AMP-binding protein, partial [Grimontia indica]
Protein Classification
acyl-CoA synthetase family protein( domain architecture ID 102275)
acyl-CoA synthetase family protein functions in fatty acid synthesis, and may catalyze the ATP-dependent activation of fatty acids in a two-step reaction to form acyl-CoA esters; belongs to the class I adenylate-forming enzyme superfamily
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| AFD_class_I super family | cl17068 | Adenylate forming domain, Class I superfamily; This family includes acyl- and aryl-CoA ligases, ... |
1-180 | 1.32e-77 | ||||
Adenylate forming domain, Class I superfamily; 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. The actual alignment was detected with superfamily member cd12114: Pssm-ID: 473059 [Multi-domain] Cd Length: 477 Bit Score: 239.10 E-value: 1.32e-77
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| Name | Accession | Description | Interval | E-value | ||||
| A_NRPS_TlmIV_like | cd12114 | The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
1-180 | 1.32e-77 | ||||
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: 239.10 E-value: 1.32e-77
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| EntF | COG1020 | EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1-175 | 4.57e-59 | ||||
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: 198.54 E-value: 4.57e-59
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| AA-adenyl-dom | TIGR01733 | amino acid adenylation domain; This model represents a domain responsible for the specific ... |
1-175 | 6.42e-53 | ||||
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: 173.61 E-value: 6.42e-53
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| PRK12467 | PRK12467 | peptide synthase; Provisional |
1-175 | 6.67e-37 | ||||
peptide synthase; Provisional Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 134.90 E-value: 6.67e-37
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| AMP-binding | pfam00501 | AMP-binding enzyme; |
1-175 | 3.94e-36 | ||||
AMP-binding enzyme; Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 129.74 E-value: 3.94e-36
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| Name | Accession | Description | Interval | E-value | ||||
| A_NRPS_TlmIV_like | cd12114 | The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
1-180 | 1.32e-77 | ||||
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: 239.10 E-value: 1.32e-77
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| EntF | COG1020 | EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1-175 | 4.57e-59 | ||||
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: 198.54 E-value: 4.57e-59
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| AA-adenyl-dom | TIGR01733 | amino acid adenylation domain; This model represents a domain responsible for the specific ... |
1-175 | 6.42e-53 | ||||
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: 173.61 E-value: 6.42e-53
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| A_NRPS | cd05930 | The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
1-175 | 2.20e-42 | ||||
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: 146.52 E-value: 2.20e-42
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| A_NRPS_Ta1_like | cd12116 | The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
1-174 | 5.12e-38 | ||||
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: 135.50 E-value: 5.12e-38
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| PRK12467 | PRK12467 | peptide synthase; Provisional |
1-175 | 6.67e-37 | ||||
peptide synthase; Provisional Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 134.90 E-value: 6.67e-37
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| AMP-binding | pfam00501 | AMP-binding enzyme; |
1-175 | 3.94e-36 | ||||
AMP-binding enzyme; Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 129.74 E-value: 3.94e-36
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| A_NRPS_AB3403-like | cd17646 | Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
1-174 | 1.04e-34 | ||||
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: 127.01 E-value: 1.04e-34
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| DltA | cd05945 | D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
1-175 | 7.33e-34 | ||||
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: 124.28 E-value: 7.33e-34
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| A_NRPS_VisG_like | cd17651 | similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
1-162 | 2.47e-33 | ||||
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: 123.22 E-value: 2.47e-33
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| A_NRPS_Srf_like | cd12117 | The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
1-163 | 1.28e-30 | ||||
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: 115.76 E-value: 1.28e-30
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| entF | PRK10252 | enterobactin non-ribosomal peptide synthetase EntF; |
1-172 | 4.82e-30 | ||||
enterobactin non-ribosomal peptide synthetase EntF; Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 115.14 E-value: 4.82e-30
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| PRK12316 | PRK12316 | peptide synthase; Provisional |
1-175 | 9.02e-30 | ||||
