Species | Bacillus licheniformis | |||||||||||
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Lineage | Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; Bacillus licheniformis | |||||||||||
CAZyme ID | MGYG000002357_03889 | |||||||||||
CAZy Family | GT2 | |||||||||||
CAZyme Description | Dimodular nonribosomal peptide synthase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 3723746; End: 3730903 Strand: - |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
NF038078 | NRPS_MxcG | 0.0 | 5 | 1040 | 1 | 1049 | myxochelin non-ribosomal peptide synthetase MxcG. |
PRK12467 | PRK12467 | 0.0 | 1042 | 2119 | 39 | 1108 | peptide synthase; Provisional |
PRK12467 | PRK12467 | 0.0 | 8 | 2120 | 49 | 2173 | peptide synthase; Provisional |
cd17651 | A_NRPS_VisG_like | 0.0 | 1522 | 2027 | 1 | 491 | 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. |
cd17652 | A_NRPS_CmdD_like | 0.0 | 1530 | 2027 | 1 | 436 | 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). |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QND46664.1 | 0.0 | 11 | 2245 | 563 | 2800 |
ACX49739.1 | 1.31e-291 | 10 | 1767 | 11 | 1816 |
BAZ75991.1 | 1.62e-244 | 965 | 2371 | 2140 | 3559 |
BAZ00088.1 | 1.62e-244 | 965 | 2371 | 2140 | 3559 |
BAY90071.1 | 4.35e-243 | 965 | 2371 | 2131 | 3550 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5U89_A | 0.0 | 439 | 1504 | 3 | 1072 | Crystalstructure of a cross-module fragment from the dimodular NRPS DhbF [Geobacillus sp. Y4.1MC1] |
6MFZ_A | 1.15e-273 | 464 | 2107 | 209 | 1794 | Crystalstructure of dimodular LgrA in a condensation state [Brevibacillus parabrevis],6MFZ_B Crystal structure of dimodular LgrA in a condensation state [Brevibacillus parabrevis] |
6MFY_A | 8.04e-260 | 464 | 2034 | 209 | 1720 | Crystalstructure of a 5-domain construct of LgrA in the substrate donation state [Brevibacillus parabrevis],6MG0_A Crystal structure of a 5-domain construct of LgrA in the thiolation state [Brevibacillus parabrevis],6MG0_B Crystal structure of a 5-domain construct of LgrA in the thiolation state [Brevibacillus parabrevis] |
6P1J_A | 1.02e-208 | 1054 | 2026 | 7 | 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] |
6N8E_A | 3.23e-183 | 1027 | 2269 | 11 | 1234 | Crystalstructure of holo-ObiF1, a five domain nonribosomal peptide synthetase from Burkholderia diffusa [Burkholderia diffusa] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q70LM5 | 0.0 | 7 | 2107 | 2607 | 4688 | Linear gramicidin synthase subunit C OS=Brevibacillus parabrevis OX=54914 GN=lgrC PE=3 SV=1 |
P39846 | 0.0 | 10 | 2110 | 12 | 2076 | Plipastatin synthase subunit B OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsB PE=1 SV=1 |
P39845 | 0.0 | 11 | 2106 | 8 | 2073 | Plipastatin synthase subunit A OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsA PE=1 SV=2 |
P39847 | 0.0 | 10 | 2107 | 12 | 2070 | Plipastatin synthase subunit C OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsC PE=1 SV=2 |
Q70LM6 | 0.0 | 7 | 2107 | 8 | 2094 | Linear gramicidin synthase subunit B OS=Brevibacillus parabrevis OX=54914 GN=lgrB PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000052 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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