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Conserved domains on  [gi|1896964077|ref|WP_186905268|]
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AMP-binding protein, partial [Undibacterium curvum]

Protein Classification

Graphical summary

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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, ...
 1-85 8.97e-35

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 cd05930:

Pssm-ID: 473059 [Multi-domain]  Cd Length: 444  Bit Score: 122.25  E-value: 8.97e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077   1 IINVYGPTETTIDASTWQLPPAESEaiaqlPAILPIGQPLANYQAYVLDAHWQLAAMGVEGELFLGGAGLARGYLGQPGL 80
Cdd:cd05930   237 LVNLYGPTEATVDATYYRVPPDDEE-----DGRVPIGRPIPNTRVYVLDENLRPVPPGVPGELYIGGAGLARGYLNRPEL 311


                  ....*
gi 1896964077  81 TAERF 85
Cdd:cd05930   312 TAERF 316
 
Name Accession Description Interval E-value
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
 1-85 8.97e-35

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: 122.25  E-value: 8.97e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077   1 IINVYGPTETTIDASTWQLPPAESEaiaqlPAILPIGQPLANYQAYVLDAHWQLAAMGVEGELFLGGAGLARGYLGQPGL 80
Cdd:cd05930   237 LVNLYGPTEATVDATYYRVPPDDEE-----DGRVPIGRPIPNTRVYVLDENLRPVPPGVPGELYIGGAGLARGYLNRPEL 311


                  ....*
gi 1896964077  81 TAERF 85
Cdd:cd05930   312 TAERF 316
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 1-85 3.10e-32

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: 117.27  E-value: 3.10e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077    1 IINVYGPTETTIDASTWQLPPAESEAiaqlpAILPIGQPLANYQAYVLDAHWQLAAMGVEGELFLGGAGLARGYLGQPGL 80
Cdd:COG1020    760 LVNLYGPTETTVDSTYYEVTPPDADG-----GSVPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPEL 834


                   ....*
gi 1896964077   81 TAERF 85
Cdd:COG1020    835 TAERF 839
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
 1-85 5.17e-32

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: 114.67  E-value: 5.17e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077   1 IINVYGPTETTIDASTWQLPPAEseaiAQLPAILPIGQPLANYQAYVLDAHWQLAAMGVEGELFLGGAGLARGYLGQPGL 80
Cdd:TIGR01733 264 LINLYGPTETTVWSTATLVDPDD----APRESPVPIGRPLANTRLYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPEL 339


                  ....*
gi 1896964077  81 TAERF 85
Cdd:TIGR01733 340 TAERF 344
PRK12467 PRK12467
peptide synthase; Provisional
 1-85 5.83e-26

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 99.08  E-value: 5.83e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077    1 IINVYGPTETTIDASTWQLPPAESEAIAqlpaiLPIGQPLANYQAYVLDAHWQLAAMGVEGELFLGGAGLARGYLGQPGL 80
Cdd:PRK12467   800 LINHYGPTETTVGVSTYELSDEERDFGN-----VPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPAL 874


                   ....*
gi 1896964077   81 TAERF 85
Cdd:PRK12467   875 TAERF 879
AMP-binding pfam00501
AMP-binding enzyme;
1-85 1.04e-18

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 78.12  E-value: 1.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077   1 IINVYGPTETTIdASTWQLPPAESEAiaqlpAILPIGQPLANYQAYVLDAHW-QLAAMGVEGELFLGGAGLARGYLGQPG 79
Cdd:pfam00501 305 LVNGYGLTETTG-VVTTPLPLDEDLR-----SLGSVGRPLPGTEVKIVDDETgEPVPPGEPGELCVRGPGVMKGYLNDPE 378


                  ....*.
gi 1896964077  80 LTAERF 85
Cdd:pfam00501 379 LTAEAF 384
 
Name Accession Description Interval E-value
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
 1-85 8.97e-35

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: 122.25  E-value: 8.97e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077   1 IINVYGPTETTIDASTWQLPPAESEaiaqlPAILPIGQPLANYQAYVLDAHWQLAAMGVEGELFLGGAGLARGYLGQPGL 80
Cdd:cd05930   237 LVNLYGPTEATVDATYYRVPPDDEE-----DGRVPIGRPIPNTRVYVLDENLRPVPPGVPGELYIGGAGLARGYLNRPEL 311


