|
Name |
Accession |
Description |
Interval |
E-value |
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1-241 |
1.18e-106 |
|
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: 334.90 E-value: 1.18e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 1 PQTDFPQEALIHELFEQQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGIL 80
Cdd:COG1020 468 TAAPYPADATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVL 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 81 KAGAAYLPLDPAYPAERLAYMLSDAAPVALLTQSALVETLDSH-LPTVVLDArspSALDGAPDSNPdsrARGITSRHLAY 159
Cdd:COG1020 548 KAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARLPELgVPVLALDA---LALAAEPATNP---PVPVTPDDLAY 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 160 VIYTSGSTGQPKGVMVEHANILRLLAATQDYFRFSHHDVWTLFHSFAFDFSVWELWGALAYGGRLVIVPAACARSPQAFY 239
Cdd:COG1020 622 VIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALA 701
|
..
gi 2646261543 240 AL 241
Cdd:COG1020 702 EL 703
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
23-241 |
1.48e-103 |
|
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: 307.31 E-value: 1.48e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 23 PDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYML 102
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 103 SDAAPVALLTQsalvetldshlptvvldarspsaldgapdsnPDsrargitsrHLAYVIYTSGSTGQPKGVMVEHANILR 182
Cdd:cd17643 81 ADSGPSLLLTD-------------------------------PD---------DLAYVIYTSGSTGRPKGVVVSHANVLA 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2646261543 183 LLAATQDYFRFSHHDVWTLFHSFAFDFSVWELWGALAYGGRLVIVPAACARSPQAFYAL 241
Cdd:cd17643 121 LFAATQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARL 179
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
1-241 |
7.10e-89 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 287.06 E-value: 7.10e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 1 PQTDFPQEALIHELFEQQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGIL 80
Cdd:PRK12467 1566 THTGYPLARLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAIL 1645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 81 KAGAAYLPLDPAYPAERLAYMLSDAAPVALLTQSALVETLDS--HLPTVVLDARSpSALDGAPDSNPDSRargITSRHLA 158
Cdd:PRK12467 1646 KAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARLPLpdGLRSLVLDQED-DWLEGYSDSNPAVN---LAPQNLA 1721
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 159 YVIYTSGSTGQPKGVMVEHANILRLLAATQDYFRFSHHDVWTLFHSFAFDFSVWELWGALAYGGRLVIVPAACARSPQAF 238
Cdd:PRK12467 1722 YVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQL 1801
|
...
gi 2646261543 239 YAL 241
Cdd:PRK12467 1802 IQL 1804
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
13-241 |
5.73e-86 |
|
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: 263.29 E-value: 5.73e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 13 ELFEQQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPA 92
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 93 YPAERLAYMLSDAAPVALLTQSALVETLDSHLPTVVLDArspsALDGAPDSNPdsrARGITSRHLAYVIYTSGSTGQPKG 172
Cdd:cd12117 81 LPAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVIDE----ALDAGPAGNP---AVPVSPDDLAYVMYTSGSTGRPKG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2646261543 173 VMVEHANILRlLAATQDYFRFSHHDVWTLFHSFAFDFSVWELWGALAYGGRLVIVPAACARSPQAFYAL 241
Cdd:cd12117 154 VAVTHRGVVR-LVKNTNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGAL 221
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
23-241 |
6.17e-86 |
|
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: 262.08 E-value: 6.17e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 23 PDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYML 102
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 103 SDAAPVALLTQsalvetldshlptvvldarspsaldgapdsnpdsrargitSRHLAYVIYTSGSTGQPKGVMVEHANILR 182
Cdd:cd05930 81 EDSGAKLVLTD----------------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVN 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2646261543 183 LLAATQDYFRFSHHDVWTLFHSFAFDFSVWELWGALAYGGRLVIVPAACARSPQAFYAL 241
Cdd:cd05930 121 LLLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADL 179
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
36-241 |
2.32e-83 |
|
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: 254.50 E-value: 2.32e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 36 SYGELNRRANRLAHHLL-TLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYMLSDAAPVALLTQS 114
Cdd:TIGR01733 1 TYRELDERANRLARHLRaAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 115 ALVETLDSHLPTVVLDARSPSALDGApDSNPDSRARGITSRHLAYVIYTSGSTGQPKGVMVEHANILRLLAATQDYFRFS 194
Cdd:TIGR01733 81 ALASRLAGLVLPVILLDPLELAALDD-APAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2646261543 195 HHDVWTLFHSFAFDFSVWELWGALAYGGRLVIVPAACARSPQAFYAL 241
Cdd:TIGR01733 160 PDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAA 206
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
15-241 |
1.10e-81 |
|
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: 252.65 E-value: 1.10e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 15 FEQQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYP 94
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 95 AERLAYMLSDAAPVALLTQSALVETLDSHLPTVVLDARSPsaldgAPDSNPDSRARGITSRHLAYVIYTSGSTGQPKGVM 174
Cdd:cd17651 81 AERLAFMLADAGPVLVLTHPALAGELAVELVAVTLLDQPG-----AAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2646261543 175 VEHANILRLLAATQDYFRFSHHDVWTLFHSFAFDFSVWELWGALAYGGRLVIVPAACARSPQAFYAL 241
Cdd:cd17651 156 MPHRSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAW 222
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
11-241 |
2.59e-80 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 262.40 E-value: 2.59e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 11 IHELFEQQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLD 90
Cdd:PRK12467 514 VHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLD 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 91 PAYPAERLAYMLSDAAPVALLTQSALVETLD--SHLPTVVLDARSPSaLDGAPDSNPDSRargITSRHLAYVIYTSGSTG 168
Cdd:PRK12467 594 PEYPQDRLAYMLDDSGVRLLLTQSHLLAQLPvpAGLRSLCLDEPADL-LCGYSGHNPEVA---LDPDNLAYVIYTSGSTG 669
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2646261543 169 QPKGVMVEHANILRLLAATQDYFRFSHHDVWTLFHSFAFDFSVWELWGALAYGGRLVIVPAACARSPQAFYAL 241
Cdd:PRK12467 670 QPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAAL 742
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
13-238 |
2.18e-78 |
|
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: 244.16 E-value: 2.18e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 13 ELFEQQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPA 92
Cdd:cd17655 1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 93 YPAERLAYMLSDAAPVALLTQSALVETLDsHLPTVVLDARSPSALDGAPDSNPDSRargitSRHLAYVIYTSGSTGQPKG 172
Cdd:cd17655 81 YPEERIQYILEDSGADILLTQSHLQPPIA-FIGLIDLLDEDTIYHEESENLEPVSK-----SDDLAYVIYTSGSTGKPKG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2646261543 173 VMVEHANILRLLAATQDYFRFSHHDVWTLFHSFAFDFSVWELWGALAYGGRLVIVPAACARSPQAF 238
Cdd:cd17655 155 VMIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQAL 220
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
23-241 |
8.32e-77 |
|
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: 238.31 E-value: 8.32e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 23 PDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYML 102
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 103 SDAAPVALLTQSAlvetldshlptvvldarspsaldgapdsnpdsrargitsrHLAYVIYTSGSTGQPKGVMVEHANILR 182
Cdd:cd17652 81 ADARPALLLTTPD----------------------------------------NLAYVIYTSGSTGRPKGVVVTHRGLAN 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2646261543 183 LLAATQDYFRFSHHDVWTLFHSFAFDFSVWELWGALAYGGRLVIVPAACARSPQAFYAL 241
Cdd:cd17652 121 LAAAQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADL 179
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
3-228 |
4.90e-76 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 250.08 E-value: 4.90e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 3 TDFPQEALIHELFEQQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKA 82
Cdd:PRK12467 3089 AAYPSERLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKA 3168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 83 GAAYLPLDPAYPAERLAYMLSDAAPVALLTQSALVETL--DSHLPTVVLDArspSALDGAPDSNPDSRARGitsRHLAYV 160
Cdd:PRK12467 3169 GGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQLpaPAGDTALTLDR---LDLNGYSENNPSTRVMG---ENLAYV 3242
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2646261543 161 IYTSGSTGQPKGVMVEHANILRLLAATQDYFRFSHHDVWTLFHSFAFDFSVWELWGALAYGGRLVIVP 228
Cdd:PRK12467 3243 IYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRD 3310
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
5-241 |
6.81e-76 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 249.87 E-value: 6.81e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 5 FPQEALIHELFEQQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGA 84
Cdd:PRK12316 507 YPLQRGVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGG 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 85 AYLPLDPAYPAERLAYMLSDAAPVALLTQSALVETLDSHLPTVVLDARSPSA-LDGAPDSNPDSRargITSRHLAYVIYT 163
Cdd:PRK12316 587 AYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKLPLAAGVQVLDLDRPAAwLEGYSEENPGTE---LNPENLAYVIYT 663
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2646261543 164 SGSTGQPKGVMVEHANILRLLAATQDYFRFSHHDVWTLFHSFAFDFSVWELWGALAYGGRLVIVPAACARSPQAFYAL 241
Cdd:PRK12316 664 SGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVEL 741
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
12-241 |
2.32e-74 |
|
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: 233.71 E-value: 2.32e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 12 HELFEQQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDP 91
Cdd:cd17646 1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 92 AYPAERLAYMLSDAAPVALLTQSALVETL-DSHLPTVVLDAR--SPSALDGAPDSNPDsrargitsrHLAYVIYTSGSTG 168
Cdd:cd17646 81 GYPADRLAYMLADAGPAVVLTTADLAARLpAGGDVALLGDEAlaAPPATPPLVPPRPD---------NLAYVIYTSGSTG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2646261543 169 QPKGVMVEHANILRLLAATQDYFRFSHHDVWTLFHSFAFDFSVWELWGALAYGGRLVIVPAACARSPQAFYAL 241
Cdd:cd17646 152 RPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAAL 224
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
3-241 |
2.31e-71 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 236.78 E-value: 2.31e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 3 TDFPQEALIHELFEQQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKA 82
Cdd:PRK12316 4545 AGYPATRCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKA 4624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 83 GAAYLPLDPAYPAERLAYMLSDAAPVALLTQSALVETLDSHLPTVVLDARSPSALDGAPDSNPDSRARGitsRHLAYVIY 162
Cdd:PRK12316 4625 GGAYVPLDPEYPRERLAYMMEDSGAALLLTQSHLLQRLPIPDGLASLALDRDEDWEGFPAHDPAVRLHP---DNLAYVIY 4701
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2646261543 163 TSGSTGQPKGVMVEHANILRLLAATQDYFRFSHHDVWTLFHSFAFDFSVWELWGALAYGGRLVIvPAACARSPQAFYAL 241
Cdd:PRK12316 4702 TSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVI-RDDSLWDPERLYAE 4779
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1-240 |
3.18e-71 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 236.39 E-value: 3.18e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 1 PQTDFPQEALIHELFEQQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGIL 80
Cdd:PRK12316 1995 TPEAYPRGPGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVL 2074
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 81 KAGAAYLPLDPAYPAERLAYMLSDAAPVALLTQSALVETLDSHLPTVVLDARSPSALDGAPDSNPDSRARGITsrhLAYV 160
Cdd:PRK12316 2075 KAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLERLPLPAGVARLPLDRDAEWADYPDTAPAVQLAGEN---LAYV 2151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 161 IYTSGSTGQPKGVMVEHANILRLLAATQDYFRFSHHDVWTLFHSFAFDFSVWELWGALAYGGRLVIVPAAcARSPQAFYA 240
Cdd:PRK12316 2152 IYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDE-LWDPEQLYD 2230
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
15-241 |
3.75e-71 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 223.34 E-value: 3.75e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 15 FEQQAMLAPDAIAVVCA-GQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAY 93
Cdd:pfam00501 1 LERQAARTPDKTALEVGeGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 94 PAERLAYMLSDAAPVALLTQSALV--------ETLDSHLPTVVLDARSPSALD-----GAPDSNPDSRARGITSRHLAYV 160
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDALKleellealGKLEVVKLVLVLDRDPVLKEEplpeeAKPADVPPPPPPPPDPDDLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 161 IYTSGSTGQPKGVMVEHANILRLLAA----TQDYFRFSHHDVWTLFHSFAFDFSV-WELWGALAYGGRLVIVPAACARSP 235
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRNLVANVLSikrvRPRGFGLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFPALDP 240
|
....*.
