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Conserved domains on  [gi|2582602089|ref|WP_311613021|]
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AMP-binding protein, partial [Streptomyces sp. DSM 41859]

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, ...
 2-85 3.32e-24

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 cd12117:

Pssm-ID: 473059 [Multi-domain]  Cd Length: 483  Bit Score: 93.80  E-value: 3.32e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582602089   2 THRSVVDLAVDPAW-EITADDRVLMQAPHAFDGSTYELWAPLLAGATVVIAPPGEL-TAARVRDLTHTHHLTTISLTAGL 79
Cdd:cd12117   157 THRGVVRLVKNTNYvTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLlDPDALGALIAEEGVTVLWLTAAL 236


                  ....*.
gi 2582602089  80 FSVLAE 85
Cdd:cd12117   237 FNQLAD 242
 
Name Accession Description Interval E-value
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
 2-85 3.32e-24

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: 93.80  E-value: 3.32e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582602089   2 THRSVVDLAVDPAW-EITADDRVLMQAPHAFDGSTYELWAPLLAGATVVIAPPGEL-TAARVRDLTHTHHLTTISLTAGL 79
Cdd:cd12117   157 THRGVVRLVKNTNYvTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLlDPDALGALIAEEGVTVLWLTAAL 236


                  ....*.
gi 2582602089  80 FSVLAE 85
Cdd:cd12117   237 FNQLAD 242
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
 2-85 3.12e-18

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: 76.92  E-value: 3.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582602089   2 THRSVVDLAVD--PAWEITADDRVLMQAPHAFDGSTYELWAPLLAGATVVIAPPGEL--TAARVRDLTHTHHLTTISLTA 77
Cdd:TIGR01733 141 THRSLVNLLAWlaRRYGLDPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEErdDAALLAALIAEHPVTVLNLTP 220


                  ....*...
gi 2582602089  78 GLFSVLAE 85
Cdd:TIGR01733 221 SLLALLAA 228
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 1-85 4.61e-15

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: 68.34  E-value: 4.61e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582602089    1 MTHRSVVDLAVD--PAWEITADDRVLMQAPHAFDGSTYELWAPLLAGATVVIAPPGELT-AARVRDLTHTHHLTTISLTA 77
Cdd:COG1020    637 VEHRALVNLLAWmqRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRdPAALAELLARHRVTVLNLTP 716


                   ....*...
gi 2582602089   78 GLFSVLAE 85
Cdd:COG1020    717 SLLRALLD 724
PRK12316 PRK12316
peptide synthase; Provisional
 3-85 1.04e-12

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 61.51  E-value: 1.04e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582602089    3 HRSVVDL--AVDPAWEITADDRVLMQAPHAFDGSTYELWAPLLAGATVVIAPPGELTAARVRDLTHTHHLTTISLTAGLF 80
Cdd:PRK12316  4716 HGSLVNHlhATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSLWDPERLYAEIHEHRVTVLVFPPVYL 4795


                   ....*
gi 2582602089   81 SVLAE 85
Cdd:PRK12316  4796 QQLAE 4800
AMP-binding pfam00501
AMP-binding enzyme;
1-85 5.07e-09

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 50.77  E-value: 5.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582602089   1 MTHRSVVDLAV------DPAWEITADDRVLMQAPHAFDGS-TYELWAPLLAGATVVIAPPGE-LTAARVRDLTHTHHLTT 72
Cdd:pfam00501 175 LTHRNLVANVLsikrvrPRGFGLGPDDRVLSTLPLFHDFGlSLGLLGPLLAGATVVLPPGFPaLDPAALLELIERYKVTV 254

                          90
                  ....*....|...
gi 2582602089  73 ISLTAGLFSVLAE 85
Cdd:pfam00501 255 LYGVPTLLNMLLE 267
 
Name Accession Description Interval E-value
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
 2-85 3.32e-24

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: 93.80  E-value: 3.32e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582602089   2 THRSVVDLAVDPAW-EITADDRVLMQAPHAFDGSTYELWAPLLAGATVVIAPPGEL-TAARVRDLTHTHHLTTISLTAGL 79
Cdd:cd12117   157 THRGVVRLVKNTNYvTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLlDPDALGALIAEEGVTVLWLTAAL 236


                  ....*.
gi 2582602089  80 FSVLAE 85
Cdd:cd12117   237 FNQLAD 242
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
 2-85 3.12e-18

