|
Name |
Accession |
Description |
Interval |
E-value |
| PA_CoA_ligase |
TIGR02155 |
phenylacetate-CoA ligase; Phenylacetate-CoA ligase (PA-CoA ligase) catalyzes the first step in ... |
11-432 |
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: 844.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 11 ETASVDELQALQTQRLKWTLKHAYENVPMYRRKFDAAGVHPDDFRELSDLRKFPCTTKQDLRDNYPFDTFAVPMEQVVRI 90
Cdd:TIGR02155 1 ETASLDELRALQTQRLKWTVKHAYENVPHYRKAFDAAGVHPDDLQSLSDLAKFPFTQKHDLRDNYPFGLFAVPREQVVRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 91 HASSGTTGKPTVVGYTQNDIDNWANIVARSLRAAGGTPKDKIHVAYGYGLFTGGLGAHYGAERLGATVIPMSGGQTEKQA 170
Cdd:TIGR02155 81 HASSGTTGKPTVVGYTQNDIDTWSSVVARSIRAAGGRPGDLIHNAYGYGLFTGGLGAHYGAEKLGCTVVPISGGQTEKQV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 171 QLIRDFQPDMIMVTPSYCLNLIEELERQlGGDASGCSLRVGVFGAEPWTQAMRKEIERRLGITALDIYGLSEVMGPGVAM 250
Cdd:TIGR02155 161 QLIQDFKPDIIMVTPSYMLNLLEELKRM-GIDPAQTSLQVGIFGAEPWTNAMRKEIEARLGMKATDIYGLSEVIGPGVAM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 251 ECLETTDGPTIWEDHFYPEIVNPHDGTPLADGEHGELLFTTLTKEALPVIRYRTRDLTRLLPGTARTMRRMDRISGRSDD 330
Cdd:TIGR02155 240 ECVETQDGLHIWEDHFYPEIIDPHTGEVLPDGEEGELVFTTLTKEALPVIRYRTRDLTRLLPGTARTMRRMDRITGRSDD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 331 MLIIRGVNVFPSQLEEEIVKFEHLSPHYQLEVNRRGHLDSLSVKVELK-ESSLTLTHEQRCQVCHQLRHRIKSMVGISTD 409
Cdd:TIGR02155 320 MLIIRGVNVFPTQLEEVILKMDELSPHYQLELTRNGHMDELTLKVELKpESYTLRLHEQASLLAGEIQHTIKQEVGVSMD 399
|
410 420
....*....|....*....|...
gi 323157347 410 VMIVNCGSIPRSEGKACRVFDLR 432
Cdd:TIGR02155 400 VHLVEPGSLPRSEGKARRVVDLR 422
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
8-432 |
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: 711.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 8 DPIETASVDELQALQTQRLKWTLKHAYENVPMYRRKFDAAGVHPDDFRELSDLRKFPCTTKQDLRDNYPFDTFAVPMEQV 87
Cdd:cd05913 1 EEIETMSRDELDALQLARLKWTVRHAYENVPFYRRKFAAAGIDPDDIKSLDDLRKLPFTTKEDLRDNYPFGLFAVPREKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 88 VRIHASSGTTGKPTVVGYTQNDIDNWANIVARSLRAAGGTPKDKIHVAYGYGLFTGGLGAHYGAERLGATVIPMSGGQTE 167
Cdd:cd05913 81 VRIHASSGTTGKPTVVGYTKNDLDVWAELVARCLDAAGVTPGDRVQNAYGYGLFTGGLGFHYGAERLGALVIPAGGGNTE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 168 KQAQLIRDFQPDMIMVTPSYCLNLIEELERQlGGDASGCSLRVGVFGAEPWTQAMRKEIERRLGITALDIYGLSEVMGPG 247
Cdd:cd05913 161 RQLQLIKDFGPTVLCCTPSYALYLAEEAEEE-GIDPRELSLKVGIFGAEPWTEEMRKRIERRLGIKAYDIYGLTEIIGPG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 248 VAMECLEtTDGPTIWEDHFYPEIVNPHDGTPLADGEHGELLFTTLTKEALPVIRYRTRDLTRLLPGTA---RTMRRMDRI 324
Cdd:cd05913 240 VAFECEE-KDGLHIWEDHFIPEIIDPETGEPVPPGEVGELVFTTLTKEAMPLIRYRTRDITRLLPGPCpcgRTHRRIDRI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 325 SGRSDDMLIIRGVNVFPSQLEEEIVKFEHLSPHYQLEVNRRGHLDSLSVKVELKESSltLTHEQRCQVCHQLRHRIKSMV 404
Cdd:cd05913 319 TGRSDDMLIIRGVNVFPSQIEDVLLKIPGLGPHYQLILTRQEHLDELTIKVEVRPEA--DDDEKLEALKQRLERHIKSVL 396
|
410 420
....*....|....*....|....*...
gi 323157347 405 GISTDVMIVNCGSIPRSEGKACRVFDLR 432
Cdd:cd05913 397 GVTVEVELVEPGSLPRSEGKAKRVIDKR 424
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
3-431 |
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: 677.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 3 TNTKLDPIETASVDELQALQTQRLKWTLKHAYENVPMYRRKFDAAGVHPDDFRELSDLRKFPCTTKQDLRDNYPFDTFAV 82
Cdd:COG1541 1 SEMYWNPIETLSREELEALQLERLRATVARAYENSPFYRRKFDEAGVDPDDIKSLEDLAKLPFTTKEDLRDNYPFGLFAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 83 PMEQVVRIHASSGTTGKPTVVGYTQNDIDNWANIVARSLRAAGGTPKDKIHVAYGYGLFTGGLGAHYGAERLGATVIPMS 162
Cdd:COG1541 81 PLEEIVRIHASSGTTGKPTVVGYTRKDLDRWAELFARSLRAAGVRPGDRVQNAFGYGLFTGGLGLHYGAERLGATVIPAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 163 GGQTEKQAQLIRDFQPDMIMVTPSYCLNLIEELERQlGGDASGCSLRVGVFGAEPWTQAMRKEIERRLGITALDIYGLSE 242
Cdd:COG1541 161 GGNTERQLRLMQDFGPTVLVGTPSYLLYLAEVAEEE-GIDPRDLSLKKGIFGGEPWSEEMRKEIEERWGIKAYDIYGLTE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 243 vMGPGVAMEClETTDGPTIWEDHFYPEIVNPHDGTPLADGEHGELLFTTLTKEALPVIRYRTRDLTRLLPG---TARTMR 319
Cdd:COG1541 240 -VGPGVAYEC-EAQDGLHIWEDHFLVEIIDPETGEPVPEGEEGELVVTTLTKEAMPLIRYRTGDLTRLLPEpcpCGRTHP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 320 RMDRISGRSDDMLIIRGVNVFPSQLEEEIVKFEHLSPHYQLEVNRRGHLDSLSVKVELKESsltlthEQRCQVCHQLRHR 399
Cdd:COG1541 318 RIGRILGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYQIVVDREGGLDELTVRVELAPG------ASLEALAEAIAAA 391
|
410 420 430
....*....|....*....|....*....|..