peptide synthase; Provisional Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 114.67 E-value: 9.02e-30
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| PRK12467 | PRK12467 | peptide synthase; Provisional |
1-179 | 1.45e-29 | ||||
peptide synthase; Provisional Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 114.10 E-value: 1.45e-29
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| PRK12316 | PRK12316 | peptide synthase; Provisional |
1-175 | 5.73e-28 | ||||
peptide synthase; Provisional Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 109.28 E-value: 5.73e-28
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| A_NRPS_Sfm_like | cd12115 | The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
1-173 | 5.34e-27 | ||||
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: 105.48 E-value: 5.34e-27
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| A_NRPS_Bac | cd17655 | bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
1-174 | 9.53e-27 | ||||
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: 105.10 E-value: 9.53e-27
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| PRK12467 | PRK12467 | peptide synthase; Provisional |
1-179 | 2.16e-26 | ||||
peptide synthase; Provisional Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 104.86 E-value: 2.16e-26
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| A_NRPS_GliP_like | cd17653 | nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
1-174 | 2.53e-26 | ||||
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: 103.54 E-value: 2.53e-26
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| A_NRPS_SidN3_like | cd05918 | The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
1-162 | 2.57e-26 | ||||
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: 103.78 E-value: 2.57e-26
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| A_NRPS_Cytc1-like | cd17643 | similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
1-168 | 6.04e-26 | ||||
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: 102.39 E-value: 6.04e-26
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| PRK12316 | PRK12316 | peptide synthase; Provisional |
1-179 | 8.76e-24 | ||||
peptide synthase; Provisional Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 97.34 E-value: 8.76e-24
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| A_NRPS_CmdD_like | cd17652 | similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
1-174 | 1.32e-23 | ||||
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: 96.17 E-value: 1.32e-23
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| A_NRPS_ApnA-like | cd17644 | similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
1-174 | 4.11e-23 | ||||
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: 94.81 E-value: 4.11e-23
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| AFD_class_I | cd04433 | Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
71-180 | 1.06e-22 | ||||
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: 92.35 E-value: 1.06e-22
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| D-ala-DACP-lig | TIGR01734 | D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ... |
1-175 | 3.62e-22 | ||||
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also called D-alanine-D-alanyl carrier protein ligase) which activates D-alanine as an adenylate via the reaction D-ala + ATP -> D-ala-AMP + PPi, and further catalyzes the condensation of the amino acid adenylate with the D-alanyl carrier protein (D-ala-ACP). The D-alanine is then further transferred to teichoic acid in the biosynthesis of lipoteichoic acid (LTA) and wall teichoic acid (WTA) in gram positive bacteria, both polysacchatides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan] Pssm-ID: 273780 [Multi-domain] Cd Length: 502 Bit Score: 92.51 E-value: 3.62e-22
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| PRK04813 | PRK04813 | D-alanine--poly(phosphoribitol) ligase subunit DltA; |
1-175 | 6.69e-22 | ||||
D-alanine--poly(phosphoribitol) ligase subunit DltA; Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 91.50 E-value: 6.69e-22
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| A_NRPS_PpsD_like | cd17650 | similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
1-175 | 1.17e-21 | ||||
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: 90.60 E-value: 1.17e-21
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| PRK12316 | PRK12316 | peptide synthase; Provisional |
1-175 | 1.52e-21 | ||||
peptide synthase; Provisional Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 91.17 E-value: 1.52e-21
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| A_NRPS_PvdJ-like | cd17649 | non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
1-180 | 3.56e-21 | ||||
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: 89.35 E-value: 3.56e-21
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| PRK05691 | PRK05691 | peptide synthase; Validated |
1-171 | 4.05e-21 | ||||
peptide synthase; Validated Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 89.84 E-value: 4.05e-21
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| MenE/FadK | COG0318 | O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
1-179 | 6.92e-21 | ||||
