| Species | Kurthia senegalensis | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes; Bacilli; Bacillales_A; Planococcaceae; Kurthia; Kurthia senegalensis | |||||||||||
| CAZyme ID | MGYG000002309_00254 | |||||||||||
| CAZy Family | GT2 | |||||||||||
| CAZyme Description | Dimodular nonribosomal peptide synthase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 15858; End: 18812 Strand: - | |||||||||||
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| PRK12467 | PRK12467 | 0.0 | 11 | 709 | 1439 | 2159 | peptide synthase; Provisional |
| PRK10252 | entF | 0.0 | 98 | 968 | 413 | 1287 | enterobactin non-ribosomal peptide synthetase EntF. |
| cd05930 | A_NRPS | 0.0 | 162 | 631 | 5 | 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 | 0.0 | 11 | 705 | 374 | 1089 | peptide synthase; Provisional |
| cd17643 | A_NRPS_Cytc1-like | 0.0 | 160 | 631 | 3 | 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. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| BAY90071.1 | 8.96e-160 | 5 | 737 | 437 | 1201 |
| BAZ00088.1 | 1.88e-158 | 11 | 713 | 444 | 1178 |
| BAZ75991.1 | 1.88e-158 | 11 | 713 | 444 | 1178 |
| BAY30132.1 | 8.62e-158 | 11 | 713 | 444 | 1180 |
| AFZ04852.1 | 1.63e-137 | 5 | 832 | 443 | 1306 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 6N8E_A | 4.70e-136 | 65 | 770 | 403 | 1128 | Crystalstructure of holo-ObiF1, a five domain nonribosomal peptide synthetase from Burkholderia diffusa [Burkholderia diffusa] |
| 4ZXH_A | 1.38e-129 | 3 | 832 | 325 | 1162 | ChainA, ABBFA_003403 [Acinetobacter baumannii AB307-0294],4ZXI_A Chain A, Tyrocidine synthetase 3 [Acinetobacter baumannii AB307-0294] |
| 5U89_A | 3.21e-125 | 126 | 717 | 6 | 606 | Crystalstructure of a cross-module fragment from the dimodular NRPS DhbF [Geobacillus sp. Y4.1MC1] |
| 5JA1_A | 3.45e-117 | 24 | 968 | 339 | 1286 | EntF,a Terminal Nonribosomal Peptide Synthetase Module Bound to the MbtH-Like Protein YbdZ [Escherichia coli K-12],5JA2_A EntF, a Terminal Nonribosomal Peptide Synthetase Module Bound to the non-Native MbtH-Like Protein PA2412 [Escherichia coli K-12],5T3D_A Crystal structure of holo-EntF a nonribosomal peptide synthetase in the thioester-forming conformation [Escherichia coli K-12] |
| 6MFZ_A | 2.50e-115 | 5 | 709 | 1089 | 1793 | 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 | 7.56e-278 | 1 | 972 | 1365 | 2370 | Dimodular nonribosomal peptide synthase OS=Bacillus subtilis (strain 168) OX=224308 GN=dhbF PE=1 SV=4 |
| P39846 | 9.80e-149 | 5 | 709 | 1361 | 2072 | Plipastatin synthase subunit B OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsB PE=1 SV=1 |
| P0DUV3 | 8.03e-142 | 27 | 972 | 4582 | 5525 | Malpicyclin synthetase OS=Mortierella alpina OX=64518 GN=mpcA PE=1 SV=1 |
| P0DUV4 | 1.39e-139 | 27 | 971 | 4592 | 5534 | Malpibaldin synthetase OS=Mortierella alpina OX=64518 GN=mpbA PE=1 SV=1 |
| Q0E7C4 | 1.23e-128 | 31 | 968 | 1872 | 2820 | Vanchrobactin synthase VabF OS=Vibrio anguillarum OX=55601 GN=vabF PE=3 SV=1 |
| 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 |
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