gi 323157347 400 IKSMVGISTDVMIVNCGSIPRSEGKACRVFDL 431
Cdd:COG1541 392 LKAVLGLRAEVELVEPGSLPRSEGKAKRVIDR 423
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
86-350 |
2.48e-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: 147.05 E-value: 2.48e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 86 QVVRIHASSGTTGKPTVVGYTQNDIDNWANIVARSLraaGGTPKDKIHVAYGYGlFTGGLGAHYGAERLGATVIPMSGGQ 165
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASG---GLTEGDVFLSTLPLF-HIGGLFGLLGALLAGGTVVLLPKFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 166 TEKQAQLIRDFQPDMIMVTPSYcLNLIEELERQLGGDASgcSLRVGVFGAEPWTQAMRKEIERRLGITALDIYGLSEVMG 245
Cdd:cd04433 77 PEAALELIEREKVTILLGVPTL-LARLLKAPESAGYDLS--SLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 246 PGVAM-----ECLETTDGPTIweDHFYPEIVNPhDGTPLADGEHGELLFTT------------LTKEALPVIRYRTRDLT 308
Cdd:cd04433 154 TVATGppdddARKPGSVGRPV--PGVEVRIVDP-DGGELPPGEIGELVVRGpsvmkgywnnpeATAAVDEDGWYRTGDLG 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 323157347 309 RLLPgtartmrrmD---RISGRSDDMLIIRGVNVFPSQLEEEIVK 350
Cdd:cd04433 231 RLDE---------DgylYIVGRLKDMIKSGGENVYPAEVEAVLLG 266
|
|
| AMP-binding_C_2 |
pfam14535 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
336-432 |
2.46e-37 |
|
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: 131.44 E-value: 2.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 336 GVNVFPSQLEEEIVKFEHLSPHYQLEVNRRGHLDSLSVKVELKEsSLTLTHEQRCQVCHQLRHRIKSMVGISTDVMIVNC 415
Cdd:pfam14535 1 GVNVFPSQIEEVLLEIPGVGPEYQIIVTREGGLDELEVKVEVAE-GFSDEIKDLEALEKRIAKELKSVLGVSVKVELVEP 79
|
90
....*....|....*..
gi 323157347 416 GSIPRSEGKACRVFDLR 432
Cdd:pfam14535 80 GTLPRSEGKAKRVIDLR 96
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
93-348 |
4.74e-26 |
|
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: 109.51 E-value: 4.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 93 SSGTTGKPTVVGYTQNdidNWANIVARSLRAAGGTPKDKIHVA----YGYGLFTGGLGAHYgaerLGATVIPMSGGQTEK 168
Cdd:COG0318 108 TSGTTGRPKGVMLTHR---NLLANAAAIAAALGLTPGDVVLVAlplfHVFGLTVGLLAPLL----AGATLVLLPRFDPER 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 169 QAQLIRDFQPDMIMVTPSYCLNLIEELERQlGGDASgcSLRVGVFGAEPWTQAMRKEIERRLGITALDIYGLSE-----V 243
Cdd:COG0318 181 VLELIERERVTVLFGVPTMLARLLRHPEFA-RYDLS--SLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTEtspvvT 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 244 MGPGVAMECLETTDGPTIWEDHFypEIVNPhDGTPLADGEHGELLF------------TTLTKEALPVIRYRTRDLtrll 311
Cdd:COG0318 258 VNPEDPGERRPGSVGRPLPGVEV--RIVDE-DGRELPPGEVGEIVVrgpnvmkgywndPEATAEAFRDGWLRTGDL---- 330
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 323157347 312 pGtartmrRMD-----RISGRSDDMLIIRGVNVFPSQLEEEI 348
Cdd:COG0318 331 -G------RLDedgylYIVGRKKDMIISGGENVYPAEVEEVL 365
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
93-335 |
4.91e-17 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 82.75 E-value: 4.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 93 SSGTTGKPT-VVGYTQNDIDNWANIVARSLRAAGGTPKDKIH----VAYGYGLFTGGLGAHYgaerLGATVIPMSGGQT- 166
Cdd:pfam00501 163 TSGTTGKPKgVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLstlpLFHDFGLSLGLLGPLL----AGATVVLPPGFPAl 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 167 --EKQAQLIRDFQPDMIMVTPSYcLNLIEELERQLGGDASgcSLRVGVFGAEPWTQAMRKEIERRLGITALDIYGLSEvM 244
Cdd:pfam00501 239 dpAALLELIERYKVTVLYGVPTL-LNMLLEAGAPKRALLS--SLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTE-T 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 245 GPGVAMECLETTD-------GPTIWEDHFYpeIVNPHDGTPLADGEHGELLF------------TTLTKEALPVIR-YRT 304
Cdd:pfam00501 315 TGVVTTPLPLDEDlrslgsvGRPLPGTEVK--IVDDETGEPVPPGEPGELCVrgpgvmkgylndPELTAEAFDEDGwYRT 392
|
250 260 270
....*....|....*....|....*....|....