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: 76.92  E-value: 3.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582602089   2 THRSVVDLAVD--PAWEITADDRVLMQAPHAFDGSTYELWAPLLAGATVVIAPPGEL--TAARVRDLTHTHHLTTISLTA 77
Cdd:TIGR01733 141 THRSLVNLLAWlaRRYGLDPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEErdDAALLAALIAEHPVTVLNLTP 220


                  ....*...
gi 2582602089  78 GLFSVLAE 85
Cdd:TIGR01733 221 SLLALLAA 228
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
 2-85 2.11e-15

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: 69.09  E-value: 2.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582602089   2 THRSVVDL--AVDPAWEITADDRVLMQAPHAFDGSTYELWAPLLAGATVVIAPPGE-LTAARVRDLTHTHHLTTISLTAG 78
Cdd:cd05930   114 EHRGLVNLllWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVrKDPEALADLLAEEGITVLHLTPS 193


                  ....*..
gi 2582602089  79 LFSVLAE 85
Cdd:cd05930   194 LLRLLLQ 200
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 1-85 4.61e-15

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: 68.34  E-value: 4.61e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582602089    1 MTHRSVVDLAVD--PAWEITADDRVLMQAPHAFDGSTYELWAPLLAGATVVIAPPGELT-AARVRDLTHTHHLTTISLTA 77
Cdd:COG1020    637 VEHRALVNLLAWmqRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRdPAALAELLARHRVTVLNLTP 716


                   ....*...
gi 2582602089   78 GLFSVLAE 85
Cdd:COG1020    717 SLLRALLD 724
PRK12316 PRK12316
peptide synthase; Provisional
 3-85 1.04e-12

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 61.51  E-value: 1.04e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582602089    3 HRSVVDL--AVDPAWEITADDRVLMQAPHAFDGSTYELWAPLLAGATVVIAPPGELTAARVRDLTHTHHLTTISLTAGLF 80
Cdd:PRK12316  4716 HGSLVNHlhATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSLWDPERLYAEIHEHRVTVLVFPPVYL 4795


                   ....*
gi 2582602089   81 SVLAE 85
Cdd:PRK12316  4796 QQLAE 4800
PRK12467 PRK12467
peptide synthase; Provisional
 2-85 6.63e-12

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 59.40  E-value: 6.63e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582602089    2 THRSVVDL--AVDPAWEITADDRVLMQAPHAFDGSTYELWAPLLAGATVVIAPPGE-LTAARVRDLTHTHHLTTISLTAG 78
Cdd:PRK12467  1739 RHGALVNRlcATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAhRDPEQLIQLIERQQVTTLHFVPS 1818


                   ....*..
gi 2582602089   79 LFSVLAE 85
Cdd:PRK12467  1819 MLQQLLQ 1825
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
 2-83 5.04e-11

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: 56.49  E-value: 5.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582602089   2 THRSVVDLAVD--PAWEITADDRVLMQAPHAFDGSTYELWAPLLAGATVVIAPPGELTA-ARVRDLTHTHHLTTISLTAG 78
Cdd:cd17652   114 THRGLANLAAAqiAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPgEPLADLLREHRITHVTLPPA 193


                  ....*
gi 2582602089  79 LFSVL 83
Cdd:cd17652   194 ALAAL 198
PRK12467 PRK12467
peptide synthase; Provisional
 14-85 3.29e-10

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 54.40  E-value: 3.29e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2582602089   14 AWEITADDRVLMQAPHAFDGSTYELWAPLLAGATVVIAPPGELTAARVRDLTHTHHLTTISLTAGLFSVLAE 85
Cdd:PRK12467  3272 AYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDNDLWDPEELWQAIHAHRISIACFPPAYLQQFAE 3343
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
 17-72 1.21e-09

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: 52.66  E-value: 1.21e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2582602089  17 ITADDRVLMQAPHAFDGSTYELWAPLLAGATVVIAPPGELT-AARVRDLTHTHHLTT 72
Cdd:cd17646   176 LGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRdPAYLAALIREHGVTT 232
AMP-binding pfam00501
AMP-binding enzyme;
1-85 5.07e-09

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 50.77  E-value: 5.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582602089   1 MTHRSVVDLAV------DPAWEITADDRVLMQAPHAFDGS-TYELWAPLLAGATVVIAPPGE-LTAARVRDLTHTHHLTT 72
Cdd:pfam00501 175 LTHRNLVANVLsikrvrPRGFGLGPDDRVLSTLPLFHDFGlSLGLLGPLLAGATVVLPPGFPaLDPAALLELIERYKVTV 254

