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CAZyme Information: MGYG000001453_00487
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Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | Aneurinibacillus aneurinilyticus | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes; Bacilli; Aneurinibacillales; Aneurinibacillaceae; Aneurinibacillus; Aneurinibacillus aneurinilyticus | |||||||||||
| CAZyme ID | MGYG000001453_00487 | |||||||||||
| CAZy Family | GT2 | |||||||||||
| CAZyme Description | Linear gramicidin synthase subunit B | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 29340; End: 33917 Strand: - | |||||||||||
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| PRK10252 | entF | 0.0 | 8 | 1054 | 9 | 1059 | enterobactin non-ribosomal peptide synthetase EntF. |
| cd17644 | A_NRPS_ApnA-like | 0.0 | 458 | 957 | 1 | 465 | 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. |
| cd17643 | A_NRPS_Cytc1-like | 0.0 | 471 | 956 | 1 | 450 | 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. |
| PRK05691 | PRK05691 | 0.0 | 8 | 1513 | 1730 | 3245 | peptide synthase; Validated |
| PRK12316 | PRK12316 | 0.0 | 7 | 1491 | 1557 | 3024 | peptide synthase; Provisional |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| BAY90071.1 | 1.04e-222 | 183 | 1038 | 304 | 1175 |
| BAZ00088.1 | 1.64e-215 | 225 | 1038 | 349 | 1176 |
| BAY30132.1 | 1.64e-215 | 225 | 1038 | 349 | 1178 |
| BAZ75991.1 | 1.64e-215 | 225 | 1038 | 349 | 1176 |
| AFY93865.1 | 9.30e-180 | 431 | 1017 | 305 | 905 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 6N8E_A | 2.45e-155 | 8 | 1011 | 31 | 1042 | Crystalstructure of holo-ObiF1, a five domain nonribosomal peptide synthetase from Burkholderia diffusa [Burkholderia diffusa] |
| 6P1J_A | 4.31e-150 | 7 | 956 | 6 | 964 | 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] |
| 6MFZ_A | 3.83e-148 | 1 | 1037 | 780 | 1794 | Crystalstructure of dimodular LgrA in a condensation state [Brevibacillus parabrevis],6MFZ_B Crystal structure of dimodular LgrA in a condensation state [Brevibacillus parabrevis] |
| 5U89_A | 1.31e-141 | 436 | 1484 | 4 | 1045 | Crystalstructure of a cross-module fragment from the dimodular NRPS DhbF [Geobacillus sp. Y4.1MC1] |
| 4D4G_A | 1.99e-130 | 457 | 995 | 30 | 573 | Understandingbi-specificity of A-domains [Planktothrix agardhii],4D4H_A Understanding bi-specificity of A-domains [Planktothrix agardhii],4D4I_A Understanding bi-specificity of A-domains [Planktothrix agardhii],4D56_A Understanding bi-specificity of A-domains [Planktothrix agardhii],4D57_A Understanding bi-specificity of A-domains [Planktothrix agardhii] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q70LM5 | 3.00e-318 | 8 | 1513 | 1075 | 2596 | Linear gramicidin synthase subunit C OS=Brevibacillus parabrevis OX=54914 GN=lgrC PE=3 SV=1 |
| Q70LM6 | 8.78e-315 | 1 | 1524 | 3627 | 5154 | Linear gramicidin synthase subunit B OS=Brevibacillus parabrevis OX=54914 GN=lgrB PE=1 SV=1 |
| Q70LM4 | 3.99e-287 | 8 | 1514 | 1058 | 2570 | Linear gramicidin synthase subunit D OS=Brevibacillus parabrevis OX=54914 GN=lgrD PE=1 SV=1 |
| P39846 | 1.72e-274 | 7 | 1521 | 1056 | 2559 | Plipastatin synthase subunit B OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsB PE=1 SV=1 |
| P27206 | 6.62e-253 | 7 | 1516 | 2101 | 3584 | Surfactin synthase subunit 1 OS=Bacillus subtilis (strain 168) OX=224308 GN=srfAA PE=1 SV=4 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000063 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |