|
Name |
Accession |
Description |
Interval |
E-value |
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
8-247 |
7.26e-92 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 277.27 E-value: 7.26e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 8 DWLKVLRTVDVVISTPSILVSHDPADYPNIRVVATAGESCPVALADRWGQNATFYNCCGPTEVTIVNTMHHHSLGTPLTI 87
Cdd:cd17653 182 PFAHVARTVDALMSTPSILSTLSPQDFPNLKTIFLGGEAVPPSLLDRWSPGRRLYNAYGPTECTISSTMTELLPGQPVTI 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 88 GKPTPNNTIYVLDDNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDPFSPeGGMMFNTGDIGRLRDDGELDYLG 167
Cdd:cd17653 262 GKPIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWP-GSRMYRTGDYGRWTEDGGLEFLG 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 168 RIDDQVKIQGFRVELDGVSASI-SACPGVVQACAMLIQDELWAFYTPIEVPADAVQDVVAQLQPKYSVPKRYRALAALPL 246
Cdd:cd17653 341 REDNQVKVRGFRINLEEIEEVVlQSQPEVTQAAAIVVNGRLVAFVTPETVDVDGLRSELAKHLPSYAVPDRIIALDSFPL 420
|
.
gi 807744961 247 T 247
Cdd:cd17653 421 T 421
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
16-247 |
2.94e-74 |
|
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: 232.42 E-value: 2.94e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 16 VDVVISTPSIL---VSH-DPADYPNIRVVATAGESCPVALADRW---GQNATFYNCCGPTEVTIVNTMHH----HSLGTP 84
Cdd:cd05930 185 ITVLHLTPSLLrllLQElELAALPSLRLVLVGGEALPPDLVRRWrelLPGARLVNLYGPTEATVDATYYRvppdDEEDGR 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 85 LTIGKPTPNNTIYVLDDNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDPFSPeGGMMFNTGDIGRLRDDGELD 164
Cdd:cd05930 265 VPIGRPIPNTRVYVLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGP-GERMYRTGDLVRWLPDGNLE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 165 YLGRIDDQVKIQGFRVELDGVSASISACPGVVQACAMLIQDE-----LWAFYTPIEVPADAVQDVVAQLQ---PKYSVPK 236
Cdd:cd05930 344 FLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGdgekrLVAYVVPDEGGELDEEELRAHLAerlPDYMVPS 423
|
250
....*....|.
gi 807744961 237 RYRALAALPLT 247
Cdd:cd05930 424 AFVVLDALPLT 434
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
3-247 |
2.27e-67 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 214.42 E-value: 2.27e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 3 GPHRVDWLKVLRtVDVVISTPSILVSHDPADYPNIRVVATAGESCPVALADRWGQNATFYNCCGPTEVTIVNTMHH-HSL 81
Cdd:cd17652 173 GEPLADLLREHR-ITHVTLPPAALAALPPDDLPDLRTLVVAGEACPAELVDRWAPGRRMINAYGPTETTVCATMAGpLPG 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 82 GTPLTIGKPTPNNTIYVLDDNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDPFSPEGGMMFNTGDIGRLRDDG 161
Cdd:cd17652 252 GGVPPIGRPVPGTRVYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFGAPGSRMYRTGDLARWRADG 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 162 ELDYLGRIDDQVKIQGFRVELDGVSASISACPGVVQACAMLIQDE-----LWAFYTPIEVPADAVQDVVAQLQ---PKYS 233
Cdd:cd17652 332 QLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRpgdkrLVAYVVPAPGAAPTAAELRAHLAerlPGYM 411
|
250
....*....|....
gi 807744961 234 VPKRYRALAALPLT 247
Cdd:cd17652 412 VPAAFVVLDALPLT 425
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
8-247 |
3.45e-64 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 216.26 E-value: 3.45e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 8 DWLKVLRT--VDVVISTPS---ILVSHDPADYPNIRVVATAGESCPVALADRWGQ---NATFYNCCGPTEVTIVNTMH-- 77
Cdd:COG1020 699 ALAELLARhrVTVLNLTPSllrALLDAAPEALPSLRLVLVGGEALPPELVRRWRArlpGARLVNLYGPTETTVDSTYYev 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 78 --HHSLGTPLTIGKPTPNNTIYVLDDNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDPFSPEGGMMFNTGDIG 155
Cdd:COG1020 779 tpPDADGGSVPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGFPGARLYRTGDLA 858
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 156 RLRDDGELDYLGRIDDQVKIQGFRVELDGVSASISACPGVVQACAMLIQDE----LWAFY----TPIEVPADAVQDVVAQ 227
Cdd:COG1020 859 RWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDApgdkRLVAYvvpeAGAAAAAALLRLALAL 938
|
250 260
....*....|....*....|
gi 807744961 228 LQPKYSVPKRYRALAALPLT 247
Cdd:COG1020 939 LLPPYMVPAAVVLLLPLPLT 958
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
1-200 |
9.54e-64 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 204.04 E-value: 9.54e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 1 MRGPHRVDWLKVLRT--VDVVISTPSI---LVSHDPADYPNIRVVATAGESCPVALADRW---GQNATFYNCCGPTEVTI 72
Cdd:TIGR01733 196 EERDDAALLAALIAEhpVTVLNLTPSLlalLAAALPPALASLRLVILGGEALTPALVDRWrarGPGARLINLYGPTETTV 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 73 VNTMHHHSLG-----TPLTIGKPTPNNTIYVLDDNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDPFSPE-GG 146
Cdd:TIGR01733 276 WSTATLVDPDdapreSPVPIGRPLANTRLYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELTAERFVPDPFAGGdGA 355
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 807744961 147 MMFNTGDIGRLRDDGELDYLGRIDDQVKIQGFRVELDGVSASISACPGVVQACA 200
Cdd:TIGR01733 356 RLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
26-247 |
1.20e-58 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 192.80 E-value: 1.20e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 26 LVSHDPADYPNIRVVATAGESCPVALADRWGQNA---TFYNCCGPTEVTIVNTMHH----HSLGTPLTIGKPTPNNTIYV 98
Cdd:cd12117 240 LADEDPECFAGLRELLTGGEVVSPPHVRRVLAACpglRLVNGYGPTENTTFTTSHVvtelDEVAGSIPIGRPIANTRVYV 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 99 LDDNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDPFSPeGGMMFNTGDIGRLRDDGELDYLGRIDDQVKIQGF 178
Cdd:cd12117 320 LDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGP-GERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGF 398
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 807744961 179 RVELDGVSASISACPGVVQACAMLIQDE-----LWAFYTPIE-VPADAVQDVVAQLQPKYSVPKRYRALAALPLT 247
Cdd:cd12117 399 RIELGEIEAALRAHPGVREAVVVVREDAggdkrLVAYVVAEGaLDAAELRAFLRERLPAYMVPAAFVVLDELPLT 473
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
30-247 |
7.22e-58 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 190.95 E-value: 7.22e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 30 DPADYPNIRVVATAGESCPVALADRWGQ--NATFYNCCGPTEVTIvNTMHHHSLG----TPLTIGKPTPNNTIYVLDDNL 103
Cdd:cd17646 248 AAGSCASLRRVFCSGEALPPELAARFLAlpGAELHNLYGPTEAAI-DVTHWPVRGpaetPSVPIGRPVPNTRLYVLDDAL 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 104 QPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDPFSPeGGMMFNTGDIGRLRDDGELDYLGRIDDQVKIQGFRVELD 183
Cdd:cd17646 327 RPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGP-GSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPG 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 807744961 184 GVSASISACPGVVQACAMLIQDE-----LWAFYTP----IEVPADAVQDVVAQLQPKYSVPKRYRALAALPLT 247
Cdd:cd17646 406 EIEAALAAHPAVTHAVVVARAAPagaarLVGYVVPaagaAGPDTAALRAHLAERLPEYMVPAAFVVLDALPLT 478
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
18-247 |
1.54e-57 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 189.81 E-value: 1.54e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 18 VVISTPS---ILVSHDPADYPNIRVVAtAGESCPVALADRW-GQNATFYNCCGPTEVTIVNTMHHHSLG-TPLTIGKPTP 92
Cdd:cd12116 220 VMQATPAtwrMLLDAGWQGRAGLTALC-GGEALPPDLAARLlSRVGSLWNLYGPTETTIWSTAARVTAAaGPIPIGRPLA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 93 NNTIYVLDDNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDPFSPEGGMMFNTGDIGRLRDDGELDYLGRIDDQ 172
Cdd:cd12116 299 NTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGPGSRLYRTGDLVRRRADGRLEYLGRADGQ 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 173 VKIQGFRVELDGVSASISACPGVVQACAMLIQDE----LWAFYTPIEVPA---DAVQDVVAQLQPKYSVPKRYRALAALP 245
Cdd:cd12116 379 VKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGgdrrLVAYVVLKAGAApdaAALRAHLRATLPAYMVPSAFVRLDALP 458
|
..
gi 807744961 246 LT 247
Cdd:cd12116 459 LT 460
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
14-248 |
2.97e-57 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 188.67 E-value: 2.97e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 14 RTVDVVISTPSI---LVS---HDPADYPNIRVVATAGESCPVALADRWGQN-----ATFYNCCGPTEVTIVNTMHHHS-- 80
Cdd:cd17643 183 EGVTVLNQTPSAfyqLVEaadRDGRDPLALRYVIFGGEALEAAMLRPWAGRfgldrPQLVNMYGITETTVHVTFRPLDaa 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 81 ---LGTPLTIGKPTPNNTIYVLDDNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDPFSPEGGMMFNTGDIGRL 157
Cdd:cd17643 263 dlpAAAASPIGRPLPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGGPGSRMYRTGDLARR 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 158 RDDGELDYLGRIDDQVKIQGFRVELDGVSASISACPGVVQACAMLIQDE-----LWAFYTPIEVPADAVQDVVAQLQ--- 229
Cdd:cd17643 343 LPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEpgdtrLVAYVVADDGAAADIAELRALLKell 422
|
250
....*....|....*....
gi 807744961 230 PKYSVPKRYRALAALPLTR 248
Cdd:cd17643 423 PDYMVPARYVPLDALPLTV 441
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
16-247 |
5.71e-55 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 183.30 E-value: 5.71e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 16 VDVVISTPSILVSHDPAD---YPNIRVVATAGESCPVALADRW----GQNATFYNCCGPTEVTIVNTMHHHSLGTPLT-- 86
Cdd:cd17655 229 ITIIDLTPAHLKLLDAADdseGLSLKHLIVGGEALSTELAKKIielfGTNPTITNAYGPTETTVDASIYQYEPETDQQvs 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 87 --IGKPTPNNTIYVLDDNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDPFSPeGGMMFNTGDIGRLRDDGELD 164
Cdd:cd17655 309 vpIGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVP-GERMYRTGDLARWLPDGNIE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 165 YLGRIDDQVKIQGFRVELDGVSASISACPGVVQACAMLIQDE-----LWAFY-TPIEVPADAVQDVVAQLQPKYSVPKRY 238
Cdd:cd17655 388 FLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEqgqnyLCAYIvSEKELPVAQLREFLARELPDYMIPSYF 467
|
....*....
gi 807744961 239 RALAALPLT 247
Cdd:cd17655 468 IKLDEIPLT 476
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
26-247 |
1.17e-53 |
|
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: 179.10 E-value: 1.17e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 26 LVSHDPADYPNIRVVATAGESCPVALADRWGQNA-TFYNCCGPTEVTIVNTMHH-----HSLGTPLTIGKPTPNNTIYVL 99
Cdd:cd17649 203 ADRTGDGRPPSLRLYIFGGEALSPELLRRWLKAPvRLFNAYGPTEATVTPLVWKceagaARAGASMPIGRPLGGRSAYIL 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 100 DDNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDPFSPEGGMMFNTGDIGRLRDDGELDYLGRIDDQVKIQGFR 179
Cdd:cd17649 283 DADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFR 362
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 807744961 180 VELDGVSASISACPGV----VQACAMLIQDELWAFYTPIEvpADAVQDVVAQLQ-------PKYSVPKRYRALAALPLT 247
Cdd:cd17649 363 IELGEIEAALLEHPGVreaaVVALDGAGGKQLVAYVVLRA--AAAQPELRAQLRtalraslPDYMVPAHLVFLARLPLT 439
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
26-248 |
1.80e-53 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 178.67 E-value: 1.80e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 26 LVSHDPADyPNIRVVATAGESCPVALADRWGQNAT---FYNCCGPTEVTIVNTMH---HHSLGTPlTIGKPTPNNTIYVL 99
Cdd:cd12115 205 LLRHDALP-ASVRVVNLAGEPLPRDLVQRLYARLQverVVNLYGPSEDTTYSTVApvpPGASGEV-SIGRPLANTQAYVL 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 100 DDNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDPFSPeGGMMFNTGDIGRLRDDGELDYLGRIDDQVKIQGFR 179
Cdd:cd12115 283 DRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGP-GARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFR 361
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 807744961 180 VELDGVSASISACPGVVQACAMLIQDE-----LWAFYTPIEVPADAVQDVVAQLQ---PKYSVPKRYRALAALPLTR 248
Cdd:cd12115 362 IELGEIEAALRSIPGVREAVVVAIGDAagerrLVAYIVAEPGAAGLVEDLRRHLGtrlPAYMVPSRFVRLDALPLTP 438
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
35-248 |
1.79e-52 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 176.77 E-value: 1.79e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 35 PNIRVVATAGESCPVALADR----WGQNATFYNCCGPTEVTIVNTmhhHSL-------GTPLTIGKPTPNNTIYVLDDNL 103
Cdd:cd17651 253 AALRYLLTGGEQLVLTEDLRefcaGLPGLRLHNHYGPTETHVVTA---LSLpgdpaawPAPPPIGRPIDNTRVYVLDAAL 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 104 QPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDPFSPeGGMMFNTGDIGRLRDDGELDYLGRIDDQVKIQGFRVELD 183
Cdd:cd17651 330 RPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVP-GARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELG 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 807744961 184 GVSASISACPGVVQAcAMLIQDE------LWAFYTP---IEVPADAVQDVVAQLQPKYSVPKRYRALAALPLTR 248
Cdd:cd17651 409 EIEAALARHPGVREA-VVLAREDrpgekrLVAYVVGdpeAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTP 481
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
14-247 |
1.27e-50 |
|
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: 171.28 E-value: 1.27e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 14 RTVDVVISTPSILV------SHDPADYPNIRVVATAGESCPVALADRWGQ---NATFYNCCGPTEVTIVNTMHH---HSL 81
Cdd:cd05945 187 HGITVWVSTPSFAAmcllspTFTPESLPSLRHFLFCGEVLPHKTARALQQrfpDARIYNTYGPTEATVAVTYIEvtpEVL 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 82 G--TPLTIGKPTPNNTIYVLDDNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFardpFSPEGGMMFNTGDIGRLRD 159
Cdd:cd05945 267 DgyDRLPIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAF----FPDEGQRAYRTGDLVRLEA 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 160 DGELDYLGRIDDQVKIQGFRVELDGVSASISACPGVVQACAMLIQ-----DELWAFYTPIE----VPADAVQDVVAQLQP 230
Cdd:cd05945 343 DGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYkgekvTELIAFVVPKPgaeaGLTKAIKAELAERLP 422
|
250
....*....|....*..
gi 807744961 231 KYSVPKRYRALAALPLT 247
Cdd:cd05945 423 PYMIPRRFVYLDELPLN 439
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
16-247 |
3.07e-49 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 168.10 E-value: 3.07e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 16 VDVVISTPSILVSHDPADYPNIRVVATAGESCPVALADRWGQNATFYNCCGPTEVTIVNTMHH-HSLGTPLTIGKPTPNN 94
Cdd:cd05918 196 VTWAFLTPSVARLLDPEDVPSLRTLVLGGEALTQSDVDTWADRVRLINAYGPAECTIAATVSPvVPSTDPRNIGRPLGAT 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 95 TiYVLD--DNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDPF------SPEGGMMFNTGDIGRLRDDGELDYL 166
Cdd:cd05918 276 C-WVVDpdNHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAwlkqegSGRGRRLYRTGDLVRYNPDGSLEYV 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 167 GRIDDQVKIQGFRVELDGVSASISAC-PGVVQACAMLI-------QDELWAFYTP-------------IEVPADAVQDVV 225
Cdd:cd05918 355 GRKDTQVKIRGQRVELGEIEHHLRQSlPGAKEVVVEVVkpkdgssSPQLVAFVVLdgsssgsgdgdslFLEPSDEFRALV 434
|
250 260
....*....|....*....|....*....