                          90
                  ....*....|...
gi 2582602089  73 ISLTAGLFSVLAE 85
Cdd:pfam00501 255 LYGVPTLLNMLLE 267
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
17-54 7.60e-09

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 50.43  E-value: 7.60e-09
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2582602089   17 ITADDRVLMQAPHAFDGSTYELWAPLLAGATVVIAPPG 54
Cdd:PRK10252   636 LTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPE 673
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
 2-85 1.06e-08

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: 50.00  E-value: 1.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582602089   2 THRSVVDL--AVDPAWEITADDRVLMQAPHAFDGSTYELWAPLLAGATVVIAPPG-ELTAARVRDLTHTHHLTTISLTAG 78
Cdd:cd17643   114 SHANVLALfaATQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEvARSPEDFARLLRDEGVTVLNQTPS 193


                  ....*..
gi 2582602089  79 LFSVLAE 85
Cdd:cd17643   194 AFYQLVE 200
PRK12316 PRK12316
peptide synthase; Provisional
 2-75 1.66e-08

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 49.57  E-value: 1.66e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2582602089    2 THRSVVDL--AVDPAWEITADDRVLMQAPHAFDGSTYELWAPLLAGATVVIAPPGELT-AARVRDLTHTHHLTTISL 75
Cdd:PRK12316   676 RHRALSNRlcWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRdPAKLVELINREGVDTLHF 752
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
 1-52 6.98e-08

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: 47.54  E-value: 6.98e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2582602089   1 MTHRSVVD--LAVDPAWEITADDRVLMQAPHAFDGSTYELWAPLLAGATVVIAP 52
Cdd:cd05918   126 IEHRALSTsaLAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPS 179
PRK12467 PRK12467
peptide synthase; Provisional
 3-83 1.64e-07

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 46.69  E-value: 1.64e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582602089    3 HRSVVDL--AVDPAWEITADDRVLMQAPHAFDGSTYELWAPLLAGATVVIAPPGEL-TAARVRDLTHTHHLTTISLTAGL 79
Cdd:PRK12467   678 HGALANYvcVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCArDAEAFAALMADQGVTVLKIVPSH 757


                   ....
gi 2582602089   80 FSVL 83
Cdd:PRK12467   758 LQAL 761
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
 3-79 3.24e-07

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: 46.01  E-value: 3.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582602089   3 HRSVVDLAV--DPAWEITADDRVLMQAPHAFDGSTYELWAPLLAGATVVIAPPG-ELTAARVRDLTHTHHLTTISLTAGL 79
Cdd:cd17645   126 HHNLVNLCEwhRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSErRLDLDALNDYFNQEGITISFLPTGA 205
PRK12316 PRK12316
peptide synthase; Provisional
 10-85 3.54e-07

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 45.72  E-value: 3.54e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2582602089   10 AVDPAWEITADDRVLMQAPHAFDGSTYELWAPLLAGATVVIAPPGELTAARVRDLTHTHHLTTISLTAGLFSVLAE 85
Cdd:PRK12316  2177 AAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDELWDPEQLYDEMERHGVTILDFPPVYLQQLAE 2252
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
 14-85 5.36e-07

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: 45.05  E-value: 5.36e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2582602089  14 AWEITADDRVLMQAPHAFDGSTYELWAPLLAGATVVIAPPGE-LTAARVRDLTHTHHLTTISLTAGLFSVLAE 85
Cdd:cd17649   129 RYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELwASADELAEMVRELGVTVLDLPPAYLQQLAE 201
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
 2-85 7.44e-07

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: 44.63  E-value: 7.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582602089   2 THRSVVDL--AVDPAWEITADDRVLMQAPHAFDGSTYELWAPLLAGATVVIAPPGELT-AARVRDLTHTHHLTTISLTAG 78
Cdd:cd17655   158 EHRGVVNLveWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLdGQALTQYIRQNRITIIDLTPA 237


                  ....*..
gi 2582602089  79 LFSVLAE 85
Cdd:cd17655   238 HLKLLDA 244
PRK05691 PRK05691
peptide synthase; Validated
 20-85 8.38e-07

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 44.77  E-value: 8.38e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2582602089   20 DDRVLMQ-APHAFDGSTYELWAPLLAGATVVIAPPGE-LTAARVRDLTHTHHLTTISLTAGLFSVLAE 85
Cdd:PRK05691  1313 DSDVLMQkAPISFDVSVWECFWPLITGCRLVLAGPGEhRDPQRIAELVQQYGVTTLHFVPPLLQLFID 1380
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
 1-85 8.60e-07