gi 323157347 305 RDLTRLLPgtartmrrmD---RISGRSDDMLIIR 335
Cdd:pfam00501 393 GDLGRRDE---------DgylEIVGRKKDQIKLG 417
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
81-352 |
4.77e-13 |
|
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: 70.33 E-value: 4.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 81 AVPMEQVVRIHASSGTTGKPTVVGYTQndiDNWANIVARSLRAAGGTPKDK-IHVAygyGLF-TGGLGAHYGAERL-GAT 157
Cdd:cd17631 94 KVLFDDLALLMYTSGTTGRPKGAMLTH---RNLLWNAVNALAALDLGPDDVlLVVA---PLFhIGGLGVFTLPTLLrGGT 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 158 VIPMSGGQTEKQAQLIRDFQPDMIMVTPSYcLNLIEELERQLGGDASgcSLRVGVFGAEPWTQAMRKEIERRlGITALDI 237
Cdd:cd17631 168 VVILRKFDPETVLDLIERHRVTSFFLVPTM-IQALLQHPRFATTDLS--SLRAVIYGGAPMPERLLRALQAR-GVKFVQG 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 238 YGLSEvMGPGVAMecLETtdgptiwEDHF-------YP------EIVNPhDGTPLADGEHGELlfttltkealpVIRYRT 304
Cdd:cd17631 244 YGMTE-TSPGVTF--LSP-------EDHRrklgsagRPvffvevRIVDP-DGREVPPGEVGEI-----------VVRGPH 301
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 305 rdltrLLPG-------TARTMR----------RMDR-----ISGRSDDMLIIRGVNVFPSQLEEEIVKFE 352
Cdd:cd17631 302 -----VMAGywnrpeaTAAAFRdgwfhtgdlgRLDEdgylyIVDRKKDMIISGGENVYPAEVEDVLYEHP 366
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
85-350 |
1.58e-10 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 62.30 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 85 EQVVRIHASSGTTGKPTVVGYTQNDIDNWANIVARSLraaGGTPKDKIHVAYG----YGLFTGGLGA-HYGAerlgATVI 159
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERL---GLTEQDRLCIPVPlfhcFGSVLGVLAClTHGA----TMVF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 160 PMSGGQTEKQAQLIRDFQPDMIMVTPSYclnLIEELERQLGGDASGCSLRVGVFGAEPWTQAMRKEIERRLGITALDI-Y 238
Cdd:cd05917 75 PSPSFDPLAVLEAIEKEKCTALHGVPTM---FIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIaY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 239 GLSEVmGPGVAMEclETTDGP-----TIWE--DHFYPEIVNPHDGTPLADGEHGELL---FTTL---------TKEALPV 299
Cdd:cd05917 152 GMTET-SPVSTQT--RTDDSIekrvnTVGRimPHTEAKIVDPEGGIVPPVGVPGELCirgYSVMkgywndpekTAEAIDG 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 323157347 300 IR-YRTRDLtrllpGTartmrrMD-----RISGRSDDMLIIRGVNVFPSQLEEEIVK 350
Cdd:cd05917 229 DGwLHTGDL-----AV------MDedgycRIVGRIKDMIIRGGENIYPREIEEFLHT 274
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
93-357 |
7.35e-10 |
|
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: 60.47 E-value: 7.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 93 SSGTTGKPTVVGYTQNDIdnWANIVARsLRAAGGTPKDKIHVAYGYGLFTGGLGAHYGAERLGATVIPMSGGQTEKQAQL 172
Cdd:cd05903 101 TSGTTGEPKGVMHSHNTL--SASIRQY-AERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALAL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 173 IRDFQPDMIMVTPSYCLNLIEELERQlggDASGCSLRVGVFGAEPWTQAMRKEIERRLGITALDIYGLSEVMGpgvAMEC 252
Cdd:cd05903 178 MREHGVTFMMGATPFLTDLLNAVEEA---GEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPG---AVTS 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 253 LETTDGPTIWEDHFYP----EI-VNPHDGTPLADGEHGELLFTT------------LTKEALPVIRYRTRDLTrllpgta 315
Cdd:cd05903 252 ITPAPEDRRLYTDGRPlpgvEIkVVDDTGATLAPGVEGELLSRGpsvflgyldrpdLTADAAPEGWFRTGDLA------- 324
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 323157347 316 rtmrRMD-----RISGRSDDmLIIRGVNVFPSqLEEEIVKFEHLSPH 357
Cdd:cd05903 325 ----RLDedgylRITGRSKD-IIIRGGENIPV-LEVEDLLLGHPGVI 365
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
76-353 |
1.05e-09 |
|
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: 60.27 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 76 PFDTFAVPMEQVVRIHASSGTTGKPTVVGYTQNDIdnWANIVA-RSLRAAGGTPKDKI-------HVaygYGLFTGGLga 147
Cdd:cd05936 116 LGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNL--VANALQiKAWLEDLLEGDDVVlaalplfHV---FGLTVALL-- 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 148 hYGAeRLGATVIPMSGGQTEKQAQLIRDFQPDMIMVTP---SYCLNLIEELERQLGgdasgcSLRVGVFGAEPWTQAMRK 224
Cdd:cd05936 189 -LPL-ALGATIVLIPRFRPIGVLKEIRKHRVTIFPGVPtmyIALLNAPEFKKRDFS------SLRLCISGGAPLPVEVAE 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 225 EIERRLGITALDIYGLSEvMGPGVAMECLETTD-----GPTIWedHFYPEIVNPhDGTPLADGEHGELlfttltkealpV 299
Cdd:cd05936 261 RFEELTGVPIVEGYGLTE-TSPVVAVNPLDGPRkpgsiGIPLP--GTEVKIVDD-DGEELPPGEVGEL-----------W 325
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 323157347 300 IR--------YRTRDLT--RLLPGTART--MRRMD-----RISGRSDDMLIIRGVNVFPSQLEEEIvkFEH 353
Cdd:cd05936 326 VRgpqvmkgyWNRPEETaeAFVDGWLRTgdIGYMDedgyfFIVDRKKDMIIVGGFNVYPREVEEVL--YEH 394
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
93-355 |
4.88e-09 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 58.14 E-value: 4.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 93 SSGTTGKPTVVGYTQNDIdnWANIV--ARSLRAAGGtpkDKIHVAYGYGLFTGGLgahYGAE---RLGATVIPMSGGQTE 167