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: 88.33 E-value: 6.92e-21
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| A_NRPS_ProA | cd17656 | gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
1-163 | 1.51e-19 | ||||
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: 84.83 E-value: 1.51e-19
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| A_NRPS_LgrA-like | cd17645 | adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
1-163 | 1.76e-18 | ||||
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: 81.83 E-value: 1.76e-18
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| A_NRPS_ACVS-like | cd17648 | N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
1-173 | 5.07e-18 | ||||
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: 80.52 E-value: 5.07e-18
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| Acs | COG0365 | Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
50-175 | 4.96e-17 | ||||
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 77.46 E-value: 4.96e-17
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| PRK05691 | PRK05691 | peptide synthase; Validated |
1-168 | 7.72e-16 | ||||
peptide synthase; Validated Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 74.43 E-value: 7.72e-16
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| A_NRPS_acs4 | cd17654 | acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
1-174 | 3.49e-15 | ||||
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: 72.12 E-value: 3.49e-15
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| FACL_like_6 | cd05922 | Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
28-174 | 3.67e-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: 72.09 E-value: 3.67e-15
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| FAAL | cd05931 | Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
1-163 | 7.09e-14 | ||||
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: 68.42 E-value: 7.09e-14
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| PRK07656 | PRK07656 | long-chain-fatty-acid--CoA ligase; Validated |
58-174 | 1.66e-13 | ||||
long-chain-fatty-acid--CoA ligase; Validated Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 67.62 E-value: 1.66e-13
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| FACL_DitJ_like | cd05934 | Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
70-180 | 7.35e-13 | ||||
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: 65.39 E-value: 7.35e-13
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| MACS_like_4 | cd05969 | Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
67-175 | 1.58e-12 | ||||
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria. Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 64.45 E-value: 1.58e-12
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| MACS_like | cd05972 | Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
50-175 | 2.75e-12 | ||||
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: 63.90 E-value: 2.75e-12
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| PRK04319 | PRK04319 | acetyl-CoA synthetase; Provisional |
58-175 | 5.18e-12 | ||||
acetyl-CoA synthetase; Provisional Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 62.99 E-value: 5.18e-12
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| PRK05691 | PRK05691 | peptide synthase; Validated |
1-171 | 1.00e-11 | ||||
peptide synthase; Validated Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 62.49 E-value: 1.00e-11
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| AFD_YhfT-like | cd17633 | fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
70-174 | 1.36e-11 | ||||
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 61.65 E-value: 1.36e-11
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| CBAL | cd05923 | 4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
41-179 | 3.98e-11 | ||||
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: 60.60 E-value: 3.98e-11
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| ACS-like | cd17634 | acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
58-175 | 4.72e-11 | ||||
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: 60.28 E-value: 4.72e-11
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| FC-FACS_FadD_like | cd05936 | Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
2-175 | 1.93e-10 | ||||
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: 58.34 E-value: 1.93e-10
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| CHC_CoA_lg | cd05903 | Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
68-180 | 3.51e-10 | ||||
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA. Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 57.78 E-value: 3.51e-10
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| Firefly_Luc_like | cd05911 | Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
21-174 | 4.66e-10 | ||||
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light. Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 57.61 E-value: 4.66e-10
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| PRK12406 | PRK12406 | long-chain-fatty-acid--CoA ligase; Provisional |
3-175 | 5.39e-10 | ||||
long-chain-fatty-acid--CoA ligase; Provisional Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 57.40 E-value: 5.39e-10