gi 2646261543 236 QAFYAL 241
Cdd:pfam00501 241 AALLEL 246
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
23-241 |
1.42e-70 |
|
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: 223.32 E-value: 1.42e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 23 PDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYML 102
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 103 SDAAPVALLTQSALVETLDSHLPTVVLDARspsaldgAPDSNPDSRARGITSRHLAYVIYTSGSTGQPKGVMVEHANILR 182
Cdd:cd12116 81 EDAEPALVLTDDALPDRLPAGLPVLLLALA-------AAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVN 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2646261543 183 LLAATQDYFRFSHHDVWTLFHSFAFDFSVWELWGALAYGGRLVIVPAACARSPQAFYAL 241
Cdd:cd12116 154 FLHSMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARL 212
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
11-240 |
1.17e-66 |
|
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: 213.07 E-value: 1.17e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 11 IHELFEQQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLD 90
Cdd:cd17644 2 IHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 91 PAYPAERLAYMLSDAAPVALLTQsalvetldshlptvvldarspsaldgapdsnpdsrargitSRHLAYVIYTSGSTGQP 170
Cdd:cd17644 82 PNYPQERLTYILEDAQISVLLTQ----------------------------------------PENLAYVIYTSGSTGKP 121
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 171 KGVMVEHANILRLLAATQDYFRFSHHDVWTLFHSFAFDFSVWELWGALAYGGRLVIVPAACARSPQAFYA 240
Cdd:cd17644 122 KGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQ 191
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
23-241 |
4.01e-65 |
|
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: 208.76 E-value: 4.01e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 23 PDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYML 102
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 103 SDAApvalltqsalVETLDSHLPtvvldarspsaldgapdsnpdsrargitsRHLAYVIYTSGSTGQPKGVMVEHANILR 182
Cdd:cd17649 81 EDSG----------AGLLLTHHP-----------------------------RQLAYVIYTSGSTGTPKGVAVSHGPLAA 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2646261543 183 LLAATQDYFRFSHHDVWTLFHSFAFDFSVWELWGALAYGGRLVIVPAACARSPQAFYAL 241
Cdd:cd17649 122 HCQATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEM 180
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
23-235 |
2.04e-63 |
|
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: 204.81 E-value: 2.04e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 23 PDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYML 102
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 103 SDAAPVALLTQSALVETLDSH--LPTVVLDARSPSALDGAPDSNPDSrargitsrhLAYVIYTSGSTGQPKGVMVEHANI 180
Cdd:cd12114 81 ADAGARLVLTDGPDAQLDVAVfdVLILDLDALAAPAPPPPVDVAPDD---------LAYVIFTSGSTGTPKGVMISHRAA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2646261543 181 LRLLAATQDYFRFSHHDVWTLFHSFAFDFSVWELWGALAYGGRLVIVPAACARSP 235
Cdd:cd12114 152 LNTILDINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDP 206
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
11-227 |
3.94e-62 |
|
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: 200.62 E-value: 3.94e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 11 IHELFEQQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLD 90
Cdd:cd12115 1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 91 PAYPAERLAYMLSDAAPVALLTQSAlvetldshlptvvldarspsaldgapdsnpdsrargitsrHLAYVIYTSGSTGQP 170
Cdd:cd12115 81 PAYPPERLRFILEDAQARLVLTDPD----------------------------------------DLAYVIYTSGSTGRP 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 171 KGVMVEHANILRLLAATQDYFRfshHDVW--TLFH-SFAFDFSVWELWGALAYGGRLVIV 227
Cdd:cd12115 121 KGVAIEHRNAAAFLQWAAAAFS---AEELagVLAStSICFDLSVFELFGPLATGGKVVLA 177
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
11-226 |
3.94e-62 |
|
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: 201.62 E-value: 3.94e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 11 IHELFEQQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLD 90
Cdd:cd05918 1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 91 PAYPAERLAYMLSDaapvallTQSALVETldshlptvvldarspsaldgapdSNPDsrargitsrHLAYVIYTSGSTGQP 170
Cdd:cd05918 81 PSHPLQRLQEILQD-------TGAKVVLT-----------------------SSPS---------DAAYVIFTSGSTGKP 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2646261543 171 KGVMVEHANILRLLAATQDYFRFSHHDVWTLFHSFAFDFSVWELWGALAYGGRLVI 226
Cdd:cd05918 122 KGVVIEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCI 177
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
12-230 |
8.90e-62 |
|
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: 199.70 E-value: 8.90e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 12 HELFEQQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDP 91
Cdd:cd17645 1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 92 AYPAERLAYMLSDAAPVALLTQSAlvetldshlptvvldarspsaldgapdsnpdsrargitsrHLAYVIYTSGSTGQPK 171
Cdd:cd17645 81 DYPGERIAYMLADSSAKILLTNPD----------------------------------------DLAYVIYTSGSTGLPK 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2646261543 172 GVMVEHANILRLLAATQDYFRFSHHDVWTLFHSFAFDFSVWELWGALAYGGRLVIVPAA 230
Cdd:cd17645 121 GVMIEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSE 179
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
6-241 |
1.63e-61 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 208.48 E-value: 1.63e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 6 PQEALIHELFEQQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAA 85
Cdd:PRK05691 1128 PAQAWLPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGA 1207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 86 YLPLDPAYPAERLAYMLSDAAPVALLTQSALVETLDS--HLPTVVLDARSpsaLDGAPDSNPDSRARGitsRHLAYVIYT 163
Cdd:PRK05691 1208 YVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQaeGVSAIALDSLH---LDSWPSQAPGLHLHG---DNLAYVIYT 1281
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2646261543 164 SGSTGQPKGVMVEHANILRLLAATQDYFRFSHHDVWTLFHSFAFDFSVWELWGALAYGGRLVIVPAACARSPQAFYAL 241
Cdd:PRK05691 1282 SGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAEL 1359
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
6-237 |
1.75e-59 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 202.58 E-value: 1.75e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 6 PQEALIhELFEQQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAA 85
Cdd:PRK10252 456 PETTLS-ALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAA 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 86 YLPLDPAYPAERLAYMLSDAAPVALLTQSALVETLdSHLPTVVLDarSPSALDGAPDSNPDSRARgitSRHLAYVIYTSG 165
Cdd:PRK10252 535 WLPLDTGYPDDRLKMMLEDARPSLLITTADQLPRF-ADVPDLTSL--CYNAPLAPQGAAPLQLSQ---PHHTAYIIFTSG 608
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2646261543 166 STGQPKGVMVEHANILRLLAATQDYFRFSHHDVWTLFHSFAFDFSVWELWGALAYGGRLVIVPAACARSPQA 237
Cdd:PRK10252 609 STGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLA 680
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
23-233 |
1.26e-58 |
|
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: 192.69 E-value: 1.26e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 23 PDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYML 102
Cdd:cd17656 2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 103 SDAAPVALLTQSALVETLDSHLPTVVLDARSPSALDgapDSNPDSRargITSRHLAYVIYTSGSTGQPKGVMVEHANILR 182
Cdd:cd17656 82 LDSGVRVVLTQRHLKSKLSFNKSTILLEDPSISQED---TSNIDYI---NNSDDLLYIIYTSGTTGKPKGVQLEHKNMVN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2646261543 183 LLAATQDYFRFSHHDVWTLFHSFAFDFSVWELWGALAYGGRLVIVPAACAR 233
Cdd:cd17656 156 LLHFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKR 206
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
4-226 |
1.40e-58 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 200.01 E-value: 1.40e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 4 DFPQEALIHELFEQQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAG 83
Cdd:PRK05691 2183 EARLDQTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAG 2262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 84 AAYLPLDPAYPAERLAYMLSDAAPVALLTQSALVETLdSHLPTVV----LDARSPsALDGAPDSNPDSRArgiTSRHLAY 159
Cdd:PRK05691 2263 GAYVPLDPEYPLERLHYMIEDSGIGLLLSDRALFEAL-GELPAGVarwcLEDDAA-ALAAYSDAPLPFLS---LPQHQAY 2337
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2646261543 160 VIYTSGSTGQPKGVMVEHANILRLLAATQDYFRFSHHDVWTLFHSFAFDFSVWELWGALAYGGRLVI 226
Cdd:PRK05691 2338 LIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGARVVL 2404
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
4-241 |
2.45e-58 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 199.41 E-value: 2.45e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 4 DFPQEALIHELFEQQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAG 83
Cdd:PRK12316 3052 EYPLERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAG 3131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 84 AAYLPLDPAYPAERLAYMLSDAAPVALLTQSALVETLDSHLPTVVLDARSpsalDGAPDSNPDSRargITSRHLAYVIYT 163
Cdd:PRK12316 3132 GAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHLRLPLAQGVQVLDLDRGD----ENYAEANPAIR---TMPENLAYVIYT 3204
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2646261543 164 SGSTGQPKGVMVEHANILRLLAATQDYFRFSHHDVWTLFHSFAFDFSVWELWGALAYGGRLVIVPAACARSPQAFYAL 241
Cdd:PRK12316 3205 SGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVEL 3282
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
23-239 |
1.05e-55 |
|
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: 184.21 E-value: 1.05e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 23 PDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYML 102
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 103 SDAAPVALLTQsalvetldshlptvvldarspsaldgaPDSnpdsrargitsrhLAYVIYTSGSTGQPKGVMVEHANILR 182
Cdd:cd17650 81 EDSGAKLLLTQ---------------------------PED-------------LAYVIYTSGTTGKPKGVMVEHRNVAH 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2646261543 183 LLAATQDYFRFSHHDVWTL-FHSFAFDFSVWELWGALAYGGRLVIVPAACARSPQAFY 239
Cdd:cd17650 121 AAHAWRREYELDSFPVRLLqMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALY 178
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
13-225 |
7.01e-55 |
|
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: 181.74 E-value: 7.01e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 13 ELFEQQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPA 92
Cdd:cd17653 1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 93 YPAERLAYMLSDaapvallTQSALVETLDShlptvvldarspsaldgapdsnPDSrargitsrhLAYVIYTSGSTGQPKG 172
Cdd:cd17653 81 LPSARIQAILRT-------SGATLLLTTDS----------------------PDD---------LAYIIFTSGSTGIPKG 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2646261543 173 VMVEHANILRLLAATQDYFRFSHHDVWTLFHSFAFDFSVWELWGALAYGGRLV 225
Cdd:cd17653 123 VMVPHRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLV 175
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
11-241 |
5.17e-54 |
|
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: 179.62 E-value: 5.17e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 11 IHELFEQQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLD 90
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 91 PAYPAERLAYMLSDAAPVALLTqsalvetldshlptvvldarspsaldgapdsnpdsrargitsrhlAYVIYTSGSTGQP 170
Cdd:COG0318 81 PRLTAEELAYILEDSGARALVT---------------------------------------------ALILYTSGTTGRP 115
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2646261543 171 KGVMVEHANILRLLAATQDYFRFSHHDVW----TLFHSFAFdfsVWELWGALAYGGRLVIVPaacARSPQAFYAL 241
Cdd:COG0318 116 KGVMLTHRNLLANAAAIAAALGLTPGDVVlvalPLFHVFGL---TVGLLAPLLAGATLVLLP---RFDPERVLEL 184
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
23-241 |
4.56e-52 |
|
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: 174.90 E-value: 4.56e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 23 PDAIAVVCAGQSLSYGELNRRANRLAHHLLTLG-VQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYM 101
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 102 LSDAAPVALLTqsalvetldshlptvvldarspsaldgapdsnpdsrargiTSRHLAYVIYTSGSTGQPKGVMVEHANIL 181
Cdd:cd17648 81 LEDTGARVVIT----------------------------------------NSTDLAYAIYTSGTTGKPKGVLVEHGSVV 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2646261543 182 RLLAATQDYFRFSHHD--VWTLFHSFAFDFSVWELWGALAYGGRLVIVPAACARSPQAFYAL 241
Cdd:cd17648 121 NLRTSLSERYFGRDNGdeAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAY 182
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
22-240 |
2.60e-51 |
|
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: 172.82 E-value: 2.60e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 22 APDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYM 101
Cdd:cd05945 4 NPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 102 LSDAAPVALLTqsalvetldshlptvvldarspsaldgAPDSNpdsrargitsrhlAYVIYTSGSTGQPKGVMVEHANIL 181
Cdd:cd05945 84 LDAAKPALLIA---------------------------DGDDN-------------AYIIFTSGSTGRPKGVQISHDNLV 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2646261543 182 RLLAATQDYFRFSHHDVWTLFHSFAFDFSVWELWGALAYGGRLVIVPAACARSPQAFYA 240
Cdd:cd05945 124 SFTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFR 182
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
4-240 |
2.30e-48 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 170.73 E-value: 2.30e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 4 DFPQEALIHELFEQQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAG 83
Cdd:PRK05691 3715 DYPLEQSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAG 3794
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 84 AAYLPLDPAYPAERLAYMLS-DAAPVALLTQS------ALVETLDSHLPTVVLDARSPSAlDGAPDSNPdsrarGITS-- 154
Cdd:PRK05691 3795 AGYLPLDPGLPAQRLQRIIElSRTPVLVCSAAcreqarALLDELGCANRPRLLVWEEVQA-GEVASHNP-----GIYSgp 3868
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 155 RHLAYVIYTSGSTGQPKGVMVEHANILRLLAATQDYFRFSHHDVWTLFHSFAFDFSVWELWGALAYGGRLVIVPAACARS 234
Cdd:PRK05691 3869 DNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDISVWQFLAAPLFGARVEIVPNAIAHD 3948
|
....*.
gi 2646261543 235 PQAFYA 240
Cdd:PRK05691 3949 PQGLLA 3954
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
4-227 |
6.12e-40 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 143.79 E-value: 6.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 4 DFPQEALIHELFEQQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAG 83
Cdd:PRK06187 1 MQDYPLTIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 84 AAYLPLDPAYPAERLAYMLSDAAPVALLTQSALVETLDS---HLPTV---VLDARSPSA------------LDGAPDSNP 145
Cdd:PRK06187 81 AVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAilpQLPTVrtvIVEGDGPAAplapevgeyeelLAAASDTFD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 146 DsraRGITSRHLAYVIYTSGSTGQPKGVMVEHANILRLLAATQDYFRFSHHDVWT----LFHSFAfdfsvwelWG----A 217
Cdd:PRK06187 161 F---PDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLvivpMFHVHA--------WGlpylA 229
|
250
....*....|
gi 2646261543 218 LAYGGRLVIV 227
Cdd:PRK06187 230 LMAGAKQVIP 239
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
11-205 |
1.28e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 137.34 E-value: 1.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 11 IHELFEQQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLD 90
Cdd:PRK07656 7 LPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 91 PAYPAERLAYMLSDAAPVALLTQSALV---ETLDSHLPT----VVLDARSPSALDGAPDS--------NPDSRARGITSR 155
Cdd:PRK07656 87 TRYTADEAAYILARGDAKALFVLGLFLgvdYSATTRLPAlehvVICETEEDDPHTEKMKTftdflaagDPAERAPEVDPD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2646261543 156 HLAYVIYTSGSTGQPKGVMVEHANILRLLAATQDYFRFSHHD----VWTLFHSF 205
Cdd:PRK07656 167 DVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDrylaANPFFHVF 220
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
11-228 |
2.54e-37 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 136.56 E-value: 2.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 11 IHELFEQQamlaPDAIAVVCAGQSLSYGELNRRANRLAHHLLTLgvQPDDRVAICV--ERSPEMVVGLLGILKAGAAYLP 88
Cdd:PRK04813 8 IEEFAQTQ----PDFPAYDYLGEKLTYGQLKEDSDALAAFIDSL--KLPDKSPIIVfgHMSPEMLATFLGAVKAGHAYIP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 89 LDPAYPAERLAYMLSDAAPVALLTQSALVETLDsHLPTVVLDArSPSALDGAPDSNPDSRARGITSrhlAYVIYTSGSTG 168
Cdd:PRK04813 82 VDVSSPAERIEMIIEVAKPSLIIATEELPLEIL-GIPVITLDE-LKDIFATGNPYDFDHAVKGDDN---YYIIFTSGTTG 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2646261543 169 QPKGVMVEHANILRLLA-ATQDyFRFSHHDVWTLFHSFAFDFSVWELWGALAYGGRLVIVP 228
Cdd:PRK04813 157 KPKGVQISHDNLVSFTNwMLED-FALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALP 216
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
11-235 |
5.98e-37 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 136.38 E-value: 5.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 11 IHELFEQQAMLAPDAIAVVC----AGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAY 86
Cdd:COG1022 13 LPDLLRRRAARFPDRVALREkedgIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 87 LPLDPAYPAERLAYMLSDAAPVALLTQS-ALVETLDSH---LPT----VVLDARSPSALD-----------GAPDSNP-- 145
Cdd:COG1022 93 VPIYPTSSAEEVAYILNDSGAKVLFVEDqEQLDKLLEVrdeLPSlrhiVVLDPRGLRDDPrllsldellalGREVADPae 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 146 -DSRARGITSRHLAYVIYTSGSTGQPKGVMVEHANILRLLAATQDYFRFSHHDVWTLF----HSFAFDFSVwelwGALAY 220
Cdd:COG1022 173 lEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFlplaHVFERTVSY----YALAA 248
|
250
....*....|....*
gi 2646261543 221 GGRLvivpaACARSP 235
Cdd:COG1022 249 GATV-----AFAESP 258
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
13-228 |
4.25e-35 |
|
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: 129.99 E-value: 4.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 13 ELFEQQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPA 92
Cdd:cd05936 3 DLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 93 YPAERLAYMLSDAAPVALLTQSALVETLDSHLPTVVLDARSPSAldgapdsnpdsrargitsrhLAYVIYTSGSTGQPKG 172
Cdd:cd05936 83 YTPRELEHILNDSGAKALIVAVSFTDLLAAGAPLGERVALTPED--------------------VAVLQYTSGTTGVPKG 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2646261543 173 VMVEHANILRLLAATQDYFRFSHHD------VWTLFHSFAFDFSvweLWGALAYGGRLVIVP 228
Cdd:cd05936 143 AMLTHRNLVANALQIKAWLEDLLEGddvvlaALPLFHVFGLTVA---LLLPLALGATIVLIP 201
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
19-203 |
1.19e-33 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 126.53 E-value: 1.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 19 AMLAPDAIAV-VCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAER 97
Cdd:PRK07514 12 AFADRDAPFIeTPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 98 LAYMLSDAAPVALLTQSA---------------LVETLDshlptvvlDARSPSALDGAPDSNPDSRARGITSRHLAYVIY 162
Cdd:PRK07514 92 LDYFIGDAEPALVVCDPAnfawlskiaaaagapHVETLD--------ADGTGSLLEAAAAAPDDFETVPRGADDLAAILY 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2646261543 163 TSGSTGQPKGVMVEHANILRLLAATQDYFRFSHHDVwtLFH 203
Cdd:PRK07514 164 TSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDV--LIH 202
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
14-190 |
7.39e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 121.92 E-value: 7.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 14 LFEQQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAY 93
Cdd:PRK07798 8 LFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 94 PAERLAYMLSDAAPVALLTQSAL---VETLDSHLPTV-----VLDARSPSALDGAPD------SNPDSRARGITSRHLAY 159
Cdd:PRK07798 88 VEDELRYLLDDSDAVALVYEREFaprVAEVLPRLPKLrtlvvVEDGSGNDLLPGAVDyedalaAGSPERDFGERSPDDLY 167
|
170 180 190
....*....|....*....|....*....|.
gi 2646261543 160 VIYTSGSTGQPKGVMVEHANILRLLAATQDY 190
Cdd:PRK07798 168 LLYTGGTTGMPKGVMWRQEDIFRVLLGGRDF 198
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
10-226 |
1.84e-31 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 120.66 E-value: 1.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 10 LIHELFEQQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPL 89
Cdd:TIGR03098 1 LLHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 90 DPAYPAERLAYMLSDAAPVALLTQSALVETLDSHLP------TVVLDARSPSALDGAPDSNPDSRARGIT---------- 153
Cdd:TIGR03098 81 NPLLKAEQVAHILADCNVRLLVTSSERLDLLHPALPgchdlrTLIIVGDPAHASEGHPGEEPASWPKLLAlgdadpphpv 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2646261543 154 -SRHLAYVIYTSGSTGQPKGVMVEHANILRLLAATQDYFRFSHHDVWTLFHSFAFDFSVWELWGALAYGGRLVI 226
Cdd:TIGR03098 161 iDSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVL 234
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
6-226 |
3.02e-31 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 120.75 E-value: 3.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 6 PQEALIHELFEQQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAA 85
Cdd:PRK08279 34 DSKRSLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 86 YLPLDPAYPAERLAYMLSDAAPVALLTQSALVETLDSHLPTVVLDARSP-----------------SALDGAPDSNPDSR 148
Cdd:PRK08279 114 VALLNTQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARADLARPPRLWvaggdtlddpegyedlaAAAAGAPTTNPASR 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 149 aRGITSRHLAYVIYTSGSTGQPKGVMVEHANILRLLAATQDYFRFSHHDVW----TLFHSFAFDFSvwelWG-ALAYGGR 223
Cdd:PRK08279 194 -SGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLycclPLYHNTGGTVA----WSsVLAAGAT 268
|
...
