELVfT-------------SLTKEAMPVVRY-RTRDLtrllpGTARP-GFRRmekITGRCDDMMIVR 338
Cdd:PRK08315 386 DPETGETVPRGEQGELC-TrgysvmkgywndpEKTAEAIDADGWmHTGDL-----AVMDEeGYVN---IVGRIKDMIIRG 456
|
170
....*....|....*.
gi 1021858603 339 GVNVFPSQIEELILKH 354
Cdd:PRK08315 457 GENIYPREIEEFLYTH 472
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
90-354 |
3.41e-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: 45.57 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 90 IARIHASSGTTGKPTVV----GYTLADIETWAGLvarsiraAGARRGDKVHV------SYGY--GLFTGGLgahygaerA 157
Cdd:cd17638 2 VSDIMFTSGTTGRSKGVmcahRQTLRAAAAWADC-------ADLTEDDRYLIinpffhTFGYkaGIVACLL--------T 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 158 GLTVIPFGGGQTERQVQLIRDFEPQIIMVTPSYMLAIADEFERQGMDpaASSLQIGIFGAEPWTPEMRAAIEARMGLSAV 237
Cdd:cd17638 67 GATVVPVAVFDVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFD--LSSLRAAVTGAATVPVELVRRMRSELGFETV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 238 -DIYGLSEVmgpGVASECAETKDGPTIWE------DHFYPEIIDPntGDVLPDGE---FGELVFTSLTKEAMPVVRY-RT 306
Cdd:cd17638 145 lTAYGLTEA---GVATMCRPGDDAETVATtcgracPGFEVRIADD--GEVLVRGYnvmQGYLDDPEATAEAIDADGWlHT 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1021858603 307 RDLTRLlpgTARPGFRrmekITGRCDDMMIVRGVNVFPSQIEELILKH 354
Cdd:cd17638 220 GDVGEL---DERGYLR----ITDRLKDMYIVGGFNVYPAEVEGALAEH 260
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
272-351 |
4.59e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 45.93 E-value: 4.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 272 IIDPNTGDVLPDGEFGElVFTSLTKEAMPVVR-----------------YRTRDLtrllpgtarpGFRRMEK--ITGRCD 332
Cdd:PRK05691 383 IVDPQSLEVLGDNRVGE-IWASGPSIAHGYWRnpeasaktfvehdgrtwLRTGDL----------GFLRDGElfVTGRLK 451
|
90
....*....|....*....
gi 1021858603 333 DMMIVRGVNVFPSQIEELI 351
Cdd:PRK05691 452 DMLIVRGHNLYPQDIEKTV 470
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
93-354 |
6.14e-05 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 45.50 E-value: 6.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 93 IHASSGTTGKPTVV----GYTLADIE-TWAGLVARSIraagarrgDKV---HVSYGYGLFTGGLgahYGAERAGLTVIPF 164
Cdd:PTZ00237 259 ILYTSGTTGNSKAVvrsnGPHLVGLKyYWRSIIEKDI--------PTVvfsHSSIGWVSFHGFL---YGSLSLGNTFVMF 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 165 GGGQTeRQVQLIRDFEPQIIMVTPSYMLAIADEFERQ-GMDPAA---------SSLQIGIFGAEPWTPEMRAAIEARMGL 234
Cdd:PTZ00237 328 EGGII-KNKHIEDDLWNTIEKHKVTHTLTLPKTIRYLiKTDPEAtiirskydlSNLKEIWCGGEVIEESIPEYIENKLKI 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 235 SAVDIYGLSE-----VMGPGVASECAETKDGPTIWedhFYPEIIDPNtGDVLPDGEFGELVFtsltKEAMP----VVRYR 305
Cdd:PTZ00237 407 KSSRGYGQTEigityLYCYGHINIPYNATGVPSIF---IKPSILSED-GKELNVNEIGEVAF----KLPMPpsfaTTFYK 478
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1021858603 306 TRDLTRLL----PGTARPG---FRRME---KITGRCDDMMIVRGVNVFPSQIEELILKH 354
Cdd:PTZ00237 479 NDEKFKQLfskfPGYYNSGdlgFKDENgyyTIVSRSDDQIKISGNKVQLNTIETSILKH 537
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
88-358 |
6.45e-05 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 45.04 E-value: 6.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 88 DRIARIHASSGTTGKPTVVGYTLADIetWAGLVArSIRAAGARRGDKVHVSYGYGLFTGGLgahYGAEragltvIPFGGG 167
Cdd:PRK13295 197 DDVTQLIYTSGTTGEPKGVMHTANTL--MANIVP-YAERLGLGADDVILMASPMAHQTGFM---YGLM------MPVMLG 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 168 QT---------ERQVQLIRDFEPQIIMVTPSYMLAIADEFERQGMDpaASSLQIGIFGAEPWTPEMRAAIEARMGLSAVD 238
Cdd:PRK13295 265 ATavlqdiwdpARAAELIRTEGVTFTMASTPFLTDLTRAVKESGRP--VSSLRTFLCAGAPIPGALVERARAALGAKIVS 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 239 IYGLSE-----VMGPGVASECAETKDGptiwedhfYP------EIIDPNtGDVLPDGEFGELVFTS-------LTKEAMP 300