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| PRK07638 | PRK07638 | acyl-CoA synthetase; Validated |
54-174 | 9.62e-10 | ||||
acyl-CoA synthetase; Validated Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 56.71 E-value: 9.62e-10
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| BCL_4HBCL | cd05959 | Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
58-170 | 1.26e-09 | ||||
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process. Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 56.22 E-value: 1.26e-09
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| FACL_FadD13-like | cd17631 | fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
71-175 | 1.35e-09 | ||||
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: 56.08 E-value: 1.35e-09
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| PRK09274 | PRK09274 | peptide synthase; Provisional |
62-162 | 2.63e-09 | ||||
peptide synthase; Provisional Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 55.29 E-value: 2.63e-09
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| AAS_C | cd05909 | C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
64-172 | 2.99e-09 | ||||
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases. Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 55.03 E-value: 2.99e-09
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| FACL_fum10p_like | cd05926 | Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
11-180 | 4.40e-09 | ||||
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: 54.63 E-value: 4.40e-09
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| FACL_like_1 | cd05910 | Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
71-174 | 5.79e-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: 54.39 E-value: 5.79e-09
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| BCL_like | cd05919 | Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
64-170 | 8.65e-09 | ||||
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP. Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 53.62 E-value: 8.65e-09
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| PRK08633 | PRK08633 | 2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
65-163 | 1.05e-08 | ||||
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 53.77 E-value: 1.05e-08
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| PrpE | cd05967 | Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
62-168 | 1.70e-08 | ||||
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: 53.09 E-value: 1.70e-08
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| FAA1 | COG1022 | Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
66-115 | 2.20e-08 | ||||
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 52.41 E-value: 2.20e-08
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| caiC | PRK08008 | putative crotonobetaine/carnitine-CoA ligase; Validated |
60-176 | 2.61e-08 | ||||
putative crotonobetaine/carnitine-CoA ligase; Validated Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 52.38 E-value: 2.61e-08
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| PLN02246 | PLN02246 | 4-coumarate--CoA ligase |
15-168 | 2.86e-08 | ||||
4-coumarate--CoA ligase Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 52.29 E-value: 2.86e-08
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| prpE | PRK10524 | propionyl-CoA synthetase; Provisional |
7-174 | 3.39e-08 | ||||
propionyl-CoA synthetase; Provisional Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 52.26 E-value: 3.39e-08
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| PRK08314 | PRK08314 | long-chain-fatty-acid--CoA ligase; Validated |
63-177 | 7.79e-08 | ||||
long-chain-fatty-acid--CoA ligase; Validated Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 51.11 E-value: 7.79e-08
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| AACS_like | cd05968 | Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
41-175 | 1.08e-07 | ||||
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: 50.57 E-value: 1.08e-07
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| EntE | COG1021 | EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
58-175 | 1.17e-07 | ||||
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism]; Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 50.53 E-value: 1.17e-07
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| PLN02860 | PLN02860 | o-succinylbenzoate-CoA ligase |
47-180 | 1.50e-07 | ||||
o-succinylbenzoate-CoA ligase Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 50.18 E-value: 1.50e-07
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| 23DHB-AMP_lg | cd05920 | 2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
71-180 | 1.68e-07 | ||||
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system. Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 50.02 E-value: 1.68e-07
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| PRK06187 | PRK06187 | long-chain-fatty-acid--CoA ligase; Validated |
18-175 | 2.97e-07 | ||||
long-chain-fatty-acid--CoA ligase; Validated Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 49.41 E-value: 2.97e-07
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| PRK06087 | PRK06087 | medium-chain fatty-acid--CoA ligase; |
55-180 | 3.29e-07 | ||||