gi 2646261543 224 LVI 226
Cdd:PRK08279 269 LAL 271
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
32-228 |
2.25e-30 |
|
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: 117.31 E-value: 2.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 32 GQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYMLSDAAPVALL 111
Cdd:cd05911 8 GKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 112 TQSALVE----------------TLDSHLPTVVLDARSPSALDGAPDSNPDsRARGITSRHLAYVIYTSGSTGQPKGVMV 175
Cdd:cd05911 88 TDPDGLEkvkeaakelgpkdkiiVLDDKPDGVLSIEDLLSPTLGEEDEDLP-PPLKDGKDDTAAILYSSGTTGLPKGVCL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2646261543 176 EHANILR--LLAATQDYFRFSHHDVW----TLFHSFAFDFSVWelwgALAYGGRLVIVP 228
Cdd:cd05911 167 SHRNLIAnlSQVQTFLYGNDGSNDVIlgflPLYHIYGLFTTLA----SLLNGATVIIMP 221
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
12-226 |
5.09e-30 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 116.75 E-value: 5.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 12 HELFEQQAMLAPDAIAVVCAG-----QSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAY 86
Cdd:COG0365 12 YNCLDRHAEGRGDKVALIWEGedgeeRTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 87 LPLDPAYPAERLAYMLSDAAPVALLTQSALV---------ETLD---SHLPTV----VLD-ARSPSALDGA-------PD 142
Cdd:COG0365 92 SPVFPGFGAEALADRIEDAEAKVLITADGGLrggkvidlkEKVDealEELPSLehviVVGrTGADVPMEGDldwdellAA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 143 SNPDSRARGITSRHLAYVIYTSGSTGQPKGVMVEHANIlrlLAATQDYFRFsHHDV-------------WTLFHSfafdf 209
Cdd:COG0365 172 ASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGY---LVHAATTAKY-VLDLkpgdvfwctadigWATGHS----- 242
|
250
....*....|....*..
gi 2646261543 210 svWELWGALAYGGRLVI 226
Cdd:COG0365 243 --YIVYGPLLNGATVVL 257
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
15-229 |
6.89e-30 |
|
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: 115.40 E-value: 6.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 15 FEQQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYP 94
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 95 AERLAYMLSDAApvalltqsalvetldshlPTVVLDArspsaldgapdsnpdsrargitsrhLAYVIYTSGSTGQPKGVM 174
Cdd:cd17631 81 PPEVAYILADSG------------------AKVLFDD-------------------------LALLMYTSGTTGRPKGAM 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2646261543 175 VEHANILRLLAATQDYFRFSHHDVWT----LFHSFAFDFSVwelWGALAYGGRLVIVPA 229
Cdd:cd17631 118 LTHRNLLWNAVNALAALDLGPDDVLLvvapLFHIGGLGVFT---LPTLLRGGTVVILRK 173
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
24-198 |
2.27e-28 |
|
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: 111.23 E-value: 2.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 24 DAIAVVCAGQSLSYGELNRRANRLAHHLLTLG-VQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYML 102
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 103 SDAAPvalltqsalvetldshlpTVVLDarspsaldgapdsnpdsrargitsrhLAYVIYTSGSTGQPKGVMVEHANILR 182
Cdd:cd05941 81 TDSEP------------------SLVLD--------------------------PALILYTSGTTGRPKGVVLTHANLAA 116
|
170
....*....|....*.
gi 2646261543 183 LLAATQDYFRFSHHDV 198
Cdd:cd05941 117 NVRALVDAWRWTEDDV 132
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
23-203 |
1.07e-27 |
|
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: 110.41 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 23 PDAIAVV------CAGQSLSYGELNRRANRLAHHLLTLGvQPDDRVAICVERSPEMVVGLLGILKAGA----AYLPlDPA 92
Cdd:cd05931 7 PDRPAYTflddegGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAiavpLPPP-TPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 93 YPAERLAYMLSDAAPVALLTQSALVETLDSHLPTVVLDARSPSALDGAPDSNP--DSRARGITSRHLAYVIYTSGSTGQP 170
Cdd:cd05931 85 RHAERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPRLLVVDLLPDTSaaDWPPPSPDPDDIAYLQYTSGSTGTP 164
|
170 180 190
....*....|....*....|....*....|....*..
gi 2646261543 171 KGVMVEHANILRLLAATQDYFRFSHHDVWT----LFH 203
Cdd:cd05931 165 KGVVVTHRNLLANVRQIRRAYGLDPGDVVVswlpLYH 201
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
23-228 |
1.51e-27 |
|
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: 109.63 E-value: 1.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 23 PDAIAVVCA--GQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAY 100
Cdd:cd05904 19 PSRPALIDAatGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 101 MLSDAAPVALLTQSALVETL-DSHLPTVVLD-ARSPSALDGAPDSNPDSRARG---ITSRHLAYVIYTSGSTGQPKGVMV 175
Cdd:cd05904 99 QVKDSGAKLAFTTAELAEKLaSLALPVVLLDsAEFDSLSFSDLLFEADEAEPPvvvIKQDDVAALLYSSGTTGRSKGVML 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2646261543 176 EHANILRLLAATQDYFR--FSHHDVW----TLFHSFAFdfsVWELWGALAYGGRLVIVP 228
Cdd:cd05904 179 THRNLIAMVAQFVAGEGsnSDSEDVFlcvlPMFHIYGL---SSFALGLLRLGATVVVMP 234
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
23-177 |
8.54e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 104.63 E-value: 8.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 23 PDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYML 102
Cdd:PRK08316 25 PDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYIL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 103 SDAAPVALLTQSALVETLDS------HLPTVVLDARSPSALDG-----------APDSNPDSRARGitsRHLAYVIYTSG 165
Cdd:PRK08316 105 DHSGARAFLVDPALAPTAEAalallpVDTLILSLVLGGREAPGgwldfadwaeaGSVAEPDVELAD---DDLAQILYTSG 181
|
170
....*....|..
gi 2646261543 166 STGQPKGVMVEH 177
Cdd:PRK08316 182 TESLPKGAMLTH 193
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
19-187 |
4.43e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 102.81 E-value: 4.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 19 AMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERL 98
Cdd:PRK06178 43 ARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHEL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 99 AYMLSDAAPVALLTQSALVETLDSHL--------------------PTVVLDA--RSPSAL-DGAPDSNPDSRARGITSR 155
Cdd:PRK06178 123 SYELNDAGAEVLLALDQLAPVVEQVRaetslrhvivtsladvlpaePTLPLPDslRAPRLAaAGAIDLLPALRACTAPVP 202
|
170 180 190
....*....|....*....|....*....|....*....
gi 2646261543 156 H-------LAYVIYTSGSTGQPKGVMVEHANILRLLAAT 187
Cdd:PRK06178 203 LpppaldaLAALNYTGGTTGMPKGCEHTQRDMVYTAAAA 241
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
34-238 |
6.51e-25 |
|
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: 101.78 E-value: 6.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 34 SLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYMLSDAAPVALLTQ 113
Cdd:cd17654 16 TVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 114 SAL-VETLDSHLPTVVLDARSPSALdgapdsnpdsrargitsrhlAYVIYTSGSTGQPKGVMVEHANILRLLAATQDYFR 192
Cdd:cd17654 96 KELdNAPLSFTPEHRHFNIRTDECL--------------------AYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2646261543 193 FSHHDVWTLFHSFAFDFSVWELWGALAYGGRLVIVPAACARSPQAF 238
Cdd:cd17654 156 ITSEDILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKL 201
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
23-229 |
1.50e-24 |
|
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: 101.23 E-value: 1.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 23 PDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYML 102
Cdd:cd05926 3 APALVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 103 SDAAPVALLTQS---------------ALVE-TLDSHLPTVVLDARSPSALDGAPDSN-PDSRARGitsRHLAYVIYTSG 165
Cdd:cd05926 83 ADLGSKLVLTPKgelgpasraasklglAILElALDVGVLIRAPSAESLSNLLADKKNAkSEGVPLP---DDLALILHTSG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2646261543 166 STGQPKGVMVEHANILRLLAATQDYFRFSHHD----VWTLFHSFAFdfsVWELWGALAYGGRLVIVPA 229
Cdd:cd05926 160 TTGRPKGVPLTHRNLAASATNITNTYKLTPDDrtlvVMPLFHVHGL---VASLLSTLAAGGSVVLPPR 224
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
32-234 |
1.93e-24 |
|
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: 100.06 E-value: 1.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 32 GQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYMLSDAAPVALL 111
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 112 TQsalvetldshlptvvldarspsaldgapdsnpdsrargitsrhLAYVIYTSGSTGQPKGVMVEHANILRLLAATQDYF 191
Cdd:cd05934 81 VD-------------------------------------------PASILYTSGTTGPPKGVVITHANLTFAGYYSARRF 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2646261543 192 RFSHHDVW----TLFHSFAfdfSVWELWGALAYGGRLVIVPAACARS 234
Cdd:cd05934 118 GLGEDDVYltvlPLFHINA---QAVSVLAALSVGATLVLLPRFSASR 161
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
33-230 |
3.07e-24 |
|
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: 99.98 E-value: 3.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 33 QSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYMLSDAAPVALLT 112
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 113 qsalvetldshlptvvldarspsaldgapdSNPDsrargitsrHLAYVIYTSGSTGQPKGVMVEHANILRLLAATQDYFR 192
Cdd:cd05907 84 ------------------------------EDPD---------DLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLP 124
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2646261543 193 FSHHDVWTLF----HSFAfdfSVWELWGALAYGGRLVIVPAA 230
Cdd:cd05907 125 ATEGDRHLSFlplaHVFE---RRAGLYVPLLAGARIYFASSA 163
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
10-228 |
3.69e-24 |
|
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: 100.14 E-value: 3.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 10 LIHELFEQQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPL 89
Cdd:cd05959 5 AATLVDLNLNEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 90 DPAYPAERLAYMLSDAAPVALLTQSALVETLDSHLPTVVLDARSPSALDGAPDSNPDSRARGITSRH------------- 156
Cdd:cd05959 85 NTLLTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLIVSGGAGPEAGALLLAELVAAEaeqlkpaathadd 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 157 LAYVIYTSGSTGQPKGVMVEHANIL--------RLLAATQDYFRFShhdVWTLFHSFAFDFSvweLWGALAYGGRLVIVP 228
Cdd:cd05959 165 PAFWLYSSGSTGRPKGVVHLHADIYwtaelyarNVLGIREDDVCFS---AAKLFFAYGLGNS---LTFPLSVGATTVLMP 238
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
11-241 |
7.60e-24 |
|
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: 99.45 E-value: 7.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 11 IHELFEQQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAayLPLD 90
Cdd:COG1021 27 LGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGA--IPVF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 91 pAYPAER---LAYMLSDAAPVALLTQS--------ALVETLDSHLPT-----VVLDARSPSALDGAPDSNPDSRARGITS 154
Cdd:COG1021 105 -ALPAHRraeISHFAEQSEAVAYIIPDrhrgfdyrALARELQAEVPSlrhvlVVGDAGEFTSLDALLAAPADLSEPRPDP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 155 RHLAYVIYTSGSTGQPKGVMVEHANILRLLAATQDYFRFSHHDVwTLF-----HSFAfdFSVWELWGALAYGGRLVIVPA 229
Cdd:COG1021 184 DDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTV-YLAalpaaHNFP--LSSPGVLGVLYAGGTVVLAPD 260
|
250
....*....|..
gi 2646261543 230 AcarSPQAFYAL 241
Cdd:COG1021 261 P---SPDTAFPL 269
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
8-181 |
2.08e-23 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 98.28 E-value: 2.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 8 EALIHELFEQQAMLAPDAIAVV-CAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAY 86
Cdd:PRK06087 22 DASLADYWQQTARAMPDKIAVVdNHGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 87 LPLDPAYPAERLAYMLSDAAPVALLTQS------------ALVETLDSHLPTVVLDARSPSALDGA-----PDSNPDSRA 149
Cdd:PRK06087 102 VPLLPSWREAELVWVLNKCQAKMFFAPTlfkqtrpvdlilPLQNQLPQLQQIVGVDKLAPATSSLSlsqiiADYEPLTTA 181
|
170 180 190
....*....|....*....|....*....|..
gi 2646261543 150 RGITSRHLAYVIYTSGSTGQPKGVMVEHANIL 181
Cdd:PRK06087 182 ITTHGDELAAVLFTSGTEGLPKGVMLTHNNIL 213
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
4-228 |
3.03e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 94.64 E-value: 3.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 4 DFPQEALIHELfEQQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLL-TLGVQPDDRVAICVERSPEMVVGLLGILKA 82
Cdd:PRK08314 6 TLPETSLFHNL-EVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQqECGVRKGDRVLLYMQNSPQFVIAYYAILRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 83 GAAYLPLDPAYPAERLAYMLSDAAPVALLTQSALVE---------------------TLDSH----LPTVVLDARSPSAL 137
Cdd:PRK08314 85 NAVVVPVNPMNREEELAHYVTDSGARVAIVGSELAPkvapavgnlrlrhvivaqysdYLPAEpeiaVPAWLRAEPPLQAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 138 DG--------APDSNPDSRARGITSRHLAYVIYTSGSTGQPKGVMVEHANILRLLAATQDYFRFSHHDVWT----LFHSF 205
Cdd:PRK08314 165 APggvvawkeALAAGLAPPPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLavlpLFHVT 244
|
250 260
....*....|....*....|...
gi 2646261543 206 AFDFSvweLWGALAYGGRLVIVP 228
Cdd:PRK08314 245 GMVHS---MNAPIYAGATVVLMP 264
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
34-226 |
6.89e-22 |
|
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: 93.31 E-value: 6.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 34 SLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYMLSDAAPVALLTQ 113
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 114 SALVEtldshlptvvldarspsaldgapdsnpdsrargitsrhLAYVIYTSGSTGQPKGVMVEHANILRLLAATQDYFRF 193
Cdd:cd05935 81 SELDD--------------------------------------LALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGL 122
|
170 180 190
....*....|....*....|....*....|....*..
gi 2646261543 194 SHHDVWT----LFHSFAFDFSvweLWGALAYGGRLVI 226
Cdd:cd05935 123 TPSDVILaclpLFHVTGFVGS---LNTAVYVGGTYVL 156
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
25-173 |
1.00e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 93.04 E-value: 1.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 25 AIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYMLSD 104
Cdd:PRK08276 2 AVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 105 AAPVALLTQSALVETLD-------SHLPTVVLDA-------RSPSALDGAPDSNPDSRARGitsrhlAYVIYTSGSTGQP 170
Cdd:PRK08276 82 SGAKVLIVSAALADTAAelaaelpAGVPLLLVVAgpvpgfrSYEEALAAQPDTPIADETAG------ADMLYSSGTTGRP 155
|
...
gi 2646261543 171 KGV 173
Cdd:PRK08276 156 KGI 158
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
9-181 |
1.65e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 92.70 E-value: 1.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 9 ALIHELFEQQamlaPDAIAVV-------CAG--QSLSYGELNRRANRLAHHLLTLGVqPDDRVAICVERSPEMVVGLLGI 79
Cdd:PRK05850 5 SLLRERASLQ----PDDAAFTfidyeqdPAGvaETLTWSQLYRRTLNVAEELRRHGS-TGDRAVILAPQGLEYIVAFLGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 80 LKAGAAYLPLDPAYPA---ERLAYMLSDAAPVALLTQSALVETLDSHL--------PTVV----LDARSPSALDGAPDSN 144
Cdd:PRK05850 80 LQAGLIAVPLSVPQGGahdERVSAVLRDTSPSVVLTTSAVVDDVTEYVapqpgqsaPPVIevdlLDLDSPRGSDARPRDL 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 2646261543 145 PDSrargitsrhlAYVIYTSGSTGQPKGVMVEHANIL 181
Cdd:PRK05850 160 PST----------AYLQYTSGSTRTPAGVMVSHRNVI 186
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
11-230 |
3.26e-21 |
|
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: 92.05 E-value: 3.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 11 IHELFEQQAMLAPDAIAVV-----CAGQS----LSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILK 81
Cdd:TIGR03443 238 IHDIFADNAEKHPDRTCVVetpsfLDPSSktrsFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLK 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 82 AGAAYLPLDPAYPAERLAYMLSDAAPVALL------TQSALVET-------LDSHLPTVVLDARSP---SALDGA----- 140
Cdd:TIGR03443 318 AGATFSVIDPAYPPARQTIYLSVAKPRALIviekagTLDQLVRDyidkeleLRTEIPALALQDDGSlvgGSLEGGetdvl 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 141 ----------------PDSNPDsrargitsrhlayVIYTSGSTGQPKGVMVEHANILRLLAATQDYFRFSHHDVWTLFHS 204
Cdd:TIGR03443 398 apyqalkdtptgvvvgPDSNPT-------------LSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFGLSENDKFTMLSG 464
|
250 260
....*....|....*....|....*.