Cdd:PRK13295 205 TSGTTGEPKGVMHTANTL--MANIVpyAERLGLGAD---DVILMASPMAHQTGFM---YGLMmpvMLGATAVLQDIWDPA 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 168 KQAQLIRDFQPDMIMVTPSYCLNLIEELErQLGGDASgcSLRVGVFGAEPWTQAMRKEIERRLGITALDIYGLSE----- 242
Cdd:PRK13295 277 RAAELIRTEGVTFTMASTPFLTDLTRAVK-ESGRPVS--SLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTEngavt 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 243 VMGPGVAMECLETTDGptiwedhfYP------EIVNPhDGTPLADGEHGELLFTT-------LTKEALPVIR----YRTR 305
Cdd:PRK13295 354 LTKLDDPDERASTTDG--------CPlpgvevRVVDA-DGAPLPAGQIGRLQVRGcsnfggyLKRPQLNGTDadgwFDTG 424
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 323157347 306 DLTRLLPGTARtmrrmdRISGRSDDmLIIRGVNVFPSqLEEEIVKFEHLS 355
Cdd:PRK13295 425 DLARIDADGYI------RISGRSKD-VIIRGGENIPV-VEIEALLYRHPA 466
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
84-288 |
9.04e-09 |
|
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: 57.10 E-value: 9.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 84 MEQVVRIHASSGTTGKPTVVGYTQNDIdnWANiVARSLRAAGGTPKDKIHVAYGYGLFTGGLGAHYGAERLGATVIPMSG 163
Cdd:cd05935 83 LDDLALIPYTSGTTGLPKGCMHTHFSA--AAN-ALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMAR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 164 GQTEKQAQLIRDFQPDMIMVTPSYCLNLIEELERQlggDASGCSLRVGVFGAEPWTQAMRKEIERRLGITALDIYGLSEV 243
Cdd:cd05935 160 WDRETALELIEKYKVTFWTNIPTMLVDLLATPEFK---TRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTET 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 323157347 244 MGP-------GVAMECLETtdgPTIWEDhfyPEIVNPHDGTPLADGEHGELL 288
Cdd:cd05935 237 MSQthtnpplRPKLQCLGI---P*FGVD---ARVIDIETGRELPPNEVGEIV 282
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
94-353 |
9.16e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 57.22 E-value: 9.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 94 SGTTGKPTVVGYT-QNDIDN---WANIvarslraAGGTPKDKI-------HVaYGYglfTGGLGAHYGAerlGATVIPMS 162
Cdd:PRK07656 175 SGTTGRPKGAMLThRQLLSNaadWAEY-------LGLTEGDRYlaanpffHV-FGY---KAGVNAPLMR---GATILPLP 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 163 GGQTEKQAQLIRDFQPDMIMVTPS-YclNLIEELERQLGGDASgcSLRVGVFGAEPWTQAMRKEIERRLGI-TALDIYGL 240
Cdd:PRK07656 241 VFDPDEVFRLIETERITVLPGPPTmY--NSLLQHPDRSAEDLS--SLRLAVTGAASMPVALLERFESELGVdIVLTGYGL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 241 SEVMG------PGVAMECLETTDGPTIWedHFYPEIVNPHdGTPLADGEHGELL---FTTL---------TKEAlpvIRY 302
Cdd:PRK07656 317 SEASGvttfnrLDDDRKTVAGTIGTAIA--GVENKIVNEL-GEEVPVGEVGELLvrgPNVMkgyyddpeaTAAA---IDA 390
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 303 ----RTRDLTrllpgtartmrRMD-----RISGRSDDMLIIRGVNVFPSQLEEeiVKFEH 353
Cdd:PRK07656 391 dgwlHTGDLG-----------RLDeegylYIVDRKKDMFIVGGFNVYPAEVEE--VLYEH 437
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
48-289 |
2.22e-08 |
|
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: 56.07 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 48 GVHPDDFRELSDLRKFPCTTkqdlRDNYPFDTFAVPMEQVVRIHASSGTTGKPTVVGYTQNdidnwaNIVARSLRAAGGT 127
Cdd:cd05911 113 DDKPDGVLSIEDLLSPTLGE----EDEDLPPPLKDGKDDTAAILYSSGTTGLPKGVCLSHR------NLIANLSQVQTFL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 128 PKDKIH--VAYG-------YGLFTgglgAHYGAERlGATVIPMSGGQTEKQAQLIRDFQPDMIMVTPSYCLNLIE--ELE 196
Cdd:cd05911 183 YGNDGSndVILGflplyhiYGLFT----TLASLLN-GATVIIMPKFDSELFLDLIEKYKITFLYLVPPIAAALAKspLLD 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 197 RQlggDASgcSLRVGVFGAEPWTQAMRKEIERRLGITAL-DIYGLSEvMGPGVAMeclettdgpTIWEDHFYP------- 268
Cdd:cd05911 258 KY---DLS--SLRVILSGGAPLSKELQELLAKRFPNATIkQGYGMTE-TGGILTV---------NPDGDDKPGsvgrllp 322
|
250 260
....*....|....*....|....*
gi 323157347 269 ----EIVNPHDGTPLADGEHGELLF 289
Cdd:cd05911 323 nveaKIVDDDGKDSLGPNEPGEICV 347
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
93-350 |
2.47e-08 |
|
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: 55.93 E-value: 2.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 93 SSGTTGKPTVVGYTQNDIDNWANIVARslRAAGGTPKDKIHVA----YGYGLFTGGLGAHYgaerLGATVIPMSGGQT-E 167
Cdd:cd05919 99 SSGTTGPPKGVMHAHRDPLLFADAMAR--EALGLTPGDRVFSSakmfFGYGLGNSLWFPLA----VGASAVLNPGWPTaE 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 168 KQAQLIRDFQPDMIMVTPSYCLNLIEElerQLGGDASGCSLRVGVFGAEPWTQAMRKEIERRLGITALDIYGLSEVMG-- 245
Cdd:cd05919 173 RVLATLARFRPTVLYGVPTFYANLLDS---CAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHif 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 246 ----PGVAMecLETTDGPTIWedhFYPEIVNPhDGTPLADGEHGELLfttLTKEALPVIRYRTRDLTR--LLPGTARTMR 319
Cdd:cd05919 250 lsnrPGAWR--LGSTGRPVPG---YEIRLVDE-EGHTIPPGEEGDLL---VRGPSAAVGYWNNPEKSRatFNGGWYRTGD 320
|
250 260 270
....*....|....*....|....*....|....*...