                  ....*
gi 1896964077  81 TAERF 85
Cdd:cd05930   312 TAERF 316
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 1-85 3.10e-32

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: 117.27  E-value: 3.10e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077    1 IINVYGPTETTIDASTWQLPPAESEAiaqlpAILPIGQPLANYQAYVLDAHWQLAAMGVEGELFLGGAGLARGYLGQPGL 80
Cdd:COG1020    760 LVNLYGPTETTVDSTYYEVTPPDADG-----GSVPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPEL 834


                   ....*
gi 1896964077   81 TAERF 85
Cdd:COG1020    835 TAERF 839
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
 1-85 5.17e-32

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: 114.67  E-value: 5.17e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077   1 IINVYGPTETTIDASTWQLPPAEseaiAQLPAILPIGQPLANYQAYVLDAHWQLAAMGVEGELFLGGAGLARGYLGQPGL 80
Cdd:TIGR01733 264 LINLYGPTETTVWSTATLVDPDD----APRESPVPIGRPLANTRLYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPEL 339


                  ....*
gi 1896964077  81 TAERF 85
Cdd:TIGR01733 340 TAERF 344
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
 1-85 5.12e-28

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: 104.59  E-value: 5.12e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077   1 IINVYGPTETTIDASTWQLPPAESEAIAqlpaiLPIGQPLANYQAYVLDAHWQLAAMGVEGELFLGGAGLARGYLGQPGL 80
Cdd:cd12117   278 LVNGYGPTENTTFTTSHVVTELDEVAGS-----IPIGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPAL 352


                  ....*
gi 1896964077  81 TAERF 85
Cdd:cd12117   353 TAERF 357
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
 1-85 5.13e-28

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: 104.33  E-value: 5.13e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077   1 IINVYGPTETTIDASTWQLPPAEseaiAQLPAIlPIGQPLANYQAYVLDAHWQLAAMGVEGELFLGGAGLARGYLGQPGL 80
Cdd:cd17655   281 ITNAYGPTETTVDASIYQYEPET----DQQVSV-PIGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPEL 355


                  ....*
gi 1896964077  81 TAERF 85
Cdd:cd17655   356 TAEKF 360
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
 2-85 1.47e-27

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: 102.83  E-value: 1.47e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077   2 INVYGPTETTIDASTWQLPPAESEAiaqlPAILPIGQPLANYQAYVLDAHWQLAAMGVEGELFLGGAGLARGYLGQPGLT 81
Cdd:cd17649   240 FNAYGPTEATVTPLVWKCEAGAARA----GASMPIGRPLGGRSAYILDADLNPVPVGVTGELYIGGEGLARGYLGRPELT 315


                  ....
gi 1896964077  82 AERF 85
Cdd:cd17649   316 AERF 319
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
 1-85 4.13e-27

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: 101.56  E-value: 4.13e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077   1 IINVYGPTETTIDASTWQLPPAEseaiaqlpAILPIGQPLANYQAYVLDAHWQLAAMGVEGELFLGGAGLARGYLGQPGL 80
Cdd:cd17652   230 MINAYGPTETTVCATMAGPLPGG--------GVPPIGRPVPGTRVYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGL 301


                  ....*
gi 1896964077  81 TAERF 85
Cdd:cd17652   302 TAERF 306
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
 3-85 9.95e-27

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: 100.81  E-value: 9.95e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077   3 NVYGPTETTIDASTWQLPPAESeaiaqlPAILPIGQPLANYQAYVLDAHWQLAAMGVEGELFLGGAGLARGYLGQPGLTA 82
Cdd:cd17646   283 NLYGPTEAAIDVTHWPVRGPAE------TPSVPIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTA 356


                  ...
gi 1896964077  83 ERF 85
Cdd:cd17646   357 ERF 359
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
 1-85 5.38e-26

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: 98.54  E-value: 5.38e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077   1 IINVYGPTETTIDASTWQLPPAESEAIaqlpailPIGQPLANYQAYVLDAHWQLAAMGVEGELFLGGAGLARGYLGQPGL 80
Cdd:cd12115   242 VVNLYGPSEDTTYSTVAPVPPGASGEV-------SIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGL 314


                  ....*
gi 1896964077  81 TAERF 85
Cdd:cd12115   315 TAERF 319
PRK12467 PRK12467
peptide synthase; Provisional
 1-85 5.83e-26