gi 2646261543 205 FAFDFSVWELWGALAYGGRLvIVPAA 230
Cdd:TIGR03443 465 IAHDPIQRDMFTPLFLGAQL-LVPTA 489
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
34-186 |
1.21e-20 |
|
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: 89.75 E-value: 1.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 34 SLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYMLSDAAPVALLTQ 113
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2646261543 114 SalvetldshlptvVLDARSPSALDGAPdsnpdsrargitsrhlAYVIYTSGSTGQPKGVMVEHANILRLLAA 186
Cdd:cd05903 81 E-------------RFRQFDPAAMPDAV----------------ALLLFTSGTTGEPKGVMHSHNTLSASIRQ 124
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
3-205 |
1.99e-20 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 89.48 E-value: 1.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 3 TDFPQ-EALIHELFEQQAMLAPDAIAVVCAGQSL--SYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGI 79
Cdd:PRK08315 9 TDVPLlEQTIGQLLDRTAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFAT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 80 LKAGAAYLPLDPAYPAERLAYMLSDAAPVALLT-----QSALVETLDS-------------------HLPTVV-LDARSP 134
Cdd:PRK08315 89 AKIGAILVTINPAYRLSELEYALNQSGCKALIAadgfkDSDYVAMLYElapelatcepgqlqsarlpELRRVIfLGDEKH 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 135 S--------ALDGAPDSNPDSRARGIT-SRHLAYVI-YTSGSTGQPKGVMVEHANIL---RLLAATQdyfRFSHHD---- 197
Cdd:PRK08315 169 PgmlnfdelLALGRAVDDAELAARQATlDPDDPINIqYTSGTTGFPKGATLTHRNILnngYFIGEAM---KLTEEDrlci 245
|
....*....
gi 2646261543 198 -VwTLFHSF 205
Cdd:PRK08315 246 pV-PLYHCF 253
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
23-230 |
2.60e-20 |
|
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: 89.11 E-value: 2.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 23 PDAIAVV-------CAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPA 95
Cdd:cd17647 2 PERTCVVetpslnsSKTRSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 96 ERLAYMLSDAAPVALLT-QSALVetldshlptVVldarspsaldgAPDSNPDsrargitsrhlayVIYTSGSTGQPKGVM 174
Cdd:cd17647 82 ARQNIYLGVAKPRGLIViRAAGV---------VV-----------GPDSNPT-------------LSFTSGSEGIPKGVL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2646261543 175 VEHANILRLLAATQDYFRFSHHDVWTLFHSFAFDFSVWELWGALAYGGRLvIVPAA 230
Cdd:cd17647 129 GRHFSLAYYFPWMAKRFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQL-LVPTQ 183
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
10-226 |
2.95e-20 |
|
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: 89.09 E-value: 2.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 10 LIHELFEQQAMLAPDAIAVVCAGQ-----SLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGA 84
Cdd:cd05968 62 IVEQLLDKWLADTRTRPALRWEGEdgtsrTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 85 AYLPLDPAYPAERLAYMLSDAAPVALLTQSA---------LVETLD---SHLPTV--VLDARSPSALDGAPDSN------ 144
Cdd:cd05968 142 IVVPIFSGFGKEAAATRLQDAEAKALITADGftrrgrevnLKEEADkacAQCPTVekVVVVRHLGNDFTPAKGRdlsyde 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 145 ----PDSRARGITSRHLAYVIYTSGSTGQPKGVMVEHANiLRLLAATQDYFRFS--HHDVWTLFHSFAFDFSVWELWGAL 218
Cdd:cd05968 222 eketAGDGAERTESEDPLMIIYTSGTTGKPKGTVHVHAG-FPLKAAQDMYFQFDlkPGDLLTWFTDLGWMMGPWLIFGGL 300
|
....*...
gi 2646261543 219 AYGGRLVI 226
Cdd:cd05968 301 ILGATMVL 308
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
19-240 |
4.14e-20 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 88.39 E-value: 4.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 19 AMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERL 98
Cdd:PRK09029 13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 99 AymlsdaapvALLTQSAL--VETLDSHLPTVVLDARSPSALDGAPDSNPDSRArgitsrhLAYVIYTSGSTGQPKGVMVE 176
Cdd:PRK09029 93 E---------ELLPSLTLdfALVLEGENTFSALTSLHLQLVEGAHAVAWQPQR-------LATMTLTSGSTGLPKAAVHT 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2646261543 177 HANILRLLAATQDYFRFSHHDVW----TLFHsfafdFS----VWElWgaLAYGGRLVIvpaacaRSPQAFYA 240
Cdd:PRK09029 157 AQAHLASAEGVLSLMPFTAQDSWllslPLFH-----VSgqgiVWR-W--LYAGATLVV------RDKQPLEQ 214
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
11-227 |
4.51e-20 |
|
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: 88.33 E-value: 4.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 11 IHELFEQQAMLAPDAIAVVCA--GQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLP 88
Cdd:cd05923 3 VFEMLRRAASRAPDACAIADParGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 89 LDPAYPAERLAYMLSDAAPVALLTQSALVETLDSHLPTVVLDARSPSALDGAPDSNPDS-RARGITSRHLAYVIYTSGST 167
Cdd:cd05923 83 INPRLKAAELAELIERGEMTAAVIAVDAQVMDAIFQSGVRVLALSDLVGLGEPESAGPLiEDPPREPEQPAFVFYTSGTT 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2646261543 168 GQPKGVMVEHANIL-RLLA-ATQDYFRFSHHDV----WTLFHSFAFdFSVweLWGALAYGGRLVIV 227
Cdd:cd05923 163 GLPKGAVIPQRAAEsRVLFmSTQAGLRHGRHNVvlglMPLYHVIGF-FAV--LVAALALDGTYVVV 225
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
33-181 |
5.80e-20 |
|
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: 87.80 E-value: 5.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 33 QSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYMLSDAAPVALLt 112
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV- 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2646261543 113 qsalvetldshlptvvldarspsaLDGAPDSnpdsrargitsrhLAYVIYTSGSTGQPKGVMVEHANIL 181
Cdd:cd17640 83 ------------------------VENDSDD-------------LATIIYTSGTTGNPKGVMLTHANLL 114
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
33-177 |
7.52e-20 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 87.64 E-value: 7.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 33 QSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYMLSDAAPVALLT 112
Cdd:PRK04319 72 EKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLIT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 113 QSAL-----VETLdSHLPTVVLDARSPSALDGAPD-------SNPDSRARGITSRHLAYVIYTSGSTGQPKGV------M 174
Cdd:PRK04319 152 TPALlerkpADDL-PSLKHVLLVGEDVEEGPGTLDfnalmeqASDEFDIEWTDREDGAILHYTSGSTGKPKGVlhvhnaM 230
|
...
gi 2646261543 175 VEH 177
Cdd:PRK04319 231 LQH 233
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
6-178 |
8.63e-20 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 87.51 E-value: 8.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 6 PQEALIHELFEQQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAA 85
Cdd:PRK06155 18 PSERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 86 YLPLDPAYPAERLAYMLSDAAPVALLTQSALVETLDsHLPTVVLDARSPSALDGAPDSNPDSR--------------ARG 151
Cdd:PRK06155 98 AVPINTALRGPQLEHILRNSGARLLVVEAALLAALE-AADPGDLPLPAVWLLDAPASVSVPAGwstaplppldapapAAA 176
|
170 180
....*....|....*....|....*..
gi 2646261543 152 ITSRHLAYVIYTSGSTGQPKGVMVEHA 178
Cdd:PRK06155 177 VQPGDTAAILYTSGTTGPSKGVCCPHA 203
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
27-241 |
1.21e-19 |
|
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: 86.75 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 27 AVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYMLSDAA 106
Cdd:cd05919 3 AFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 107 PVALLTQSAlvetldshlptvvldarspsaldgapdsnpdsrargitsrHLAYVIYTSGSTGQPKGVMVEHANIL---RL 183
Cdd:cd05919 83 ARLVVTSAD----------------------------------------DIAYLLYSSGTTGPPKGVMHAHRDPLlfaDA 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2646261543 184 LAatQDYFRFSHHDVWTLFHSFAFDFSVW-ELWGALAYGGRLVIVPAacARSPQAFYAL 241
Cdd:cd05919 123 MA--REALGLTPGDRVFSSAKMFFGYGLGnSLWFPLAVGASAVLNPG--WPTAERVLAT 177
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
16-173 |
1.73e-19 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 86.67 E-value: 1.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 16 EQQAMLAPDAIAVVCA--GQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAY 93
Cdd:PRK13391 4 GIHAQTTPDKPAVIMAstGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 94 PAERLAYMLSDAAPVALLTQSA---LVETLDSHLPTV----VLDA--------RSPSALDGAPDSNPDSRARGitsrhlA 158
Cdd:PRK13391 84 TPAEAAYIVDDSGARALITSAAkldVARALLKQCPGVrhrlVLDGdgelegfvGYAEAVAGLPATPIADESLG------T 157
|
170
....*....|....*
gi 2646261543 159 YVIYTSGSTGQPKGV 173
Cdd:PRK13391 158 DMLYSSGTTGRPKGI 172
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
16-233 |
2.36e-19 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 86.27 E-value: 2.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 16 EQQAMLAPDAIAVVcagQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPA 95
Cdd:PRK08008 22 HKTALIFESSGGVV---RRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 96 ERLAYMLSDAAPVALLTQSAL------VETLDSHLPTVVLDARSPS-ALDGAPD------SNPDS--RARGITSRHLAYV 160
Cdd:PRK08008 99 EESAWILQNSQASLLVTSAQFypmyrqIQQEDATPLRHICLTRVALpADDGVSSftqlkaQQPATlcYAPPLSTDDTAEI 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2646261543 161 IYTSGSTGQPKGVMVEHANIL--RLLAATQDYFRFShhDVW-TLFHSFAFDFSVWELWGALAYGGRLVIVPAACAR 233
Cdd:PRK08008 179 LFTSGTTSRPKGVVITHYNLRfaGYYSAWQCALRDD--DVYlTVMPAFHIDCQCTAAMAAFSAGATFVLLEKYSAR 252
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
32-181 |
2.60e-19 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 85.96 E-value: 2.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 32 GQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYMLSDAAPVALL 111
Cdd:cd05914 5 GEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIF 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 112 TqsalvetldshlptvvldarspsaldgapdSNPDSrargitsrhLAYVIYTSGSTGQPKGVMVEHANIL 181
Cdd:cd05914 85 V------------------------------SDEDD---------VALINYTSGTTGNSKGVMLTYRNIV 115
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
11-205 |
2.68e-19 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 86.37 E-value: 2.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 11 IHELFEQQAMLAPDAIAVVCAGQSL--SYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLP 88
Cdd:PRK12583 20 IGDAFDATVARFPDREALVVRHQALryTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 89 LDPAYPAERLAYMLSDAAPVALLTQSAL-----VETLDSHLP--------------------TVVLDARSPSALDGAPDS 143
Cdd:PRK12583 100 INPAYRASELEYALGQSGVRWVICADAFktsdyHAMLQELLPglaegqpgalacerlpelrgVVSLAPAPPPGFLAWHEL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2646261543 144 NpdSRARGITSRHLAY------------VIYTSGSTGQPKGVMVEHANILRLLAATQDYFRFSHHDVWT----LFHSF 205
Cdd:PRK12583 180 Q--ARGETVSREALAErqasldrddpinIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCvpvpLYHCF 255
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
22-237 |
1.36e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 83.89 E-value: 1.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 22 APDAIAVVCAGQSLSYGELNRRANRLAHHLLTLgvqpdDRVAICVERSPEMVVGLLGILKAGAAYLPLDP-AYPAERlAY 100
Cdd:PRK07787 13 ADIADAVRIGGRVLSRSDLAGAATAVAERVAGA-----RRVAVLATPTLATVLAVVGALIAGVPVVPVPPdSGVAER-RH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 101 MLSDAAPVALLTqSALVETLDSHLPTVVLDARSPSALDGAPDSNPdsrargitsrhlAYVIYTSGSTGQPKGVMVEHANI 180
Cdd:PRK07787 87 ILADSGAQAWLG-PAPDDPAGLPHVPVRLHARSWHRYPEPDPDAP------------ALIVYTSGTTGPPKGVVLSRRAI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2646261543 181 LRLLAATQDYFRFSHHDVWT----LFHSFAFdfsVWELWGALAYGGRLVIV----PAACARSPQA 237
Cdd:PRK07787 154 AADLDALAEAWQWTADDVLVhglpLFHVHGL---VLGVLGPLRIGNRFVHTgrptPEAYAQALSE 215
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
10-226 |
3.31e-18 |
|
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: 83.01 E-value: 3.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 10 LIHELFEQQAMLAPDAIAVVCAG------QSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAG 83
Cdd:cd17634 54 LAANALDRHLRENGDRTAIIYEGddtsqsRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 84 AAYLPLDPAYPAERLAYMLSDAAPVALLTQSALV-------------ETLDSHLP---TVVLDARSPSALDGAP------ 141
Cdd:cd17634 134 AVHSVIFGGFAPEAVAGRIIDSSSRLLITADGGVragrsvplkknvdDALNPNVTsveHVIVLKRTGSDIDWQEgrdlww 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 142 -----DSNPDSRARGITSRHLAYVIYTSGSTGQPKGVMveHANILRLLAATQDY---FRFSHHDVWTLFHSFAFDFS-VW 212
Cdd:cd17634 214 rdliaKASPEHQPEAMNAEDPLFILYTSGTTGKPKGVL--HTTGGYLVYAATTMkyvFDYGPGDIYWCTADVGWVTGhSY 291
|
250
....*....|....
gi 2646261543 213 ELWGALAYGGRLVI 226
Cdd:cd17634 292 LLYGPLACGATTLL 305
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
17-179 |
7.16e-18 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 81.93 E-value: 7.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 17 QQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAE 96
Cdd:PRK03640 10 QRAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 97 RLAYMLSDAAPVALLTQSALVETLDSHLPTVVldarspSALDGAPDSNPDSrargITSRHL---AYVIYTSGSTGQPKGV 173
Cdd:PRK03640 90 ELLWQLDDAEVKCLITDDDFEAKLIPGISVKF------AELMNGPKEEAEI----QEEFDLdevATIMYTSGTTGKPKGV 159
|
....*.
gi 2646261543 174 MVEHAN 179
Cdd:PRK03640 160 IQTYGN 165
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
13-241 |
1.03e-17 |
|
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: 81.61 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 13 ELFEQQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPA 92
Cdd:cd05920 19 DLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 93 YPAERLAYMLSDAAPVALltqsalvetldshlptVVLDARSPSaldgapdsnpDSRARGITSRH----LAYVIYTSGSTG 168
Cdd:cd05920 99 HRRSELSAFCAHAEAVAY----------------IVPDRHAGF----------DHRALARELAEsipeVALFLLSGGTTG 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2646261543 169 QPKGVMVEHANILRLLAATQDYFRFSHHDVW----TLFHSFAfdFSVWELWGALAYGGRLVIVPAAcarSPQAFYAL 241
Cdd:cd05920 153 TPKLIPRTHNDYAYNVRASAEVCGLDQDTVYlavlPAAHNFP--LACPGVLGTLLAGGRVVLAPDP---SPDAAFPL 224
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
11-174 |
2.58e-17 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 80.48 E-value: 2.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 11 IHELFEQQAMLAPDAIAVVC------AGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGA 84
Cdd:PRK13295 26 INDDLDACVASCPDKTAVTAvrlgtgAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 85 AYLPLDPAYPAERLAYMLSDA-APVALLTQS-------ALVETLDSHLPT----VVLD---ARSPSALDGAPDSNPDSRA 149
Cdd:PRK13295 106 VLNPLMPIFRERELSFMLKHAeSKVLVVPKTfrgfdhaAMARRLRPELPAlrhvVVVGgdgADSFEALLITPAWEQEPDA 185
|
170 180 190
....*....|....*....|....*....|.
gi 2646261543 150 RGITSRH------LAYVIYTSGSTGQPKGVM 174
Cdd:PRK13295 186 PAILARLrpgpddVTQLIYTSGTTGEPKGVM 216
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
156-228 |
2.97e-17 |
|
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: 79.25 E-value: 2.97e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2646261543 156 HLAYVIYTSGSTGQPKGVMVEHANILRLLAATQDYFRFSHHDVWTLFHSFAFDFSVWELWGALAYGGRLVIVP 228
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLP 73
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
36-193 |
4.90e-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: 79.40 E-value: 4.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 36 SYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYMLSDAAPVALLTqsa 115
Cdd:cd05971 8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT--- 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2646261543 116 lvetldshlptvvldarspsalDGAPDsnpdsrargitsrhLAYVIYTSGSTGQPKGVMVEHANILRLLAATQDYFRF 193
Cdd:cd05971 85 ----------------------DGSDD--------------PALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNL 126
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
36-225 |
5.36e-17 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 79.60 E-value: 5.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 36 SYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYMLSDAAPVALLTQS- 114
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVDRd 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 115 --ALVETLDSHLPTV----VLDARSPSALDGAP----------DSNPDSRARGITSRHLAYVIYTSGSTGQPKGVMVEH- 177
Cdd:cd12119 107 flPLLEAIAPRLPTVehvvVMTDDAAMPEPAGVgvlayeellaAESPEYDWPDFDENTAAAICYTSGTTGNPKGVVYSHr 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2646261543 178 ANILRLLAA-TQDYFRFSHHDVW----TLFHSFAfdfsvwelWG----ALAYGGRLV 225
Cdd:cd12119 187 SLVLHAMAAlLTDGLGLSESDVVlpvvPMFHVNA--------WGlpyaAAMVGAKLV 235
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
16-180 |
6.70e-17 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 79.13 E-value: 6.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 16 EQQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLT-LGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYP 94
Cdd:PRK06839 9 EKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYeLNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 95 AERLAYMLSDAAPVALLTQSALVETLDShLPTVVLDAR--SPSALDGAPDSNPDSRARGITSRhlAYVI-YTSGSTGQPK 171
Cdd:PRK06839 89 ENELIFQLKDSGTTVLFVEKTFQNMALS-MQKVSYVQRviSITSLKEIEDRKIDNFVEKNESA--SFIIcYTSGTTGKPK 165
|
....*....