Cdd:PRK13295 343 AWGMTEngavtLTKLDDPDERASTTDG--------CPlpgvevRVVDAD-GAPLPAGQIGRLQVRGcsnfggyLKRPQLN 413
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1021858603 301 VVR----YRTRDLTRLLPGtarpGFRRmekITGRCDDMMIVRGVNVFPSQIEELILKHAALS 358
Cdd:PRK13295 414 GTDadgwFDTGDLARIDAD----GYIR---ISGRSKDVIIRGGENIPVVEIEALLYRHPAIA 468
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
272-358 |
1.17e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 44.26 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 272 IIDPNTGDVLPDGEFGELVFTS------------LTKEAMPVVRYRTRDLTRLlpgTARPGFRRMekitGRCDDMMIVRG 339
Cdd:PRK06178 400 ICDFETGELLPLGAEGEIVVRTpsllkgywnkpeATAEALRDGWLHTGDIGKI---DEQGFLHYL----GRRKEMLKVNG 472
|
90
....*....|....*....
gi 1021858603 340 VNVFPSQIEELILKHAALS 358
Cdd:PRK06178 473 MSVFPSEVEALLGQHPAVL 491
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
327-354 |
3.12e-04 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 42.39 E-value: 3.12e-04
10 20
....*....|....*....|....*...
gi 1021858603 327 ITGRCDDMMIVRGVNVFPSQIEELILKH 354
Cdd:cd17633 226 LVGRESDMIIIGGINIFPTEIESVLKAI 253
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
95-354 |
4.67e-04 |
|
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: 42.36 E-value: 4.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 95 ASSGTTGKPTVV----GYTLADIET---WAGLVARSiraagarrGDKVHVSYGYGLFTGGLGAHYGAERAGLTVIPFGGG 167
Cdd:cd05929 132 YSGGTTGRPKGIkrglPGGPPDNDTlmaAALGFGPG--------ADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLMEKF 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 168 QTERQVQLIRDFEPQIIMVTPSY---MLAIADEfERQGMDpaASSLQIGIFGAEPWTPEMRAAIEARMGLSAVDIYGLSE 244
Cdd:cd05929 204 DPEEFLRLIERYRVTFAQFVPTMfvrLLKLPEA-VRNAYD--LSSLKRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGGTE 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 245 vmgpGVASECAETKDgptiWEDHfyP-----------EIIDPNtGDVLPDGEFGELVFTsltkeAMPVVRYrTRDLTRLL 313
Cdd:cd05929 281 ----GQGLTIINGEE----WLTH--PgsvgravlgkvHILDED-GNEVPPGEIGEVYFA-----NGPGFEY-TNDPEKTA 343
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1021858603 314 PGTARPGFRRMEKI-----------TGRCDDMMIVRGVNVFPSQIEELILKH 354
Cdd:cd05929 344 AARNEGGWSTLGDVgyldedgylylTDRRSDMIISGGVNIYPQEIENALIAH 395
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
89-358 |
9.09e-04 |
|
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: 41.51 E-value: 9.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 89 RIARIHASSGTTGKPTVVGYTLADIETwaglVARSIRAAGARRGDKV--HV---SYGYGLFTGGLGAHYgaerAGLTVI- 162
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAA----NVRALVDAWRWTEDDVllHVlplHHVHGLVNALLCPLF----AGASVEf 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 163 --PFgggqtERQVQLIRDFEPQI--IMVTPSYMLAIADEFERQGMDP------AASSLQIGIFGAEPWTPEMRAAIEARM 232
Cdd:cd05941 162 lpKF-----DPKEVAISRLMPSItvFMGVPTIYTRLLQYYEAHFTDPqfaraaAAERLRLMVSGSAALPVPTLEEWEAIT 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 233 GLSAVDIYGLSEVmgpGVASEC---AETKDGPTIWedhfyP------EIIDPNTGDVLPDGEFGEL------VFTSL--- 294
Cdd:cd05941 237 GHTLLERYGMTEI---GMALSNpldGERRPGTVGM-----PlpgvqaRIVDEETGEPLPRGEVGEIqvrgpsVFKEYwnk 308
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1021858603 295 ---TKEAMPVVRY-RTRDLtrllpgtarpGFRRME---KITGRCDDMMI-VRGVNVFPSQIEELILKHAALS 358
Cdd:cd05941 309 peaTKEEFTDDGWfKTGDL----------GVVDEDgyyWILGRSSVDIIkSGGYKVSALEIERVLLAHPGVS 370
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
150-352 |
1.35e-03 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 40.71 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 150 AHYGAERAGLTVIPFGGG--------QTERQVQLIRDFEPQIIMVTPSYMLAIADEFerQGMDPAASSLQIGIFGAEPWT 221