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 99.08  E-value: 5.83e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077    1 IINVYGPTETTIDASTWQLPPAESEAIAqlpaiLPIGQPLANYQAYVLDAHWQLAAMGVEGELFLGGAGLARGYLGQPGL 80
Cdd:PRK12467   800 LINHYGPTETTVGVSTYELSDEERDFGN-----VPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPAL 874


                   ....*
gi 1896964077   81 TAERF 85
Cdd:PRK12467   875 TAERF 879
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
 1-85 1.79e-25

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: 97.41  E-value: 1.79e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077   1 IINVYGPTETTIdASTWQLPPAESEAiaqlPAILPIGQPLANYQAYVLDAHWQLAAMGVEGELFLGGAGLARGYLGQPGL 80
Cdd:cd17651   283 LHNHYGPTETHV-VTALSLPGDPAAW----PAPPPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPEL 357


                  ....*
gi 1896964077  81 TAERF 85
Cdd:cd17651   358 TAERF 362
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
 2-85 2.38e-25

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: 97.12  E-value: 2.38e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077   2 INVYGPTETTIDASTWQLPPAESEAIAQLPailpIGQPLANYQAYVLDAHWQLAAMGVEGELFLGGAGLARGYLGQPGLT 81
Cdd:cd17644   255 INVYGPTEATIAATVCRLTQLTERNITSVP----IGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELT 330


                  ....
gi 1896964077  82 AERF 85
Cdd:cd17644   331 AEKF 334
PRK12316 PRK12316
peptide synthase; Provisional
 1-85 2.64e-25

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 97.34  E-value: 2.64e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077    1 IINVYGPTETTIDASTWQLPPAESEAiaqlPAILPIGQPLANYQAYVLDAHWQLAAMGVEGELFLGGAGLARGYLGQPGL 80
Cdd:PRK12316  2290 LFNGYGPTEAVVTPLLWKCRPQDPCG----AAYVPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGL 2365


                   ....*
gi 1896964077   81 TAERF 85
Cdd:PRK12316  2366 TAERF 2370
PRK12316 PRK12316
peptide synthase; Provisional
 1-85 5.52e-25

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 96.56  E-value: 5.52e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077    1 IINVYGPTETTIDASTWQLPPAESEAiaqlPAILPIGQPLANYQAYVLDAHWQLAAMGVEGELFLGGAGLARGYLGQPGL 80
Cdd:PRK12316  4838 LFNGYGPTETTVTVLLWKARDGDACG----AAYMPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPAL 4913


                   ....*
gi 1896964077   81 TAERF 85
Cdd:PRK12316  4914 TAERF 4918
PRK12467 PRK12467
peptide synthase; Provisional
 1-85 7.23e-25

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 96.00  E-value: 7.23e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077    1 IINVYGPTETTIDASTWQLPPAESEAiaqlPAILPIGQPLANYQAYVLDAHWQLAAMGVEGELFLGGAGLARGYLGQPGL 80
Cdd:PRK12467  1863 LFNLYGPTETAVDVTHWTCRRKDLEG----RDSVPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPAL 1938


                   ....*
gi 1896964077   81 TAERF 85
Cdd:PRK12467  1939 TAERF 1943
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
 2-85 1.75e-24

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: 94.67  E-value: 1.75e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077   2 INVYGPTETTIdASTWQLPPAESEAIaqlpailPIGQPLANYQAYVLDAHWQLAAMGVEGELFLGGAGLARGYLGQPGLT 81
Cdd:cd12116   267 WNLYGPTETTI-WSTAARVTAAAGPI-------PIGRPLANTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALT 338


                  ....
gi 1896964077  82 AERF 85
Cdd:cd12116   339 AERF 342
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
 1-85 3.57e-24

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: 93.69  E-value: 3.57e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077   1 IINVYGPTETTIDASTWQLPPAESEAIAQLPailpIGQPLANYQAYVLDAHWQLAAMGVEGELFLGGAGLARGYLGQPGL 80
Cdd:cd17650   241 IINSYGVTEATIDSTYYEEGRDPLGDSANVP----IGRPLPNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPEL 316


                  ....*
gi 1896964077  81 TAERF 85
Cdd:cd17650   317 TAERF 321
PRK12316 PRK12316
peptide synthase; Provisional
 1-85 3.75e-24