medium-chain fatty-acid--CoA ligase; Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 48.98 E-value: 3.29e-07
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| PRK13295 | PRK13295 | cyclohexanecarboxylate-CoA ligase; Reviewed |
59-180 | 3.35e-07 | ||||
cyclohexanecarboxylate-CoA ligase; Reviewed Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 49.28 E-value: 3.35e-07
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| PRK06188 | PRK06188 | acyl-CoA synthetase; Validated |
55-175 | 4.24e-07 | ||||
acyl-CoA synthetase; Validated Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 48.83 E-value: 4.24e-07
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| PRK06814 | PRK06814 | acyl-[ACP]--phospholipid O-acyltransferase; |
57-141 | 4.78e-07 | ||||
acyl-[ACP]--phospholipid O-acyltransferase; Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 48.81 E-value: 4.78e-07
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| LC-FACS_euk | cd05927 | Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
61-97 | 4.92e-07 | ||||
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: 48.75 E-value: 4.92e-07
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| ACS | cd05966 | Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
62-175 | 4.94e-07 | ||||
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: 48.71 E-value: 4.94e-07
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| LC_FACS_euk1 | cd17639 | Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
67-115 | 6.79e-07 | ||||
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: 48.37 E-value: 6.79e-07
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| A_NRPS_TubE_like | cd05906 | The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
19-163 | 1.15e-06 | ||||
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: 47.66 E-value: 1.15e-06
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| VL_LC_FACS_like | cd05907 | Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
68-115 | 1.34e-06 | ||||
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: 47.20 E-value: 1.34e-06
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| PRK07867 | PRK07867 | acyl-CoA synthetase; Validated |
5-110 | 2.00e-06 | ||||
acyl-CoA synthetase; Validated Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 46.98 E-value: 2.00e-06
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| PRK06164 | PRK06164 | acyl-CoA synthetase; Validated |
59-162 | 2.34e-06 | ||||
acyl-CoA synthetase; Validated Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 46.66 E-value: 2.34e-06
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| MCS | cd05941 | Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
1-168 | 2.39e-06 | ||||
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: 46.51 E-value: 2.39e-06
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| PRK13388 | PRK13388 | acyl-CoA synthetase; Provisional |
29-110 | 4.30e-06 | ||||
acyl-CoA synthetase; Provisional Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 45.79 E-value: 4.30e-06
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| PRK13391 | PRK13391 | acyl-CoA synthetase; Provisional |
10-168 | 4.50e-06 | ||||
acyl-CoA synthetase; Provisional Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 45.84 E-value: 4.50e-06
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| A_NRPS_alphaAR | cd17647 | Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
29-174 | 4.57e-06 | ||||
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: 45.97 E-value: 4.57e-06
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| LC_FACS_like | cd05935 | Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
72-175 | 4.63e-06 | ||||
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 45.55 E-value: 4.63e-06
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| A_NRPS_MycA_like | cd05908 | The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
72-166 | 5.52e-06 | ||||
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: 45.56 E-value: 5.52e-06
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| PLN02387 | PLN02387 | long-chain-fatty-acid-CoA ligase family protein |
58-91 | 5.80e-06 | ||||
long-chain-fatty-acid-CoA ligase family protein Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 45.49 E-value: 5.80e-06
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| ttLC_FACS_AlkK_like | cd12119 | Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
17-175 | 6.79e-06 | ||||
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: 45.31 E-value: 6.79e-06
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| FACL_like_5 | cd05924 | Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
73-163 | 9.47e-06 | ||||
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 44.68 E-value: 9.47e-06
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| PRK07787 | PRK07787 | acyl-CoA synthetase; Validated |
38-99 | 1.94e-05 | ||||
acyl-CoA synthetase; Validated Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 43.83 E-value: 1.94e-05
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| PRK03640 | PRK03640 | o-succinylbenzoate--CoA ligase; |
29-175 | 1.95e-05 | ||||
o-succinylbenzoate--CoA ligase; Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 43.80 E-value: 1.95e-05