gi 323157347 320 RMDRIS-------GRSDDMLIIRGVNVFPSQLEEEIVK 350
Cdd:cd05919 321 KFCRDAdgwythaGRADDMLKVGGQWVSPVEVESLIIQ 358
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
93-349 |
7.46e-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: 54.30 E-value: 7.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 93 SSGTTGKPTVVGYTQNDIDNWANIVARslRAAGGTPKD------KIHVAYGYGlftgglGAHYGAERLGATVIPMSGGQT 166
Cdd:cd05959 171 SSGSTGRPKGVVHLHADIYWTAELYAR--NVLGIREDDvcfsaaKLFFAYGLG------NSLTFPLSVGATTVLMPERPT 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 167 EKQ-AQLIRDFQPDMIMVTPSYCLNLieeLERQLGGDASGCSLRVGVFGAEPWTQAMRKEIERRLGITALDIYGLSEVMG 245
Cdd:cd05959 243 PAAvFKRIRRYRPTVFFGVPTLYAAM---LAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLDILDGIGSTEMLH 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 246 ------PGvAMEcLETTDGPTiweDHFYPEIVNPhDGTPLADGEHGELLfttLTKEALPVIRYRTRDLTR--LLPGTART 317
Cdd:cd05959 320 iflsnrPG-RVR-YGTTGKPV---PGYEVELRDE-DGGDVADGEPGELY---VRGPSSATMYWNNRDKTRdtFQGEWTRT 390
|
250 260 270
....*....|....*....|....*....|....*....
gi 323157347 318 MRRMDR-------ISGRSDDMLIIRGVNVFPSQLEEEIV 349
Cdd:cd05959 391 GDKYVRdddgfytYAGRADDMLKVSGIWVSPFEVESALV 429
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
94-353 |
8.54e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 54.42 E-value: 8.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 94 SGTTGKPTVVGYTQndidnwANIVARSLRAAGG---TPKDKI-------HVaygyglftGGLGAHYGAERLGATVIpmsg 163
Cdd:PRK06187 176 SGTTGHPKGVVLSH------RNLFLHSLAVCAWlklSRDDVYlvivpmfHV--------HAWGLPYLALMAGAKQV---- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 164 gqtekqaqLIRDFQPDMIM-------VTPSYC----LNLIEELERQLGGDASgcSLRVGVFGAEPWTQAMRKEIERRLGI 232
Cdd:PRK06187 238 --------IPRRFDPENLLdlieterVTFFFAvptiWQMLLKAPRAYFVDFS--SLRLVIYGGAALPPALLREFKEKFGI 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 233 TALDIYGLSEvMGPGVAMECLETTDgPTIWEDH-----FYP----EIVNPhDGTPLA--DGEHGELlfttltkealpVIR 301
Cdd:PRK06187 308 DLVQGYGMTE-TSPVVSVLPPEDQL-PGQWTKRrsagrPLPgveaRIVDD-DGDELPpdGGEVGEI-----------IVR 373
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 323157347 302 --YRTRDLTRLLPGTARTMR----------RMD-----RISGRSDDMLIIRGVNVFPSQLEEEIVKFEH 353
Cdd:PRK06187 374 gpWLMQGYWNRPEATAETIDggwlhtgdvgYIDedgylYITDRIKDVIISGGENIYPRELEDALYGHPA 442
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
93-349 |
2.09e-07 |
|
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: 52.68 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 93 SSGTTGKPTVVGYTQNDIDNWANIVARSLRAaggTPKDKIHVA----YGYGLFTGGLGAHYGaerlGATVIPMSGGQTEK 168
Cdd:cd05934 89 TSGTTGPPKGVVITHANLTFAGYYSARRFGL---GEDDVYLTVlplfHINAQAVSVLAALSV----GATLVLLPRFSASR 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 169 QAQLIRDFQ----------PDMIMVTPsyclnlieELERqlggDASGCsLRVgVFGAEPwTQAMRKEIERRLGITALDIY 238
Cdd:cd05934 162 FWSDVRRYGatvtnylgamLSYLLAQP--------PSPD----DRAHR-LRA-AYGAPN-PPELHEEFEERFGVRLLEGY 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 239 GLSEVMGPGVAmecleTTDGPTIW------EDHFYPEIVNPHdGTPLADGEHGELLFTTL---------------TKEAL 297
Cdd:cd05934 227 GMTETIVGVIG-----PRDEPRRPgsigrpAPGYEVRIVDDD-GQELPAGEPGELVIRGLrgwgffkgyynmpeaTAEAM 300
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 323157347 298 PVIRYRTRDLTRLLP-GTArtmrrmdRISGRSDDMLIIRGVNVFPSQLEEEIV 349
Cdd:cd05934 301 RNGWFHTGDLGYRDAdGFF-------YFVDRKKDMIRRRGENISSAEVERAIL 346
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
94-337 |
3.83e-07 |
|
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: 52.14 E-value: 3.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 94 SGTTGKP--TVVGYtqndiDNWANIVARSLRAAGGTPKDKI--HVAYGyglFTGGLGAHYGAERLGATVIPMSGGQT--- 166
Cdd:cd05930 102 SGSTGKPkgVMVEH-----RGLVNLLLWMQEAYPLTPGDRVlqFTSFS---FDVSVWEIFGALLAGATLVVLPEEVRkdp 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 167 EKQAQLIRDFQPDMIMVTPSYCLNLIEELERQLGGdasgcSLRVGVFGAEPWTQAMRKEIERRL-GITALDIYGLSEVMG 245
Cdd:cd05930 174 EALADLLAEEGITVLHLTPSLLRLLLQELELAALP-----SLRLVLVGGEALPPDLVRRWRELLpGARLVNLYGPTEATV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 246 PGVAMECLE---TTDGPTI----WEDHFYpeIVNPHdGTPLADGEHGELLFTT------------LTKE---ALPVIR-- 301
Cdd:cd05930 249 DATYYRVPPddeEDGRVPIgrpiPNTRVY--VLDEN-LRPVPPGVPGELYIGGaglargylnrpeLTAErfvPNPFGPge 325
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 323157347 302 --YRTRDLTRLLPGtartmrrmDRIS--GRSDDMLIIRGV 337
Cdd:cd05930 326 rmYRTGDLVRWLPD--------GNLEflGRIDDQVKIRGY 357
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
270-427 |
8.03e-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: 51.09 E-value: 8.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 270 IVNPHDGTPLADGEHGELLF---------------TTLTKEALPVIR----YRTRDLTRLLpgtartmrrmDR---ISGR 327
Cdd:cd05931 368 IVDPETGRELPDGEVGEIWVrgpsvasgywgrpeaTAETFGALAATDeggwLRTGDLGFLH----------DGelyITGR 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 328 SDDMLIIRGVNVFPSQLEEEIvkfEHLSPHYqlevnRRGHLDSLSV-------KVELKESSLTLTHEQRCQVCHQLRHRI 400
Cdd:cd05931 438 LKDLIIVRGRNHYPQDIEATA---EEAHPAL-----RPGCVAAFSVpddgeerLVVVAEVERGADPADLAAIAAAIRAAV 509
|
170 180 190
....*....|....*....|....*....|...