Cdd:cd17635 53 THIGGLWWILTCLIHGGLcvtggentTYKSLFKILTTNAVTTTCLVPTLLSKLVSEL--KSANATVPSLRLIGYGGSRAI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 222 PEMRAAIEARMGLSAVDIYGLSEVmgpgVASECAETKDGPTIWED--HFYP----EIIDpNTGDVLPDGEFGELVFTSlt 295
Cdd:cd17635 131 AADVRFIEATGLTNTAQVYGLSET----GTALCLPTDDDSIEINAvgRPYPgvdvYLAA-TDGIAGPSASFGTIWIKS-- 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1021858603 296 kEAMPVVRYRTRDLT--RLLPG---TARPGFRRMEK---ITGRCDDMMIVRGVNVFPSQIEELIL 352
Cdd:cd17635 204 -PANMLGYWNNPERTaeVLIDGwvnTGDLGERREDGflfITGRSSESINCGGVKIAPDEVERIAE 267
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
96-353 |
1.94e-03 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 40.45 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 96 SSGTTGKPTVVGYTLADIETWAGLVARSIRAAGARRGDKV-------HVS-YGYGLFTGGLGAhygaeraGLTVIP-Fgg 166
Cdd:PRK12406 160 TSGTTGHPKGVRRAAPTPEQAAAAEQMRALIYGLKPGIRAlltgplyHSApNAYGLRAGRLGG-------VLVLQPrF-- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 167 gQTERQVQLIRDFEPQIIMVTPSY---MLAIADEFeRQGMDpaASSLQIGIFGAEPWTPEMRAAIEARMGLSAVDIYGLS 243
Cdd:PRK12406 231 -DPEELLQLIERHRITHMHMVPTMfirLLKLPEEV-RAKYD--VSSLRHVIHAAAPCPADVKRAMIEWWGPVIYEYYGST 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 244 EVmgpGVA----SECAETKDGPT--IWEDHFYpEIIDPNtGDVLPDGEFGELVFTSltkEAMPVVRYRTRDltrllpgTA 317
Cdd:PRK12406 307 ES---GAVtfatSEDALSHPGTVgkAAPGAEL-RFVDED-GRPLPQGEIGEIYSRI---AGNPDFTYHNKP-------EK 371
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1021858603 318 RPGFRRMEKIT----------GR---CD---DMMIVRGVNVFPSQIEELILK 353
Cdd:PRK12406 372 RAEIDRGGFITsgdvgyldadGYlflCDrkrDMVISGGVNIYPAEIEAVLHA 423
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
96-356 |
2.45e-03 |
|
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: 40.04 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 96 SSGTTGKPTVVGYTLADIetwAGLVARSIRAAGARRGDKVHVSYGYGlFTGGLGAHYGAERAGLTVIPFGGGQ---TERQ 172
Cdd:cd17649 102 TSGSTGTPKGVAVSHGPL---AAHCQATAERYGLTPGDRELQFASFN-FDGAHEQLLPPLICGACVVLRPDELwasADEL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 173 VQLIRDFEPQIIMVTPSYMLAIADEFERQGMDPAASsLQIGIFGAEPWTPE-MRAAIEARMGLsaVDIYGLSE-VMGPGV 250
Cdd:cd17649 178 AEMVRELGVTVLDLPPAYLQQLAEEADRTGDGRPPS-LRLYIFGGEALSPElLRRWLKAPVRL--FNAYGPTEaTVTPLV 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 251 ASECAETKDGPTiwedhfYPEI----------IDPNTGDVLPDGEFGELVFTS------------LTKE-------AMPV 301
Cdd:cd17649 255 WKCEAGAARAGA------SMPIgrplggrsayILDADLNPVPVGVTGELYIGGeglargylgrpeLTAErfvpdpfGAPG 328
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1021858603 302 VR-YRTRDLTRLLP-GTArpgfrrmeKITGRCDDMMIVRGVNVFPSQIEELILKHAA 356
Cdd:cd17649 329 SRlYRTGDLARWRDdGVI--------EYLGRVDHQVKIRGFRIELGEIEAALLEHPG 377
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
191-356 |
4.50e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 39.16 E-value: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 191 MLAIADEFERQGMDPAASSLqigIFGAEPwtPEmrAAIEA--RMGLSAVDIYGLSEVMGPgvASECAEtKDGptiWEDHF 268
Cdd:PRK08162 283 ALINAPAEWRAGIDHPVHAM---VAGAAP--PA--AVIAKmeEIGFDLTHVYGLTETYGP--ATVCAW-QPE---WDALP 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 269 YPE-------------------IIDPNTGDVLP-DGE-FGELVF------------TSLTKEAMPVVRYRTRDLTRLLP- 314
Cdd:PRK08162 350 LDEraqlkarqgvryplqegvtVLDPDTMQPVPaDGEtIGEIMFrgnivmkgylknPKATEEAFAGGWFHTGDLAVLHPd 429
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1021858603 315 GTArpgfrrmeKITGRCDDMMIVRGVNVFPSQIEELILKHAA 356
Cdd:PRK08162 430 GYI--------KIKDRSKDIIISGGENISSIEVEDVLYRHPA 463
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
327-354 |
4.78e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 39.14 E-value: 4.78e-03
10 20
....*....|....*....|....*...