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| LC_FACS_bac | cd05932 | Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
56-115 | 2.67e-05 | ||||
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: 43.61 E-value: 2.67e-05
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| LC_FACS_like | cd17640 | Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
67-116 | 2.85e-05 | ||||
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: 43.50 E-value: 2.85e-05
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| MACS_AAE_MA_like | cd05970 | Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
57-175 | 3.49e-05 | ||||
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: 43.25 E-value: 3.49e-05
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| OSB_CoA_lg | cd05912 | O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
72-175 | 3.92e-05 | ||||
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: 43.10 E-value: 3.92e-05
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| PRK09192 | PRK09192 | fatty acyl-AMP ligase; |
57-163 | 4.55e-05 | ||||
fatty acyl-AMP ligase; Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 42.68 E-value: 4.55e-05
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| MACS_like_3 | cd05971 | Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
56-92 | 4.59e-05 | ||||
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria. Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 42.80 E-value: 4.59e-05
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| PRK13382 | PRK13382 | bile acid CoA ligase; |
33-175 | 5.04e-05 | ||||
bile acid CoA ligase; Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 42.82 E-value: 5.04e-05
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| PTZ00237 | PTZ00237 | acetyl-CoA synthetase; Provisional |
58-145 | 5.98e-05 | ||||
acetyl-CoA synthetase; Provisional Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 42.42 E-value: 5.98e-05
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| ACLS-CaiC | cd17637 | acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
74-180 | 6.66e-05 | ||||
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 42.26 E-value: 6.66e-05
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| Firefly_Luc | cd17642 | insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
72-174 | 7.77e-05 | ||||
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: 42.13 E-value: 7.77e-05
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| FADD10 | cd17635 | adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
71-174 | 8.83e-05 | ||||
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: 41.86 E-value: 8.83e-05
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| PRK05605 | PRK05605 | long-chain-fatty-acid--CoA ligase; Validated |
18-179 | 9.37e-05 | ||||
long-chain-fatty-acid--CoA ligase; Validated Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 41.91 E-value: 9.37e-05
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| PRK06839 | PRK06839 | o-succinylbenzoate--CoA ligase; |
64-170 | 1.14e-04 | ||||
o-succinylbenzoate--CoA ligase; Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 41.77 E-value: 1.14e-04
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| ttLC_FACS_AEE21_like | cd12118 | Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
65-174 | 1.17e-04 | ||||
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: 41.52 E-value: 1.17e-04
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| FACL_like_2 | cd05917 | Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
68-179 | 1.34e-04 | ||||
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 41.11 E-value: 1.34e-04
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| PRK07470 | PRK07470 | acyl-CoA synthetase; Validated |
62-174 | 1.74e-04 | ||||
acyl-CoA synthetase; Validated Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 41.18 E-value: 1.74e-04
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| PRK09088 | PRK09088 | acyl-CoA synthetase; Validated |
47-145 | 1.82e-04 | ||||
acyl-CoA synthetase; Validated Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 40.95 E-value: 1.82e-04
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| PRK05850 | PRK05850 | acyl-CoA synthetase; Validated |
1-92 | 1.84e-04 | ||||
acyl-CoA synthetase; Validated Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 41.08 E-value: 1.84e-04
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| PRK13390 | PRK13390 | acyl-CoA synthetase; Provisional |
30-175 | 1.92e-04 | ||||
acyl-CoA synthetase; Provisional Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 41.15 E-value: 1.92e-04
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| PLN02430 | PLN02430 | long-chain-fatty-acid-CoA ligase |
61-95 | 1.96e-04 | ||||
long-chain-fatty-acid-CoA ligase Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 40.95 E-value: 1.96e-04
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| PRK08043 | PRK08043 | bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
59-93 | 3.53e-04 | ||||
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 40.46 E-value: 3.53e-04
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| PRK06145 | PRK06145 | acyl-CoA synthetase; Validated |
29-179 | 4.23e-04 | ||||
acyl-CoA synthetase; Validated Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 39.87 E-value: 4.23e-04