gi 807744961 226 AQLQ-------PKYSVPKRYRALAALPLT 247
Cdd:cd05918 435 AELRsklrqrlPSYMVPSVFLPLSHLPLT 463
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
22-247 |
1.17e-48 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 166.04 E-value: 1.17e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 22 TPSILVSHDPADYPNIRVVATAGE--SCPVALADRWGQNATFYNCCGPTEVTIVNTMHHHSLGTPL--TIGKPTPNNTIY 97
Cdd:cd17648 194 TPSVLQQYDLARLPHLKRVDAAGEefTAPVFEKLRSRFAGLIINAYGPTETTVTNHKRFFPGDQRFdkSLGRPVRNTKCY 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 98 VLDDNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDPFSPEG-------GMMFNTGDIGRLRDDGELDYLGRID 170
Cdd:cd17648 274 VLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTEQerargrnARLYKTGDLVRWLPSGELEYLGRND 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 171 DQVKIQGFRVELDGVSASISACPGVVQaCAML-----------IQDELWAFYTPIEVPADAvQDVVAQLQ---PKYSVPK 236
Cdd:cd17648 354 FQVKIRGQRIEPGEVEAALASYPGVRE-CAVVakedasqaqsrIQKYLVGYYLPEPGHVPE-SDLLSFLRaklPRYMVPA 431
|
250
....*....|.
gi 807744961 237 RYRALAALPLT 247
Cdd:cd17648 432 RLVRLEGIPVT 442
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
16-247 |
1.85e-48 |
|
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: 165.33 E-value: 1.85e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 16 VDVVISTPSIL------VSHDPADYPNIRVVATAGESC----PVALADRWGQNATFYNCCGPTEVTIVNTMHHHSLGTPL 85
Cdd:cd17650 186 ITLMESTPALIrpvmayVYRNGLDLSAMRLLIVGSDGCkaqdFKTLAARFGQGMRIINSYGVTEATIDSTYYEEGRDPLG 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 86 T-----IGKPTPNNTIYVLDDNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDPFSPeGGMMFNTGDIGRLRDD 160
Cdd:cd17650 266 DsanvpIGRPLPNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAP-GERMYRTGDLARWRAD 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 161 GELDYLGRIDDQVKIQGFRVELDGVSASISACPGVVQACAMLIQD-----ELWAFYTPIEVP-ADAVQDVVAQLQPKYSV 234
Cdd:cd17650 345 GNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDkggeaRLCAYVVAAATLnTAELRAFLAKELPSYMI 424
|
250
....*....|...
gi 807744961 235 PKRYRALAALPLT 247
Cdd:cd17650 425 PSYYVQLDALPLT 437
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
27-247 |
3.22e-48 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 165.30 E-value: 3.22e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 27 VSHDPADYPN-IRVVATAGESCPVALADRW----GQNATFYNCCGPTEVTIVNTMHH-----HSLGTPLTIGKPTPNNTI 96
Cdd:cd17644 215 LLLSTIDLPSsLRLVIVGGEAVQPELVRQWqknvGNFIQLINVYGPTEATIAATVCRltqltERNITSVPIGRPIANTQV 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 97 YVLDDNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDPF-SPEGGMMFNTGDIGRLRDDGELDYLGRIDDQVKI 175
Cdd:cd17644 295 YILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFnSSESERLYKTGDLARYLPDGNIEYLGRIDNQVKI 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 176 QGFRVELDGVSASISACPGVVQACAMLIQDE-----LWAFYtpieVPADAVQDVVAQLQ-------PKYSVPKRYRALAA 243
Cdd:cd17644 375 RGFRIELGEIEAVLSQHNDVKTAVVIVREDQpgnkrLVAYI----VPHYEESPSTVELRqflkaklPDYMIPSAFVVLEE 450
|
....
gi 807744961 244 LPLT 247
Cdd:cd17644 451 LPLT 454
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
14-247 |
1.14e-45 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 163.20 E-value: 1.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 14 RTVDVVISTPSI---LVSHDPAD--YPNIRVVATAGESCPVALADRW---GQNATFYNCCGPTEVTIVNTMHHHSLGTP- 84
Cdd:PRK12316 4783 HRVTVLVFPPVYlqqLAEHAERDgePPSLRVYCFGGEAVAQASYDLAwraLKPVYLFNGYGPTETTVTVLLWKARDGDAc 4862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 85 ----LTIGKPTPNNTIYVLDDNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDPFSPEGGMMFNTGDIGRLRDD 160
Cdd:PRK12316 4863 gaayMPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGGRLYRTGDLARYRAD 4942
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 161 GELDYLGRIDDQVKIQGFRVELDGVSASISACPGVVQAcAMLIQD-----ELWAFYTPIE---VPADAVQ-DVVAQLQ-- 229
Cdd:PRK12316 4943 GVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREA-VVIAQEgavgkQLVGYVVPQDpalADADEAQaELRDELKaa 5021
|
250 260
....*....|....*....|...
gi 807744961 230 -----PKYSVPKRYRALAALPLT 247
Cdd:PRK12316 5022 lrerlPEYMVPAHLVFLARMPLT 5044
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
1-247 |
1.15e-45 |
|
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: 158.05 E-value: 1.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 1 MRGPHRVDWLKVLRT--VDVVISTPSI---LVSH---DPADYPNIRVVATAGESCPVALADRWGQ--NATFYNCCGPTEV 70
Cdd:COG0318 173 LPRFDPERVLELIERerVTVLFGVPTMlarLLRHpefARYDLSSLRLVVSGGAPLPPELLERFEErfGVRIVEGYGLTET 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 71 TIVNTMH--HHSLGTPLTIGKPTPNNTIYVLDDNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFaRDPFspeggmm 148
Cdd:COG0318 253 SPVVTVNpeDPGERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGW------- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 149 FNTGDIGRLRDDGELDYLGRIDDQVKIQGFRVELDGVSASISACPGVVQACAMLIQDELW-----AFYTP---IEVPADA 220
Cdd:COG0318 325 LRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWgervvAFVVLrpgAELDAEE 404
|
250 260
....*....|....*....|....*..
gi 807744961 221 VQDVVAQLQPKYSVPKRYRALAALPLT 247
Cdd:COG0318 405 LRAFLRERLARYKVPRRVEFVDELPRT 431
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
35-247 |
1.28e-45 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 163.20 E-value: 1.28e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 35 PNIRVVATAGESCPVALADRWG---QNATFYNCCGPTEVTIVNTMHHHSLGTP-----LTIGKPTPNNTIYVLDDNLQPT 106
Cdd:PRK12316 2261 PAVRVYCFGGEAVPAASLRLAWealRPVYLFNGYGPTEAVVTPLLWKCRPQDPcgaayVPIGRALGNRRAYILDADLNLL 2340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 107 PRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDPFSPEGGMMFNTGDIGRLRDDGELDYLGRIDDQVKIQGFRVELDGVS 186
Cdd:PRK12316 2341 APGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSASGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIE 2420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 807744961 187 ASISACPGVVQAcAMLIQD-----ELWAFYTPIEVPADAVQDVVAQLQ---PKYSVPKRYRALAALPLT 247
Cdd:PRK12316 2421 ARLQAHPAVREA-VVVAQDgasgkQLVAYVVPDDAAEDLLAELRAWLAarlPAYMVPAHWVVLERLPLN 2488
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
2-247 |
1.49e-45 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 158.20 E-value: 1.49e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 2 RGPHRvdWLKVLRT--VDVVISTPSI---LVSHDPA---DYPNIRVVATAGESCPVALADRWGQ---NATFYNCCGPTEV 70
Cdd:cd12114 204 RDPAH--WAELIERhgVTLWNSVPALlemLLDVLEAaqaLLPSLRLVLLSGDWIPLDLPARLRAlapDARLISLGGATEA 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 71 TIVNTMHhhSLGTPLTI------GKPTPNNTIYVLDDNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDPfspE 144
Cdd:cd12114 282 SIWSIYH--PIDEVPPDwrsipyGRPLANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP---D 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 145 GGMMFNTGDIGRLRDDGELDYLGRIDDQVKIQGFRVELDGVSASISACPGVVQACAMLIQDE----LWAFYTPIE----V 216
Cdd:cd12114 357 GERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPggkrLAAFVVPDNdgtpI 436
|
250 260 270
....*....|....*....|....*....|.
gi 807744961 217 PADAVQDVVAQLQPKYSVPKRYRALAALPLT 247
Cdd:cd12114 437 APDALRAFLAQTLPAYMIPSRVIALEALPLT 467
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
14-247 |
2.37e-45 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 162.25 E-value: 2.37e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 14 RTVDVVISTPSILVS----HDPADYPNIRVVATAGESCPVA---LADRWGQNATFYNCCGPTEVTIVNTM-----HHHSL 81
Cdd:PRK12467 3326 HRISIACFPPAYLQQfaedAGGADCASLDIYVFGGEAVPPAafeQVKRKLKPRGLTNGYGPTEAVVTVTLwkcggDAVCE 3405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 82 GTPLTIGKPTPNNTIYVLDDNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDPFSPEGGMMFNTGDIGRLRDDG 161
Cdd:PRK12467 3406 APYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSGSGGRLYRTGDLARYRADG 3485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 162 ELDYLGRIDDQVKIQGFRVELDGVSASISACPGVVQAcAMLIQD-----ELWAFYTPIEVPADAVQDVVAQLQ---PKYS 233
Cdd:PRK12467 3486 VIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREA-VVLARDgaggkQLVAYVVPADPQGDWRETLRDHLAaslPDYM 3564
|
250
....*....|....
gi 807744961 234 VPKRYRALAALPLT 247
Cdd:PRK12467 3565 VPAQLLVLAAMPLG 3578
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
16-247 |
8.36e-45 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 160.89 E-value: 8.36e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 16 VDVVISTPSI----LVSHDPADYPNIRVVATAGESCPVALADRWGQNATFYNCCGPTEVTIVNTMHHHSLGTP--LTIGK 89
Cdd:PRK12316 3288 VDVLHAYPSMlqafLEEEDAHRCTSLKRIVCGGEALPADLQQQVFAGLPLYNLYGPTEATITVTHWQCVEEGKdaVPIGR 3367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 90 PTPNNTIYVLDDNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDPFSPeGGMMFNTGDIGRLRDDGELDYLGRI 169
Cdd:PRK12316 3368 PIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFVP-GERLYRTGDLARYRADGVIEYIGRV 3446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 170 DDQVKIQGFRVELDGVSASISACPGVVQACAMLIQ-DELWAFYTPIEVPADAVQDVVAQLQ---PKYSVPKRYRALAALP 245
Cdd:PRK12316 3447 DHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDgRQLVAYVVPEDEAGDLREALKAHLKaslPEYMVPAHLLFLERMP 3526
|
..
gi 807744961 246 LT 247
Cdd:PRK12316 3527 LT 3528
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
16-247 |
1.01e-44 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 160.33 E-value: 1.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 16 VDVVISTPS----ILVSHDPADYPNIRVVATAGESCPVALADRW---GQNATFYNCCGPTEVTIVNTMHHHSL------G 82
Cdd:PRK12467 748 VTVLKIVPShlqaLLQASRVALPRPQRALVCGGEALQVDLLARVralGPGARLINHYGPTETTVGVSTYELSDeerdfgN 827
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 83 TPltIGKPTPNNTIYVLDDNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDPFSPEGGMMFNTGDIGRLRDDGE 162
Cdd:PRK12467 828 VP--IGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFGADGGRLYRTGDLARYRADGV 905
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 163 LDYLGRIDDQVKIQGFRVELDGVSASISACPGVVQAcAMLIQDE-----LWAFYTPIEVPA--------DAVQDVVAQLQ 229
Cdd:PRK12467 906 IEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREA-VVLAQPGdaglqLVAYLVPAAVADgaehqatrDELKAQLRQVL 984
|
250
....*....|....*...
gi 807744961 230 PKYSVPKRYRALAALPLT 247
Cdd:PRK12467 985 PDYMVPAHLLLLDSLPLT 1002
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
37-247 |
1.17e-42 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 154.43 E-value: 1.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 37 IRVVATAGESCPVALADRWGQ--NATFYNCCGPTEVTIVNTMH-------HHSLGTPLTIGKPTPNNTIYVLDDNLQPTP 107
Cdd:PRK10252 719 LRQVFCSGEALPADLCREWQQltGAPLHNLYGPTEAAVDVSWYpafgeelAAVRGSSVPIGYPVWNTGLRILDARMRPVP 798
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 108 RGMPGVMWAGGPCVCLGYVNRPELNRNKFARDPFSPeGGMMFNTGDIGRLRDDGELDYLGRIDDQVKIQGFRVELDGVSA 187
Cdd:PRK10252 799 PGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAP-GERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDR 877
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 807744961 188 SISACPGVVQACA---MLIQDE--------LWAFYTP-IEVPAD--AVQDVVAQLQPKYSVPKRYRALAALPLT 247
Cdd:PRK10252 878 AMQALPDVEQAVThacVINQAAatggdarqLVGYLVSqSGLPLDtsALQAQLRERLPPHMVPVVLLQLDQLPLS 951
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
16-247 |
1.19e-42 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 154.55 E-value: 1.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 16 VDVVISTPSIL---VSHDPADY--PNIRVVATAGESCPVALADRWGQ---NATFYNCCGPTEVTIVNTMHHHSLGTP--- 84
Cdd:PRK12467 1810 VTTLHFVPSMLqqlLQMDEQVEhpLSLRRVVCGGEALEVEALRPWLErlpDTGLFNLYGPTETAVDVTHWTCRRKDLegr 1889
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 85 --LTIGKPTPNNTIYVLDDNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDPFSPEGGMMFNTGDIGRLRDDGE 162
Cdd:PRK12467 1890 dsVPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFGTVGSRLYRTGDLARYRADGV 1969
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 163 LDYLGRIDDQVKIQGFRVELDGVSASISACPGVVQAcAMLIQD-----ELWAFYTPI--EVPADAVQDVVAQLQ------ 229
Cdd:PRK12467 1970 IEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREA-VVIAQDgangkQLVAYVVPTdpGLVDDDEAQVALRAIlknhlk 2048
|
250 260
....*....|....*....|.
gi 807744961 230 ---PKYSVPKRYRALAALPLT 247
Cdd:PRK12467 2049 aslPEYMVPAHLVFLARMPLT 2069
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
16-247 |
1.15e-41 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 151.65 E-value: 1.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 16 VDVVISTPSILVS----HDPADYPNIRVVATAGESCPVALADRWGQ---NATFYNCCGPTEVTIVNTmhHHSL----GTP 84
Cdd:PRK12316 747 VDTLHFVPSMLQAflqdEDVASCTSLRRIVCSGEALPADAQEQVFAklpQAGLYNLYGPTEAAIDVT--HWTCveegGDS 824
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 85 LTIGKPTPNNTIYVLDDNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDPFSpEGGMMFNTGDIGRLRDDGELD 164
Cdd:PRK12316 825 VPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFV-AGERMYRTGDLARYRADGVIE 903
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 165 YLGRIDDQVKIQGFRVELDGVSASISACPGVVQAcAMLIQD--ELWAFYTPIEVPADAVQDVVAQLQ---PKYSVPKRYR 239
Cdd:PRK12316 904 YAGRIDHQVKLRGLRIELGEIEARLLEHPWVREA-AVLAVDgkQLVGYVVLESEGGDWREALKAHLAaslPEYMVPAQWL 982
|
....*...
gi 807744961 240 ALAALPLT 247
Cdd:PRK12316 983 ALERLPLT 990
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
57-247 |
2.58e-41 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 147.24 E-value: 2.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 57 QNATFYNCCGPTEVTIVNTMH-HHSLGTPL--TIGKPTPNNTIYVLDDNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNR 133
Cdd:cd17656 270 HNVHLHNHYGPSETHVVTTYTiNPEAEIPElpPIGKPISNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 134 NKFARDPFSPEGgMMFNTGDIGRLRDDGELDYLGRIDDQVKIQGFRVELDGVSASISACPGVVQACAMLIQD-----ELW 208
Cdd:cd17656 350 EKFFPDPFDPNE-RMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADdkgekYLC 428
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 807744961 209 AFYTPI-EVPADAVQDVVAQLQPKYSVPKRYRALAALPLT 247
Cdd:cd17656 429 AYFVMEqELNISQLREYLAKQLPEYMIPSFFVPLDQLPLT 468
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
2-247 |
6.67e-41 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 149.55 E-value: 6.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 2 RGPHRVDWLKVLRTVDVVISTPSILV----SHDPADYPNIRVVATAGESCPVALADRWGQ---NATFYNCCGPTEvTIVN 74
Cdd:PRK05691 1351 RDPQRIAELVQQYGVTTLHFVPPLLQlfidEPLAAACTSLRRLFSGGEALPAELRNRVLQrlpQVQLHNRYGPTE-TAIN 1429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 75 TMHHH---SLGTPLTIGKPTPNNTIYVLDDNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDPFSPEGGMMFNT 151
Cdd:PRK05691 1430 VTHWQcqaEDGERSPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLGEDGARLYRT 1509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 152 GDIGRLRDDGELDYLGRIDDQVKIQGFRVELDGVSASISACPGVVQAcAMLIQD-----ELWAFYT---PIEVPADAVQD 223
Cdd:PRK05691 1510 GDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQA-AVLVREgaagaQLVGYYTgeaGQEAEAERLKA 1588
|
250 260
....*....|....*....|....