gi 2646261543 172 GVMVEHANI 180
Cdd:PRK06839 166 GAVLTQENM 174
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
1-180 |
2.01e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 77.73 E-value: 2.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 1 PQTDFPQEALIHeLFEQQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGIL 80
Cdd:PRK05605 25 HDLDYGDTTLVD-LYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 81 KAGAAYLPLDPAYPAERLAYMLSD-AAPVALL--TQSALVETL--DSHLPTVV-------------LDARSP-------- 134
Cdd:PRK05605 104 RLGAVVVEHNPLYTAHELEHPFEDhGARVAIVwdKVAPTVERLrrTTPLETIVsvnmiaampllqrLALRLPipalrkar 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2646261543 135 SALDG-APDSNP-----DSRARG---------ITSRHLAYVIYTSGSTGQPKGVMVEHANI 180
Cdd:PRK05605 184 AALTGpAPGTVPwetlvDAAIGGdgsdvshprPTPDDVALILYTSGTTGKPKGAQLTHRNL 244
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
16-180 |
2.04e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 77.90 E-value: 2.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 16 EQQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPA 95
Cdd:PRK07786 24 ARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 96 ERLAYMLSDAAPVALLTQSAL------VETLDSHLPTVVL-----DARSPSALDGAPDSNPDSRARGITSRHLAYVIYTS 164
Cdd:PRK07786 104 PEIAFLVSDCGAHVVVTEAALapvataVRDIVPLLSTVVVaggssDDSVLGYEDLLAEAGPAHAPVDIPNDSPALIMYTS 183
|
170
....*....|....*.
gi 2646261543 165 GSTGQPKGVMVEHANI 180
Cdd:PRK07786 184 GTTGRPKGAVLTHANL 199
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
35-236 |
3.67e-16 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 77.09 E-value: 3.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 35 LSYGELNRRANRLAHHLLTLgVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPL-DPAYP--AERLAYMLSDAAPVALL 111
Cdd:PRK12476 69 LTWTQLGVRLRAVGARLQQV-AGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELPghAERLDTALRDAEPTVVL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 112 TQSALVETLDSHLPTVVLDARsPSALdgAPDSNPDSRARGITSRHL-----AYVIYTSGSTGQPKGVMVEH----ANILR 182
Cdd:PRK12476 148 TTTAAAEAVEGFLRNLPRLRR-PRVI--AIDAIPDSAGESFVPVELdtddvSHLQYTSGSTRPPVGVEITHravgTNLVQ 224
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2646261543 183 LLAATQDYFRFSHHDVW-TLFHsfafDFSVWELWGALAYGGRLVIV-PAACARSPQ 236
Cdd:PRK12476 225 MILSIDLLDRNTHGVSWlPLYH----DMGLSMIGFPAVYGGHSTLMsPTAFVRRPQ 276
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
35-194 |
3.98e-16 |
|
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: 76.79 E-value: 3.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 35 LSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYpaerlaymlsdaAPVALLTQs 114
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAF------------GPKAIEHR- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 115 alVETLDSHLptVVLDARSPSALDGAPdsnpdsrargitsrhlAYVIYTSGSTGQPKGVMVEhaniLRLLAATQDYFRFS 194
Cdd:cd05973 68 --LRTSGARL--VVTDAANRHKLDSDP----------------FVMMFTSGTTGLPKGVPVP----LRALAAFGAYLRDA 123
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
16-222 |
5.45e-16 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 76.57 E-value: 5.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 16 EQQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPA 95
Cdd:cd12118 11 ERAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 96 ERLAYMLSDAAPVALLTQSALvETLDshlptvVLDARSPSALDGAPDSNPDSRArgitsrhlayVIYTSGSTGQPKGVMV 175
Cdd:cd12118 91 EEIAFILRHSEAKVLFVDREF-EYED------LLAEGDPDFEWIPPADEWDPIA----------LNYTSGTTGRPKGVVY 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2646261543 176 EHANILRLLAATQDYFRFSHHDV--WTL--FHSFAFDFSvwelWGALAYGG 222
Cdd:cd12118 154 HHRGAYLNALANILEWEMKQHPVylWTLpmFHCNGWCFP----WTVAAVGG 200
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
35-177 |
6.09e-16 |
|
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: 76.39 E-value: 6.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 35 LSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYMLSDAAPVALLTQS 114
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2646261543 115 ALVETLDSHLPTvvldarspsaldgapdsnpdsrargitsrhlaYVIYTSGSTGQPKGVMVEH 177
Cdd:cd05969 81 ELYERTDPEDPT--------------------------------LLHYTSGTTGTPKGVLHVH 111
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
11-240 |
1.00e-15 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 75.69 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 11 IHELFEQQAMLAPDAIAVVCAGQ--SLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLP 88
Cdd:PRK05852 18 IADLVEVAATRLPEAPALVVTADriAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 89 LDPAYP-AERLAYMLSDAAPVALLTQSALVET-LDSH--LPTVVLDARSPSALDGAP----DSNPDSRARGITSRHL--- 157
Cdd:PRK05852 98 LDPALPiAEQRVRSQAAGARVVLIDADGPHDRaEPTTrwWPLTVNVGGDSGPSGGTLsvhlDAATEPTPATSTPEGLrpd 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 158 -AYVIYTSGSTGQPKGVMVEHANILRLLAATQDYFRFSHHD----VWTLFHSFAFdfsVWELWGALAYGGRlVIVPAACA 232
Cdd:PRK05852 178 dAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDatvaVMPLYHGHGL---IAALLATLASGGA-VLLPARGR 253
|
....*...
gi 2646261543 233 RSPQAFYA 240
Cdd:PRK05852 254 FSAHTFWD 261
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
10-180 |
1.31e-15 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 75.98 E-value: 1.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 10 LIHELfEQQAMLAPDAIAVVCAGQS------LSYGELNRRANRLAHHLLTLGvQPDDRVAICVERSPEMVVGLLGILKAG 83
Cdd:PRK05691 11 LVQAL-QRRAAQTPDRLALRFLADDpgegvvLSYRDLDLRARTIAAALQARA-SFGDRAVLLFPSGPDYVAAFFGCLYAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 84 AAYLPldpAYPAE--------RLAYMLSDAAPVALLTQSALVETLDSHLPTVVLDARSPSALDGAPDSNPDS-RARGITS 154
Cdd:PRK05691 89 VIAVP---AYPPEsarrhhqeRLLSIIADAEPRLLLTVADLRDSLLQMEELAAANAPELLCVDTLDPALAEAwQEPALQP 165
|
170 180
....*....|....*....|....*.
gi 2646261543 155 RHLAYVIYTSGSTGQPKGVMVEHANI 180
Cdd:PRK05691 166 DDIAFLQYTSGSTALPKGVQVSHGNL 191
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
32-207 |
1.89e-15 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 75.02 E-value: 1.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 32 GQSLSYGELNRRANRLAHHLLT-LGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYMLSDAAPVAL 110
Cdd:cd05938 3 GETYTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 111 LTQSALVETLDSHLPTV--------VLDARSPS--------ALDGAPD-SNPDSRARGITSRHLAYVIYTSGSTGQPKGV 173
Cdd:cd05938 83 VVAPELQEAVEEVLPALradgvsvwYLSHTSNTegvislldKVDAASDePVPASLRAHVTIKSPALYIYTSGTTGLPKAA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2646261543 174 MVEHaniLRLLAATQDYFRF--SHHDV----WTLFHSFAF 207
Cdd:cd05938 163 RISH---LRVLQCSGFLSLCgvTADDViyitLPLYHSSGF 199
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
42-228 |
2.67e-15 |
|
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: 74.40 E-value: 2.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 42 RRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAA----YLPLDPAYPAERLAYMLSDAAPVALLTQSALV 117
Cdd:cd05922 1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 118 ETLDSHL-----PTVVLDArspsalDGAPDSNPDSRARGITSRHLAYVIYTSGSTGQPKGVMVEHANILRLLAATQDYFR 192
Cdd:cd05922 81 DRLRDALpaspdPGTVLDA------DGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLG 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 2646261543 193 FSHHDVWTLFHSFAFDFSVWELWGALAYGGRLVIVP 228
Cdd:cd05922 155 ITADDRALTVLPLSYDYGLSVLNTHLLRGATLVLTN 190
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
14-226 |
4.07e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 73.81 E-value: 4.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 14 LFEQQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAY 93
Cdd:PRK07788 54 LVAHAARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGF 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 94 PAERLAYMLSDAAPVALLTQSALVETLDSHLPTVVL--------DARSPSA-----LDGAPDSNPDSRARGITsRHLAYV 160
Cdd:PRK07788 134 SGPQLAEVAAREGVKALVYDDEFTDLLSALPPDLGRlrawggnpDDDEPSGstdetLDDLIAGSSTAPLPKPP-KPGGIV 212
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 161 IYTSGSTGQPKGVMVEHANILRLLAATQDYFRFSHHDVWTL----FHSFAfdFSVWELwgALAYGGRLVI 226
Cdd:PRK07788 213 ILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLpapmFHATG--WAHLTL--AMALGSTVVL 278
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
13-192 |
5.95e-15 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 73.37 E-value: 5.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 13 ELFEQQAMLAPDAIAVVCAG-----QSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYL 87
Cdd:PRK08180 43 DRLVHWAQEAPDRVFLAERGadggwRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 88 PLDPAYPA-----ERLAYML----------SDAAPVAlltqSALVETLDSHLPTVVLDARSPSA--------LDGAPDSN 144
Cdd:PRK08180 123 PVSPAYSLvsqdfGKLRHVLelltpglvfaDDGAAFA----RALAAVVPADVEVVAVRGAVPGRaatpfaalLATPPTAA 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2646261543 145 PDSRARGITSRHLAYVIYTSGSTGQPKGVMVEHanilRLLAATQDYFR 192
Cdd:PRK08180 199 VDAAHAAVGPDTIAKFLFTSGSTGLPKAVINTH----RMLCANQQMLA 242
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
18-180 |
7.12e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 73.30 E-value: 7.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 18 QAMLAPDAIAVV--CAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPA 95
Cdd:PRK09088 4 HARLQPQRLAAVdlALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 96 ERLAYMLSDAAPVALLTqsalvetlDSHLPTVVLDARSPSALDGAPDSNPDSRARGITSRHLAYVIYTSGSTGQPKGVMV 175
Cdd:PRK09088 84 SELDALLQDAEPRLLLG--------DDAVAAGRTDVEDLAAFIASADALEPADTPSIPPERVSLILFTSGTSGQPKGVML 155
|
....*
gi 2646261543 176 EHANI 180
Cdd:PRK09088 156 SERNL 160
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
11-178 |
7.48e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 73.16 E-value: 7.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 11 IHELFEQQAMLAPDAIAVV----CAGQ--SLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGA 84
Cdd:PRK12582 51 IPHLLAKWAAEAPDRPWLAqrepGHGQwrKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 85 AYLPLDPAYPA-----ERLAYMLSDAAPVALLTQSAL-----VETLDSHLPTVVLDARSPSALDG---------APDSNP 145
Cdd:PRK12582 131 PAAPVSPAYSLmshdhAKLKHLFDLVKPRVVFAQSGApfaraLAALDLLDVTVVHVTGPGEGIASiafadlaatPPTAAV 210
|
170 180 190
....*....|....*....|....*....|...
gi 2646261543 146 DSRARGITSRHLAYVIYTSGSTGQPKGVMVEHA 178
Cdd:PRK12582 211 AAAIAAITPDTVAKYLFTSGSTGMPKAVINTQR 243
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
11-181 |
8.18e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 73.14 E-value: 8.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 11 IHELFEQQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLD 90
Cdd:PRK06710 26 LHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 91 PAYPAERLAYMLSDAAPVALL-----------TQSA------LVETLDSHLP--------------TVVLDARSPSALDG 139
Cdd:PRK06710 106 PLYTERELEYQLHDSGAKVILcldlvfprvtnVQSAtkiehvIVTRIADFLPfpknllypfvqkkqSNLVVKVSESETIH 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2646261543 140 APDSNPDSRARGIT-----SRHLAYVIYTSGSTGQPKGVMVEHANIL 181
Cdd:PRK06710 186 LWNSVEKEVNTGVEvpcdpENDLALLQYTGGTTGFPKGVMLTHKNLV 232
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
33-188 |
1.02e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 72.84 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 33 QSLSYGELNRRANRLAHHLLTLGvQPDDRVAICVERSPEMVVGLLGILKAGAAYLPL-DPAYP--AERLAYMLSDAAPVA 109
Cdd:PRK07769 54 RDLTWSQFGARNRAVGARLQQVT-KPGDRVAILAPQNLDYLIAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCTPSA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 110 LLTQSALVETLDSHLPTVVLDARsPS--ALDGAPDSNPDSRAR-GITSRHLAYVIYTSGSTGQPKGVMVEH----ANILR 182
Cdd:PRK07769 133 ILTTTDSAEGVRKFFRARPAKER-PRviAVDAVPDEVGATWVPpEANEDTIAYLQYTSGSTRIPAGVQITHlnlpTNVLQ 211
|
....*.
gi 2646261543 183 LLAATQ 188
Cdd:PRK07769 212 VIDALE 217
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
17-191 |
1.09e-14 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 72.62 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 17 QQAMLAPDAIAVVCAG----------QSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAY 86
Cdd:PRK09274 14 RAAQERPDQLAVAVPGgrgadgklayDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 87 LPLDPAYPAERLAYMLSDAAPVALLTQSA--LVETL-----DSHLPTVVLDAR------SPSALDGAPDSNPdSRARGIT 153
Cdd:PRK09274 94 VLVDPGMGIKNLKQCLAEAQPDAFIGIPKahLARRLfgwgkPSVRRLVTVGGRllwggtTLATLLRDGAAAP-FPMADLA 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 2646261543 154 SRHLAYVIYTSGSTGQPKGVMVEHANILRLLAATQDYF 191
Cdd:PRK09274 173 PDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDY 210
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
13-198 |
1.46e-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: 72.31 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 13 ELFEQQAMLAPDA----IAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLP 88
Cdd:cd05906 14 ELLLRAAERGPTKgityIDADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 89 LDPA----YPAERLAY------MLSDaaPVaLLTQSALV------ETLDSHLPTVVL---DARSPSALDGAPDSNPDSra 149
Cdd:cd05906 94 LTVPptydEPNARLRKlrhiwqLLGS--PV-VLTDAELVaefaglETLSGLPGIRVLsieELLDTAADHDLPQSRPDD-- 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2646261543 150 rgitsrhLAYVIYTSGSTGQPKGVMVEHANILRLLAATQDYFRFSHHDV 198
Cdd:cd05906 169 -------LALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDV 210
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
35-186 |
1.65e-14 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 72.35 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 35 LSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAG--AAYLPLdPAYPAERLAY------MLSDAA 106
Cdd:PRK09192 50 LPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGlvPVPLPL-PMGFGGRESYiaqlrgMLASAQ 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 107 PVALLTQSALVETLDShlPTVVLDAR---SPSALDGAPDsnPDSRARGITSRHLAYVIYTSGSTGQPKGVMVEHANILRL 183
Cdd:PRK09192 129 PAAIITPDELLPWVNE--ATHGNPLLhvlSHAWFKALPE--ADVALPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMAN 204
|
...