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 94.25  E-value: 3.75e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077    1 IINVYGPTETTIDASTWQlppaeseAIAQLPAILPIGQPLANYQAYVLDAHWQLAAMGVEGELFLGGAGLARGYLGQPGL 80
Cdd:PRK12316   799 LYNLYGPTEAAIDVTHWT-------CVEEGGDSVPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGL 871


                   ....*
gi 1896964077   81 TAERF 85
Cdd:PRK12316   872 TAERF 876
PRK05691 PRK05691
peptide synthase; Validated
 3-85 6.95e-24

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 93.31  E-value: 6.95e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077    3 NVYGPTETTIDASTWQLPPAESEAIaqlpailPIGQPLANYQAYVLDAHWQLAAMGVEGELFLGGAGLARGYLGQPGLTA 82
Cdd:PRK05691  1419 NRYGPTETAINVTHWQCQAEDGERS-------PIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTA 1491


                   ...
gi 1896964077   83 ERF 85
Cdd:PRK05691  1492 ERF 1494
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
 1-85 1.21e-23

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: 92.37  E-value: 1.21e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077   1 IINVYGPTETTIDASTWQLPPAESEAIAQLPailpIGQPLANYQAYVLDAHWQLAAMGVEGELFLGGAGLARGYLGQPGL 80
Cdd:cd17643   241 LVNMYGITETTVHVTFRPLDAADLPAAAASP----IGRPLPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPEL 316


                  ....*
gi 1896964077  81 TAERF 85
Cdd:cd17643   317 TAERF 321
PRK12467 PRK12467
peptide synthase; Provisional
 1-85 3.61e-23

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 91.38  E-value: 3.61e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077    1 IINVYGPTETTIDASTWQLPpaeSEAIAQLPAiLPIGQPLANYQAYVLDAHWQLAAMGVEGELFLGGAGLARGYLGQPGL 80
Cdd:PRK12467  3380 LTNGYGPTEAVVTVTLWKCG---GDAVCEAPY-APIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSL 3455


                   ....*
gi 1896964077   81 TAERF 85
Cdd:PRK12467  3456 TAERF 3460
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
3-85 6.94e-22

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 87.41  E-value: 6.94e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077    3 NVYGPTETTIDASTWqlpPAESEAIAQLP-AILPIGQPLANYQAYVLDAHWQLAAMGVEGELFLGGAGLARGYLGQPGLT 81
Cdd:PRK10252   747 NLYGPTEAAVDVSWY---PAFGEELAAVRgSSVPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLT 823


                   ....
gi 1896964077   82 AERF 85
Cdd:PRK10252   824 ASRF 827
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
 1-85 1.84e-20

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: 83.22  E-value: 1.84e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077   1 IINVYGPTETTIDASTWQLPPAEseaiaqlPAILPIGQPLANYQAYVLDAHWQLAAMGVEGELFLGGAGLARGYLGQPGL 80
Cdd:cd17648   235 IINAYGPTETTVTNHKRFFPGDQ-------RFDKSLGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPEL 307


                  ....*
gi 1896964077  81 TAERF 85
Cdd:cd17648   308 TAERF 312
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
 1-85 2.19e-20

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: 83.13  E-value: 2.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077   1 IINVYGPTETTIDASTWQLPPAESeaiaqlpaiLPIGQPLANYQAYVLDAHWQLAAMGVEGELFLGGAGLARGYLGQPGL 80
Cdd:cd17653   235 LYNAYGPTECTISSTMTELLPGQP---------VTIGKPIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPAL 305


                  ....*
gi 1896964077  81 TAERF 85
Cdd:cd17653   306 TASKF 310
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
 1-85 8.76e-20

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: 81.45  E-value: 8.76e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077   1 IINVYGPTETTIDASTWQLPPAESEaiaqlpaiLPIGQPLANYQAYVLDAHWQLAAMGVEGELFLGGAGLARGYLGQPGL 80
Cdd:cd17645   237 LVNNYGPTENTVVATSFEIDKPYAN--------IPIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPEL 308


                  ....*
gi 1896964077  81 TAERF 85
Cdd:cd17645   309 TAEKF 313
AMP-binding pfam00501
AMP-binding enzyme;
1-85 1.04e-18