gi 807744961 224 VVAQLQPKYSVPKRYRALAALPLT 247
Cdd:PRK05691 1589 ALAAELPEYMVPAQLIRLDQMPLG 1612
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
1-248 |
5.18e-38 |
|
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: 135.49 E-value: 5.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 1 MRGPHRVDWLKVLRT--VDVVISTPSILV------SHDPADYPNIRVVATAGESCPVALADRWGQ--NATFYNCCGPTEV 70
Cdd:cd04433 72 LPKFDPEAALELIERekVTILLGVPTLLArllkapESAGYDLSSLRALVSGGAPLPPELLERFEEapGIKLVNGYGLTET 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 71 TIVNT-----MHHHSLGTpltIGKPTPNNTIYVLDDNLQPTPRGMPGVMWAGGPCVCLGYVNRPElnrnkfARDPFSPEG 145
Cdd:cd04433 152 GGTVAtgppdDDARKPGS---VGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPE------ATAAVDEDG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 146 gmMFNTGDIGRLRDDGELDYLGRIDDQVKIQGFRVELDGVSASISACPGVVQACAMLIQDELW-----AFYTPIE---VP 217
Cdd:cd04433 223 --WYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWgervvAVVVLRPgadLD 300
|
250 260 270
....*....|....*....|....*....|.
gi 807744961 218 ADAVQDVVAQLQPKYSVPKRYRALAALPLTR 248
Cdd:cd04433 301 AEELRAHVRERLAPYKVPRRVVFVDALPRTA 331
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
33-247 |
2.23e-37 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 136.14 E-value: 2.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 33 DYPNIRVVATAGESCPVALADRWgqnaTFYNCCGPTEVTIVNTMH--HHSLGTpLTIGKPTPNNTIYVLDDNLQPTPRGM 110
Cdd:cd17645 213 DNQSLRVLLTGGDKLKKIERKGY----KLVNNYGPTENTVVATSFeiDKPYAN-IPIGKPIDNTRVYILDEALQLQPIGV 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 111 PGVMWAGGPCVCLGYVNRPELNRNKFARDPFSPeGGMMFNTGDIGRLRDDGELDYLGRIDDQVKIQGFRVELDGVSASIS 190
Cdd:cd17645 288 AGELCIAGEGLARGYLNRPELTAEKFIVHPFVP-GERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLM 366
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 807744961 191 ACPGVVQACAMLIQDE-----LWAFYT-PIEVPADAVQDVVAQLQPKYSVPKRYRALAALPLT 247
Cdd:cd17645 367 NHPLIELAAVLAKEDAdgrkyLVAYVTaPEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLT 429
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
4-176 |
1.46e-34 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 127.81 E-value: 1.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 4 PHRVDWLKVLRT--VDVVISTPSILV------SHDPADYPNIRVVATAGESCPVALADRWGQ--NATFYNCCGPTEVTIV 73
Cdd:pfam00501 238 LDPAALLELIERykVTVLYGVPTLLNmlleagAPKRALLSSLRLVLSGGAPLPPELARRFRElfGGALVNGYGLTETTGV 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 74 ---NTMHHHSLGTPLTIGKPTPNNTIYVLDDN-LQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDPfspeggmMF 149
Cdd:pfam00501 318 vttPLPLDEDLRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDG-------WY 390
|
170 180
....*....|....*....|....*..
gi 807744961 150 NTGDIGRLRDDGELDYLGRIDDQVKIQ 176
Cdd:pfam00501 391 RTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
57-247 |
1.44e-32 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 125.28 E-value: 1.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 57 QNATFYNCCGPTEvTIVntMHHHSLG--------TPLTIGKPTPNNTIYVLDDNLQPTPRGMPGVMWAGGPCVCLGYVNR 128
Cdd:PRK05691 2473 APQLFFNAYGPTE-TVV--MPLACLApeqleegaASVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDR 2549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 129 PELNRNKFARDPFSPEGGMMFNTGDIGRLRDDGELDYLGRIDDQVKIQGFRVELDGVSASISACPGVVQAcAMLIQD--- 205
Cdd:PRK05691 2550 PGLTAERFVADPFAADGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREA-VVLALDtps 2628
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 807744961 206 --ELWAFY-TPIEVPADAVQD-----VVAQLQ---PKYSVPKRYRALAALPLT 247
Cdd:PRK05691 2629 gkQLAGYLvSAVAGQDDEAQAalreaLKAHLKqqlPDYMVPAHLILLDSLPLT 2681
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
16-247 |
5.26e-30 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 117.96 E-value: 5.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 16 VDVVISTPSI---LVSHDPADYPNIRVVATAGESCPVALADRWGQ---NATFYNCCGPTE----VTIVNTMHHHSLGTPL 85
Cdd:PRK05691 3961 ITVLESVPSLiqgMLAEDRQALDGLRWMLPTGEAMPPELARQWLQrypQIGLVNAYGPAEcsddVAFFRVDLASTRGSYL 4040
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 86 TIGKPTPNNTIYVLDDNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDPFSPEGGMMFNTGDIGRLRDDGELDY 165
Cdd:PRK05691 4041 PIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFGAPGERLYRTGDLARRRSDGVLEY 4120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 166 LGRIDDQVKIQGFRVELDGVSASISACPGVVQAcAMLIQDELWAFY-TPIEVPADAVQDVVAQLQ----------PKYSV 234
Cdd:PRK05691 4121 VGRIDHQVKIRGYRIELGEIEARLHEQAEVREA-AVAVQEGVNGKHlVGYLVPHQTVLAQGALLErikqrlraelPDYMV 4199
|
250
....*....|...
gi 807744961 235 PKRYRALAALPLT 247
Cdd:PRK05691 4200 PLHWLWLDRLPLN 4212
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
16-247 |
4.14e-27 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 108.44 E-value: 4.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 16 VDVVISTPS------ILVSHDPADYPNIRVVATAGESCPV----ALADRWgQNATFYNCCGPTEVT-----------IVN 74
Cdd:PRK04813 235 INVWVSTPSfadmclLDPSFNEEHLPNLTHFLFCGEELPHktakKLLERF-PSATIYNTYGPTEATvavtsieitdeMLD 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 75 TMhhhslgTPLTIGKPTPNNTIYVLDDNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFardpFSPEGGMMFNTGDI 154
Cdd:PRK04813 314 QY------KRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAF----FTFDGQPAYHTGDA 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 155 GRLrDDGELDYLGRIDDQVKIQGFRVELDGVSASISACPGVVQACAMLIQDE-----LWAFYTPIEVPAD-------AVQ 222
Cdd:PRK04813 384 GYL-EDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDhkvqyLIAYVVPKEEDFErefeltkAIK 462
|
250 260
....*....|....*....|....*
gi 807744961 223 DVVAQLQPKYSVPKRYRALAALPLT 247
Cdd:PRK04813 463 KELKERLMEYMIPRKFIYRDSLPLT 487
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
19-247 |
1.05e-26 |
|
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: 107.14 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 19 VISTPSIL--VSHDPADYPNIRVVATAGESCPVALADRW---GQNATFYNCCGPTEVT-IVNTMHHHSLGT-PLTIGKPT 91
Cdd:cd05922 213 VPSTYAMLtrLGFDPAKLPSLRYLTQAGGRLPQETIARLrelLPGAQVYVMYGQTEATrRMTYLPPERILEkPGSIGLAI 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 92 PNNTIYVLDDNLQPTPRGMPGVMWAGGPCVCLGYVNRPelnrnkfARDPFSPEGGMMFNTGDIGRLRDDGELDYLGRIDD 171
Cdd:cd05922 293 PGGEFEILDDDGTPTPPGEPGEIVHRGPNVMKGYWNDP-------PYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDR 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 172 QVKIQGFRVELDGVSASISACPGVVQACAMLIQDELW----AFYT-PIEVPADAVQDVVAQLQPKYSVPKRYRALAALPL 246
Cdd:cd05922 366 MIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPLGeklaLFVTaPDKIDPKDVLRSLAERLPPYKVPATVRVVDELPL 445
|
.
gi 807744961 247 T 247
Cdd:cd05922 446 T 446
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
30-247 |
5.01e-24 |
|
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: 99.22 E-value: 5.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 30 DPADYPNIRVVATAGESCPVALADRW-GQNATFYNCCGPTEVTIVNTM--HHHSLGTPLTIGKPTPNNTIYVLDDNLQPT 106
Cdd:cd17631 208 ATTDLSSLRAVIYGGAPMPERLLRALqARGVKFVQGYGMTETSPGVTFlsPEDHRRKLGSAGRPVFFVEVRIVDPDGREV 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 107 PRGMPGVMWAGGPCVCLGYVNRPELNRNKFardpfspEGGmMFNTGDIGRLRDDGELDYLGRIDDQVKIQGFRVELDGVS 186
Cdd:cd17631 288 PPGEVGEIVVRGPHVMAGYWNRPEATAAAF-------RDG-WFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVE 359
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 807744961 187 ASISACPGVVQACAMLIQDELW-----AFYTP---IEVPADAVQDVVAQLQPKYSVPKRYRALAALPLT 247
Cdd:cd17631 360 DVLYEHPAVAEVAVIGVPDEKWgeavvAVVVPrpgAELDEDELIAHCRERLARYKIPKSVEFVDALPRN 428
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
36-247 |
1.28e-22 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 95.62 E-value: 1.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 36 NIRVVATAGESCPVALADR-WGQ--NAT-FYNCCGPTEVTIVNTMHH-HSLGTPLTIGKPTPNNTIYVLDDNlqptPRGM 110
Cdd:cd17654 239 SLRVLALGGEPFPSLVILSsWRGkgNRTrIFNIYGITEVSCWALAYKvPEEDSPVQLGSPLLGTVIEVRDQN----GSEG 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 111 PGVMWAGGpcvclgyvnrpeLNRNKFARDPFSPEGGMMFNTGDIGRlRDDGELDYLGRIDDQVKIQGFRVELDGVSASIS 190
Cdd:cd17654 315 TGQVFLGG------------LNRVCILDDEVTVPKGTMRATGDFVT-VKDGELFFLGRKDSQIKRRGKRINLDLIQQVIE 381
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 807744961 191 ACPGVVQACAMLI-QDELWAFYTPIEVPADAVQDVVAQLQPKYSVPKRYRALAALPLT 247
Cdd:cd17654 382 SCLGVESCAVTLSdQQRLIAFIVGESSSSRIHKELQLTLLSSHAIPDTFVQIDKLPLT 439
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
16-239 |
6.38e-19 |
|
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: 85.34 E-value: 6.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 16 VDVVISTPSILVS------HDPADYPNIRVVATAGESCPVALADR---WGQNATFYNCCGPTEVTIVNTMHHHSLGTPLT 86
Cdd:cd05911 237 ITFLYLVPPIAAAlaksplLDKYDLSSLRVILSGGAPLSKELQELlakRFPNATIKQGYGMTETGGILTVNPDGDDKPGS 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 87 IGKPTPNNTIYVLDDNL-QPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDPFspeggmmFNTGDIGRLRDDGELDY 165
Cdd:cd05911 317 VGRLLPNVEAKIVDDDGkDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGW-------LHTGDIGYFDEDGYLYI 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 166 LGRIDDQVKIQGFRV---ELDGVsasISACPGVVQACAMLIQDELWAfytpiEVPADAV----------QDVVAQLQPKy 232
Cdd:cd05911 390 VDRKKELIKYKGFQVapaELEAV---LLEHPGVADAAVIGIPDEVSG-----ELPRAYVvrkpgeklteKEVKDYVAKK- 460
|
....*..
gi 807744961 233 sVPKRYR 239
Cdd:cd05911 461 -VASYKQ 466
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
32-247 |
1.29e-18 |
|
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: 84.15 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 32 ADYPNIRVVATAGESCPVALADRWGQ--NATFYNCCGPTE---VTIVNTMHHHSlgTPLTIGKPTPNNTIYVLDDNLQPT 106
Cdd:cd05936 239 RDFSSLRLCISGGAPLPVEVAERFEEltGVPIVEGYGLTEtspVVAVNPLDGPR--KPGSIGIPLPGTEVKIVDDDGEEL 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 107 PRGMPGVMWAGGPCVCLGYVNRPELNRNKFaRDPFspeggmmFNTGDIGRLRDDGELDYLGRIDDQVKIQGFRV---ELD 183
Cdd:cd05936 317 PPGEVGELWVRGPQVMKGYWNRPEETAEAF-VDGW-------LRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVyprEVE 388
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 807744961 184 GVsasISACPGVVQACAMLIQDELW-----AFYTPIEVPADAVQDVVAQLQ---PKYSVPKRYRALAALPLT 247
Cdd:cd05936 389 EV---LYEHPAVAEAAVVGVPDPYSgeavkAFVVLKEGASLTEEEIIAFCReqlAGYKVPRQVEFRDELPKS 457
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
33-206 |
6.63e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 82.50 E-value: 6.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 33 DYPNIRVVATAGESCPVALADRWgQNATFYNCC---GPTE---VTIVNTMHHHSLGTpltIGKPTPNNTIYVLDDNLQPT 106
Cdd:PRK05677 324 DFSALKLTLSGGMALQLATAERW-KEVTGCAICegyGMTEtspVVSVNPSQAIQVGT---IGIPVPSTLCKVIDDDGNEL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 107 PRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDPFspeggmmFNTGDIGRLRDDGELDYLGRIDDQVKIQGFRV---ELD 183
Cdd:PRK05677 400 PLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGW-------LKTGDIALIQEDGYMRIVDRKKDMILVSGFNVypnELE 472
|
170 180
....*....|....*....|...
gi 807744961 184 GVSASIsacPGVVQACAMLIQDE 206
Cdd:PRK05677 473 DVLAAL---PGVLQCAAIGVPDE 492
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
36-247 |
1.32e-17 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 81.32 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 36 NIRVVATAGESCPVALAdRWGQNA------TFYnccGPTEVTIVnTMHHHSLGT--PLTIGKPTPNNTIYVLDDNLQPTP 107
Cdd:cd05971 208 KLRAIATGGESLGEELL-GWAREQfgvevnEFY---GQTECNLV-IGNCSALFPikPGSMGKPIPGHRVAIVDDNGTPLP 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 108 RGMPGVMWAGGPC--VCLGYVNRPELNRNKFARDpfspeggmMFNTGDIGRLRDDGELDYLGRIDDQVKIQGFRVELDGV 185
Cdd:cd05971 283 PGEVGEIAVELPDpvAFLGYWNNPSATEKKMAGD--------WLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEI 354
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 807744961 186 SASISACPGVVQACAMLIQDE-----------LWAFYTPIEVPADAVQDVVAQLQPKYSVPKRYRALAALPLT 247
Cdd:cd05971 355 EECLLKHPAVLMAAVVGIPDPirgeivkafvvLNPGETPSDALAREIQELVKTRLAAHEYPREIEFVNELPRT 427
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
24-248 |
2.84e-17 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 80.43 E-value: 2.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 24 SILVSHDPAD----YPNIRVVATAGESCPVALADRWgqNATF-------YnccGPTEVTivntmhHHSLGTPL------- 85
Cdd:cd05926 250 QILLNRPEPNpespPPKLRFIRSCSASLPPAVLEAL--EATFgapvleaY---GMTEAA------HQMTSNPLppgprkp 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 86 -TIGKPTpNNTIYVLDDNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDPFspeggmmFNTGDIGRLRDDGELD 164
Cdd:cd05926 319 gSVGKPV-GVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW-------FRTGDLGYLDADGYLF 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 165 YLGRIDDQVKIQGFRV---ELDGVSASisaCPGVVQACAMLIQDEL-----WAFYTPIEVPADAVQDVVAQLQPK---YS 233
Cdd:cd05926 391 LTGRIKELINRGGEKIsplEVDGVLLS---HPAVLEAVAFGVPDEKygeevAAAVVLREGASVTEEELRAFCRKHlaaFK 467
|
250
....*....|....*
gi 807744961 234 VPKRYRALAALPLTR 248
Cdd:cd05926 468 VPKKVYFVDELPKTA 482
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
9-248 |
1.95e-16 |
|
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: 77.76 E-value: 1.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 9 WLKVLRT--VDVVISTPSI---LVSHDPADY--PNIRVVATAGESCPVALADRWGQ--NATFYNCCGPTEVTIVNTMHHH 79
Cdd:cd05972 164 ILELLERygVTSFCGPPTAyrmLIKQDLSSYkfSHLRLVVSAGEPLNPEVIEWWRAatGLPIRDGYGQTETGLTVGNFPD 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 80 SLGTPLTIGKPTPNNTIYVLDDNLQPTPRGMPG-----VMWAGgpcVCLGYVNRPELNRNKFardpfspeGGMMFNTGDI 154
Cdd:cd05972 244 MPVKPGSMGRPTPGYDVAIIDDDGRELPPGEEGdiaikLPPPG---LFLGYVGDPEKTEASI--------RGDYYLTGDR 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 155 GRLRDDGELDYLGRIDDQVKIQGFRVELDGVSASISACPGVVQACAMLIQDELW-----AF------YTPIEVPADAVQD 223
Cdd:cd05972 313 AYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRgevvkAFvvltsgYEPSEELAEELQG 392
|
250 260
....*....|....*....|....*
gi 807744961 224 VVAQLQPKYSVPKRYRALAALPLTR 248
Cdd:cd05972 393 HVKKVLAPYKYPREIEFVEELPKTI 417
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
111-247 |
2.48e-16 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 76.60 E-value: 2.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 111 PGVMWAGGPCVCLGYVNRPElnrnkfaRDPFSPEGgmMFNTGDIGRLRDDGELDYLGRIDDQVKIQGFRVELDGVSASIS 190
Cdd:cd17630 178 DGEIWVGGASLAMGYLRGQL-------VPEFNEDG--WFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALA 248
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 807744961 191 ACPGVVQACAMLIQDELW-----AFYTP-IEVPADAVQDVVAQLQPKYSVPKRYRALAALPLT 247
Cdd:cd17630 249 AHPAVRDAFVVGVPDEELgqrpvAVIVGrGPADPAELRAWLKDKLARFKLPKRIYPVPELPRT 311
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
33-248 |
4.76e-16 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 77.07 E-value: 4.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 33 DYPNIRVVATAGESCP------------VALADRWGQnatfynccgpTEVT--IVNTMHhhslGTPL---TIGKPTPNNT 95
Cdd:COG0365 304 DLSSLRLLGSAGEPLNpevwewwyeavgVPIVDGWGQ----------TETGgiFISNLP----GLPVkpgSMGKPVPGYD 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 96 IYVLDDNLQPTPRGMPGVMWAGG--PCVCLGYVNRPELNRNKFardpFSPEGGMMFnTGDIGRLRDDGELDYLGRIDDQV 173
Cdd:COG0365 370 VAVVDEDGNPVPPGEEGELVIKGpwPGMFRGYWNDPERYRETY----FGRFPGWYR-TGDGARRDEDGYFWILGRSDDVI 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 174 KIQGFRV---EldgVSASISACPGVVQACAMLIQDEL-----WAF------YTPIEVPADAVQDVVAQLQPKYSVPKRYR 239
Cdd:COG0365 445 NVSGHRIgtaE---IESALVSHPAVAEAAVVGVPDEIrgqvvKAFvvlkpgVEPSDELAKELQAHVREELGPYAYPREIE 521
|
....*....