gi 323157347 401 KSMVGIS-TDVMIVNCGSIPR-SEGK----ACR 427
Cdd:cd05931 510 AREHGVApADVVLVRPGSIPRtSSGKiqrrACR 542
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
45-345 |
1.48e-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: 50.20 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 45 DAAGVHPDDFreLSDLRKFPCTTKQDLRDNYPF-DTFAVPM---EQVVRIHASSGTTGKPTVVGYTQNDIDNWANIVA-- 118
Cdd:cd05923 108 VDAQVMDAIF--QSGVRVLALSDLVGLGEPESAgPLIEDPPrepEQPAFVFYTSGTTGLPKGAVIPQRAAESRVLFMStq 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 119 ------RSLRAAGGTPKdkIHVAYGYGLFTGGLGahygaerLGATVIPMSGGQTEKQAQLIRDFQPDMIMVTPSYCLNLI 192
Cdd:cd05923 186 aglrhgRHNVVLGLMPL--YHVIGFFAVLVAALA-------LDGTYVVVEEFDPADALKLIEQERVTSLFATPTHLDALA 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 193 EELErQLGGDASgcSLRVGVFGAEPWTQAMRKEIERRLGITALDIYGLSEVMGPGVAMECLETTDGptiwEDHFYPEI-V 271
Cdd:cd05923 257 AAAE-FAGLKLS--SLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTEAMNSLYMRDARTGTEM----RPGFFSEVrI 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 272 NPHDGTP---LADGEHGELLFTTLTKEALpvIRYRTR---DLTRLLPGTARTMRR--MD-----RISGRSDDMLIIRGVN 338
Cdd:cd05923 330 VRIGGSPdeaLANGEEGELIVAAAADAAF--TGYLNQpeaTAKKLQDGWYRTGDVgyVDpsgdvRILGRVDDMIISGGEN 407
|
....*..
gi 323157347 339 VFPSQLE 345
Cdd:cd05923 408 IHPSEIE 414
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
155-345 |
4.79e-06 |
|
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: 48.27 E-value: 4.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 155 GATVIPMSGGQTEKQAQLIRDFQPDMIMVTPSYCLNLIEELERQlGGDASgcSLRVGVFGAEPWTQAMRKEIERRLGI-T 233
Cdd:cd17638 67 GATVVPVAVFDVDAILEAIERERITVLPGPPTLFQSLLDHPGRK-KFDLS--SLRAAVTGAATVPVELVRRMRSELGFeT 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 234 ALDIYGLSE-VMG----PGVAMECLETTDGPTIweDHFYPEIVNphDGTPLADGEH---GELLFTTLTKEALPVIRY-RT 304
Cdd:cd17638 144 VLTAYGLTEaGVAtmcrPGDDAETVATTCGRAC--PGFEVRIAD--DGEVLVRGYNvmqGYLDDPEATAEAIDADGWlHT 219
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 323157347 305 RDLTRLlpgtarTMRRMDRISGRSDDMLIIRGVNVFPSQLE 345
Cdd:cd17638 220 GDVGEL------DERGYLRITDRLKDMYIVGGFNVYPAEVE 254
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
93-427 |
1.01e-05 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 47.70 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 93 SSGTTGKPTVV-----------GYTQNDIDNWANIVARSLRAaggTPKDKIHVaygyglftGGLGAHYGAERLGATVIpM 161
Cdd:PRK05857 177 TSGTTGEPKAVllanrtffavpDILQKEGLNWVTWVVGETTY---SPLPATHI--------GGLWWILTCLMHGGLCV-T 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 162 SGGQTEKQAQLIRDFQPDMIMVTPSYCLNLIEELERqlgGDASGCSLRVGVFGAEPWTQAMRKEIERRlGITALDIYGLS 241
Cdd:PRK05857 245 GGENTTSLLEILTTNAVATTCLVPTLLSKLVSELKS---ANATVPSLRLVGYGGSRAIAADVRFIEAT-GVRTAQVYGLS 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 242 EVmgpGVAMECLETTDGPTIWEDHF-----YPEI----VNPHDGTPLADGEHGELLFTTL-TKEALPVIRY-----RTRD 306
Cdd:PRK05857 321 ET---GCTALCLPTDDGSIVKIEAGavgrpYPGVdvylAATDGIGPTAPGAGPSASFGTLwIKSPANMLGYwnnpeRTAE 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 307 LtrLLPGTART----MRRMD---RISGRSDDMLIIRGVNVFPSQLEE---------EIVKFEHLSPHYqlevnrrGHLDS 370
Cdd:PRK05857 398 V--LIDGWVNTgdllERREDgffYIKGRSSEMIICGGVNIAPDEVDRiaegvsgvrEAACYEIPDEEF-------GALVG 468
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 371 LSV--KVELKESSltlTHEQRCQVCHQLRHRIKSMVGISTDVMIVNcgsIPRSE-GKACR 427
Cdd:PRK05857 469 LAVvaSAELDESA---ARALKHTIAARFRRESEPMARPSTIVIVTD---IPRTQsGKVMR 522
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
85-350 |
1.00e-04 |
|
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: 44.38 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 85 EQVVRIHASSGTTGKPTVVGYTQNdidNWANIVA--RSLRAAGGTPKDKIHVA-YGYGLFTGGLGAhygAERLGATVIPM 161
Cdd:cd17650 93 EDLAYVIYTSGTTGKPKGVMVEHR---NVAHAAHawRREYELDSFPVRLLQMAsFSFDVFAGDFAR---SLLNGGTLVIC 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 162 SGGQTEKQAQL---IRDFQPDMIMVTPSYCLNLIEELERQlGGDASgcSLRVGVFGAEPWTQAMRKEIERRLG--ITALD 236
Cdd:cd17650 167 PDEVKLDPAALydlILKSRITLMESTPALIRPVMAYVYRN-GLDLS--AMRLLIVGSDGCKAQDFKTLAARFGqgMRIIN 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 237 IYGLSEVMgpgVAMECLETTDGPTIWED-----------HFYpeIVNPHDgTPLADGEHGELLF------------TTLT 293
Cdd:cd17650 244 SYGVTEAT---IDSTYYEEGRDPLGDSAnvpigrplpntAMY--VLDERL-QPQPVGVAGELYIggagvargylnrPELT 317
