Species | Streptomyces albus | |||||||||||
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Lineage | Bacteria; Actinobacteriota; Actinomycetia; Streptomycetales; Streptomycetaceae; Streptomyces; Streptomyces albus | |||||||||||
CAZyme ID | MGYG000001443_04863 | |||||||||||
CAZy Family | GT2 | |||||||||||
CAZyme Description | D-alanine--poly(phosphoribitol) ligase subunit 1 | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 2756266; End: 2759130 Strand: + |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd17643 | A_NRPS_Cytc1-like | 0.0 | 364 | 855 | 1 | 446 | 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. |
cd05930 | A_NRPS | 1.49e-177 | 364 | 859 | 1 | 444 | 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. |
PRK12467 | PRK12467 | 6.12e-154 | 313 | 951 | 1537 | 2167 | peptide synthase; Provisional |
PRK12467 | PRK12467 | 3.46e-150 | 22 | 954 | 101 | 1104 | peptide synthase; Provisional |
cd12117 | A_NRPS_Srf_like | 7.50e-150 | 358 | 859 | 5 | 483 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
BAY30132.1 | 6.16e-130 | 282 | 952 | 512 | 1185 |
BAZ00088.1 | 5.12e-129 | 222 | 952 | 450 | 1183 |
BAZ75991.1 | 5.12e-129 | 222 | 952 | 450 | 1183 |
BAY90071.1 | 2.17e-126 | 313 | 947 | 541 | 1177 |
AFY93865.1 | 4.60e-121 | 363 | 948 | 344 | 930 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6N8E_A | 2.11e-111 | 222 | 947 | 391 | 1066 | Crystalstructure of holo-ObiF1, a five domain nonribosomal peptide synthetase from Burkholderia diffusa [Burkholderia diffusa] |
6P1J_A | 2.24e-103 | 250 | 855 | 369 | 960 | Thestructure of condensation and adenylation domains of teixobactin-producing nonribosomal peptide synthetase Txo2 serine module [Eleftheria terrae],6P1J_B The structure of condensation and adenylation domains of teixobactin-producing nonribosomal peptide synthetase Txo2 serine module [Eleftheria terrae] |
5N9W_A | 2.04e-99 | 349 | 855 | 17 | 517 | Structureof adenylation domain THR1 involved in the biosynthesis of 4-chlorothreonine in Streptomyces SP.OH-5093, apo structure [Streptomyces sp.],5N9W_B Structure of adenylation domain THR1 involved in the biosynthesis of 4-chlorothreonine in Streptomyces SP.OH-5093, apo structure [Streptomyces sp.],5N9X_A Structure of adenylation domain THR1 involved in the biosynthesis of 4-chlorothreonine in Streptomyces SP.OH-5093, ligand bound structure [Streptomyces sp.],5N9X_B Structure of adenylation domain THR1 involved in the biosynthesis of 4-chlorothreonine in Streptomyces SP.OH-5093, ligand bound structure [Streptomyces sp.] |
3VNQ_A | 8.49e-99 | 360 | 855 | 45 | 529 | Co-crystalstructure of NRPS adenylation protein CytC1 with ATP from streptomyces [Streptomyces sp.],3VNR_A Co-crystal structure of NRPS adenylation protein CytC1 with aminobutyric acid and AMP from streptomyces [Streptomyces sp.],3VNS_A Co-crystal structure of NRPS adenylation protein CytC1 with D-valine and AMP from streptomyces [Streptomyces sp.] |
6MFZ_A | 2.87e-91 | 328 | 952 | 1203 | 1802 | Crystalstructure of dimodular LgrA in a condensation state [Brevibacillus parabrevis],6MFZ_B Crystal structure of dimodular LgrA in a condensation state [Brevibacillus parabrevis] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P45745 | 6.48e-136 | 315 | 924 | 1480 | 2084 | Dimodular nonribosomal peptide synthase OS=Bacillus subtilis (strain 168) OX=224308 GN=dhbF PE=1 SV=4 |
Q52400 | 1.03e-128 | 345 | 922 | 16 | 581 | Syringomycin synthase SyrB1 OS=Pseudomonas syringae pv. syringae OX=321 GN=syrB1 PE=1 SV=2 |
P39846 | 2.79e-119 | 270 | 944 | 1423 | 2073 | Plipastatin synthase subunit B OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsB PE=1 SV=1 |
Q70LM6 | 4.68e-101 | 288 | 946 | 4032 | 4670 | Linear gramicidin synthase subunit B OS=Brevibacillus parabrevis OX=54914 GN=lgrB PE=1 SV=1 |
Q70LM4 | 9.60e-96 | 251 | 947 | 1419 | 2093 | Linear gramicidin synthase subunit D OS=Brevibacillus parabrevis OX=54914 GN=lgrD PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000043 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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