gi 807744961 240 ALAALPLTR 248
Cdd:COG0365 522 FVDELPKTR 530
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
4-247 |
1.30e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 75.61 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 4 PHRVDWLKVLRTVD---VVIST--PSIL--VSHDPA----DYPNIRVVATAGESCPVALADRWGQ--NATFYNCCGPTE- 69
Cdd:PRK06187 239 PRRFDPENLLDLIEterVTFFFavPTIWqmLLKAPRayfvDFSSLRLVIYGGAALPPALLREFKEkfGIDLVQGYGMTEt 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 70 --VTIVNTMHHHSLGT---PLTIGKPTPNNTIYVLDDNLQPTPR--GMPGVMWAGGPCVCLGYVNRPELNRNKFardpfs 142
Cdd:PRK06187 319 spVVSVLPPEDQLPGQwtkRRSAGRPLPGVEARIVDDDGDELPPdgGEVGEIIVRGPWLMQGYWNRPEATAETI------ 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 143 pEGGMMFnTGDIGRLRDDGELDYLGRIDDQVKIQG---FRVELDGVsasISACPGVVQACAMLIQDELW-----AFYTPI 214
Cdd:PRK06187 393 -DGGWLH-TGDVGYIDEDGYLYITDRIKDVIISGGeniYPRELEDA---LYGHPAVAEVAVIGVPDEKWgerpvAVVVLK 467
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 807744961 215 E-VPADA------VQDVVAqlqpKYSVPKRYRALAALPLT 247
Cdd:PRK06187 468 PgATLDAkelrafLRGRLA----KFKLPKRIAFVDELPRT 503
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
4-247 |
1.40e-15 |
|
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: 75.48 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 4 PHRVdwLKVLRTV--DVVISTP----SILVSHDPADY--PNIRVVATAGESCPVALADRWgqNATF----YNCCGPTEVT 71
Cdd:cd05959 243 PAAV--FKRIRRYrpTVFFGVPtlyaAMLAAPNLPSRdlSSLRLCVSAGEALPAEVGERW--KARFgldiLDGIGSTEML 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 72 ---IVNTMHHHSLGTPltiGKPTPNNTIYVLDDNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFardpfspEGGmM 148
Cdd:cd05959 319 hifLSNRPGRVRYGTT---GKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTF-------QGE-W 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 149 FNTGDIGRLRDDGELDYLGRIDDQVKIQGFRVELDGVSASISACPGVVQACAMLIQDE-----LWAF------YTPIEVP 217
Cdd:cd05959 388 TRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEdgltkPKAFvvlrpgYEDSEAL 467
|
250 260 270
....*....|....*....|....*....|
gi 807744961 218 ADAVQDVVAQLQPKYSVPKRYRALAALPLT 247
Cdd:cd05959 468 EEELKEFVKDRLAPYKYPRWIVFVDELPKT 497
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
31-247 |
2.53e-14 |
|
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: 71.72 E-value: 2.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 31 PADYPNIRVVATAGESCPVALADRWgqnATFYNC-----CGPTEVT---IVNTMHHHSLGTpltIGKPTPNNTIYVLDDN 102
Cdd:cd05919 204 PDALRSLRLCVSAGEALPRGLGERW---MEHFGGpildgIGATEVGhifLSNRPGAWRLGS---TGRPVPGYEIRLVDEE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 103 LQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFArdpfspegGMMFNTGDIGRLRDDGELDYLGRIDDQVKIQGFRVEL 182
Cdd:cd05919 278 GHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFN--------GGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSP 349
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 807744961 183 DGVSASISACPGVVQACAMLIQDE-----LWAF------YTPIEVPADAVQDVVAQLQPKYSVPKRYRALAALPLT 247
Cdd:cd05919 350 VEVESLIIQHPAVAEAAVVAVPEStglsrLTAFvvlkspAAPQESLARDIHRHLLERLSAHKVPRRIAFVDELPRT 425
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
86-247 |
3.68e-14 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 71.33 E-value: 3.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 86 TIGKP-TPNNTIYVLDDNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDPFspeggmmFNTGDIGRLRDDGELD 164
Cdd:COG1021 354 TQGRPiSPDDEVRIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFTPDGF-------YRTGDLVRRTPDGYLV 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 165 YLGRIDDQV-----KIQGFRVELdgvsaSISACPGVVQACAMLIQDELW-----AFYTPIEVPADAVqDVVAQLQ----P 230
Cdd:COG1021 427 VEGRAKDQInrggeKIAAEEVEN-----LLLAHPAVHDAAVVAMPDEYLgerscAFVVPRGEPLTLA-ELRRFLRerglA 500
|
170
....*....|....*..
gi 807744961 231 KYSVPKRYRALAALPLT 247
Cdd:COG1021 501 AFKLPDRLEFVDALPLT 517
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
37-247 |
5.25e-14 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 70.62 E-value: 5.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 37 IRVVATAGESCPVALADRWGQN--ATFYNCCGPTEVTIVNTMHHHsLGTPL---TIGKPTPNNTIYVLDDNLQPTPRGMP 111
Cdd:cd05973 207 LRRVSSAGEPLTPEVIRWFDAAlgVPIHDHYGQTELGMVLANHHA-LEHPVhagSAGRAMPGWRVAVLDDDGDELGPGEP 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 112 GVmwaggpcVCLGYVNRPELNRNKFARDPFSPEGGMMFNTGDIGRLRDDGELDYLGRIDDQVKIQGFRVELDGVSASISA 191
Cdd:cd05973 286 GR-------LAIDIANSPLMWFRGYQLPDTPAIDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIE 358
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 807744961 192 CPGVVQACAMLIQDE-----LWAF------YTPIEVPADAVQDVVAQLQPKYSVPKRYRALAALPLT 247
Cdd:cd05973 359 HPAVAEAAVIGVPDPertevVKAFvvlrggHEGTPALADELQLHVKKRLSAHAYPRTIHFVDELPKT 425
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
86-247 |
5.78e-14 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 70.82 E-value: 5.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 86 TIGKP-TPNNTIYVLDDNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDPFspeggmmFNTGDIGRLRDDGELD 164
Cdd:cd05920 309 TQGRPmSPDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF-------YRTGDLVRRTPDGYLV 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 165 YLGRIDDQVKIQGFRVELDGVSASISACPGVVQACAMLIQDELW-----AFYTPIEVPADAVQdVVAQLQ----PKYSVP 235
Cdd:cd05920 382 VEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLgerscAFVVLRDPPPSAAQ-LRRFLRerglAAYKLP 460
|
170
....*....|..
gi 807744961 236 KRYRALAALPLT 247
Cdd:cd05920 461 DRIEFVDSLPLT 472
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
4-246 |
8.17e-14 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 70.44 E-value: 8.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 4 PHRVDWLKVLRTVD-----VVISTPS----ILVSHDPADYPNIRVVATAGESCPVALADRWGQnaTF----YNCCGPTE- 69
Cdd:cd05909 221 PNPLDYKKIPELIYdkkatILLGTPTflrgYARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQE--KFgiriLEGYGTTEc 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 70 --VTIVNT--MHHHslgtPLTIGKPTPNNTIYVLD-DNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFardpfspe 144
Cdd:cd05909 299 spVISVNTpqSPNK----EGTVGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF-------- 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 145 GGMMFNTGDIGRLRDDGELDYLGRIDDQVKIQGFRVELDGVSASIS-ACPGVVQACAMLIQDE-----LWAFYTPIEVPA 218
Cdd:cd05909 367 GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSeILPEDNEVAVVSVPDGrkgekIVLLTTTTDTDP 446
|
250 260
....*....|....*....|....*....
gi 807744961 219 DAVQDVVAQLQ-PKYSVPKRYRALAALPL 246
Cdd:cd05909 447 SSLNDILKNAGiSNLAKPSYIHQVEEIPL 475
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
28-247 |
8.60e-14 |
|
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: 70.01 E-value: 8.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 28 SHDPADYPnIRVVATAG--ESCPVALADRWGqnATFYNCCGPTEVTIVNTMHHHSLGTPLTIGKPTPNNTIYVLDDNLQP 105
Cdd:cd05934 190 SPDDRAHR-LRAAYGAPnpPELHEEFEERFG--VRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDDDGQE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 106 TPRGMPG---VMWAGGPCVCLGYVNRPELNRNKFArdpfspegGMMFNTGDIGRLRDDGELDYLGRIDDQVKIQGFRVEL 182
Cdd:cd05934 267 LPAGEPGelvIRGLRGWGFFKGYYNMPEATAEAMR--------NGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISS 338
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 807744961 183 DGVSASISACPGVVQACAMLIQDELwafyTPIEVPADAV---------QDVVAQLQ---PKYSVPKRYRALAALPLT 247
Cdd:cd05934 339 AEVERAILRHPAVREAAVVAVPDEV----GEDEVKAVVVlrpgetldpEELFAFCEgqlAYFKVPRYIRFVDDLPKT 411
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
87-235 |
9.21e-14 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 70.00 E-value: 9.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 87 IGKPTPNNTIYVLDDNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDPFspeggmmFNTGDIGRLrDDGELDYL 166
Cdd:cd05906 356 LGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGW-------FRTGDLGFL-DNGNLTIT 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 167 GRIDDQVKIQG---FRVELDgvsASISACPGV----VQACAMLIQ----DELWAFYTPIEVPAD-------AVQDVVAQ- 227
Cdd:cd05906 428 GRTKDTIIVNGvnyYSHEIE---AAVEEVPGVepsfTAAFAVRDPgaetEELAIFFVPEYDLQDalsetlrAIRSVVSRe 504
|
170
....*....|
gi 807744961 228 --LQPKYSVP 235
Cdd:cd05906 505 vgVSPAYLIP 514
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
30-246 |
1.00e-13 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 70.34 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 30 DPADYPNIRVVATAGESCPVALADRWGQ--NATFYNCCGPTE---VTIVNTMHHHSLGTPL-------TIGKPTPNNTIY 97
Cdd:PRK08633 893 HPLMFASLRLVVAGAEKLKPEVADAFEEkfGIRILEGYGATEtspVASVNLPDVLAADFKRqtgskegSVGMPLPGVAVR 972
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 98 VLD-DNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNrNKFARDpfsPEGGMMFNTGDIGRLRDDGELDYLGRIDDQVKIQ 176
Cdd:PRK08633 973 IVDpETFEELPPGEDGLILIGGPQVMKGYLGDPEKT-AEVIKD---IDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIG 1048
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 807744961 177 GFRVELDGVSASISA--CPGVVQACAMLIQDE-----LWAFYTPIEVPADAVQDVVAQLQ-PKYSVPKRYRALAALPL 246
Cdd:PRK08633 1049 GEMVPLGAVEEELAKalGGEEVVFAVTAVPDEkkgekLVVLHTCGAEDVEELKRAIKESGlPNLWKPSRYFKVEALPL 1126
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
79-247 |
1.64e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 69.24 E-value: 1.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 79 HSLGTP---LTIGKPTPNNTIYVLDDNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFArdpfspeGGMMfNTGDIG 155
Cdd:PRK06188 330 HDPDDPkrlTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFR-------DGWL-HTGDVA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 156 RLRDDGELDYLGRIDDQVKIQGFRVELDGVSASISACPGVVQACAMLIQDELWA-FYTPIEVPADAVQDVVAQLQP---- 230
Cdd:PRK06188 402 REDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGeAVTAVVVLRPGAAVDAAELQAhvke 481
|
170 180
....*....|....*....|
gi 807744961 231 -KYSV--PKRYRALAALPLT 247
Cdd:PRK06188 482 rKGSVhaPKQVDFVDSLPLT 501
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
33-206 |
3.68e-13 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 68.54 E-value: 3.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 33 DYPNIRVVATAGESCPVALADRWgQNATFYNCC---GPTE------VTIVNTMHHHSlgtplTIGKPTPNNTIYVLDDNL 103
Cdd:PRK08974 323 DFSSLKLSVGGGMAVQQAVAERW-VKLTGQYLLegyGLTEcsplvsVNPYDLDYYSG-----SIGLPVPSTEIKLVDDDG 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 104 QPTPRGMPGVMWAGGPCVCLGYVNRPElnrnkfARDPFSPEGGMmfNTGDIGRLRDDGELDYLGRIDDQVKIQGFRVELD 183
Cdd:PRK08974 397 NEVPPGEPGELWVKGPQVMLGYWQRPE------ATDEVIKDGWL--ATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPN 468
|
170 180
....*....|....*....|...