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 323157347 294 KEAL------PVIR-YRTRDLTRLLP-GTARTMrrmdrisGRSDDMLIIRGVNVFPSQLEEEIVK 350
Cdd:cd17650 318 AERFvenpfaPGERmYRTGDLARWRAdGNVELL-------GRVDHQVKIRGFRIELGEIESQLAR 375
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
94-348 |
2.92e-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: 43.05 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 94 SGTTGKPTVVGYTQNDIDNwaniVARSLRAAGG-TPKDKI-HVA---YGYGLFTGGLGAHYgaerLGATVIPMSGGQTEK 168
Cdd:cd05941 98 SGTTGRPKGVVLTHANLAA----NVRALVDAWRwTEDDVLlHVLplhHVHGLVNALLCPLF----AGASVEFLPKFDPKE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 169 QAQLIRDFQPDMIMVTPSYCLNLIEELERQLGGDASGCS-----LRVGVFGAEPWTQAMRKEIERRLGITALDIYGLSE- 242
Cdd:cd05941 170 VAISRLMPSITVFMGVPTIYTRLLQYYEAHFTDPQFARAaaaerLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEi 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 243 VM-------GP------GVAMECLETtdgptiwedhfypEIVNPHDGTPLADGEHGEL------LFTTL------TKEAL 297
Cdd:cd05941 250 GMalsnpldGErrpgtvGMPLPGVQA-------------RIVDEETGEPLPRGEVGEIqvrgpsVFKEYwnkpeaTKEEF 316
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 323157347 298 PVIRY-RTRDLTRllpgtartmRRMD---RISGRSDDMLI-IRGVNVFPSQLEEEI 348
Cdd:cd05941 317 TDDGWfKTGDLGV---------VDEDgyyWILGRSSVDIIkSGGYKVSALEIERVL 363
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
94-286 |
5.51e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 42.25 E-value: 5.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 94 SGTTGKPTVVGYTQNDIdnWANIVArSLRAAGGTPKDKI-------HVAygyGLFTGGLGAHYGaerlGATVIPMSGGQT 166
Cdd:PRK08314 199 SGTTGVPKGCMHTHRTV--MANAVG-SVLWSNSTPESVVlavlplfHVT---GMVHSMNAPIYA----GATVVLMPRWDR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 167 EKQAQLIRDFQ-------PDMI---MVTP---SYCLNlieelerqlggdasgcSLRVGVFGAEPWTQAMRKEIERRLGIT 233
Cdd:PRK08314 269 EAAARLIERYRvthwtniPTMVvdfLASPglaERDLS----------------SLRYIGGGGAAMPEAVAERLKELTGLD 332
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 323157347 234 ALDIYGLSEVMGPGVA-------MECLettdG-PTIWEDhfyPEIVNPHDGTPLADGEHGE 286
Cdd:PRK08314 333 YVEGYGLTETMAQTHSnppdrpkLQCL----GiPTFGVD---ARVIDPETLEELPPGEVGE 386
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
78-287 |
5.86e-04 |
|
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: 42.22 E-value: 5.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 78 DTFAVPMEQ--VVRIHASSGTTGKPTVVGYT-QNDIDNWANIVARslRAAGGTPKDKI-------HVaYGYGLFTgglga 147
Cdd:cd05904 149 EPPVVVIKQddVAALLYSSGTTGRSKGVMLThRNLIAMVAQFVAG--EGSNSDSEDVFlcvlpmfHI-YGLSSFA----- 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 148 hYGAERLGATVIPMSGGQTEKQAQLIRDFQPDMIMVTPSYCLNLIeelERQLGGDASGCSLRVGVFGAEPWTQAMRKEIE 227
Cdd:cd05904 221 -LGLLRLGATVVVMPRFDLEELLAAIERYKVTHLPVVPPIVLALV---KSPIVDKYDLSSLRQIMSGAAPLGKELIEAFR 296
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 323157347 228 RRLGitALDI---YGLSEvMGPGVAMECLE-------TTDGPTI--WEdhfyPEIVNPHDGTPLADGEHGEL 287
Cdd:cd05904 297 AKFP--NVDLgqgYGMTE-STGVVAMCFAPekdrakyGSVGRLVpnVE----AKIVDPETGESLPPNQTGEL 361
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
93-348 |
5.88e-04 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 42.04 E-value: 5.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 93 SSGTTGKPTVVGYTQNDIDNWANIVARSLraaGGTPKDKIHVA----YGYGLFTggLGAHYgaERLGATVIPMSGGQTEK 168
Cdd:cd05922 125 TSGSTGSPKLVRLSHQNLLANARSIAEYL---GITADDRALTVlplsYDYGLSV--LNTHL--LRGATLVLTNDGVLDDA 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 169 QAQLIRDFQPDMIMVTPSyclnLIEELERQLGGDASGCSLRVgvfgaepWTQA---MRKEIERRL-----GITALDIYGL 240
Cdd:cd05922 198 FWEDLREHGATGLAGVPS----TYAMLTRLGFDPAKLPSLRY-------LTQAggrLPQETIARLrellpGAQVYVMYGQ 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 241 SE------VMGPGVAMECLETTdGPTIWEDHFypEIVNPhDGTPLADGEHGELLFT-------------TLTKEALPVIR 301
Cdd:cd05922 267 TEatrrmtYLPPERILEKPGSI-GLAIPGGEF--EILDD-DGTPTPPGEPGEIVHRgpnvmkgywndppYRRKEGRGGGV 342
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 323157347 302 YRTRDLTRllpgtartmRRMD---RISGRSDDMLIIRGVNVFPSQLEEEI 348
Cdd:cd05922 343 LHTGDLAR---------RDEDgflFIVGRRDRMIKLFGNRISPTEIEAAA 383
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
324-350 |
7.44e-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: 41.24 E-value: 7.44e-04
10 20
....*....|....*....|....*..