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: 44.64  E-value: 8.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582602089   1 MTHRSVVDL--AVDPAWEITADDRVLMQAPHAFDGSTYELWAPLLAGATVVIAPPGELT-AARVRDLTHTHHLTTISLTA 77
Cdd:cd17651   156 MPHRSLANLvaWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTdPPALAAWLDEQRISRVFLPT 235


                  ....*...
gi 2582602089  78 GLFSVLAE 85
Cdd:cd17651   236 VALRALAE 243
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
 2-71 1.21e-06

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: 44.18  E-value: 1.21e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2582602089   2 THRSVVD--LAVDPAWEITADDRVLMQAPHAFDGSTYELWAPLLAGATVVIAPPGELT-AARVRDLTHTHHLT 71
Cdd:cd12114   147 SHRAALNtiLDINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRdPAHWAELIERHGVT 219
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
 2-54 5.17e-06

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: 42.28  E-value: 5.17e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2582602089   2 THRSVVDL--AVDPAWEITADDRVLMQAPHAFDGSTYELWAPLLAGATVVIAPPG 54
Cdd:cd12116   147 SHRNLVNFlhSMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRE 201
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
 1-52 6.59e-06

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: 42.04  E-value: 6.59e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2582602089   1 MTHRSVVDLA--VDPAWEITADDRVLMQAPHAFDGSTYELWAPLLAGATVVIAP 52
Cdd:cd17644   126 IEHQSLVNLShgLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRP 179
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
 1-56 1.97e-05

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: 40.69  E-value: 1.97e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2582602089   1 MTHRSVVDLA--VDPAWEITADDRVLMQAPHAFDGSTYELWAPLLAGATVVIAPPGEL 56
Cdd:cd05945   117 ISHDNLVSFTnwMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDAT 174
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 17-84 7.00e-05

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 39.35  E-value: 7.00e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2582602089  17 ITADDRVLMQAPHAFDGSTYELWAPLLAGATVVIAPPGELTAARVRDLTHtHHLTTISLTAGLFSVLA 84
Cdd:cd05922   155 ITADDRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVLDDAFWEDLRE-HGATGLAGVPSTYAMLT 221
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
 1-52 1.14e-04

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


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 38.73  E-value: 1.14e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2582602089   1 MTHRSVVDLAVDPA--WEITADDRVLMQAP--HAFdGSTYELWAPLLAGATVVIAP 52
Cdd:PRK07656  186 LTHRQLLSNAADWAeyLGLTEGDRYLAANPffHVF-GYKAGVNAPLMRGATILPLP 240
PRK12316 PRK12316
peptide synthase; Provisional
 10-85 1.33e-04

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 38.40  E-value: 1.33e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2582602089   10 AVDPAWEITADDRVLMQAPHAFDGSTYELWAPLLAGATVVIAPPGELTAAR-VRDLTHTHHLTTISLTAGLFSVLAE 85
Cdd:PRK12316  3227 WMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPAlLVELINSEGVDVLHAYPSMLQAFLE 3303
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
 1-85 2.31e-04

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: 37.65  E-value: 2.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582602089   1 MTHRSVVDLAVDPAW--EITADDRVLMQAPHAFDGSTYELWAPLLAGATVVIAPPGEltAARVRDLTHTHHLTTISLTAG 78
Cdd:cd04433    20 LSHRNLLAAAAALAAsgGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFD--PEAALELIEREKVTILLGVPT 97


                  ....*..
gi 2582602089  79 LFSVLAE 85
Cdd:cd04433    98 LLARLLK 104
PRK05691 PRK05691
peptide synthase; Validated
 31-85 6.71e-04

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 36.68  E-value: 6.71e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2582602089   31 FDGSTYELWAPLLAGATVVIAPPGELTAARVRDLTHTHHLTTISLTAGLFSVLAE 85
Cdd:PRK05691  2385 FDAASERLLVPLLCGARVVLRAQGQWGAEEICQLIREQQVSILGFTPSYGSQLAQ 2439
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
 17-80 8.63e-03

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: 33.21  E-value: 8.63e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2582602089  17 ITADDRVLMQAPHAFDGSTYELWAPLLAGATVVIAPPG-ELTAARVRDLTHTHH-LTTISLTAGLF 80
Cdd:cd17654   156 ITSEDILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSvKVLPSKLADILFKRHrITVLQATPTLF 221
 
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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