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 78.12  E-value: 1.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077   1 IINVYGPTETTIdASTWQLPPAESEAiaqlpAILPIGQPLANYQAYVLDAHW-QLAAMGVEGELFLGGAGLARGYLGQPG 79
Cdd:pfam00501 305 LVNGYGLTETTG-VVTTPLPLDEDLR-----SLGSVGRPLPGTEVKIVDDETgEPVPPGEPGELCVRGPGVMKGYLNDPE 378


                  ....*.
gi 1896964077  80 LTAERF 85
Cdd:pfam00501 379 LTAEAF 384
PRK12316 PRK12316
peptide synthase; Provisional
 1-85 2.37e-18

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 77.69  E-value: 2.37e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077    1 IINVYGPTETTIDASTWQLppaeseaIAQLPAILPIGQPLANYQAYVLDAHWQLAAMGVEGELFLGGAGLARGYLGQPGL 80
Cdd:PRK12316  3337 LYNLYGPTEATITVTHWQC-------VEEGKDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGL 3409


                   ....*
gi 1896964077   81 TAERF 85
Cdd:PRK12316  3410 TAERF 3414
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
 6-85 1.97e-17

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: 75.00  E-value: 1.97e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077   6 GPTETTIDASTWQLPPAESEaiaqlPAILPIGQPLANYQAYVLDAHWQLAAMGVEGELFLGGAGLARGYLGQPGLTAERF 85
Cdd:cd12114   277 GATEASIWSIYHPIDEVPPD-----WRSIPYGRPLANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARF 351
PRK05691 PRK05691
peptide synthase; Validated
 3-85 4.12e-17

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 74.05  E-value: 4.12e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077    3 NVYGPTETTIdastwqlPPAESEAIAQLP---AILPIGQPLANYQAYVLDAHWQLAAMGVEGELFLGGAGLARGYLGQPG 79
Cdd:PRK05691  2479 NAYGPTETVV-------MPLACLAPEQLEegaASVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPG 2551


                   ....*.
gi 1896964077   80 LTAERF 85
Cdd:PRK05691  2552 LTAERF 2557
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
 3-85 5.81e-17

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: 73.66  E-value: 5.81e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077   3 NVYGPTETTIdASTWQLPPAeseaiAQLPAILPIGQPLANYQAYVLDAHWQLAAMGVEGELFLGGAGLARGYLGQPGLTA 82
Cdd:cd17656   276 NHYGPSETHV-VTTYTINPE-----AEIPELPPIGKPISNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTA 349


                  ...
gi 1896964077  83 ERF 85
Cdd:cd17656   350 EKF 352
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
 1-85 1.31e-16

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: 72.28  E-value: 1.31e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077   1 IINVYGPTETTIDASTWQLPPaesEAIAQLPAiLPIGQPLANYQAYVLDAHWQLAAMGVEGELFLGGAGLARGYLGQPGL 80
Cdd:cd05945   243 IYNTYGPTEATVAVTYIEVTP---EVLDGYDR-LPIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEK 318


                  ....*
gi 1896964077  81 TAERF 85
Cdd:cd05945   319 TAAAF 323
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
 1-85 1.53e-15

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: 69.49  E-value: 1.53e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077   1 IINVYGPTETTIdASTWQLPPAESEAiaqlpaiLPIGQPLANyQAYVLDA--HWQLAAMGVEGELFLGGAGLARGYLGQP 78
Cdd:cd05918   241 LINAYGPAECTI-AATVSPVVPSTDP-------RNIGRPLGA-TCWVVDPdnHDRLVPIGAVGELLIEGPILARGYLNDP 311


                  ....*..
gi 1896964077  79 GLTAERF 85
Cdd:cd05918   312 EKTAAAF 318
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
 1-85 1.09e-13

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: 64.32  E-value: 1.09e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077    1 IINVYGPTETTIDASTWQLPP--AESEAIAQLPAILPIGQPLANYQAYVLDAH--WQLAAMGVEGELFLGGAGLARGYLG 76
Cdd:TIGR03443  558 IVNMYGTTETQRAVSYFEIPSrsSDSTFLKNLKDVMPAGKGMKNVQLLVVNRNdrTQTCGVGEVGEIYVRAGGLAEGYLG 637


                   ....*....
gi 1896964077   77 QPGLTAERF 85
Cdd:TIGR03443  638 LPELNAEKF 646
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
 1-85 5.54e-12