gi 2646261543 184 LAA 186
Cdd:PRK09192 205 LRA 207
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
15-228 |
3.99e-14 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 71.22 E-value: 3.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 15 FEQQAMLAPDAIavvcagqslSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYP 94
Cdd:PRK06060 20 YDRPAFYAADVV---------THGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 95 AERLAYMLSDAAPVALLTQSALVetlDSHLPTVVLDAR---SPSALDGAPDSNPdsrargITSRHLAYVIYTSGSTGQPK 171
Cdd:PRK06060 91 RDDHALAARNTEPALVVTSDALR---DRFQPSRVAEAAelmSEAARVAPGGYEP------MGGDALAYATYTSGTTGPPK 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2646261543 172 GVMVEHANILRLL-AATQDYFRFSHHDVW----TLFHSFAFDFSVwelWGALAYGGRLVIVP 228
Cdd:PRK06060 162 AAIHRHADPLTFVdAMCRKALRLTPEDTGlcsaRMYFAYGLGNSV---WFPLATGGSAVINS 220
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
32-197 |
4.16e-14 |
|
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: 71.05 E-value: 4.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 32 GQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYMLSDAAPVALL 111
Cdd:cd05966 82 SRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCKLVI 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 112 TQSA---------LVETLD---SHLPTV--VLDARSP---------------SALDGAPDSNPdsrARGITSRHLAYVIY 162
Cdd:cd05966 162 TADGgyrggkvipLKEIVDealEKCPSVekVLVVKRTggevpmtegrdlwwhDLMAKQSPECE---PEWMDSEDPLFILY 238
|
170 180 190
....*....|....*....|....*....|....*
gi 2646261543 163 TSGSTGQPKGVMVEHANILRLLAATQDYFrFSHHD 197
Cdd:cd05966 239 TSGSTGKPKGVVHTTGGYLLYAATTFKYV-FDYHP 272
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
35-181 |
6.60e-14 |
|
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: 70.32 E-value: 6.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 35 LSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGaayLPLDPAYPAerlaymLSDAApvallTQS 114
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN---IPIVTVYAT------LGEDA-----LIH 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2646261543 115 ALVETLDSHLPTvvldarspsaldgapDSNPDSrargitsrhLAYVIYTSGSTGQPKGVMVEHANIL 181
Cdd:cd17639 72 SLNETECSAIFT---------------DGKPDD---------LACIMYTSGSTGNPKGVMLTHGNLV 114
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
31-228 |
7.56e-14 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 70.39 E-value: 7.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 31 AGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYMLSDAAPVAL 110
Cdd:PLN02246 47 TGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLI 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 111 LTQSALVETL-----DSHLPTVVLDARSPSALDGAPDSNPDS---RARGITSRHLAYVIYTSGSTGQPKGVMVEHANILR 182
Cdd:PLN02246 127 ITQSCYVDKLkglaeDDGVTVVTIDDPPEGCLHFSELTQADEnelPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVT 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2646261543 183 LLAATQD----YFRFSHHD----VWTLFHSFAFDfSVweLWGALAYGGRLVIVP 228
Cdd:PLN02246 207 SVAQQVDgenpNLYFHSDDvilcVLPMFHIYSLN-SV--LLCGLRVGAAILIMP 257
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
35-197 |
8.72e-14 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 69.97 E-value: 8.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 35 LSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYMLSDAAPVALLTQ- 113
Cdd:TIGR02188 89 ITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALADRINDAGAKLVITAd 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 114 --------SALVETLD---SHLPTVV--------LDARSPSALDG--------APDSNPDSRARGITSRHLAYVIYTSGS 166
Cdd:TIGR02188 169 eglrggkvIPLKAIVDealEKCPVSVehvlvvrrTGNPVVPWVEGrdvwwhdlMAKASAYCEPEPMDSEDPLFILYTSGS 248
|
170 180 190
....*....|....*....|....*....|.
gi 2646261543 167 TGQPKGVMVEHANILRLLAATQDYFrFSHHD 197
Cdd:TIGR02188 249 TGKPKGVLHTTGGYLLYAAMTMKYV-FDIKD 278
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
35-178 |
1.44e-13 |
|
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: 69.29 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 35 LSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYMLSDAAPVAlltqs 114
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKA----- 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2646261543 115 alvetldshlptVVLDARSPSALdgapdsnpdsrargitsrhlayvIYTSGSTGQPKGVMVEHA 178
Cdd:cd05972 76 ------------IVTDAEDPALI-----------------------YFTSGTTGLPKGVLHTHS 104
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
23-180 |
2.35e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 68.76 E-value: 2.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 23 PDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYML 102
Cdd:PRK06145 16 PDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYIL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 103 SDAAPVALLTQSALVETLDSHLPTVVLD--ARSPSALDGAPDSnPDSRARGITSRHLAYVIYTSGSTGQPKGVMVEHANI 180
Cdd:PRK06145 96 GDAGAKLLLVDEEFDAIVALETPKIVIDaaAQADSRRLAQGGL-EIPPQAAVAPTDLVRLMYTSGTTDRPKGVMHSYGNL 174
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
32-226 |
2.38e-13 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 68.53 E-value: 2.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 32 GQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYMLSDAAPVALl 111
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 112 tqsalvetldshlptvVLDArspsaldgapdsnpdsrargitsrhlAYVIYTSGSTGQPKGVMVEHANILRLLAATQDYF 191
Cdd:cd05940 80 ----------------VVDA--------------------------ALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSG 117
|
170 180 190
....*....|....*....|....*....|....*....
gi 2646261543 192 RFSHHDVW----TLFHSFAfdfSVWELWGALAYGGRLVI 226
Cdd:cd05940 118 GALPSDVLytclPLYHSTA---LIVGWSACLASGATLVI 153
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
10-195 |
5.53e-13 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 67.55 E-value: 5.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 10 LIHELFEQQAMLaPDAIAVVCA--GQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYL 87
Cdd:cd17642 19 QLHKAMKRYASV-PGTIAFTDAhtGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 88 PLDPAYPAERLAYMLSDAAP-VALLTQSAL--VETLDSHLPTV----VLDAR----------------SPSALDgAPDSN 144
Cdd:cd17642 98 PTNDIYNERELDHSLNISKPtIVFCSKKGLqkVLNVQKKLKIIktiiILDSKedykgyqclytfitqnLPPGFN-EYDFK 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2646261543 145 PDSRARgitSRHLAYVIYTSGSTGQPKGVMVEHANILrllaatqdyFRFSH 195
Cdd:cd17642 177 PPSFDR---DEQVALIMNSSGSTGLPKGVQLTHKNIV---------ARFSH 215
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
27-173 |
9.35e-13 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 67.03 E-value: 9.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 27 AVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYMLSDAA 106
Cdd:PRK12406 4 TIISGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 107 PVALLTQSALVETLDSHLPT--VVLDARSPSALDGAPDSNPDSRA------------------RGITSRHLAYVIYTSGS 166
Cdd:PRK12406 84 ARVLIAHADLLHGLASALPAgvTVLSVPTPPEIAAAYRISPALLTppagaidwegwlaqqepyDGPPVPQPQSMIYTSGT 163
|
....*..
gi 2646261543 167 TGQPKGV 173
Cdd:PRK12406 164 TGHPKGV 170
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
32-204 |
1.72e-12 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 66.29 E-value: 1.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 32 GQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYMLSDAAPVALL 111
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 112 T--QSALVETLDSHLPTvvldarspsaldgAPDSNPDSRargitsrhLAYvIYTSGSTGQPKGVMVEHANILRLLAATQD 189
Cdd:cd05939 81 FnlLDPLLTQSSTEPPS-------------QDDVNFRDK--------LFY-IYTSGTTGLPKAAVIVHSRYYRIAAGAYY 138
|
170
....*....|....*....
gi 2646261543 190 YFRFSHHDVW----TLFHS 204
Cdd:cd05939 139 AFGMRPEDVVydclPLYHS 157
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
16-203 |
1.89e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 66.12 E-value: 1.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 16 EQQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPA 95
Cdd:PRK08162 25 ERAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 96 ERLAYMLSDAAPVALLTQSALVET------LDSHLPTVVLDARSPSALDGAP-----------DSNPDSRARGITSRHLA 158
Cdd:PRK08162 105 ASIAFMLRHGEAKVLIVDTEFAEVarealaLLPGPKPLVIDVDDPEYPGGRFigaldyeaflaSGDPDFAWTLPADEWDA 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2646261543 159 YVI-YTSGSTGQPKGVMVEH--------ANILRllaatqdyFRFSHHDV--WTL--FH 203
Cdd:PRK08162 185 IALnYTSGTTGNPKGVVYHHrgaylnalSNILA--------WGMPKHPVylWTLpmFH 234
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
33-179 |
1.91e-12 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 65.95 E-value: 1.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 33 QSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYMLSDAAPVALlt 112
Cdd:cd05932 5 VEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKAL-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 113 qsaLVETLDSHLPTV-VLDARSPSALDGAPDSNPDSRA-RGITSRH-------------LAYVIYTSGSTGQPKGVMVEH 177
Cdd:cd05932 83 ---FVGKLDDWKAMApGVPEGLISISLPPPSAANCQYQwDDLIAQHppleerptrfpeqLATLIYTSGTTGQPKGVMLTF 159
|
..
gi 2646261543 178 AN 179
Cdd:cd05932 160 GS 161
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
33-173 |
2.11e-12 |
|
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: 66.18 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 33 QSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYMLSDAAPVALLT 112
Cdd:cd05967 81 RTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKLIVT 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 113 QSALVE---------------TLDSHLPTVVL----DARSPSALDGAPDSNPDSRARGITSR--------HLAYVIYTSG 165
Cdd:cd05967 161 ASCGIEpgkvvpykplldkalELSGHKPHHVLvlnrPQVPADLTKPGRDLDWSELLAKAEPVdcvpvaatDPLYILYTSG 240
|
....*...
gi 2646261543 166 STGQPKGV 173
Cdd:cd05967 241 TTGKPKGV 248
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
17-177 |
2.39e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 65.83 E-value: 2.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 17 QQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAE 96
Cdd:PRK07470 15 QAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 97 RLAYMLSDAAPVALLTQS------ALVETLDSHLPTVVLDARSPSALD--GAPDSNPDSRARGITSRH--LAYVIYTSGS 166
Cdd:PRK07470 95 EVAYLAEASGARAMICHAdfpehaAAVRAASPDLTHVVAIGGARAGLDyeALVARHLGARVANAAVDHddPCWFFFTSGT 174
|
170
....*....|.
gi 2646261543 167 TGQPKGVMVEH 177
Cdd:PRK07470 175 TGRPKAAVLTH 185
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
34-183 |
5.84e-12 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 64.78 E-value: 5.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 34 SLSYGELNRRANRLAH-HLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYMLSDAAPvALLT 112
Cdd:cd17632 67 TITYAELWERVGAVAAaHDPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEP-RLLA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 113 QS------ALVETLDSHLPT--VVLDARSP-----SALDGA---------------------PDSNPDSRARGITSRH-L 157
Cdd:cd17632 146 VSaehldlAVEAVLEGGTPPrlVVFDHRPEvdahrAALESArerlaavgipvttltliavrgRDLPPAPLFRPEPDDDpL 225
|
170 180
....*....|....*....|....*.
gi 2646261543 158 AYVIYTSGSTGQPKGVMVEHANILRL 183
Cdd:cd17632 226 ALLIYTSGSTGTPKGAMYTERLVATF 251
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
6-229 |
6.84e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 64.38 E-value: 6.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 6 PQEALIHELFEQQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAA 85
Cdd:PRK06164 7 PRADTLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGAT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 86 YLPLDPAYPAERLAYMLSDAAPVALLTQSA-----LVETLDSHLPTVVLDARSPSALDGAPDSNPDsRARGITSRH---- 156
Cdd:PRK06164 87 VIAVNTRYRSHEVAHILGRGRARWLVVWPGfkgidFAAILAAVPPDALPPLRAIAVVDDAADATPA-PAPGARVQLfalp 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 157 -----------------LAYVIYTSGSTGQPKGVMVEHANILRLLAATQDYFRFSHHDVWTLFHSFAFDFSVWELWGALA 219
Cdd:PRK06164 166 dpappaaageraadpdaGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALA 245
|
250
....*....|
gi 2646261543 220 YGGRLVIVPA 229
Cdd:PRK06164 246 GGAPLVCEPV 255
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
35-186 |
7.73e-12 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 64.37 E-value: 7.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 35 LSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYMLSDAAPVALLTQS 114
Cdd:PLN02387 107 ITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDS 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 115 ALVETL---DSHLPTV----VLDARSPSALDGAPDS-----------------NPdSRARGITSRHLAYVIYTSGSTGQP 170
Cdd:PLN02387 187 KQLKKLidiSSQLETVkrviYMDDEGVDSDSSLSGSsnwtvssfseveklgkeNP-VDPDLPSPNDIAVIMYTSGSTGLP 265
|
170
....*....|....*.
gi 2646261543 171 KGVMVEHANILRLLAA 186
Cdd:PLN02387 266 KGVMMTHGNIVATVAG 281
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
3-192 |
1.06e-11 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 63.87 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 3 TDFPQEALihELFEQQAMLAPDAIAVV-CAGQS-LSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGIL 80
Cdd:PRK05857 10 PQLPSTVL--DRVFEQARQQPEAIALRrCDGTSaLRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 81 KAGAAYLPLDPAYPAERLAYMLSDAAPVALLT-------QSALVETLDShLPTVVLDARSPSALDGA------PDSNPDS 147
Cdd:PRK05857 88 KLGAIAVMADGNLPIAAIERFCQITDPAAALVapgskmaSSAVPEALHS-IPVIAVDIAAVTRESEHsldaasLAGNADQ 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2646261543 148 RArgitSRHLAyVIYTSGSTGQPKGVMVEHanilRLLAATQDYFR 192
Cdd:PRK05857 167 GS----EDPLA-MIFTSGTTGEPKAVLLAN----RTFFAVPDILQ 202
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
1-187 |
1.13e-11 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 63.84 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 1 PQTDFPQEALIHELFEQQAMLAPDAIAVVCA--GQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLG 78
Cdd:PLN02330 20 PSVPVPDKLTLPDFVLQDAELYADKVAFVEAvtGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 79 ILKAGAAYLPLDPAYPAERLAYMLSDAAPVALLTQSALVETLDS-HLPTVVLDARSPSA-------LDGAPDSNPDSRAR 150
Cdd:PLN02330 100 IMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVKGlGLPVIVLGEEKIEGavnwkelLEAADRAGDTSDNE 179
|
170 180 190
....*....|....*....|....*....|....*..
gi 2646261543 151 GITSRHLAYVIYTSGSTGQPKGVMVEHANILRLLAAT 187
Cdd:PLN02330 180 EILQTDLCALPFSSGTTGISKGVMLTHRNLVANLCSS 216
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
34-203 |
1.78e-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: 63.13 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 34 SLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYMLSDAApvalltq 113
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSD------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 114 salvetldshlptVVLDArspsaldgapdsnpdsrargitsrhLAYVIYTSGSTGQPKGVMVEHANILRLLAATQDYFRF 193
Cdd:cd05912 74 -------------VKLDD-------------------------IATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGL 115
|
170
....*....|....
gi 2646261543 194 SHHDVW----TLFH 203
Cdd:cd05912 116 TEDDNWlcalPLFH 129
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
23-177 |
1.81e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 63.08 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 23 PDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYML 102
Cdd:PRK06188 26 PDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 103 SDAAPVALLTQS--------ALVETLDShLPTVVLDARSPSALD--GAPDSNPDSRAR-GITSRHLAYVIYTSGSTGQPK 171
Cdd:PRK06188 106 EDAGISTLIVDPapfveralALLARVPS-LKHVLTLGPVPDGVDllAAAAKFGPAPLVaAALPPDIAGLAYTGGTTGKPK 184
|
....*.
gi 2646261543 172 GVMVEH 177
Cdd:PRK06188 185 GVMGTH 190
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
36-230 |
2.13e-11 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 62.85 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 36 SYGELNRRANRLAHHLLTLGVQPDDRVAIC---VERSPEMVVGLLGIlkaGAAYLPLDPAYPAERLAYMLSDAAPVAL-- 110
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIawnTWRHLEAWYGIMGI---GAICHTVNPRLFPEQIAWIINHAEDRVVit 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 111 -LTQSALVETLDSHLPTV----VL--DARSP-SALDGA-------PDSNPDSRARGITSRHLAYVIYTSGSTGQPKGVMV 175
Cdd:PRK06018 118 dLTFVPILEKIADKLPSVeryvVLtdAAHMPqTTLKNAvayeewiAEADGDFAWKTFDENTAAGMCYTSGTTGDPKGVLY 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2646261543 176 EH-ANILRLLAATQ-DYFRFSHHD----VWTLFHSFAfdfsvwelWG----ALAYGGRLVIvPAA 230
Cdd:PRK06018 198 SHrSNVLHALMANNgDALGTSAADtmlpVVPLFHANS--------WGiafsAPSMGTKLVM-PGA 253
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
7-181 |
3.55e-11 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 62.35 E-value: 3.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 7 QEALIHELFEQQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAY 86
Cdd:PRK07059 21 QYPSLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 87 LPLDPAYPAERLAYMLSDAAPVALLTQSALVETLDSHLPT-----VVLDA----------------RS------PSALDG 139
Cdd:PRK07059 101 VNVNPLYTPRELEHQLKDSGAEAIVVLENFATTVQQVLAKtavkhVVVASmgdllgfkghivnfvvRRvkkmvpAWSLPG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2646261543 140 APDSNpDSRARG---------ITSRHLAYVIYTSGSTGQPKGVMVEHANIL 181
Cdd:PRK07059 181 HVRFN-DALAEGarqtfkpvkLGPDDVAFLQYTGGTTGVSKGATLLHRNIV 230
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
19-185 |
3.60e-11 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 62.51 E-value: 3.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 19 AMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERL 98
Cdd:PLN02860 17 ATLRGNAVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 99 AYMLSDAAPVALLTQSALV----ETLDSHLPT----VVLDARSPSALDGAPDS-NPD-SRARGITSRHLAY--------- 159
Cdd:PLN02860 97 KSAMLLVRPVMLVTDETCSswyeELQNDRLPSlmwqVFLESPSSSVFIFLNSFlTTEmLKQRALGTTELDYawapddavl 176
|
170 180
....*....|....*....|....*..