gi 807744961 184 GVSASISACPGVVQACAMLIQDE 206
Cdd:PRK08974 469 EIEDVVMLHPKVLEVAAVGVPSE 491
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
58-248 |
5.29e-13 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 67.29 E-value: 5.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 58 NATFYNCCGPTEVTIVNTMHHHSlGTPLTIGKPTPNNTIYVLDDNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFa 137
Cdd:cd17637 136 GATFWSLYGQTETSGLVTLSPYR-ERPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF- 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 138 RDPFSpeggmmfNTGDIGRLRDDGELDYLGRI--DDQVKIQGFRVELDGVSASISACPGVVQACAMLIQDELW------- 208
Cdd:cd17637 214 RNGWH-------HTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWgegikav 286
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 807744961 209 ------AFYTpievpADAVQDVVAQLQPKYSVPKRYRALAALPLTR 248
Cdd:cd17637 287 cvlkpgATLT-----ADELIEFVGSRIARYKKPRYVVFVEALPKTA 327
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
30-245 |
8.27e-13 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 67.48 E-value: 8.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 30 DPADYPNIRVVATAGESCP----VALADRWGQnaTFYNCCGPTEVTIVNTMHHHSL-GTPLTIGKPTPNNTIYVLDDNLQ 104
Cdd:PRK13382 307 NRYSGRSLRFAAASGSRMRpdvvIAFMDQFGD--VIYNNYNATEAGMIATATPADLrAAPDTAGRPAEGTEIRILDQDFR 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 105 PTPRGMPGVMWAGGPCVCLGYVNrpelNRNKFARDpfspegGMMfNTGDIGRLRDDGELDYLGRIDDQVKIQGFRVELDG 184
Cdd:PRK13382 385 EVPTGEVGTIFVRNDTQFDGYTS----GSTKDFHD------GFM-ASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIE 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 185 VSASISACPGVVQACAMLIQDE-----LWAFYTP----IEVPADAVQDVVAQLqPKYSVPKRYRALAALP 245
Cdd:PRK13382 454 VEKTLATHPDVAEAAVIGVDDEqygqrLAAFVVLkpgaSATPETLKQHVRDNL-ANYKVPRDIVVLDELP 522
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
86-200 |
1.59e-12 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 66.47 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 86 TIGKPTPNNTIYVLD------DNLQPTPRGMpgvMWAGGPCVCLGYVNRPELNRNKFARDPFspeggmmFNTGDIGRLRD 159
Cdd:cd17639 302 RVGPPLPCCEIKLVDweeggySTDKPPPRGE---ILIRGPNVFKGYYKNPEKTKEAFDGDGW-------FHTGDIGEFHP 371
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 807744961 160 DGELDYLGRIDDQVKIQ-GFRVELDGVSASISACPGVVQACA 200
Cdd:cd17639 372 DGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLVNNICV 413
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
33-247 |
1.81e-12 |
|
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: 66.35 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 33 DYPNIRVVATAGESCPVALADRWgQNAT---FYNCCGPTE---VTIVNTMHHHSLGTpltIGKPTPNNTIYVLDDNLQPT 106
Cdd:cd05958 211 DLSSLRKCVSAGEALPAALHRAW-KEATgipIIDGIGSTEmfhIFISARPGDARPGA---TGKPVPGYEAKVVDDEGNPV 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 107 PRGMPGVMWAGGPCVCLGyvnrpelNRNKFARDPFspeGGMMFNTGDIGRLRDDGELDYLGRIDDQVKIQGFRVELDGVS 186
Cdd:cd05958 287 PDGTIGRLAVRGPTGCRY-------LADKRQRTYV---QGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVE 356
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 807744961 187 ASISACPGvVQACAML---IQDELW---AF------YTPIEVPADAVQDVVAQLQPKYSVPKRYRALAALPLT 247
Cdd:cd05958 357 DVLLQHPA-VAECAVVghpDESRGVvvkAFvvlrpgVIPGPVLARELQDHAKAHIAPYKYPRAIEFVTELPRT 428
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
33-247 |
3.01e-12 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 65.61 E-value: 3.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 33 DYPNIRVVATAGESCPVALADRWGQ--NATFYNCCGPTEVT-IVNTMHHHSLGTPLTIGKPTPNNTIYVLDDNLQPTPRG 109
Cdd:PRK12492 331 DFSALKLTNSGGTALVKATAERWEQltGCTIVEGYGLTETSpVASTNPYGELARLGTVGIPVPGTALKVIDDDGNELPLG 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 110 MPGVMWAGGPCVCLGYVNRPELnrnkfARDPFSPEGgmMFNTGDIGRLRDDGELDYLGRIDDQVKIQGFRVELDGVSASI 189
Cdd:PRK12492 411 ERGELCIKGPQVMKGYWQQPEA-----TAEALDAEG--WFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVV 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 807744961 190 SACPGVVQACAMLIQDE-----LWAFYTPIEvPADAVQDVVAQLQPK---YSVPKRYRALAALPLT 247
Cdd:PRK12492 484 MAHPKVANCAAIGVPDErsgeaVKLFVVARD-PGLSVEELKAYCKENftgYKVPKHIVLRDSLPMT 548
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
58-245 |
6.55e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 64.57 E-value: 6.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 58 NATFYNCCGPTEVTIVNTM--HHHSLGTPLTIGKPTPNNTIYVLDDNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNK 135
Cdd:PRK08316 312 GLRFYNCYGQTEIAPLATVlgPEEHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEA 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 136 FArdpfspeGGmMFNTGDIGRLRDDGELDYLGRIDDQVKIQGFRVELDGVSASISACPGVVQACAMLIQDELW-----AF 210
Cdd:PRK08316 392 FR-------GG-WFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWieavtAV 463
|
170 180 190
....*....|....*....|....*....|....*...
gi 807744961 211 YTP---IEVPADAVQDVVAQLQPKYSVPKRYRALAALP 245
Cdd:PRK08316 464 VVPkagATVTEDELIAHCRARLAGFKVPKRVIFVDELP 501
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
16-245 |
8.24e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 64.56 E-value: 8.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 16 VDVVISTPSIL---VSHDPA-----DYPNIRVVATAGESCPVALADRwgQNATF----YNCCGPTEVTI--VNTMHHHSL 81
Cdd:PRK07788 296 ATALVVVPVMLsriLDLGPEvlakyDTSSLKIIFVSGSALSPELATR--ALEAFgpvlYNLYGSTEVAFatIATPEDLAE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 82 gTPLTIGKPTPNNTIYVLDDNLQPTPRGMPGVMWAGGPCVCLGYVNrpelNRNKFARDpfspegGMMfNTGDIGRLRDDG 161
Cdd:PRK07788 374 -APGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTD----GRDKQIID------GLL-SSGDVGYFDEDG 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 162 ELDYLGRIDDQVKIQGFRVELDGVSASISACPGVVQACAMLIQDELW-----AFYTPIE---VPADAVQDVVAQLQPKYS 233
Cdd:PRK07788 442 LLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFgqrlrAFVVKAPgaaLDEDAIKDYVRDNLARYK 521
|
250
....*....|..
gi 807744961 234 VPKRYRALAALP 245
Cdd:PRK07788 522 VPRDVVFLDELP 533
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
5-245 |
8.34e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 64.25 E-value: 8.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 5 HRVDWLKVLRTVDV-VISTPSILVSHDPadYPNIRVVATAGESCPVALADRWGQ--NATFYNCCGPTEVTIvntmhhHSL 81
Cdd:PRK13383 263 HRADAFTAVPVVLArILELPPRVRARNP--LPQLRVVMSSGDRLDPTLGQRFMDtyGDILYNGYGSTEVGI------GAL 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 82 GTPL-------TIGKPTPNNTIYVLDDNLQPTPRGMPGVMWAGGpcvclgyvnrpELNRnkfarDPFSPEGGM-----MF 149
Cdd:PRK13383 335 ATPAdlrdapeTVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGG-----------ELAG-----TRYTDGGGKavvdgMT 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 150 NTGDIGRLRDDGELDYLGRIDDQVKIQGFRVELDGVSASISACPGVVQACAMLIQDE-----LWAF---YTPIEVPADAV 221
Cdd:PRK13383 399 STGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDErfghrLAAFvvlHPGSGVDAAQL 478
|
250 260
....*....|....*....|....
gi 807744961 222 QDVVAQLQPKYSVPKRYRALAALP 245
Cdd:PRK13383 479 RDYLKDRVSRFEQPRDINIVSSIP 502
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
107-247 |
1.09e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 63.99 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 107 PRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDPFspeggmmFNTGDIGRLRDDGELDYLGRIDDQVKIQGFRVELDGVS 186
Cdd:PRK06164 373 PDGESGEIEIRAPSLMRGYLDNPDATARALTDDGY-------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIE 445
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 807744961 187 ASISACPGVVQACAMLI----QDELWAFYTPIE-VPADAvQDVVAQLQ---PKYSVPKRYRALAALPLT 247
Cdd:PRK06164 446 HALEALPGVAAAQVVGAtrdgKTVPVAFVIPTDgASPDE-AGLMAACRealAGFKVPARVQVVEAFPVT 513
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
36-174 |
1.21e-11 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 63.97 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 36 NIRVVATAGESCPVALAdrwgqnaTFYNCCG-P-------TE---VTIVNTMHHHSLGTpltIGKPTPNNTIYVLDDnlq 104
Cdd:COG1022 348 RLRFAVSGGAALGPELA-------RFFRALGiPvlegyglTEtspVITVNRPGDNRIGT---VGPPLPGVEVKIAED--- 414
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 105 ptprgmpGVMWAGGPCVCLGYVNRPELNRNKFARDPFspeggmmFNTGDIGRLRDDGELDYLGRIDDQVK 174
Cdd:COG1022 415 -------GEILVRGPNVMKGYYKNPEATAEAFDADGW-------LHTGDIGELDEDGFLRITGRKKDLIV 470
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
86-206 |
1.22e-11 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 63.89 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 86 TIGKPTPNNTIYVLDDNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDPFspeggmmFNTGDIGRLRDDGELDY 165
Cdd:PRK07059 381 TIGLPLPSTEVSIRDDDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGF-------FRTGDVGVMDERGYTKI 453
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 807744961 166 LGRIDDQVKIQGFRV---ELDGVSASisaCPGVVQACAMLIQDE 206
Cdd:PRK07059 454 VDRKKDMILVSGFNVypnEIEEVVAS---HPGVLEVAAVGVPDE 494
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
55-247 |
2.03e-11 |
|
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: 62.66 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 55 WGQNATFYNCCGPTEVTIVNTM-HHHSLGTPLTIGKPTPNNTIYVLDDNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNR 133
Cdd:cd17635 139 ATGLTNTAQVYGLSETGTALCLpTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTA 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 134 NKFArdpfspegGMMFNTGDIGRLRDDGELDYLGRIDDQVKIQGFRVELDGVSASISACPGVVQACAMLIQDELWAFYTP 213
Cdd:cd17635 219 EVLI--------DGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVG 290
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 807744961 214 IEVPADAVQD----------VVAQLqPKYSVPKRYRALAALPLT 247
Cdd:cd17635 291 LAVVASAELDenairalkhtIRREL-EPYARPSTIVIVTDIPRT 333
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
9-206 |
2.23e-11 |
|
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: 62.88 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 9 WLKVLRTVDVVISTPSILVShdpaDYPNIRVVATAGESCPVALADR-WGQNATFYN-CCGPTEV---TIVNTMHHHSLGT 83
Cdd:cd05935 177 WTNIPTMLVDLLATPEFKTR----DLSSLKVLTGGGAPMPPAVAEKlLKLTGLRFVeGYGLTETmsqTHTNPPLRPKLQC 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 84 pltIGKPTPNNTIYVLD-DNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDpfspEGGMMFNTGDIGRLRDDGE 162
Cdd:cd05935 253 ---LGIP*FGVDARVIDiETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEI----KGRRFFRTGDLGYMDEEGY 325
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 807744961 163 LDYLGRIDDQVKIQGFRVELDGVSASISACPGVVQACAMLIQDE 206
Cdd:cd05935 326 FFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDE 369
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
86-247 |
2.30e-11 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 63.09 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 86 TIGKP-TPNNTIYVLDDNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDPFspeggmmFNTGDIGRLRDDGELD 164
Cdd:PRK10946 354 TQGRPmSPDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGF-------YCSGDLVSIDPDGYIT 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 165 YLGRIDDQVKIQGFRVELDGVSASISACPGVVQACAMLIQDELW-----AFYtpieVPADAVQDVV------AQLQPKYS 233
Cdd:PRK10946 427 VVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMgekscAFL----VVKEPLKAVQlrrflrEQGIAEFK 502
|
170
....*....|....
gi 807744961 234 VPKRYRALAALPLT 247
Cdd:PRK10946 503 LPDRVECVDSLPLT 516
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
84-245 |
4.60e-11 |
|
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: 61.92 E-value: 4.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 84 PLTIGKPTPNNTIYVLDDN-LQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDPFspeggmmFNTGDIGRLRDDGE 162
Cdd:cd05941 263 PGTVGMPLPGVQARIVDEEtGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW-------FKTGDLGVVDEDGY 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 163 LDYLGRI-DDQVKIQGFRVELDGVSASISACPGVVQACAMLIQDELW-----AFYTPIE----VPADAVQDVVAQLQPKY 232
Cdd:cd05941 336 YWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWgervvAVVVLRAgaaaLSLEELKEWAKQRLAPY 415
|
170
....*....|...
gi 807744961 233 SVPKRYRALAALP 245
Cdd:cd05941 416 KRPRRLILVDELP 428
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
104-247 |
4.62e-11 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 62.21 E-value: 4.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 104 QPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDpfspeggmMFNTGDIGRLRDDGELDYLGRIDDQVKIQGFRVELD 183
Cdd:PRK05852 373 LPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFTDG--------WLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPE 444
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 807744961 184 GVSASISACPGVVQACAMLIQDELW-----AFYTPIEVPADAVQDVVAQLQPK---YSVPKRYRALAALPLT 247
Cdd:PRK05852 445 RVEGVLASHPNVMEAAVFGVPDQLYgeavaAVIVPRESAPPTAEELVQFCRERlaaFEIPASFQEASGLPHT 516
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
88-247 |
5.76e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 61.75 E-value: 5.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 88 GKPTPNNTIYVLDDNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDPFspeggmmFNTGDIGRLRDDGELDYLG 167
Cdd:PRK09088 309 GIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGW-------FRTGDIARRDADGFFWVVD 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 168 RIDDQVKIQGFRVELDGVSASISACPGVVQACAMLIQDELW-----AFYTPIEVPADAVQDVVAQLQ---PKYSVPKRYR 239
Cdd:PRK09088 382 RKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWgevgyLAIVPADGAPLDLERIRSHLStrlAKYKVPKHLR 461
|
....*...
gi 807744961 240 ALAALPLT 247
Cdd:PRK09088 462 LVDALPRT 469
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
124-246 |
7.57e-11 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 61.62 E-value: 7.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 124 GYVNRPELNRNKFARDPFSPEG---------------------GMMFNTGDIGRLRDDGELDYLGRIDDQVKIQGFRVEL 182
Cdd:TIGR03443 634 GYLGLPELNAEKFVNNWFVDPShwidldkennkperefwlgprDRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIEL 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 183 DGVSASISACPGVVQACAMLIQDE-----LWAFYTPI-----------EVPADAVQDVVAQLQ----------------- 229
Cdd:TIGR03443 714 GEIDTHLSQHPLVRENVTLVRRDKdeeptLVSYIVPQdksdeleefksEVDDEESSDPVVKGLikyrklikdireylkkk 793
|
170
....*....|....*...
gi 807744961 230 -PKYSVPKRYRALAALPL 246
Cdd:TIGR03443 794 lPSYAIPTVIVPLKKLPL 811
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
15-247 |
7.74e-11 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 61.21 E-value: 7.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 15 TVDVVISTPSILVSHDPADYP-NIRVVATAGESCPVALADRWGQ-NATFYNCCGPTE-----VTIVNTMHHHSLGTpltI 87
Cdd:cd05912 168 IISVVPTMLQRLLEILGEGYPnNLRCILLGGGPAPKPLLEQCKEkGIPVYQSYGMTEtcsqiVTLSPEDALNKIGS---A 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 88 GKPTPNNTIYVLDDNLQPtprGMPGVMWAGGPCVCLGYVNRPELNRNKFARDpfspeggmMFNTGDIGRLRDDGELDYLG 167
Cdd:cd05912 245 GKPLFPVELKIEDDGQPP---YEVGEILLKGPNVTKGYLNRPDATEESFENG--------WFKTGDIGYLDEEGFLYVLD 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 168 RIDDQVkIQG----FRVELDGVSASIsacPGVVQACAMLIQDELWAfytpiEVPADAV---QDV-VAQLQ-------PKY 232
Cdd:cd05912 314 RRSDLI-ISGgeniYPAEIEEVLLSH---PAIKEAGVVGIPDDKWG-----QVPVAFVvseRPIsEEELIaycseklAKY 384
|
250
....*....|....*
gi 807744961 233 SVPKRYRALAALPLT 247
Cdd:cd05912 385 KVPKKIYFVDELPRT 399
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
21-177 |
8.81e-11 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 61.22 E-value: 8.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 21 STPSIL-----VSHDPADYPNIRVVATAGESCPVALADRWGQ--NATFYNCCGPTEVTIVNTmhhHSLGTPL-----TIG 88
Cdd:PRK13295 293 STPFLTdltraVKESGRPVSSLRTFLCAGAPIPGALVERARAalGAKIVSAWGMTENGAVTL---TKLDDPDerastTDG 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 89 KPTPNNTIYVLDDNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFardpfspEGgmMFNTGDIGRLRDDGELDYLGR 168
Cdd:PRK13295 370 CPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGTDA-------DG--WFDTGDLARIDADGYIRISGR 440
|
....*....
