Species | Muribaculum sp003150235 | |||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; Muribaculum; Muribaculum sp003150235 | |||||||||||
CAZyme ID | MGYG000004490_00258 | |||||||||||
CAZy Family | GT2 | |||||||||||
CAZyme Description | Gramicidin S synthase 2 | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 127037; End: 134320 Strand: - |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
PRK05691 | PRK05691 | 0.0 | 373 | 2030 | 1075 | 2793 | peptide synthase; Validated |
PRK12316 | PRK12316 | 0.0 | 9 | 2030 | 1558 | 3640 | peptide synthase; Provisional |
PRK12467 | PRK12467 | 0.0 | 7 | 2030 | 49 | 2182 | peptide synthase; Provisional |
cd05930 | A_NRPS | 3.00e-153 | 1460 | 1929 | 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. |
cd05930 | A_NRPS | 1.95e-150 | 446 | 907 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QND46664.1 | 3.14e-209 | 8 | 2011 | 564 | 2661 |
ACX49739.1 | 1.14e-127 | 5 | 1726 | 7 | 1850 |
AFZ04852.1 | 8.09e-87 | 299 | 1030 | 459 | 1221 |
BAY30132.1 | 1.38e-85 | 18 | 996 | 2258 | 3298 |
BAY90071.1 | 8.93e-83 | 18 | 988 | 2247 | 3280 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6MFZ_A | 2.33e-230 | 405 | 2023 | 177 | 1808 | 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 | 2.58e-217 | 405 | 1932 | 177 | 1715 | 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] |
6MFW_A | 1.22e-132 | 405 | 1403 | 177 | 1178 | Crystalstructure of a 4-domain construct of LgrA in the substrate donation state [Brevibacillus parabrevis] |
6MFX_A | 1.82e-131 | 424 | 1403 | 201 | 1178 | Crystalstructure of a 4-domain construct of a mutant of LgrA in the substrate donation state [Brevibacillus parabrevis] |
5ES5_A | 6.95e-109 | 405 | 987 | 175 | 760 | 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] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
O68006 | 1.72e-237 | 9 | 2029 | 1673 | 3746 | Bacitracin synthase 1 OS=Bacillus licheniformis OX=1402 GN=bacA PE=3 SV=1 |
P0C064 | 1.54e-236 | 9 | 2017 | 1063 | 3127 | Gramicidin S synthase 2 OS=Brevibacillus brevis OX=1393 GN=grsB PE=1 SV=2 |
P0C063 | 2.55e-232 | 9 | 2017 | 1063 | 3128 | Gramicidin S synthase 2 OS=Aneurinibacillus migulanus OX=47500 GN=grsB PE=3 SV=2 |
Q70LM7 | 1.98e-225 | 405 | 2009 | 174 | 1791 | Linear gramicidin synthase subunit A OS=Brevibacillus parabrevis OX=54914 GN=lgrA PE=1 SV=1 |
P94459 | 9.27e-222 | 9 | 2023 | 1058 | 3115 | Plipastatin synthase subunit D OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsD PE=1 SV=2 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000046 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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