gi 1021858603 327 ITGRCDDMMIVRGVNVFPSQIEELILKH 354
Cdd:PRK07788 445 VDGRDDDMIVSGGENVFPAEVEDLLAGH 472
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
88-357 |
5.07e-03 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 39.56 E-value: 5.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 88 DRIARIHASSGTTGKPTVVGYTLADIETWAGLVARsirAAGARRGDKVhVSYGYGLFTGGLGAHYGAERAGLTVIPFGGG 167
Cdd:PRK12316 3196 ENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQ---AYGLGVGDRV-LQFTTFSFDVFVEELFWPLMSGARVVLAGPE 3271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 168 QTERQVQLIRDFEPQIIMVTPSYMLAIADEFERQGMDpAASSLQIGIFGAEPWTPEMRAAIEArmGLSAVDIYGLSEVMG 247
Cdd:PRK12316 3272 DWRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAH-RCTSLKRIVCGGEALPADLQQQVFA--GLPLYNLYGPTEATI 3348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 248 PGVASECAE-TKDGPTIWEDHFYPEI-IDPNTGDVLPDGEFGELVF------------TSLTKEAM------PVVR-YRT 306
Cdd:PRK12316 3349 TVTHWQCVEeGKDAVPIGRPIANRACyILDGSLEPVPVGALGELYLggeglargyhnrPGLTAERFvpdpfvPGERlYRT 3428
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1021858603 307 RDLtrllpgtARPGFRRMEKITGRCDDMMIVRGVNVFPSQIEELILKHAAL 357
Cdd:PRK12316 3429 GDL-------ARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWV 3472
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
88-357 |
6.50e-03 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 39.17 E-value: 6.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 88 DRIARIHASSGTTGKPTVVGYT---LADIETWAglVARSIRAAGARRGDKVHVSYGYGL--FTGGLgahygAERAGLTVI 162
Cdd:PRK12316 655 ENLAYVIYTSGSTGKPKGAGNRhraLSNRLCWM--QQAYGLGVGDTVLQKTPFSFDVSVweFFWPL-----MSGARLVVA 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 163 PFGGGQT-ERQVQLIRDFEPQIIMVTPSYMLAiadeFERQGMDPAASSLQIGIFGAEPWTPEMRAAIEARMGLSAV-DIY 240
Cdd:PRK12316 728 APGDHRDpAKLVELINREGVDTLHFVPSMLQA----FLQDEDVASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLyNLY 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858603 241 GLSEVMGPGVASECA-ETKDGPTIWED--HFYPEIIDPNTGDVlPDGEFGELVFT------------SLTKE---AMPVV 302
Cdd:PRK12316 804 GPTEAAIDVTHWTCVeEGGDSVPIGRPiaNLACYILDANLEPV-PVGVLGELYLAgrglargyhgrpGLTAErfvPSPFV 882
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1021858603 303 ----RYRTRDLTRLlpgtarpgfRRMEKI--TGRCDDMMIVRGVNVFPSQIEELILKHAAL 357
Cdd:PRK12316 883 agerMYRTGDLARY---------RADGVIeyAGRIDHQVKLRGLRIELGEIEARLLEHPWV 934
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
326-354 |
7.31e-03 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 38.46 E-value: 7.31e-03
10 20
....*....|....*....|....*....
gi 1021858603 326 KITGRCDDMMIVRGVNVFPSQIEELILKH 354
Cdd:PRK07059 452 KIVDRKKDMILVSGFNVYPNEIEEVVASH 480
|
|
| |