gi 2646261543 160 VIYTSGSTGQPKGVMVEH-ANILRLLA 185
Cdd:PLN02860 177 ICFTSGTTGRPKGVTISHsALIVQSLA 203
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
24-228 |
1.39e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 60.43 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 24 DAIAVVCAGQSLSYGELNRRANRLAHHLLTLGvQPDDR--VAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYM 101
Cdd:PRK13388 16 DTIAVRYGDRTWTWREVLAEAAARAAALIALA-DPDRPlhVGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAAD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 102 LSDAAPVALLTQSALVETLDS-HLPTV-VLDARSPS---ALDGAPDSNPdsrARGITSRHLAYVIYTSGSTGQPKGVMVE 176
Cdd:PRK13388 95 IRRADCQLLVTDAEHRPLLDGlDLPGVrVLDVDTPAyaeLVAAAGALTP---HREVDAMDPFMLIFTSGTTGAPKAVRCS 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2646261543 177 HANILRLLAATQDYFRFSHHDV----WTLFHSFAfdfsVWELWG-ALAYGGRLVIVP 228
Cdd:PRK13388 172 HGRLAFAGRALTERFGLTRDDVcyvsMPLFHSNA----VMAGWApAVASGAAVALPA 224
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
25-181 |
1.66e-10 |
|
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: 60.18 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 25 AIAVVCAGQSLSYGELNRRANRLAHHLL-TLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYMLS 103
Cdd:cd05958 1 RTCLRSPEREWTYRDLLALANRIANVLVgELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2646261543 104 DAAPvalltqsalvetldshlpTVVLDARSPSALDgapdsnpdsrargitsrHLAYVIYTSGSTGQPKGVMVEHANIL 181
Cdd:cd05958 81 KARI------------------TVALCAHALTASD-----------------DICILAFTSGTTGAPKATMHFHRDPL 123
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
22-181 |
1.81e-10 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 60.36 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 22 APDAIAVVCAG----QSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAER 97
Cdd:cd05943 82 ADDPAAIYAAEdgerTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPG 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 98 LAYMLSDAAPVALLTQSA----------------LVETLDSHLPTVVLDARSPSALDGAPDSNPDSRARGITSR------ 155
Cdd:cd05943 162 VLDRFGQIEPKVLFAVDAytyngkrhdvrekvaeLVKGLPSLLAVVVVPYTVAAGQPDLSKIAKALTLEDFLATgaagel 241
|
170 180 190
....*....|....*....|....*....|....
gi 2646261543 156 --------HLAYVIYTSGSTGQPKGVMVEHANIL 181
Cdd:cd05943 242 efeplpfdHPLYILYSSGTTGLPKCIVHGAGGTL 275
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
32-207 |
2.23e-10 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 59.75 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 32 GQSLSYGELNRRANRLAHHLL-TLGVQPDDRVAICVERSPEMVVGLLGILKAGAAylpldPAYpaerLAYMLSDAapval 110
Cdd:cd05937 3 GKTWTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAA-----PAF----INYNLSGD----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 111 ltqsALVETLD-SHLPTVVLDARSPSALdgapdsnpdsrargitsrhlayvIYTSGSTGQPKGVMVEHANILRLLAATQD 189
Cdd:cd05937 69 ----PLIHCLKlSGSRFVIVDPDDPAIL-----------------------IYTSGTTGLPKAAAISWRRTLVTSNLLSH 121
|
170 180
....*....|....*....|..
gi 2646261543 190 YFRFSHHDVW----TLFHSFAF 207
Cdd:cd05937 122 DLNLKNGDRTytcmPLYHGTAA 143
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
157-228 |
2.61e-10 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 59.94 E-value: 2.61e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2646261543 157 LAYVIYTSGSTGQPKGVMVEHANILRLLAATQDYFRFSHHDV----WTLFHSFAFdfsVWELWGALAYGGRLVIVP 228
Cdd:PRK08633 784 TATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVilssLPFFHSFGL---TVTLWLPLLEGIKVVYHP 856
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
36-225 |
3.43e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 59.33 E-value: 3.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 36 SYGELNRRANRLAHHLLTLGVQPDDRVAICV---ERSPEMVVGLLGilkAGAAYLPLDPAYPAERLAYMLSDAAPVAL-- 110
Cdd:PRK07008 41 TYRDCERRAKQLAQALAALGVEPGDRVGTLAwngYRHLEAYYGVSG---SGAVCHTINPRLFPEQIAYIVNHAEDRYVlf 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 111 -LTQSALVETLDSHLPTV---VL---DARSPS---------ALDGAPDSNPDSRArgITSRHLAYVIYTSGSTGQPKGVM 174
Cdd:PRK07008 118 dLTFLPLVDALAPQCPNVkgwVAmtdAAHLPAgstpllcyeTLVGAQDGDYDWPR--FDENQASSLCYTSGTTGNPKGAL 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2646261543 175 VEH-ANILRLLAAT-QDYFRFSHHD----VWTLFHSFAfdfsvwelWGaLAY-----GGRLV 225
Cdd:PRK07008 196 YSHrSTVLHAYGAAlPDAMGLSARDavlpVVPMFHVNA--------WG-LPYsapltGAKLV 248
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
22-183 |
4.54e-10 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 59.04 E-value: 4.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 22 APDAIAVVCAG-----QSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAE 96
Cdd:PRK03584 97 RDDRPAIIFRGedgprRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPDFGVQ 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 97 RLAYMLSDAAPVALLTQ----------------SALVETLDSHLPTVVLD----ARSPSALDGA---PDSNPDSRARGIT 153
Cdd:PRK03584 177 GVLDRFGQIEPKVLIAVdgyryggkafdrrakvAELRAALPSLEHVVVVPylgpAAAAAALPGAllwEDFLAPAEAAELE 256
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2646261543 154 SRHLA-----YVIYTSGSTGQPK-------GVMVEHANILRL 183
Cdd:PRK03584 257 FEPVPfdhplWILYSSGTTGLPKcivhghgGILLEHLKELGL 298
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
16-180 |
6.12e-10 |
|
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: 58.60 E-value: 6.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 16 EQQAMLAPDAIAVVCAG-----QSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLD 90
Cdd:cd05921 2 AHWARQAPDRTWLAEREgnggwRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 91 PAYPA-----ERLAYMLSDAAPVALLTQS------ALVETLDSHLPTVVL-------DARSPSALDGAPDSNPDSRARG- 151
Cdd:cd05921 82 PAYSLmsqdlAKLKHLFELLKPGLVFAQDaapfarALAAIFPLGTPLVVSrnavagrGAISFAELAATPPTAAVDAAFAa 161
|
170 180
....*....|....*....|....*....
gi 2646261543 152 ITSRHLAYVIYTSGSTGQPKGVMVEHANI 180
Cdd:cd05921 162 VGPDTVAKFLFTSGSTGLPKAVINTQRML 190
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
32-212 |
6.81e-10 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 58.50 E-value: 6.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 32 GQSLSYGELNRRANRLAHhLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYMLSDAAPVALL 111
Cdd:cd05909 5 GTSLTYRKLLTGAIALAR-KLAKMTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 112 TQSALVETLDSH-LPTVVLDAR---------SPSALDG--------APDSNPDSRA--RGITSRHLAYVIYTSGSTGQPK 171
Cdd:cd05909 84 TSKQFIEKLKLHhLFDVEYDARivyledlraKISKADKckaflagkFPPKWLLRIFgvAPVQPDDPAVILFTSGSEGLPK 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2646261543 172 GVMVEHANILRLLAATQDYFRFSHHDVWT----LFHSFAFDFSVW 212
Cdd:cd05909 164 GVVLSHKNLLANVEQITAIFDPNPEDVVFgalpFFHSFGLTGCLW 208
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
18-173 |
1.01e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 58.10 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 18 QAMLAPDAIAVVCA--GQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPA 95
Cdd:PRK13390 6 HAQIAPDRPAVIVAetGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 96 ERLAYMLSDAAPVALLTQSAlvetldshLPTVVLDARSPSAL--------DGAPDSNPDSRARG--ITSRHL-AYVIYTS 164
Cdd:PRK13390 86 PEADYIVGDSGARVLVASAA--------LDGLAAKVGADLPLrlsfggeiDGFGSFEAALAGAGprLTEQPCgAVMLYSS 157
|
....*....
gi 2646261543 165 GSTGQPKGV 173
Cdd:PRK13390 158 GTTGFPKGI 166
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
33-198 |
1.29e-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: 341236 [Multi-domain] Cd Length: 457 Bit Score: 57.47 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 33 QSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYMLSDAAPVALLt 112
Cdd:cd05910 1 SRLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFI- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 113 qsalvetldshlptvvldarspsaldGAPDSNPDsrargitsrhlAYVIYTSGSTGQPKGVMVEHANILRLLAATQDYFR 192
Cdd:cd05910 80 --------------------------GIPKADEP-----------AAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYG 122
|
....*.
gi 2646261543 193 FSHHDV 198
Cdd:cd05910 123 IRPGEV 128
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
33-186 |
1.56e-09 |
|
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: 57.43 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 33 QSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYMLSDAAPVALLT 112
Cdd:cd17641 10 QEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 113 ----QSALVETLDSHLPTV------------------VLDARSPSALDGAPDS-NPDSRARGITSRH---LAYVIYTSGS 166
Cdd:cd17641 90 edeeQVDKLLEIADRIPSVryviycdprgmrkyddprLISFEDVVALGRALDRrDPGLYEREVAAGKgedVAVLCTTSGT 169
|
170 180
....*....|....*....|
gi 2646261543 167 TGQPKGVMVEHANILRLLAA 186
Cdd:cd17641 170 TGKPKLAMLSHGNFLGHCAA 189
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
13-206 |
2.09e-09 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 56.99 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 13 ELFEQQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLT-LGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDP 91
Cdd:PRK08974 27 DMFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQNgLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 92 AYPAERLAYMLSDAAPVALLTQSALVETLD-----SHLPTVVL----DARS-----------------------PSALdg 139
Cdd:PRK08974 107 LYTPRELEHQLNDSGAKAIVIVSNFAHTLEkvvfkTPVKHVILtrmgDQLStakgtlvnfvvkyikrlvpkyhlPDAI-- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 140 apdSNPDSRARG---------ITSRHLAYVIYTSGSTGQPKGVMVEH----ANILRLLAATQDYFRFSHHDVWT---LFH 203
Cdd:PRK08974 185 ---SFRSALHKGrrmqyvkpeLVPEDLAFLQYTGGTTGVAKGAMLTHrnmlANLEQAKAAYGPLLHPGKELVVTalpLYH 261
|
...
gi 2646261543 204 SFA 206
Cdd:PRK08974 262 IFA 264
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
4-181 |
3.93e-09 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 56.42 E-value: 3.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 4 DFPQEALIHELFEQQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLL-TLGVQPDDRVAICVERSPEMVVGLLGILKA 82
Cdd:PRK08751 20 DLEQFRTVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLgELQLKKGDRVALMMPNCLQYPIATFGVLRA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 83 GAAYLPLDPAYPAERLAYMLSDAAPVALLT--------------------------------QSALVETLDSHLPTVVLD 130
Cdd:PRK08751 100 GLTVVNVNPLYTPRELKHQLIDSGASVLVVidnfgttvqqviadtpvkqvittglgdmlgfpKAALVNFVVKYVKKLVPE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2646261543 131 ARSPSALD-------GAPDSNPdsrARGITSRHLAYVIYTSGSTGQPKGVMVEHANIL 181
Cdd:PRK08751 180 YRINGAIRfrealalGRKHSMP---TLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLV 234
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
11-228 |
4.54e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 55.94 E-value: 4.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 11 IHELFEQQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDdRVAICVERSPEMVVGLLGILKAGAAYLPLD 90
Cdd:PRK07638 3 ITKEYKKHASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNK-TIAILLENRIEFLQLFAGAAMAGWTCVPLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 91 PAYPAERLAYMLSDAAPVALLTQSALVETL-DSHLPTVVLDARSPSALDGAPDSNPdsrarGITSRHLA-YVIYTSGSTG 168
Cdd:PRK07638 82 IKWKQDELKERLAISNADMIVTERYKLNDLpDEEGRVIEIDEWKRMIEKYLPTYAP-----IENVQNAPfYMGFTSGSTG 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2646261543 169 QPKGVMVEHANILRLLAATQDYFRFSHHD----VWTLFHSFaFdfsvweLWGA---LAYGGRLVIVP 228
Cdd:PRK07638 157 KPKAFLRAQQSWLHSFDCNVHDFHMKREDsvliAGTLVHSL-F------LYGAistLYVGQTVHLMR 216
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
22-171 |
6.40e-09 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 55.77 E-value: 6.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 22 APDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAylPLDPAYPAERL--- 98
Cdd:PRK10946 36 ASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVA--PVNALFSHQRSeln 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 99 AY--------MLSDAAPvALLTQSALVETLDSHLPT--VVLDARSPSALDGA---PDSNPDSRARGITSRHLAYVIYTSG 165
Cdd:PRK10946 114 AYasqiepalLIADRQH-ALFSDDDFLNTLVAEHSSlrVVLLLNDDGEHSLDdaiNHPAEDFTATPSPADEVAFFQLSGG 192
|
....*.
gi 2646261543 166 STGQPK 171
Cdd:PRK10946 193 STGTPK 198
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
33-205 |
1.12e-08 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 54.95 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 33 QSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYMLSDAAPVALLT 112
Cdd:PRK10524 83 RTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARIDDAKPVLIVS 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 113 QSA------------LVE---TLDSHLPTVVL---------DARSPSALDGAPDsnpdsRARG---------ITSRHLAY 159
Cdd:PRK10524 163 ADAgsrggkvvpykpLLDeaiALAQHKPRHVLlvdrglapmARVAGRDVDYATL-----RAQHlgarvpvewLESNEPSY 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2646261543 160 VIYTSGSTGQPKGVMVEHANILRLLAATQDYF--------RFSHHDV-WTLFHSF 205
Cdd:PRK10524 238 ILYTSGTTGKPKGVQRDTGGYAVALATSMDTIfggkagetFFCASDIgWVVGHSY 292
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
35-174 |
1.87e-08 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 54.38 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 35 LSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYMLSDAAPVALLT-- 112
Cdd:PRK00174 99 ITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVFGGFSAEALADRIIDAGAKLVITad 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 113 -------QSALVETLD---SHLPTV--VL------------DARS---PSALDGAPDSNPdsrARGITSRHLAYVIYTSG 165
Cdd:PRK00174 179 egvrggkPIPLKANVDealANCPSVekVIvvrrtggdvdwvEGRDlwwHELVAGASDECE---PEPMDAEDPLFILYTSG 255
|
....*....
gi 2646261543 166 STGQPKGVM 174
Cdd:PRK00174 256 STGKPKGVL 264
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
33-200 |
2.06e-08 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 54.29 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 33 QSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYMLSDAAPVALL- 111
Cdd:cd05933 7 HTLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVv 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 112 ---TQSALVETLDSHLPTV--VLDARSP---------------SALDGAPDSNPDSRARGITSRHLAYVIYTSGSTGQPK 171
Cdd:cd05933 87 enqKQLQKILQIQDKLPHLkaIIQYKEPlkekepnlyswdefmELGRSIPDEQLDAIISSQKPNQCCTLIYTSGTTGMPK 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2646261543 172 GVMVEHANI----------LRLLAATQ------DYFRFSH-----HDVWT 200
Cdd:cd05933 167 GVMLSHDNItwtakaasqhMDLRPATVgqesvvSYLPLSHiaaqiLDIWL 216
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
34-205 |
2.35e-08 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 54.13 E-value: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 34 SLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYMLSDAAPVALLTQ 113
Cdd:PLN02654 120 SLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVITC 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 114 SALVETLDS-HLPTVVLDARSPSALDG---------------------------------APDSNPDSRARGITSRHLAY 159
Cdd:PLN02654 200 NAVKRGPKTiNLKDIVDAALDESAKNGvsvgicltyenqlamkredtkwqegrdvwwqdvVPNYPTKCEVEWVDAEDPLF 279
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2646261543 160 VIYTSGSTGQPKGVMVEHANILRLLAATQDY-FRFSHHDV--------WTLFHSF 205
Cdd:PLN02654 280 LLYTSGSTGKPKGVLHTTGGYMVYTATTFKYaFDYKPTDVywctadcgWITGHSY 334
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
35-198 |
2.81e-08 |
|
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: 53.76 E-value: 2.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 35 LSYGELNRRANRLAHHLLTLGV--QPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYMLSDA------- 105
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAeisivfc 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 106 -APVALLTQSALVETLDSHLPTVVLdarspsaldGAPDsnpdsrargitsrHLAYVIYTSGSTGQPKGVMVEHANILRLL 184
Cdd:cd05927 86 dAGVKVYSLEEFEKLGKKNKVPPPP---------PKPE-------------DLATICYTSGTTGNPKGVMLTHGNIVSNV 143
|
170
....*....|....*...