gi 807744961 169 IDDqVKIQG 177
Cdd:PRK13295 441 SKD-VIIRG 448
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
31-247 |
8.82e-11 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 61.59 E-value: 8.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 31 PADYPNIRVVATAGESCPVALADRWGQ---NATFYNCCGPTEV--TIV-NTMHHHSLGTpltIGKPTPNNTIYVLDDNLQ 104
Cdd:PRK06060 256 PDSFRSLRCVVSAGEALELGLAERLMEffgGIPILDGIGSTEVgqTFVsNRVDEWRLGT---LGRVLPPYEIRVVAPDGT 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 105 PTPRGMPGVMWAGGPCVCLGYVNRPelnrnkfarDPFSPEGGMMfNTGDIGRLRDDGELDYLGRIDDQVKIQGFRVELDG 184
Cdd:PRK06060 333 TAGPGVEGDLWVRGPAIAKGYWNRP---------DSPVANEGWL-DTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPRE 402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 807744961 185 VSASISACPGVVQACAMLIQD-----ELWAFYTPIE---VPADAVQDVVAQLQPK---YSVPKRYRALAALPLT 247
Cdd:PRK06060 403 VERLIIEDEAVAEAAVVAVREstgasTLQAFLVATSgatIDGSVMRDLHRGLLNRlsaFKVPHRFAVVDRLPRT 476
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
33-245 |
8.93e-11 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 61.25 E-value: 8.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 33 DYPNIRVVATAGESCPV----ALADRWGqnATFYNCCGPTEVTIVNTmhHHS---LGTPLTIGKPTPNNTIYVLDDNLQP 105
Cdd:PRK12406 269 DVSSLRHVIHAAAPCPAdvkrAMIEWWG--PVIYEYYGSTESGAVTF--ATSedaLSHPGTVGKAAPGAELRFVDEDGRP 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 106 TPRGMPGVMW---AGGPCVClgYVNRPElNRNKFARDPFspeggmmFNTGDIGRLRDDGELDYLGRIDDQVKIQGFRVEL 182
Cdd:PRK12406 345 LPQGEIGEIYsriAGNPDFT--YHNKPE-KRAEIDRGGF-------ITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYP 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 807744961 183 DGVSASISACPGvVQACAML-IQDE-----LWAFYTP---IEVPADAVQDVVAQLQPKYSVPKRYRALAALP 245
Cdd:PRK12406 415 AEIEAVLHAVPG-VHDCAVFgIPDAefgeaLMAVVEPqpgATLDEADIRAQLKARLAGYKVPKHIEIMAELP 485
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
21-247 |
9.07e-11 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 61.30 E-value: 9.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 21 STPSI-----LVSHDPADYPNIRVVATAGESCPVALADR-WGQNATFYNCCGPTEV---TIVNtmhhhsLGTPL-----T 86
Cdd:PRK06087 283 ATPFIydllnLLEKQPADLSALRFFLCGGTTIPKKVAREcQQRGIKLLSVYGSTESsphAVVN------LDDPLsrfmhT 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 87 IGKPTPNNTIYVLDDNLQPTPRGMPGVMWAGGPCVCLGYVNRPEL-NRnkfARDpfsPEGgmMFNTGDIGRLRDDGELDY 165
Cdd:PRK06087 357 DGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELtAR---ALD---EEG--WYYSGDLCRMDEAGYIKI 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 166 LGRIDDQVKIQGFRVELDGVSASISACPGVVQACAMLIQDE-----LWAFYTPIE-VPADAVQDVVAQLQ----PKYSVP 235
Cdd:PRK06087 429 TGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDErlgerSCAYVVLKApHHSLTLEEVVAFFSrkrvAKYKYP 508
|
250
....*....|..
gi 807744961 236 KRYRALAALPLT 247
Cdd:PRK06087 509 EHIVVIDKLPRT 520
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
35-247 |
1.68e-10 |
|
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: 60.30 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 35 PNIRVVATAGESCPVALADRW-GQNATFYNCCGPTEVTIVNTMHHHSLGTPLTIGKPTPNNTIYVLDDnlqptprgmpGV 113
Cdd:cd05907 211 GRLRFAASGGAPLPAELLHFFrALGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIADD----------GE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 114 MWAGGPCVCLGYVNRPELNRNKFARDPFspeggmmFNTGDIGRLRDDGELDYLGRIDD-QVKIQGFRVELDGVSASISAC 192
Cdd:cd05907 281 ILVRGPNVMLGYYKNPEATAEALDADGW-------LHTGDLGEIDEDGFLHITGRKKDlIITSGGKNISPEPIENALKAS 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 193 PGVVQAC---------AMLIQ-----DELWA------FYTPIEVPADA-----VQDVVAQLQ---PKYSVPKRYRaLAAL 244
Cdd:cd05907 354 PLISQAVvigdgrpflVALIVpdpeaLEAWAeehgiaYTDVAELAANPavraeIEAAVEAANarlSRYEQIKKFL-LLPE 432
|
...
gi 807744961 245 PLT 247
Cdd:cd05907 433 PFT 435
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
26-209 |
1.79e-10 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 60.01 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 26 LVSHDPADYPNIRVVATAGESCPVALAD--RWGQNATFYnccGPTEVTIVNTMHHHSLGTPLTIGKPTPNNTIYVLDDNL 103
Cdd:cd17636 105 LNADGLYDLSSLRSSPAAPEWNDMATVDtsPWGRKPGGY---GQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILDEDG 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 104 QPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFArdpfspeGGmMFNTGDIGRLRDDGELDYLGRIDDQVKIQGFRVELD 183
Cdd:cd17636 182 REVPDGEVGEIVARGPTVMAGYWNRPEVNARRTR-------GG-WHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPA 253
|
170 180
....*....|....*....|....*.
gi 807744961 184 GVSASISACPGVVQACAMLIQDELWA 209
Cdd:cd17636 254 EVERCLRQHPAVADAAVIGVPDPRWA 279
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
66-171 |
2.42e-10 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 60.07 E-value: 2.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 66 GPTEVTIVNTMHHHSLGTPLTIGKPTPNNTIYVLD-DNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDPFspe 144
Cdd:cd17640 245 GLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDpEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW--- 321
|
90 100
....*....|....*....|....*..
gi 807744961 145 ggmmFNTGDIGRLRDDGELDYLGRIDD 171
Cdd:cd17640 322 ----FNTGDLGWLTCGGELVLTGRAKD 344
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
31-206 |
2.59e-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: 59.70 E-value: 2.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 31 PADYPNIRVVATAGESCPVALADRWGQNATFYNCC--GPTEV--TIVNTMHHHSLGTPLTIGKPTPNNTIYVLDDNLQPT 106
Cdd:cd05903 204 GEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSayGSTECpgAVTSITPAPEDRRLYTDGRPLPGVEIKVVDDTGATL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 107 PRGMPGVMWAGGPCVCLGYVNRPELNRNkfardpFSPEGgmMFNTGDIGRLRDDGELDYLGRIDDQVKIQGFRVELDGVS 186
Cdd:cd05903 284 APGVEGELLSRGPSVFLGYLDRPDLTAD------AAPEG--WFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVE 355
|
170 180
....*....|....*....|
gi 807744961 187 ASISACPGVVQACAMLIQDE 206
Cdd:cd05903 356 DLLLGHPGVIEAAVVALPDE 375
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
112-247 |
4.67e-10 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 58.90 E-value: 4.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 112 GVMWAGGPCVCLGYVNRPElnrnkfaRDPFSPEGgmMFNTGDIGRLrDDGELDYLGRIDDQVKIQGFRVELDGVSASISA 191
Cdd:PRK07824 208 GRIALGGPTLAKGYRNPVD-------PDPFAEPG--WFRTDDLGAL-DDGVLTVLGRADDAISTGGLTVLPQVVEAALAT 277
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 807744961 192 CPGVVQACAMLIQDE-----LWAFYTPIEVPADAVQDVVAQLQ---PKYSVPKRYRALAALPLT 247
Cdd:PRK07824 278 HPAVADCAVFGLPDDrlgqrVVAAVVGDGGPAPTLEALRAHVArtlDRTAAPRELHVVDELPRR 341
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
116-195 |
5.44e-10 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 59.07 E-value: 5.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 116 AGGpcVCLGYVNRPELNRNKFARDPFSPEG---------------------GMMFNTGDIGRLRDDGELDYLGRIDDQVK 174
Cdd:cd17647 322 AGG--LAEGYRGLPELNKEKFVNNWFVEPDhwnyldkdnnepwrqfwlgprDRLYRTGDLGRYLPNGDCECCGRADDQVK 399
|
90 100
....*....|....*....|.
gi 807744961 175 IQGFRVELDGVSASISACPGV 195
Cdd:cd17647 400 IRGFRIELGEIDTHISQHPLV 420
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
23-247 |
9.67e-10 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 58.28 E-value: 9.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 23 PSI---LVSHDPADY--PNIRVVATAGESCPVALADRWGQNA--TFYNCCGPTEVTIVNTMHHHSLGTPLTIGKPTPNNT 95
Cdd:cd05970 284 PTIyrfLIREDLSRYdlSSLRYCTTAGEALNPEVFNTFKEKTgiKLMEGFGQTETTLTIATFPWMEPKPGSMGKPAPGYE 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 96 IYVLDDNLQPTPRGMPG---VMWAGGPCVCL--GYVNRPELNRNKFaRDPFspeggmmFNTGDIGRLRDDGELDYLGRID 170
Cdd:cd05970 364 IDLIDREGRSCEAGEEGeivIRTSKGKPVGLfgGYYKDAEKTAEVW-HDGY-------YHTGDAAWMDEDGYLWFVGRTD 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 171 DQVKIQGFRVELDGVSASISACPGVVQACAMLIQDE-----------LWAFYTPIEVPADAVQDVVAQLQPKYSVPKRYR 239
Cdd:cd05970 436 DLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPirgqvvkativLAKGYEPSEELKKELQDHVKKVTAPYKYPRIVE 515
|
....*...
gi 807744961 240 ALAALPLT 247
Cdd:cd05970 516 FVDELPKT 523
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
30-206 |
9.78e-10 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 58.35 E-value: 9.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 30 DPADYPNIRVVATAGESCPVALADRWGQ--NATFYNCCGPTEVTIVNTMHhhslgtPLT-------IGKPTPNNTIYVLD 100
Cdd:PRK08751 324 DQIDFSSLKMTLGGGMAVQRSVAERWKQvtGLTLVEAYGLTETSPAACIN------PLTlkeyngsIGLPIPSTDACIKD 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 101 DNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDPFspeggmmFNTGDIGRLRDDGELDYLGRIDDQVKIQGFRV 180
Cdd:PRK08751 398 DAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGW-------LHTGDIARMDEQGFVYIVDRKKDMILVSGFNV 470
|
170 180
....*....|....*....|....*.
gi 807744961 181 ELDGVSASISACPGVVQACAMLIQDE 206
Cdd:PRK08751 471 YPNEIEDVIAMMPGVLEVAAVGVPDE 496
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
84-245 |
9.92e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 58.09 E-value: 9.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 84 PLTIGKPTPNNTIYVLD-DNLQPT-PRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDpfspeggmMFNTGDIGRLRDDG 161
Cdd:PRK05605 388 PGYVGVPFPDTEVRIVDpEDPDETmPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDG--------WFRTGDVVVMEEDG 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 162 ELDYLGRIDDQVKIQGFRVELDGVSASISACPGVVQACAMLIQDElwafytpievpaDAVQDVVA--------QLQP--- 230
Cdd:PRK05605 460 FIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPRE------------DGSEEVVAavvlepgaALDPegl 527
|
170 180
....*....|....*....|....
gi 807744961 231 ---------KYSVPKRYRALAALP 245
Cdd:PRK05605 528 raycrehltRYKVPRRFYHVDELP 551
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
1-247 |
2.24e-09 |
|
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: 56.64 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 1 MRGPHRVDWLKVLRT--VDVVISTPSI---LVSHDPADYPnIRVVATAGESCPVALADRWGQ---NATFYNCCGPTEVTI 72
Cdd:cd17633 72 QRKFNPKSWIRKINQynATVIYLVPTMlqaLARTLEPESK-IKSIFSSGQKLFESTKKKLKNifpKANLIEFYGTSELSF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 73 VNTMHHHSLGTPLTIGKPTPNNTIYVLDDNlqptpRGMPGVMWAGGPCVCLGYVNRPELNRNKFardpfspeggmmFNTG 152
Cdd:cd17633 151 ITYNFNQESRPPNSVGRPFPNVEIEIRNAD-----GGEIGKIFVKSEMVFSGYVRGGFSNPDGW------------MSVG 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 153 DIGRLRDDGELDYLGRIDDQVKIQGFRVELDGVSASISACPGVVQACAMLIQDELW-----AFYTPIEVPADAVQDVVAQ 227
Cdd:cd17633 214 DIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFgeiavALYSGDKLTYKQLKRFLKQ 293
|
250 260
....*....|....*....|
gi 807744961 228 LQPKYSVPKRYRALAALPLT 247
Cdd:cd17633 294 KLSRYEIPKKIIFVDSLPYT 313
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
101-247 |
2.42e-09 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 56.89 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 101 DNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFardpfspEGGMmFNTGDIGRLRDDGELDYLGRIDDQVKIQGFRV 180
Cdd:PRK03640 322 KDGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETF-------QDGW-FKTGDIGYLDEEGFLYVLDRRSDLIISGGENI 393
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 807744961 181 ELDGVSASISACPGVVQACAMLIQDELWAfytpiEVP-ADAVQDV---VAQLQ-------PKYSVPKRYRALAALPLT 247
Cdd:PRK03640 394 YPAEIEEVLLSHPGVAEAGVVGVPDDKWG-----QVPvAFVVKSGevtEEELRhfceeklAKYKVPKRFYFVEELPRN 466
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
66-206 |
3.15e-09 |
|
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: 56.47 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 66 GPTEVTIVNTMH---HHSLGTPLTIGKPTPNNTIYVLD-DNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDPF 141
Cdd:cd05904 309 GMTESTGVVAMCfapEKDRAKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGW 388
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 807744961 142 speggmmFNTGDIGRLRDDGELDYLGRIDDQVKIQGFRV---ELDGVSASIsacPGVVQACAMLIQDE 206
Cdd:cd05904 389 -------LHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVapaELEALLLSH---PEILDAAVIPYPDE 446
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
25-177 |
8.56e-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: 54.98 E-value: 8.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 25 ILVSHDPADYP--NIRVVATAGESCPVALADRWGQ--NATFYNCC-GPTEVTIVNTMHhhSLGTPL-----TIGKPTPNN 94
Cdd:cd05917 106 ELEHPDFDKFDlsSLRTGIMAGAPCPPELMKRVIEvmNMKDVTIAyGMTETSPVSTQT--RTDDSIekrvnTVGRIMPHT 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 95 TIYVLD--DNLQPtPRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDpfspeggMMFNTGDIGRLRDDGELDYLGRIDDQ 172
Cdd:cd05917 184 EAKIVDpeGGIVP-PVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGD-------GWLHTGDLAVMDEDGYCRIVGRIKDM 255
|
....*
gi 807744961 173 VkIQG 177
Cdd:cd05917 256 I-IRG 259
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
105-195 |
8.85e-09 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 55.51 E-value: 8.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 105 PTPRGMPGVmwaGGPCVCLGYVNRPELNRNKFARDpfspEGGMM-FNTGDIGRLRDDGELDYLGRIDDQVKIQ-GFRVEL 182
Cdd:PLN02387 499 PMPRGEIVI---GGPSVTLGYFKNQEKTDEVYKVD----ERGMRwFYTGDIGQFHPDGCLEIIDRKKDIVKLQhGEYVSL 571
|
90
....*....|...
gi 807744961 183 DGVSASISACPGV 195
Cdd:PLN02387 572 GKVEAALSVSPYV 584
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
66-221 |
1.70e-08 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 54.60 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 66 GPTEVTIVNTMHH-----HSLGTPLTIGKPTPNNTIYVLD-DNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFARD 139
Cdd:PLN02330 337 GLTEHSCITLTHGdpekgHGIAKKNSVGFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDED 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 140 PFspeggmmFNTGDIGRLRDDGELDYLGRIDDQVKIQGFRVELDGVSASISACPGVVQACAMLIQDELWAfytpiEVPAD 219
Cdd:PLN02330 417 GW-------LHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAG-----EIPAA 484
|
..
gi 807744961 220 AV 221
Cdd:PLN02330 485 CV 486
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
81-247 |
2.08e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 54.28 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 81 LGTPLTIGKPTPNNTIYVLD-DNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFaRDPFspeggmmFNTGDIGRLRD 159
Cdd:PRK06178 383 LSQPVFVGLPVPGTEFKICDfETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGW-------LHTGDIGKIDE 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 160 DGELDYLGRIDDQVKIQGFRVELDGVSASISACPGvVQACAMLIQD------ELWAFYTPI---EVPADAVQDVVAQLQP 230
Cdd:PRK06178 455 QGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPA-VLGSAVVGRPdpdkgqVPVAFVQLKpgaDLTAAALQAWCRENMA 533
|
170
....*....|....*..