gi 323157347 324 ISGRSDDMLIIRGVNVFPSQLEEEIVK 350
Cdd:cd17633 226 LVGRESDMIIIGGINIFPTEIESVLKA 252
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
94-352 |
9.31e-04 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 41.43 E-value: 9.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 94 SGTTGKPTVVGYTQndiDNWANiVARSLRAAGGTPKDKIHVAYgyglftggLG-AHYgAERLGATVIPMSGGQTEKQAQL 172
Cdd:cd05907 96 SGTTGRPKGVMLSH---RNILS-NALALAERLPATEGDRHLSF--------LPlAHV-FERRAGLYVPLLAGARIYFASS 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 173 IRDFQPDMIMVTPSYCL---------------NLIEELERQLGGDASGCSLRVGVFGAEPwtqaMRKEIERR---LGITA 234
Cdd:cd05907 163 AETLLDDLSEVRPTVFLavprvwekvyaaikvKAVPGLKRKLFDLAVGGRLRFAASGGAP----LPAELLHFfraLGIPV 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 235 LDIYGLSEVmGPGVAMECLETTDGPTIwedhfypeivnphdGTPL--------ADGE---HGELLFT-------TLTKEA 296
Cdd:cd05907 239 YEGYGLTET-SAVVTLNPPGDNRIGTV--------------GKPLpgvevriaDDGEilvRGPNVMLgyyknpeATAEAL 303
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 323157347 297 LPVIRYRTRDLTRLLP-GTArtmrrmdRISGRSDDMLIIR-GVNVFPSQLEEEIVKFE 352
Cdd:cd05907 304 DADGWLHTGDLGEIDEdGFL-------HITGRKKDLIITSgGKNISPEPIENALKASP 354
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
93-352 |
1.98e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 40.50 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 93 SSGTTGKPTVVGYTQNDIDNWANIVARSLraaGGTPKDKIHVAY---GYGLFTGGLGAHYGaerlGATVIPMSGGQTEKQ 169
Cdd:PRK06164 189 TSGTTSGPKLVLHRQATLLRHARAIARAY---GYDPGAVLLAALpfcGVFGFSTLLGALAG----GAPLVCEPVFDAART 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 170 AQLIRDFQpdmimVTPSYCLN-LIEELERQLGGDASGCSLRVgvFGAEPWTQAMRKEIERRL--GITALDIYGLSEVMgp 246
Cdd:PRK06164 262 ARALRRHR-----VTHTFGNDeMLRRILDTAGERADFPSARL--FGFASFAPALGELAALARarGVPLTGLYGSSEVQ-- 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 247 gvAMECLETTDGPtiWEDHF-------YPE----IVNPHDGTPLADGEHGEL------LFTTL------TKEALPVIRY- 302
Cdd:PRK06164 333 --ALVALQPATDP--VSVRIegggrpaSPEarvrARDPQDGALLPDGESGEIeirapsLMRGYldnpdaTARALTDDGYf 408
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 323157347 303 RTRDLTRLLPgtartmrrmDR---ISGRSDDMLIIRGVNVFPSQLEEEIVKFE 352
Cdd:PRK06164 409 RTGDLGYTRG---------DGqfvYQTRMGDSLRLGGFLVNPAEIEHALEALP 452
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
270-346 |
2.74e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 39.98 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 270 IVNPHD-GTPLADGEHGELLfttltkealpvIR-------YRTR-DLTR--LLPGTART--MRRMD-----RISGRSDDM 331
Cdd:PRK05605 402 IVDPEDpDETMPDGEEGELL-----------VRgpqvfkgYWNRpEETAksFLDGWFRTgdVVVMEedgfiRIVDRIKEL 470
|
90
....*....|....*
gi 323157347 332 LIIRGVNVFPSQLEE 346
Cdd:PRK05605 471 IITGGFNVYPAEVEE 485
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
94-346 |
6.67e-03 |
|
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: 38.77 E-value: 6.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 94 SGTTGKPTVVGYTQNDID---NWAnivarslRAAGGTPKDKI---HVAYGYGLFTGGLgahYGAERLGATVIPMSGGQTE 167
Cdd:cd05945 106 SGSTGRPKGVQISHDNLVsftNWM-------LSDFPLGPGDVflnQAPFSFDLSVMDL---YPALASGATLVPVPRDATA 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 168 KQAQLIRDFQPDMIMV---TPSyclnlIEELERQLGGDASGC--SLRVGVFGAEPWTQAMRKEIERRL-GITALDIYGLS 241
Cdd:cd05945 176 DPKQLFRFLAEHGITVwvsTPS-----FAAMCLLSPTFTPESlpSLRHFLFCGEVLPHKTARALQQRFpDARIYNTYGPT 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 242 EVMGP-------------------GVAMECLETtdgpTIWEDhfypeivnphDGTPLADGEHGELLFT------------ 290
Cdd:cd05945 251 EATVAvtyievtpevldgydrlpiGYAKPGAKL----VILDE----------DGRPVPPGEKGELVISgpsvskgylnnp 316
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 323157347 291 TLTKEAL----PVIRYRTRDLTRLLPGTartmrrMDRISGRSDDMLIIRGVNVfpsQLEE 346
Cdd:cd05945 317 EKTAAAFfpdeGQRAYRTGDLVRLEADG------LLFYRGRLDFQVKLNGYRI---ELEE 367
|
|
| |