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: 59.44  E-value: 5.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077   1 IINVYGPTETTIDASTwqlPPAEseaiAQLPAILPIGQPLANYQAYVLDAHWQLAAMGVEGELFLGGAGLARGYLGQPGL 80
Cdd:COG0318   243 IVEGYGLTETSPVVTV---NPED----PGERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEA 315


                  ....*
gi 1896964077  81 TAERF 85
Cdd:COG0318   316 TAEAF 320
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
1-85 9.47e-12

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 58.75  E-value: 9.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077   1 IINVYGPTETTIDASTWQLPPaesEAIAQLPAiLPIGQPLANYQAYVLDAHWQLAAMGVEGELFLGGAGLARGYLGQPGL 80
Cdd:PRK04813  289 IYNTYGPTEATVAVTSIEITD---EMLDQYKR-LPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEK 364


                  ....*
gi 1896964077  81 TAERF 85
Cdd:PRK04813  365 TAEAF 369
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
 1-85 1.60e-11

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: 57.91  E-value: 1.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077   1 IINVYGPTETTIDASTWQLPPAESEA--IAQLPAILPIGQPLANYQAYVLDAH--WQLAAMGVEGELFLGGAGLARGYLG 76
Cdd:cd17647   252 IVNMYGTTETQRAVSYFEVPSRSSDPtfLKNLKDVMPAGRGMLNVQLLVVNRNdrTQICGIGEVGEIYVRAGGLAEGYRG 331


                  ....*....
gi 1896964077  77 QPGLTAERF 85
Cdd:cd17647   332 LPELNKEKF 340
PRK05691 PRK05691
peptide synthase; Validated
 1-85 7.21e-11

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 56.33  E-value: 7.21e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077    1 IINVYGPTETTIDASTWQLPPAESEAiaqlpAILPIGQPLANYQAYVLDAHWQLAAMGVEGELFLGGAGLARGYLGQPGL 80
Cdd:PRK05691  4012 LVNAYGPAECSDDVAFFRVDLASTRG-----SYLPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLR 4086


                   ....*
gi 1896964077   81 TAERF 85
Cdd:PRK05691  4087 TALAF 4091
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
 1-85 4.28e-08

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: 48.44  E-value: 4.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077   1 IINVYGPTETTIDASTWqLPPAESEAIAqlpailPIGQPLANYQAYVLDAHWQLAAMGVEGELFLGGAGLARGYLGQPGL 80
Cdd:cd04433   142 LVNGYGLTETGGTVATG-PPDDDARKPG------SVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEA 214


                  ....*
gi 1896964077  81 TAERF 85
Cdd:cd04433   215 TAAVD 219
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
 1-78 1.20e-07

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: 47.08  E-value: 1.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077   1 IINVYGPTETTIDASTWQLPPAESEaiaqlpaiLPIGQPLANYQAYVLDahwqLAAMGVEGELFLGG---AGLARGYLGQ 77
Cdd:cd17654   268 IFNIYGITEVSCWALAYKVPEEDSP--------VQLGSPLLGTVIEVRD----QNGSEGTGQVFLGGlnrVCILDDEVTV 335


                  .
gi 1896964077  78 P 78
Cdd:cd17654   336 P 336
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
 36-85 4.13e-06

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: 42.55  E-value: 4.13e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1896964077  36 IGQPLANYQAYVLDAHWQLAAMGVEGELFLGGAGLARGYLGQPGLTAERF 85
Cdd:cd05936   297 IGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAF 346
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
 1-85 6.32e-05

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 39.40  E-value: 6.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077   1 IINVYGPTETTIDASTwqLPPaESEAIAQLPAILPIGQPLANYQAYVLDAHWQ-LAAMGVE-GELFLGGAGLARGYLGQP 78
Cdd:PRK06187  309 LVQGYGMTETSPVVSV--LPP-EDQLPGQWTKRRSAGRPLPGVEARIVDDDGDeLPPDGGEvGEIIVRGPWLMQGYWNRP 385


                  ....*..
gi 1896964077  79 GLTAERF 85
Cdd:PRK06187  386 EATAETI 392
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
 1-85 1.79e-04

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: 38.10  E-value: 1.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077   1 IINVYGPTETTIDASTwqLPPAESEAiaqlpAILPIGQPLANYQAYVLDAhwqLAAMGVEGELFLGGAGLARGYLGQPGL 80
Cdd:cd05912   216 VYQSYGMTETCSQIVT--LSPEDALN-----KIGSAGKPLFPVELKIEDD---GQPPYEVGEILLKGPNVTKGYLNRPDA 285


                  ....*
gi 1896964077  81 TAERF 85
Cdd:cd05912   286 TEESF 290
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 1-85 1.81e-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. Members of this family include DitJ from Pseudomonas and similar proteins.