gi 807744961 231 KYSVPKrYRALAALPLT 247
Cdd:PRK06178 534 VYKVPE-IRIVDALPMT 549
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
44-248 |
2.08e-08 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 54.12 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 44 GESCPVAlaDRWGQNATFYNCCGPTEVTIvntmhhhslgtPLTIGKPT---PNNTIYVLDDNLQPTPRGMPG--VMWAGG 118
Cdd:cd17634 380 KEKCPVV--DTWWQTETGGFMITPLPGAI-----------ELKAGSATrpvFGVQPAVVDNEGHPQPGGTEGnlVITDPW 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 119 PCVCLGYVNRPElnrnKFARDPFSPEGGMMFnTGDIGRLRDDGELDYLGRIDDQVKIQGFRVELDGVSASISACPGVVQA 198
Cdd:cd17634 447 PGQTRTLFGDHE----RFEQTYFSTFKGMYF-SGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEA 521
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 807744961 199 CAMLIQDEL-----WAFYT--PIEVPADAVQD-VVAQLQPKYSVPKRYRAL---AALPLTR 248
Cdd:cd17634 522 AVVGIPHAIkgqapYAYVVlnHGVEPSPELYAeLRNWVRKEIGPLATPDVVhwvDSLPKTR 582
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
33-198 |
2.79e-08 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 53.66 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 33 DYPNIRVVATAGESC-PVALadRWGQNA---TFYNCCGPTE---VTIVNTmhhhsLGTPL---TIGKPTPNNTIYVLDDN 102
Cdd:cd05969 205 DLSSLRFIHSVGEPLnPEAI--RWGMEVfgvPIHDTWWQTEtgsIMIANY-----PCMPIkpgSMGKPLPGVKAAVVDEN 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 103 LQPTPRGMPGVMW--AGGPCVCLGYVNRPELNRNKFardpfsPEGgmMFNTGDIGRLRDDGELDYLGRIDDQVKIQGFRV 180
Cdd:cd05969 278 GNELPPGTKGILAlkPGWPSMFRGIWNDEERYKNSF------IDG--WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRV 349
|
170
....*....|....*...
gi 807744961 181 ELDGVSASISACPGVVQA 198
Cdd:cd05969 350 GPFEVESALMEHPAVAEA 367
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
38-247 |
6.91e-08 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 52.84 E-value: 6.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 38 RVVATAGESCPVALADRWGQNATFYNCCGPtevtivntmhhHSLGTPLTIGKPTPNNTIYVLDDNLQPTPRGMPG--VMW 115
Cdd:PRK06155 307 ALHAAFRERFGVDLLDGYGSTETNFVIAVT-----------HGSQRPGSMGRLAPGFEARVVDEHDQELPDGEPGelLLR 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 116 AGGP-CVCLGYVNRPELN----RNkfardpfspeggMMFNTGDIGRLRDDGELDYLGRIDDQVKIQGFRVELDGVSASIS 190
Cdd:PRK06155 376 ADEPfAFATGYFGMPEKTveawRN------------LWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLL 443
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 807744961 191 ACPGVVQACAM-----LIQDELWAFYTPIEVPADAVQDVVAQLQPK---YSVPKRYRALAALPLT 247
Cdd:PRK06155 444 SHPAVAAAAVFpvpseLGEDEVMAAVVLRDGTALEPVALVRHCEPRlayFAVPRYVEFVAALPKT 508
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
29-246 |
8.21e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 52.21 E-value: 8.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 29 HDPADYPNIRVVATAGESCPVALADRWGQN------ATFYnccGPTE---VTIVNTMHHHSLGTPLTIGKPTPNNTIYVL 99
Cdd:PRK07656 275 RSAEDLSSLRLAVTGAASMPVALLERFESElgvdivLTGY---GLSEasgVTTFNRLDDDRKTVAGTIGTAIAGVENKIV 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 100 DDNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNkfARDpfsPEGGMmfNTGDIGRLRDDGELDYLGRIDDQVKIQGFR 179
Cdd:PRK07656 352 NELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAA--AID---ADGWL--HTGDLGRLDEEGYLYIVDRKKDMFIVGGFN 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 807744961 180 V---ELDGVSASIsacPGVVQACAMLIQDELW-----AFYTP---IEVPADAVQDVVAQLQPKYSVPKRYRALAALPL 246
Cdd:PRK07656 425 VypaEVEEVLYEH---PAVAEAAVIGVPDERLgevgkAYVVLkpgAELTEEELIAYCREHLAKYKVPRSIEFLDELPK 499
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
88-177 |
8.41e-08 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 52.24 E-value: 8.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 88 GKPTPNNTIYVLDDN-LQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDPFSPEGGMmFNTGDIGRLRDdGELDYL 166
Cdd:cd05931 358 GRPLPDQEVRIVDPEtGRELPDGEVGEIWVRGPSVASGYWGRPEATAETFGALAATDEGGW-LRTGDLGFLHD-GELYIT 435
|
90
....*....|.
gi 807744961 167 GRIDDQVKIQG 177
Cdd:cd05931 436 GRLKDLIIVRG 446
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
98-245 |
8.91e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 52.35 E-value: 8.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 98 VLDDNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFaRDPFspeggmmFNTGDIGRLRDDGELDYLGRIDDQVKIQG 177
Cdd:PRK07470 353 IQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAF-RDGW-------FRTGDLGHLDARGFLYITGRASDMYISGG 424
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 807744961 178 FRVELDGVSASISACPGVVQACAMLIQDELWA--------FYTPIEVPADAVQDVVAQLQPKYSVPKRYRALAALP 245
Cdd:PRK07470 425 SNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGevgvavcvARDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALP 500
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
26-237 |
1.02e-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.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 52.00 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 26 LVSHDPADYPNIRVVATAGESCPVALADRW---GQNATFYNCCGPTEVTivNTMHHHSLGTPLTIGKPT-PNNTIYVLDD 101
Cdd:cd05924 125 LRDAGPYDLSSLFAISSGGALLSPEVKQGLlelVPNITLVDAFGSSETG--FTGSGHSAGSGPETGPFTrANPDTVVLDD 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 102 NLQPTPRGMPGVMW-AGGPCVCLGYVNRPElnrnKFARDPFSPEGGMMFNTGDIGRLRDDGELDYLGRIDDQVKIQGFRV 180
Cdd:cd05924 203 DGRVVPPGSGGVGWiARRGHIPLGYYGDEA----KTAETFPEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKV 278
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 807744961 181 ELDGVSASISACPGVVQACAMLIQDELW--------AFYTPIEVPADAVQDVVAQLQPKYSVPKR 237
Cdd:cd05924 279 FPEEVEEALKSHPAVYDVLVVGRPDERWgqevvavvQLREGAGVDLEELREHCRTRIARYKLPKQ 343
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
87-239 |
3.28e-07 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 50.78 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 87 IGKPTPNNTIYVLDDN-LQPT-PRGMP----GVMWAGGPCVCLGYVNRPELNRNKFArdpfspEGGMmfNTGDIGRLRDD 160
Cdd:PRK05857 344 VGRPYPGVDVYLAATDgIGPTaPGAGPsasfGTLWIKSPANMLGYWNNPERTAEVLI------DGWV--NTGDLLERRED 415
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 807744961 161 GELDYLGRIDDQVKIQGFRVELDGVSASISACPGVVQACAMLIQDELWAFYTPIEVPADAVQDVVAQLQPKYSVPKRYR 239
Cdd:PRK05857 416 GFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVASAELDESAARALKHTIAARFR 494
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
86-245 |
4.18e-07 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 50.26 E-value: 4.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 86 TIGKPTPNNTIYVLD-DNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDPFspeggmmFNTGDIGRLRDDGELD 164
Cdd:PRK07514 322 TVGFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGF-------FITGDLGKIDERGYVH 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 165 YLGRIDDQVKIQGFRV---ELDGVsasISACPGVVQACAmliqdelwafytpIEVP-AD------AV-----------QD 223
Cdd:PRK07514 395 IVGRGKDLIISGGYNVypkEVEGE---IDELPGVVESAV-------------IGVPhPDfgegvtAVvvpkpgaaldeAA 458
|
170 180
....*....|....*....|....*
gi 807744961 224 VVAQLQ---PKYSVPKRYRALAALP 245
Cdd:PRK07514 459 ILAALKgrlARFKQPKRVFFVDELP 483
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
6-198 |
9.85e-07 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 49.00 E-value: 9.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 6 RVDWLKVLRT-----VDVVISTPSI---LVSHDPADY--PNIRVVATAGESCPVALADRWgQNAT---FYNCCGPTEVTI 72
Cdd:cd05928 252 RFDPLVILKTlssypITTFCGAPTVyrmLVQQDLSSYkfPSLQHCVTGGEPLNPEVLEKW-KAQTgldIYEGYGQTETGL 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 73 VNTMHHHSLGTPLTIGKPTPNNTIYVLDDNLQPTPRGMPG-VMWAGGP----CVCLGYVNRPElnrnKFArdpfSPEGGM 147
Cdd:cd05928 331 ICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGdIGIRVKPirpfGLFSGYVDNPE----KTA----ATIRGD 402
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 807744961 148 MFNTGDIGRLRDDGELDYLGRIDDQVKIQGFRVELDGVSASISACPGVVQA 198
Cdd:cd05928 403 FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVES 453
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
4-246 |
1.30e-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: 48.65 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 4 PHRV-DWLKVLRTVD-----VVISTPSILVS--HDPA----DYPNIRVVATAGESCPVALADRWGQNATFYNCC---GPT 68
Cdd:cd17638 72 PVAVfDVDAILEAIEreritVLPGPPTLFQSllDHPGrkkfDLSSLRAAVTGAATVPVELVRRMRSELGFETVLtayGLT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 69 EVTIVnTMHHHS---LGTPLTIGKPTPNNTIYVLDDnlqptprgmpGVMWAGGPCVCLGYVNRPELNRNKFARDPFspeg 145
Cdd:cd17638 152 EAGVA-TMCRPGddaETVATTCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAIDADGW---- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 146 gmmFNTGDIGRLRDDGELDYLGRIDDQVKIQGFRVELDGVSASISACPGVVQACAMLIQDELW-----AFYTPIEVPADA 220
Cdd:cd17638 217 ---LHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMgevgkAFVVARPGVTLT 293
|
250 260
....*....|....*....|....*....
gi 807744961 221 VQDVVAQLQPK---YSVPKRYRALAALPL 246
Cdd:cd17638 294 EEDVIAWCRERlanYKVPRFVRFLDELPR 322
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
58-247 |
1.60e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 48.62 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 58 NATFYNCCGPTEVTIVNTMHHH-SLGTPLTIGKPTPNNTIYVLDDNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNkf 136
Cdd:PRK07638 279 YAKLYEFYGASELSFVTALVDEeSERRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLARE-- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 137 ardpfSPEGGMMfNTGDIGRLRDDGELDYLGRIDDQVKIQGFRVELDGVSASISACPGVVQACAMLIQDELWAfytpiEV 216
Cdd:PRK07638 357 -----LNADGWM-TVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWG-----EK 425
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 807744961 217 P-------ADAVQ--DVVAQLQPKYSVPKRYRALAALPLT 247
Cdd:PRK07638 426 PvaiikgsATKQQlkSFCLQRLSSFKIPKEWHFVDEIPYT 465
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
66-199 |
2.77e-06 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 47.60 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 66 GPTEVTIVNTMHHHSLGTPLTIGKPTPNNTIYVLD------DNLQPTPRGMPGVMwagGPCVCLGYVNRPELNRNKFARD 139
Cdd:cd05927 307 GQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDvpemnyDAKDPNPRGEVCIR---GPNVFSGYYKDPEKTAEALDED 383
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 807744961 140 PFspeggmmFNTGDIGRLRDDGELdylgRIDDQVK-----IQGFRVELDGVSASISACPGVVQAC 199
Cdd:cd05927 384 GW-------LHTGDIGEWLPNGTL----KIIDRKKnifklSQGEYVAPEKIENIYARSPFVAQIF 437
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
33-166 |
3.53e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 47.38 E-value: 3.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 33 DYPNIRVVATAGESCPV----ALADRWGQNA-TFYNCCGPTEVTIVNTmhHHSLGTPLTIGKPTPNnTIYVLDDNLQPTP 107
Cdd:PRK13391 273 DLSSLEVAIHAAAPCPPqvkeQMIDWWGPIIhEYYAATEGLGFTACDS--EEWLAHPGTVGRAMFG-DLHILDDDGAELP 349
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 807744961 108 RGMPGVMW--AGGPcvcLGYVNRPElnRNKFARDPfspEGGMMfNTGDIGRLRDDGELdYL 166
Cdd:PRK13391 350 PGEPGTIWfeGGRP---FEYLNDPA--KTAEARHP---DGTWS-TVGDIGYVDEDGYL-YL 400
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
124-245 |
4.72e-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: 47.12 E-value: 4.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 124 GYVNRPELNRNKFArdpfspEGgmMFNTGDIGRLRDDGELDYLGRIDDQVKIQGFRVELDGVSASISACPGVVQACAMLI 203
Cdd:cd05923 360 GYLNQPEATAKKLQ------DG--WYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGV 431
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 807744961 204 QDELW-----AFYTPIEVPADAV---QDVVAQLQPKYSVPKRYRALAALP 245
Cdd:cd05923 432 ADERWgqsvtACVVPREGTLSADeldQFCRASELADFKRPRRYFFLDELP 481
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
35-195 |
4.92e-06 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 47.07 E-value: 4.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 35 PNIRVVATAGESCPVALADRWGQ----NATFYNCCGPTEVTIVNTMHHHSLGTPLT----------IGKPTPNNTIYVLD 100
Cdd:cd05910 199 PSLRRVLSAGAPVPIALAARLRKmlsdEAEILTPYGATEALPVSSIGSRELLATTTaatsggagtcVGRPIPGVRVRIIE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 101 ---------DNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDPfspEGGMMFNTGDIGRLRDDGELDYLGRIDD 171
Cdd:cd05910 279 iddepiaewDDTLELPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDN---SEGFWHRMGDLGYLDDEGRLWFCGRKAH 355
|
170 180
....*....|....*....|....
gi 807744961 172 QVKIQGFRVELDGVSASISACPGV 195
Cdd:cd05910 356 RVITTGGTLYTEPVERVFNTHPGV 379
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
82-177 |
8.73e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 46.70 E-value: 8.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 82 GTPL-TIGKPTPNNTIYVLDDN-LQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDpfspEGGMMFNTGDIGRLRd 159
Cdd:PRK05691 366 GSVLmSCGRSQPGHAVLIVDPQsLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFVEH----DGRTWLRTGDLGFLR- 440
|
90
....*....|....*...
gi 807744961 160 DGELDYLGRIDDQVKIQG 177
Cdd:PRK05691 441 DGELFVTGRLKDMLIVRG 458
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
149-205 |
1.04e-05 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 46.27 E-value: 1.04e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 807744961 149 FNTGDIGRLRDDGELDYLGRIDDQVKIQGFRVELDGVSASISACPGVVQACAMLIQD 205
Cdd:PTZ00237 494 YNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYD 550
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
84-245 |
1.52e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 45.37 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 84 PLTIGKPTPNNTIYVLDDNLQPTPRGMP--GVMWAGGPCVCLGYVNRPELNRNKFARDPFspeggmmFNTGDIGRLRDDG 161
Cdd:PRK07787 292 PGWVGLPLAGVETRLVDEDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGW-------FRTGDVAVVDPDG 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 162 ELDYLGRID-DQVKIQGFRVELDGVSASISACPGVVQACAMLIQDE-----LWAFYTPIE-VPADAVQDVVAQLQPKYSV 234
Cdd:PRK07787 365 MHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDdlgqrIVAYVVGADdVAADELIDFVAQQLSVHKR 444
|
170
....*....|.
gi 807744961 235 PKRYRALAALP 245
Cdd:PRK07787 445 PREVRFVDALP 455
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
16-206 |
1.52e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 45.72 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 16 VDVvISTPSIlvshDPADYPNIRVVATAGESCPVALADRWGQ--NATFYNCCGPTEV---TIVNTMHHHSLGTpltIGKP 90
Cdd:PRK08314 291 VDF-LASPGL----AERDLSSLRYIGGGGAAMPEAVAERLKEltGLDYVEGYGLTETmaqTHSNPPDRPKLQC---LGIP 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 91 TPNNTIYVLD-DNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFardpFSPEGGMMFNTGDIGRLRDDGELDYLGRI 169
Cdd:PRK08314 363 TFGVDARVIDpETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAF----IEIDGKRFFRTGDLGRMDEEGYFFITDRL 438
|
170 180 190
....*....|....*....|....*....|....*..