gi 2646261543 185 AA----TQDYFRFSHHDV 198
Cdd:cd05927 144 AGvfkiLEILNKINPTDV 161
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
11-181 |
5.46e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 52.84 E-value: 5.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 11 IHELFEQQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLTL-GVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPL 89
Cdd:PRK05677 26 IQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 90 DPAYPAERLAYMLSDAAPVALLTQSALVETLDSHLP---------TVVLDARSP--SALDGA----------PDSNPD-- 146
Cdd:PRK05677 106 NPLYTAREMEHQFNDSGAKALVCLANMAHLAEKVLPktgvkhvivTEVADMLPPlkRLLINAvvkhvkkmvpAYHLPQav 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2646261543 147 ------SRARGITSRH-------LAYVIYTSGSTGQPKGVMVEHANIL 181
Cdd:PRK05677 186 kfndalAKGAGQPVTEanpqaddVAVLQYTGGTTGVAKGAMLTHRNLV 233
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
24-226 |
8.26e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 52.38 E-value: 8.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 24 DAIAVVCAGQSLSYGELNRRANRLAHHLLTLgvQPDDR---VAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAY 100
Cdd:PRK07867 18 DDRGLYFEDSFTSWREHIRGSAARAAALRAR--LDPTRpphVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALAR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 101 MLSDAAPVALLTQSALVETLDSHLPTV-VLDARSP---SALDGAPDSNPDsrARGITSRHLAYVIYTSGSTGQPKGVMVE 176
Cdd:PRK07867 96 DIAHADCQLVLTESAHAELLDGLDPGVrVINVDSPawaDELAAHRDAEPP--FRVADPDDLFMLIFTSGTSGDPKAVRCT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2646261543 177 HANILRLLAATQDYFRFSHHDV----WTLFHSFAF--DFSVwelwgALAYGGRLVI 226
Cdd:PRK07867 174 HRKVASAGVMLAQRFGLGPDDVcyvsMPLFHSNAVmaGWAV-----ALAAGASIAL 224
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
19-232 |
3.91e-07 |
|
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: 50.07 E-value: 3.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 19 AMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPaERL 98
Cdd:cd05929 2 EARDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAP-RAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 99 AYMLSDAAPVALLtqsALVETLDSHLPTVVLDARspsALDGAPDSNPDSRARGitsrhlAYVIYTSGSTGQPKGVMVEH- 177
Cdd:cd05929 81 ACAIIEIKAAALV---CGLFTGGGALDGLEDYEA---AEGGSPETPIEDEAAG------WKMLYSGGTTGRPKGIKRGLp 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2646261543 178 ----ANILRLLAATQDYFRF--SHHDVWTLFHSFAFDFSVwelwGALAYGGRLVIVPAACA 232
Cdd:cd05929 149 ggppDNDTLMAAALGFGPGAdsVYLSPAPLYHAAPFRWSM----TALFMGGTLVLMEKFDP 205
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
23-227 |
5.28e-07 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 50.02 E-value: 5.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 23 PDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYML 102
Cdd:PLN03102 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 103 SDAAPVALLTQSA----------LVETLDS--HLPTVVLD----ARSPSALD---------GAPDSNPDSRARGITSRHL 157
Cdd:PLN03102 108 RHAKPKILFVDRSfeplarevlhLLSSEDSnlNLPVIFIHeidfPKRPSSEEldyecliqrGEPTPSLVARMFRIQDEHD 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2646261543 158 AYVI-YTSGSTGQPKGVMVEH--ANILRLLAATQDYFRFSHHDVWTL--FHSFAFDFSvwelWGALAYGGRLVIV 227
Cdd:PLN03102 188 PISLnYTSGTTADPKGVVISHrgAYLSTLSAIIGWEMGTCPVYLWTLpmFHCNGWTFT----WGTAARGGTSVCM 258
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
34-181 |
5.68e-07 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 49.65 E-value: 5.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 34 SLSYGELNRRANRLAHHLLT-LGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYML----SDAAPV 108
Cdd:cd05905 14 TLTWGKLLSRAEKIAAVLQKkVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLgtckVRVALT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 109 ALLTQSALVETLDSHLPTVVLDARS--PSALD--GAPDSNP----DSRARGITSRH-LAYVIYTSGSTGQPKGVMVEHAN 179
Cdd:cd05905 94 VEACLKGLPKKLLKSKTAAEIAKKKgwPKILDfvKIPKSKRsklkKWGPHPPTRDGdTAYIEYSFSSDGSLSGVAVSHSS 173
|
..
gi 2646261543 180 IL 181
Cdd:cd05905 174 LL 175
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
13-181 |
7.47e-07 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 49.44 E-value: 7.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 13 ELFEQQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLT-LGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDP 91
Cdd:PRK12492 28 EVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQhTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 92 AYPAERLAYMLSDAAPVALL--------------------------------TQSALVETLDSHLPTVVLDARSP----- 134
Cdd:PRK12492 108 LYTAREMRHQFKDSGARALVylnmfgklvqevlpdtgieylieakmgdllpaAKGWLVNTVVDKVKKMVPAYHLPqavpf 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2646261543 135 -SALDGAPDSNPDSRARGITSrhLAYVIYTSGSTGQPKGVMVEHANIL 181
Cdd:PRK12492 188 kQALRQGRGLSLKPVPVGLDD--IAVLQYTGGTTGLAKGAMLTHGNLV 233
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
23-179 |
2.76e-06 |
|
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: 47.88 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 23 PDAIAVV-C--AGQS--LSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAER 97
Cdd:cd05970 31 PDKLALVwCddAGEEriFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 98 LAYMLSDA--APVALLTQSALVETLDSHLPTVVLDAR----SPSALDG-----------APDSNPDSRARGITSRHLAYV 160
Cdd:cd05970 111 IVYRIESAdiKMIVAIAEDNIPEEIEKAAPECPSKPKlvwvGDPVPEGwidfrkliknaSPDFERPTANSYPCGEDILLV 190
|
170
....*....|....*....
gi 2646261543 161 IYTSGSTGQPKgvMVEHAN 179
Cdd:cd05970 191 YFSSGTTGMPK--MVEHDF 207
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
33-180 |
3.39e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 47.66 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 33 QSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGI----LKAGAAYLPLDpaypAERLAYMLSDAAPV 108
Cdd:PTZ00216 120 RYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIwsqsMVAATVYANLG----EDALAYALRETECK 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 109 ALLTQSALVETLDS--------HLPTVVLD--------------------ARSPSALDGAPDSNPDSRARgitsrhLAYV 160
Cdd:PTZ00216 196 AIVCNGKNVPNLLRlmksggmpNTTIIYLDslpasvdtegcrlvawtdvvAKGHSAGSHHPLNIPENNDD------LALI 269
|
170 180
....*....|....*....|
gi 2646261543 161 IYTSGSTGQPKGVMVEHANI 180
Cdd:PTZ00216 270 MYTSGTTGDPKGVMHTHGSL 289
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
36-203 |
4.83e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 46.91 E-value: 4.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 36 SYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYMLSDAAPVALLTQSA 115
Cdd:PRK07768 31 TWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTPRTDLAVWAEDTLRVIGMIGAK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 116 LV----------ETLDSHLPTVVLDArspSALDGAPDSNPDsrargITSRHLAYVIYTSGSTGQPKGVMVEHANILRLLA 185
Cdd:PRK07768 111 AVvvgepflaaaPVLEEKGIRVLTVA---DLLAADPIDPVE-----TGEDDLALMQLTSGSTGSPKAVQITHGNLYANAE 182
|
170 180
....*....|....*....|...
gi 2646261543 186 ATQDYFRFS-HHDV---W-TLFH 203
Cdd:PRK07768 183 AMFVAAEFDvETDVmvsWlPLFH 205
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
23-173 |
6.45e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 46.53 E-value: 6.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 23 PDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAYPAERLAYML 102
Cdd:PRK13383 49 PGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAAL 128
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2646261543 103 SDAAPVALLTQSALVETLDSHLPTV-VLDARSPSALD--GAPDSNPDSRArgitsrhlayVIYTSGSTGQPKGV 173
Cdd:PRK13383 129 RAHHISTVVADNEFAERIAGADDAVaVIDPATAGAEEsgGRPAVAAPGRI----------VLLTSGTTGKPKGV 192
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
35-198 |
6.95e-06 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 46.63 E-value: 6.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 35 LSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVgllgILKAGAAY----LPLDPAYPAERLAYMLSDAAPVAL 110
Cdd:PLN02736 79 MTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLI----VDHACSAYsyvsVPLYDTLGPDAVKFIVNHAEVAAI 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 111 LTQSALVETLDSHL---PTV---VLDARSPSALDGAPDSN-----PDSR--ARGITSRH---------LAYVIYTSGSTG 168
Cdd:PLN02736 155 FCVPQTLNTLLSCLseiPSVrliVVVGGADEPLPSLPSGTgveivTYSKllAQGRSSPQpfrppkpedVATICYTSGTTG 234
|
170 180 190
....*....|....*....|....*....|
gi 2646261543 169 QPKGVMVEHANILRLLAATQDYFRFSHHDV 198
Cdd:PLN02736 235 TPKGVVLTHGNLIANVAGSSLSTKFYPSDV 264
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
6-193 |
9.70e-06 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 45.99 E-value: 9.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 6 PQEALIHELFEQQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLL-TLGVQPDDRVAICVERSPEMVVGLLGILKAGA 84
Cdd:PLN02574 38 PNLDAVSFIFSHHNHNGDTALIDSSTGFSISYSELQPLVKSMAAGLYhVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 85 AYLPLDPAYPAERLAYMLSDAAPVALLTQSALVETLDSHLPTVVLDARSPSALDGAPD---------SNPDSRARGITSR 155
Cdd:PLN02574 118 IVTTMNPSSSLGEIKKRVVDCSVGLAFTSPENVEKLSPLGVPVIGVPENYDFDSKRIEfpkfyelikEDFDFVPKPVIKQ 197
|
170 180 190
....*....|....*....|....*....|....*....
gi 2646261543 156 H-LAYVIYTSGSTGQPKGVMVEHANilrLLAATQDYFRF 193
Cdd:PLN02574 198 DdVAAIMYSSGTTGASKGVVLTHRN---LIAMVELFVRF 233
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
14-172 |
1.17e-05 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 45.90 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 14 LFEQQAMLAPDAIAVVCAGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPLDPAY 93
Cdd:PRK13382 48 GFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSF 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 94 PAERLAYMLSDAAPVALLTQSALVETLDshlptvvldarspSALDGAPDSN-----PDSRARGI---------------T 153
Cdd:PRK13382 128 AGPALAEVVTREGVDTVIYDEEFSATVD-------------RALADCPQATrivawTDEDHDLTvevliaahagqrpepT 194
|
170
....*....|....*....
gi 2646261543 154 SRHLAYVIYTSGSTGQPKG 172
Cdd:PRK13382 195 GRKGRVILLTSGTTGTPKG 213
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
12-238 |
1.26e-05 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 45.72 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 12 HELFEQQAMLAPDAIAVVC--------AGQSLSYGELNRRANRLAHHLLTLGVQPDDRVAICVERSPEMVVGLLGILKAG 83
Cdd:PRK07529 28 YELLSRAAARHPDAPALSFlldadpldRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 84 AAYlPLDPAYPAERLAYMLSDAAPVALLTQSAL--------VETLDSHLPTV-------------------VLDARSP-- 134
Cdd:PRK07529 108 IAN-PINPLLEPEQIAELLRAAGAKVLVTLGPFpgtdiwqkVAEVLAALPELrtvvevdlarylpgpkrlaVPLIRRKah 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 135 -------SALDGAPDSNPDSrARGITSRHLAYVIYTSGSTGQPKGVMVEHAN-------ILRLLAATQDYFRFSHhdvWT 200
Cdd:PRK07529 187 arildfdAELARQPGDRLFS-GRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNevanawlGALLLGLGPGDTVFCG---LP 262
|
250 260 270
....*....|....*....|....*....|....*...
gi 2646261543 201 LFHSFAfdfSVWELWGALAYGGRLVIVPAACARSPQAF 238
Cdd:PRK07529 263 LFHVNA---LLVTGLAPLARGAHVVLATPQGYRGPGVI 297
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
162-227 |
3.37e-05 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 44.19 E-value: 3.37e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 162 YTSGSTGQPKGVMVEHANILRLLAATQDYFRFSHHDVWT----LFHSFAfdfSVWELWGALAYGGRLVIV 227
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCipvpLFHCFG---SVLGVLACLTHGATMVFP 75
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
158-205 |
5.44e-05 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 43.80 E-value: 5.44e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2646261543 158 AYVIYTSGSTGQPKGVMVEHANILRLLAATQDYFRFSHHD----VWTLFHSF 205
Cdd:PRK06814 796 AVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDkvfnALPVFHSF 847
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
152-226 |
3.31e-04 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 41.27 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 152 ITSRHLAYVIYTSGSTGQPKGVMVEHANIL--------RLLAATQDYFRFSHHDV-WTLFHSFafdfsvweLWGALAYGG 222
Cdd:PTZ00237 251 VESSHPLYILYTSGTTGNSKAVVRSNGPHLvglkyywrSIIEKDIPTVVFSHSSIgWVSFHGF--------LYGSLSLGN 322
|
....
gi 2646261543 223 RLVI 226
Cdd:PTZ00237 323 TFVM 326
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
157-201 |
4.31e-04 |
|
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: 40.78 E-value: 4.31e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2646261543 157 LAYVIYTSGSTGQPKGVMVEHANILRLLAATQDYFRFSHHDVWTL 201
Cdd:cd17630 2 LATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLL 46
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
160-207 |
6.04e-04 |
|
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: 40.18 E-value: 6.04e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2646261543 160 VIYTSGSTGQPKGVMVEHANILRLLAATQDYFRFSHHD----VWTLFHSFAF 207
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDryliINPFFHTFGY 56
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
156-180 |
7.87e-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: 7.87e-04
10 20
....*....|....*....|....*
gi 2646261543 156 HLAYVIYTSGSTGQPKGVMVEHANI 180
Cdd:cd05908 107 ELAFIQFSSGSTGDPKGVMLTHENL 131
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
33-177 |
8.35e-04 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 40.15 E-value: 8.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 33 QSLSYGELNRRANRLAHHLL-TLGVQPDDRVAICVERSPEMVVGLLGILKAGAAYLPL---------------------- 89
Cdd:PRK05620 37 EQTTFAAIGARAAALAHALHdELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLnkqlmndqivhiinhaedeviv 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2646261543 90 -DPAYpAERLAYMLSDAAPV--ALLTQSALVETLDSHLPTVVLDARSPSALDGAPDSN--PDsrargITSRHLAYVIYTS 164
Cdd:PRK05620 117 aDPRL-AEQLGEILKECPCVraVVFIGPSDADSAAAHMPEGIKVYSYEALLDGRSTVYdwPE-----LDETTAAAICYST 190
|
170
....*....|...
gi 2646261543 165 GSTGQPKGVMVEH 177
Cdd:PRK05620 191 GTTGAPKGVVYSH 203
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
159-185 |
1.41e-03 |
|
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: 39.29 E-value: 1.41e-03
10 20
....*....|....*....|....*..
gi 2646261543 159 YVIYTSGSTGQPKGVMVEHANILRLLA 185
Cdd:cd05924 7 YILYTGGTTGMPKGVMWRQEDIFRMLM 33
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
155-226 |
4.90e-03 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 37.63 E-value: 4.90e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2646261543 155 RHLAYVIYTSGSTGQPKGVMVEHanilRLLAATQDYF-----RFSHHDVWTLFHSFAFDFSVWELWGALAYGGRLVI 226
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLAN----KTFFAVPDILqkeglNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVT 73
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
156-180 |
7.55e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 37.39 E-value: 7.55e-03
10 20
....*....|....*....|....*
gi 2646261543 156 HLAYVIYTSGSTGQPKGVMVEHANI 180
Cdd:PTZ00342 305 FITSIVYTSGTSGKPKGVMLSNKNL 329
|
|
| |