Pssm-ID: 341257 [Multi-domain]  Cd Length: 422  Bit Score: 38.04  E-value: 1.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077   1 IINVYGPTETTIdaSTWQLPPAeseaiAQLPAilPIGQPLANYQAYVLDAHWQLAAMGVEGELFL---GGAGLARGYLGQ 77
Cdd:cd05934   222 LLEGYGMTETIV--GVIGPRDE-----PRRPG--SIGRPAPGYEVRIVDDDGQELPAGEPGELVIrglRGWGFFKGYYNM 292


                  ....*...
gi 1896964077  78 PGLTAERF 85
Cdd:cd05934   293 PEATAEAM 300
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
 1-85 6.20e-04

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: 36.43  E-value: 6.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077   1 IINVYGPTETTIDASTwqLPPAESEAiaqlpAILPIGQPLANYQAYVLDAHWQLAAMGVEGELFLGGAGLARGYLGQPGL 80
Cdd:cd17631   240 FVQGYGMTETSPGVTF--LSPEDHRR-----KLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEA 312


                  ....*
gi 1896964077  81 TAERF 85
Cdd:cd17631   313 TAAAF 317
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
 37-85 1.06e-03

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: 36.06  E-value: 1.06e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1896964077  37 GQPLANYQAYVLDA-HWQLAAMGVEGELFLGGAGLARGYLGQPGLTAERF 85
Cdd:cd05931   358 GRPLPDQEVRIVDPeTGRELPDGEVGEIWVRGPSVASGYWGRPEATAETF 407
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
 1-85 1.93e-03

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: 35.05  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077   1 IINVYGPTETTidASTWQLPPAESEAIAQLPailpiGQPLANYQAYVLDAHWQLAAMGVEGELFLGGAGLARGYLGQPGL 80
Cdd:cd05903   236 VCSAYGSTECP--GAVTSITPAPEDRRLYTD-----GRPLPGVEIKVVDDTGATLAPGVEGELLSRGPSVFLGYLDRPDL 308


                  ....*
gi 1896964077  81 TAERF 85
Cdd:cd05903   309 TADAA 313
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
 1-85 2.88e-03

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: 34.60  E-value: 2.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077   1 IINVYGPTETTIDASTWQLPPAEseaiaqlPAILPIGQPLANyQAYVLDAHWQLAAMGVEGELFLGGAGLARGYLGQPGL 80
Cdd:cd05926   293 VLEAYGMTEAAHQMTSNPLPPGP-------RKPGSVGKPVGV-EVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEA 364


                  ....*
gi 1896964077  81 TAERF 85
Cdd:cd05926   365 NAEAA 369
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
 1-83 3.39e-03

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 34.41  E-value: 3.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077   1 IINVYGPTETTidastwqlPPAESEAIAQLPAILPIGQPLANYQAYVLDAHWQLAAMGVEGELFLGGAGLARGYLGQPGL 80
Cdd:PRK12492  361 IVEGYGLTETS--------PVASTNPYGELARLGTVGIPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQQPEA 432


                  ...
gi 1896964077  81 TAE 83
Cdd:PRK12492  433 TAE 435
PRK06188 PRK06188
acyl-CoA synthetase; Validated
 37-85 5.08e-03

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 33.81  E-value: 5.08e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1896964077  37 GQPLANYQAYVLDAHWQLAAMGVEGELFLGGAGLARGYLGQPGLTAERF 85
Cdd:PRK06188  342 GRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF 390
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
 1-85 9.71e-03

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: 32.96  E-value: 9.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896964077   1 IINVYGPTETTIDASTWQLPPAESEAIaqlpailpiGQPLANYQAYVLDAHW-QLAAMGVEGELFLGGAGLARGYLGQPG 79
Cdd:cd05911   291 IKQGYGMTETGGILTVNPDGDDKPGSV---------GRLLPNVEAKIVDDDGkDSLGPNEPGEICVRGPQVMKGYYNNPE 361


                  ....*.
gi 1896964077  80 LTAERF 85
Cdd:cd05911   362 ATKETF 367
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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