gi 807744961 170 DDQVKIQGFRVELDGVSASISACPGVVQACAMLIQDE 206
Cdd:PRK08314 439 KRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDP 475
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
66-206 |
2.54e-05 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 44.83 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 66 GPTEVTIVNT--MHHHSLGTPLTIGKPTPNNTIYVLD-DNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDPFs 142
Cdd:PLN02574 353 GMTESTAVGTrgFNTEKLSKYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGW- 431
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 807744961 143 peggmmFNTGDIGRLRDDGELDYLGRIDDQVKIQGFRVELDGVSASISACPGVVQACAMLIQDE 206
Cdd:PLN02574 432 ------LRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDK 489
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
58-183 |
2.92e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 44.71 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 58 NATFYNCCGPTEVTIVNTMHHHSLGTPLTIGKPTPNNT--------IYVLDDNLqptPRGMpgvMWAGGPCVCLGYVNRP 129
Cdd:PTZ00342 486 NVNYYQGYGLTETTGPIFVQHADDNNTESIGGPISPNTkykvrtweTYKATDTL---PKGE---LLIKSDSIFSGYFLEK 559
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 807744961 130 ELNRNKFARDPFspeggmmFNTGDIGRLRDDGELDYLGRIDDQVKI-QGFRVELD 183
Cdd:PTZ00342 560 EQTKNAFTEDGY-------FKTGDIVQINKNGSLTFLDRSKGLVKLsQGEYIETD 607
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
187-248 |
4.69e-05 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 40.61 E-value: 4.69e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 187 ASISACPGVVQACAMLIQDELW-----AFYTP---IEVPADAVQDVVAQLQPKYSVPKRYRALAALPLTR 248
Cdd:pfam13193 4 SALVSHPAVAEAAVVGVPDELKgeapvAFVVLkpgVELLEEELVAHVREELGPYAVPKEVVFVDELPKTR 73
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
82-207 |
5.78e-05 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 43.84 E-value: 5.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 82 GTPltiGKPTPNNTIYVLDDNLQPTPRGMPGVMWAGGP----CVCLGYVNRPELNRNKFARDPfspeggMMFNTGDIGRL 157
Cdd:cd05967 411 GSP---GKPVPGYQVQVLDEDGEPVGPNELGNIVIKLPlppgCLLTLWKNDERFKKLYLSKFP------GYYDTGDAGYK 481
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 807744961 158 RDDGELDYLGRIDDQVKIQGFRVELDGVSASISACPGVVQACAMLIQDEL 207
Cdd:cd05967 482 DEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDEL 531
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
68-177 |
6.56e-05 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 43.65 E-value: 6.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 68 TEVTIVNTM-------HHHSLGTPL-----TIGKPTPNNTIYVLD-DNLQPTPRGMPGVMWAGGPCVCLGYVNRPElnRN 134
Cdd:PRK08315 342 SEVTIAYGMtetspvsTQTRTDDPLekrvtTVGRALPHLEVKIVDpETGETVPRGEQGELCTRGYSVMKGYWNDPE--KT 419
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 807744961 135 KFARDpfspEGGMMFnTGDIGRLRDDGELDYLGRIDDQVkIQG 177
Cdd:PRK08315 420 AEAID----ADGWMH-TGDLAVMDEEGYVNIVGRIKDMI-IRG 456
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
37-243 |
7.89e-05 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 43.33 E-value: 7.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 37 IRVVATAGESCPVALADR----WGQnaTFYNCCGPTEVTIVNTmhhHSLGTPL---TIGKPTPNNTIYVLDdnlqptPRG 109
Cdd:cd05974 202 LREVVGAGEPLNPEVIEQvrraWGL--TIRDGYGQTETTALVG---NSPGQPVkagSMGRPLPGYRVALLD------PDG 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 110 MPGVmwAGGPCVCLGyVNRPELNRNKFARDPFSPEGGM---MFNTGDIGRLRDDGELDYLGRIDDQVKIQGFRV---ELD 183
Cdd:cd05974 271 APAT--EGEVALDLG-DTRPVGLMKGYAGDPDKTAHAMrggYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRIspfELE 347
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 807744961 184 GVSasisacpgvvqacamliqdelwafytpIEVPADAVQDVVAQLQP-KYSVPKRYRALAA 243
Cdd:cd05974 348 SVL---------------------------IEHPAVAEAAVVPSPDPvRLSVPKAFIVLRA 381
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
141-248 |
1.18e-04 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 42.93 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 141 FSPEGGMMFnTGDIGRLRDDGELDYLGRIDDQVKIQGFRVELDGVSASISACPGVVQACAMLIQDEL-----WAFYTP-- 213
Cdd:cd05966 464 FSKFPGYYF-TGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIkgeaiYAFVTLkd 542
|
90 100 110
....*....|....*....|....*....|....*....
gi 807744961 214 -IEVPADAVQDVVAQLQPK---YSVPKRYRALAALPLTR 248
Cdd:cd05966 543 gEEPSDELRKELRKHVRKEigpIATPDKIQFVPGLPKTR 581
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
66-171 |
1.25e-04 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 42.80 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 66 GPTEVTIVNTMHHHSLGTPLTIGKPTPNNTIYVldDNLqptprgmpGVMWAGGPCVCLGYVNRPELNRNKFARDPFspeg 145
Cdd:cd17641 356 GQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRI--DEV--------GEILVRSPGVFVGYYKNPEATAEDFDEDGW---- 421
|
90 100
....*....|....*....|....*.
gi 807744961 146 gmmFNTGDIGRLRDDGELDYLGRIDD 171
Cdd:cd17641 422 ---LHTGDAGYFKENGHLVVIDRAKD 444
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
2-247 |
1.88e-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: 341266 [Multi-domain] Cd Length: 359 Bit Score: 42.08 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 2 RGPHRVD--WLKVLR-TVDVVISTPSILVS----HDPADYPNIRVVATAGESCPVALADRWgQNATFYNCC---GPTEVT 71
Cdd:cd05944 81 RNPGLFDnfWKLVERyRITSLSTVPTVYAAllqvPVNADISSLRFAMSGAAPLPVELRARF-EDATGLPVVegyGLTEAT 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 72 IVNTMHHHslGTPLTIGK-----PTPNNTIYVLD---DNLQPTPRGMPGVMWAGGPCVCLGYVNRpELNRNKFARDPFsp 143
Cdd:cd05944 160 CLVAVNPP--DGPKRPGSvglrlPYARVRIKVLDgvgRLLRDCAPDEVGEICVAGPGVFGGYLYT-EGNKNAFVADGW-- 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 144 eggmmFNTGDIGRLRDDGELDYLGRIDDQVKIQGFRVELDGVSASISACPGVVQACAMLIQD----ELWAFYTPI----E 215
Cdd:cd05944 235 -----LNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDahagELPVAYVQLkpgaV 309
|
250 260 270
....*....|....*....|....*....|...
gi 807744961 216 VPADAVQDVVAQLQP-KYSVPKRYRALAALPLT 247
Cdd:cd05944 310 VEEEELLAWARDHVPeRAAVPKHIEVLEELPVT 342
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
107-177 |
2.85e-04 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 41.65 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 107 PRGMPGVMWAGGPCVCLGYVNRPELNRNKF-----ARDPF------SPEGGMMFNTGDIGRLRDdGELDYLGRIDDQVKI 175
Cdd:PRK12476 425 PDGEVGEIWLHGDNIGRGYWGRPEETERTFgaklqSRLAEgshadgAADDGTWLRTGDLGVYLD-GELYITGRIADLIVI 503
|
..
gi 807744961 176 QG 177
Cdd:PRK12476 504 DG 505
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
68-206 |
3.23e-04 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 41.32 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 68 TEVTIVNTMHHHSLGTplTIGKPTPNNTIYVLDDNLQPTprgmpGVMWAGGPCVCLGYVNRPELNRNKFARDPFspeggm 147
Cdd:PLN02860 349 TVNQTKSSSVHQPQGV--CVGKPAPHVELKIGLDESSRV-----GRILTRGPHVMLGYWGQNSETASVLSNDGW------ 415
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 807744961 148 mFNTGDIGRLRDDGELDYLGRIDDQVKIQGFRVELDGVSASISACPGVVQACAMLIQDE 206
Cdd:PLN02860 416 -LDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDS 473
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
79-248 |
3.75e-04 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 41.47 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 79 HSLGTPltiGKPTPNNTIYVLDDNL-QPTPRGMPGVMWAGGPCV--CLGYVNRpelNRNKFARDPFSPEGGMMFNTGDIG 155
Cdd:PRK10524 408 TRLGSP---GVPMYGYNVKLLNEVTgEPCGPNEKGVLVIEGPLPpgCMQTVWG---DDDRFVKTYWSLFGRQVYSTFDWG 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 156 RLRDDGELDYLGRIDDQVKIQGFRVELDGVSASISACPGVVQACAMLIQDEL-----WAFYTP-----IEVPADA----- 220
Cdd:PRK10524 482 IRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALkgqvaVAFVVPkdsdsLADREARlalek 561
|
170 180
....*....|....*....|....*....
gi 807744961 221 -VQDVVAQLQPKYSVPKRYRALAALPLTR 248
Cdd:PRK10524 562 eIMALVDSQLGAVARPARVWFVSALPKTR 590
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
86-245 |
3.78e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 41.30 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 86 TIGKPTPNNTIYVLDDNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFArdpfspegGMMFNTGDIGRLRDDGELDY 165
Cdd:PRK07786 346 SVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFA--------GGWFHSGDLVRQDEEGYVWV 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 166 LGRIDDQVKIQGFRVELDGVSASISACPGVVQACAMLIQDELWAfytpiEVP-------ADAVQDVVAQLQP-------K 231
Cdd:PRK07786 418 VDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWG-----EVPvavaavrNDDAALTLEDLAEfltdrlaR 492
|
170
....*....|....
gi 807744961 232 YSVPKRYRALAALP 245
Cdd:PRK07786 493 YKHPKALEIVDALP 506
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
82-177 |
3.88e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 41.08 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 82 GTPL-TIGKPTPNnTIYVLD-DNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKFA---RDPfSP--EGGMMFNTGDI 154
Cdd:PRK05850 367 GTPLvSYGSPRSP-TVRIVDpDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFGatlVDP-SPgtPEGPWLRTGDL 444
|
90 100
....*....|....*....|...
gi 807744961 155 GRLrDDGELDYLGRIDDQVKIQG 177
Cdd:PRK05850 445 GFI-SEGELFIVGRIKDLLIVDG 466
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
107-177 |
4.22e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 41.25 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 107 PRGMPGVMWAGGPCVCLGYVNRPELNRNKF-----ARDPFS-----PEGGMMFNTGDIGrLRDDGELDYLGRIDDQVKIQ 176
Cdd:PRK07769 414 PDGQIGEIWLHGNNIGTGYWGKPEETAATFqnilkSRLSEShaegaPDDALWVRTGDYG-VYFDGELYITGRVKDLVIID 492
|
.
gi 807744961 177 G 177
Cdd:PRK07769 493 G 493
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
33-230 |
4.79e-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: 40.82 E-value: 4.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 33 DYPNIRVVATAGESCPVALADR----WGQnaTFYNCCGPTE---VTIVNTmhHHSLGTPLTIGKPTpNNTIYVLDDNLQP 105
Cdd:cd05929 242 DLSSLKRVIHAAAPCPPWVKEQwidwGGP--IIWEYYGGTEgqgLTIING--EEWLTHPGSVGRAV-LGKVHILDEDGNE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 106 TPRGMPGVMW-AGGPCVclGYVNRPELNRNKFARDPFSpeggmmfNTGDIGRLRDDGELDYLGRIDDQVKIQGFRVELDG 184
Cdd:cd05929 317 VPPGEIGEVYfANGPGF--EYTNDPEKTAAARNEGGWS-------TLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQE 387
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 807744961 185 VSASISACPGVVQACAMLIQDElwafytpievpaDAVQDVVAQLQP 230
Cdd:cd05929 388 IENALIAHPKVLDAAVVGVPDE------------ELGQRVHAVVQP 421
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
107-180 |
5.56e-04 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 40.73 E-value: 5.56e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 807744961 107 PRGMPGVMWAGGPCVCLGYVNRPELNRNKFARDPFspeggmmFNTGDIGRLRDDGELDYLGRIDDQVKIQGFRV 180
Cdd:PLN02246 379 PRNQPGEICIRGPQIMKGYLNDPEATANTIDKDGW-------LHTGDIGYIDDDDELFIVDRLKELIKYKGFQV 445
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
35-174 |
7.63e-04 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 40.27 E-value: 7.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 35 PNIRVVATAGESCPVALADRW----GQNATFYNCCGPTEVTIVNTMHHHSLGTPLT----------IGKPTPNNTIYV-- 98
Cdd:PRK09274 288 PSLRRVISAGAPVPIAVIERFramlPPDAEILTPYGATEALPISSIESREILFATRaatdngagicVGRPVDGVEVRIia 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 99 LDDNLQPT-------PRGMPGVMWAGGPCVCLGYVNRPELNR-NKFARdpfsPEGGMMFNTGDIGRLRDDGELDYLGRID 170
Cdd:PRK09274 368 ISDAPIPEwddalrlATGEIGEIVVAGPMVTRSYYNRPEATRlAKIPD----GQGDVWHRMGDLGYLDAQGRLWFCGRKA 443
|
....
gi 807744961 171 DQVK 174
Cdd:PRK09274 444 HRVE 447
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
83-195 |
8.19e-04 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 40.16 E-value: 8.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 83 TPLTIGKPTPNNTIYVLDDNLQPTPRGMPGVMWAGGPCVCLGYVNRPELNRNKfardpFSPEGGMMfnTGDIGRLRdDGE 162
Cdd:cd05908 312 TFVEVGKPIDETDIRICDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKV-----FTDDGWLK--TGDLGFIR-NGR 383
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 807744961 163 LDYLGRIDDQVKIQGFRV----------ELDGV-SASISACpGV 195
Cdd:cd05908 384 LVITGREKDIIFVNGQNVyphdieriaeELEGVeLGRVVAC-GV 426
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
152-248 |
3.32e-03 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 38.24 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 152 GDIGRLRDDGELDYLGRIDDQVKIQGFRVELDGVSASISACPGVVQACAMLIQD-----ELWAF------YTPIEVPADA 220
Cdd:cd05968 476 GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHpvkgeAIVCFvvlkpgVTPTEALAEE 555
|
90 100
....*....|....*....|....*...
gi 807744961 221 VQDVVAQLQPKYSVPKRYRALAALPLTR 248
Cdd:cd05968 556 LMERVADELGKPLSPERILFVKDLPKTR 583
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
86-179 |
4.73e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 38.05 E-value: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 86 TIGKPTPNNTIYVLDDNLQPTP-RGMpGVMWAGGPCVCLGYVNRpelnrnkfarDPFSP---EGGMmFNTGDIGRLRDDG 161
Cdd:PRK07768 361 TLGPPLPGLEVRVVDEDGQVLPpRGV-GVIELRGESVTPGYLTM----------DGFIPaqdADGW-LDTGDLGYLTEEG 428
|
90
....*....|....*...
gi 807744961 162 ELDYLGRIDDqVKIQGFR 179
Cdd:PRK07768 429 EVVVCGRVKD-VIIMAGR 445
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
149-245 |
7.20e-03 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 37.28 E-value: 7.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 149 FNTGDIGRLRDDGELDYLGRiDDQVKIQG----FRVEldgVSASISACPGVVQACAMLIQDELW-----AFYTPI--EVP 217
Cdd:PRK07445 326 FETDDLGYLDAQGYLHILGR-NSQKIITGgenvYPAE---VEAAILATGLVQDVCVLGLPDPHWgevvtAIYVPKdpSIS 401
|
90 100
....*....|....*....|....*...
gi 807744961 218 ADAVQDVVAQLQPKYSVPKRYRALAALP 245
Cdd:PRK07445 402 LEELKTAIKDQLSPFKQPKHWIPVPQLP 429
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
36-205 |
7.59e-03 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 37.41 E-value: 7.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 36 NIRVVATAGESCPVALADRW--------GQNATFYNCCGPTEVTIVNTMHHHSLGTPLTIGKPTPNNTiyvlddnLQPTP 107
Cdd:cd05921 291 RLKLMFYAGAGLSQDVWDRLqalavatvGERIPMMAGLGATETAPTATFTHWPTERSGLIGLPAPGTE-------LKLVP 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 108 RGMPGVMWAGGPCVCLGYVNRPELNRNKFARDPFspeggmmFNTGDIGRLRDDGE----LDYLGRIDDQVKIQgfrvelD 183
Cdd:cd05921 364 SGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGF-------YCLGDAAKLADPDDpakgLVFDGRVAEDFKLA------S 430
|
170 180
....*....|....*....|...
gi 807744961 184 GVSASISAC-PGVVQACAMLIQD 205
Cdd:cd05921 431 GTWVSVGPLrARAVAACAPLVHD 453
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
33-166 |
8.51e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 37.19 E-value: 8.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744961 33 DYPNIRVVATAGESCPV----ALADRWGQNATFYNCCgpTE---VTIVNTmhHHSLGTPLTIGKPTpNNTIYVLDDNLQP 105
Cdd:PRK08276 260 DVSSLRVAIHAAAPCPVevkrAMIDWWGPIIHEYYAS--SEgggVTVITS--EDWLAHPGSVGKAV-LGEVRILDEDGNE 334
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 807744961 106 TPRGMPGVMWAGGPCVCLGYVNRPELNRNkfARDPfspegGMMFNTGDIGRLRDDGELdYL 166
Cdd:PRK08276 335 LPPGEIGTVYFEMDGYPFEYHNDPEKTAA--ARNP-----HGWVTVGDVGYLDEDGYL-YL 387
|
|
| |