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| alpha_am_amid | TIGR03443 | L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
64-129 | 5.37e-04 | ||||
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: 39.66 E-value: 5.37e-04
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| PRK08276 | PRK08276 | long-chain-fatty-acid--CoA ligase; Validated |
44-169 | 5.79e-04 | ||||
long-chain-fatty-acid--CoA ligase; Validated Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 39.50 E-value: 5.79e-04
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| PRK07786 | PRK07786 | long-chain-fatty-acid--CoA ligase; Validated |
42-91 | 6.15e-04 | ||||
long-chain-fatty-acid--CoA ligase; Validated Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 39.38 E-value: 6.15e-04
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| PRK06155 | PRK06155 | crotonobetaine/carnitine-CoA ligase; Provisional |
41-91 | 6.24e-04 | ||||
crotonobetaine/carnitine-CoA ligase; Provisional Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 39.36 E-value: 6.24e-04
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| PRK07008 | PRK07008 | long-chain-fatty-acid--CoA ligase; Validated |
69-175 | 6.96e-04 | ||||
long-chain-fatty-acid--CoA ligase; Validated Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 39.30 E-value: 6.96e-04
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| PRK07768 | PRK07768 | long-chain-fatty-acid--CoA ligase; Validated |
63-163 | 7.73e-04 | ||||
long-chain-fatty-acid--CoA ligase; Validated Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 39.21 E-value: 7.73e-04
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| ABCL | cd05958 | 2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
76-168 | 7.84e-04 | ||||
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: 39.00 E-value: 7.84e-04
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| PRK08180 | PRK08180 | feruloyl-CoA synthase; Reviewed |
36-87 | 8.83e-04 | ||||
feruloyl-CoA synthase; Reviewed Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 39.09 E-value: 8.83e-04
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| hsFATP2a_ACSVL_like | cd05938 | Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
18-92 | 8.86e-04 | ||||
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: 39.20 E-value: 8.86e-04
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| PLN02736 | PLN02736 | long-chain acyl-CoA synthetase |
58-91 | 1.02e-03 | ||||
long-chain acyl-CoA synthetase Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 38.93 E-value: 1.02e-03
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| PRK00174 | PRK00174 | acetyl-CoA synthetase; Provisional |
63-87 | 1.04e-03 | ||||
acetyl-CoA synthetase; Provisional Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 38.97 E-value: 1.04e-03
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| ACSBG_like | cd05933 | Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
66-146 | 1.39e-03 | ||||
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: 38.49 E-value: 1.39e-03
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| BACL_like | cd05929 | Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
35-170 | 1.46e-03 | ||||
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp. Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 38.51 E-value: 1.46e-03
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| PRK08279 | PRK08279 | long-chain-acyl-CoA synthetase; Validated |
26-140 | 1.60e-03 | ||||
long-chain-acyl-CoA synthetase; Validated Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 38.32 E-value: 1.60e-03
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| FadD3 | cd17638 | acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
74-175 | 2.01e-03 | ||||
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: 37.87 E-value: 2.01e-03
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| PRK09029 | PRK09029 | O-succinylbenzoic acid--CoA ligase; Provisional |
22-93 | 4.32e-03 | ||||
O-succinylbenzoic acid--CoA ligase; Provisional Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 36.77 E-value: 4.32e-03
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| PTZ00216 | PTZ00216 | acyl-CoA synthetase; Provisional |
63-100 | 5.50e-03 | ||||
acyl-CoA synthetase; Provisional Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 36.88 E-value: 5.50e-03
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| PLN02574 | PLN02574 | 4-coumarate--CoA ligase-like |
1-174 | 7.07e-03 | ||||
4-coumarate--CoA ligase-like Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 36.36 E-value: 7.07e-03
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| PRK06018 | PRK06018 | putative acyl-CoA synthetase; Provisional |
69-175 | 7.14e-03 | ||||
putative acyl-CoA synthetase; Provisional Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 36.27 E-value: 7.14e-03
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| PRK07514 | PRK07514 | malonyl-CoA synthase; Validated |
1-91 | 7.47e-03 | ||||
malonyl-CoA synthase; Validated Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 36.39 E-value: 7.47e-03
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| Blast search parameters | ||||
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