| Species | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; TANB77; CAG-508; CAG-269; | |||||||||||
| CAZyme ID | MGYG000000375_01345 | |||||||||||
| 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: 26374; End: 30603 Strand: - | |||||||||||
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd17655 | A_NRPS_Bac | 3.25e-154 | 457 | 938 | 2 | 489 | 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. |
| cd05930 | A_NRPS | 4.96e-143 | 466 | 935 | 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 | 9.43e-128 | 29 | 1012 | 73 | 1091 | peptide synthase; Provisional |
| PRK12316 | PRK12316 | 2.18e-126 | 29 | 1015 | 73 | 1081 | peptide synthase; Provisional |
| PRK12467 | PRK12467 | 3.26e-121 | 29 | 1015 | 1140 | 2160 | peptide synthase; Provisional |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| AFZ04852.1 | 8.51e-104 | 211 | 1018 | 348 | 1183 |
| BAY90071.1 | 3.30e-94 | 211 | 1059 | 342 | 1220 |
| BAZ75991.1 | 5.85e-94 | 212 | 1019 | 344 | 1179 |
| BAZ00088.1 | 5.85e-94 | 212 | 1019 | 344 | 1179 |
| BAY30132.1 | 1.66e-89 | 8 | 988 | 2249 | 3263 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 2VSQ_A | 1.28e-92 | 33 | 1096 | 40 | 1107 | Structureof surfactin A synthetase C (SrfA-C), a nonribosomal peptide synthetase termination module [Bacillus subtilis] |
| 1AMU_A | 2.36e-86 | 453 | 964 | 40 | 555 | PhenylalanineActivating Domain Of Gramicidin Synthetase 1 In A Complex With Amp And Phenylalanine [Brevibacillus brevis],1AMU_B Phenylalanine Activating Domain Of Gramicidin Synthetase 1 In A Complex With Amp And Phenylalanine [Brevibacillus brevis] |
| 5ES5_A | 1.62e-85 | 455 | 1018 | 206 | 764 | Crystalstructure of the initiation module of LgrA in the 'open' and 'closed ' adenylation states [Brevibacillus parabrevis],5ES5_B Crystal structure of the initiation module of LgrA in the 'open' and 'closed ' adenylation states [Brevibacillus parabrevis],5ES8_A Crystal structure of the initiation module of LgrA in the thiolation state [Brevibacillus parabrevis],5ES8_B Crystal structure of the initiation module of LgrA in the thiolation state [Brevibacillus parabrevis],5ES9_A Crystal structure of the LgrA initiation module in the formylation state [Brevibacillus parabrevis],5ES9_B Crystal structure of the LgrA initiation module in the formylation state [Brevibacillus parabrevis] |
| 6MFX_A | 5.64e-83 | 455 | 1018 | 208 | 766 | Crystalstructure of a 4-domain construct of a mutant of LgrA in the substrate donation state [Brevibacillus parabrevis] |
| 6MFW_A | 1.02e-82 | 455 | 1018 | 208 | 766 | Crystalstructure of a 4-domain construct of LgrA in the substrate donation state [Brevibacillus parabrevis] |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| O68008 | 1.19e-139 | 51 | 1018 | 5130 | 6118 | Bacitracin synthase 3 OS=Bacillus licheniformis OX=1402 GN=bacC PE=3 SV=1 |
| O30409 | 2.92e-139 | 6 | 1029 | 11 | 1047 | Tyrocidine synthase 3 OS=Brevibacillus parabrevis OX=54914 GN=tycC PE=1 SV=1 |
| Q9R9I9 | 1.03e-138 | 6 | 1015 | 1326 | 2350 | Mycosubtilin synthase subunit C OS=Bacillus subtilis OX=1423 GN=mycC PE=3 SV=1 |
| Q9R9J1 | 1.46e-138 | 6 | 1022 | 2496 | 3517 | Mycosubtilin synthase subunit A OS=Bacillus subtilis OX=1423 GN=mycA PE=1 SV=1 |
| Q9R9J0 | 1.30e-137 | 6 | 1063 | 1319 | 2396 | Mycosubtilin synthase subunit B OS=Bacillus subtilis OX=1423 GN=mycB PE=3 SV=1 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000051 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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