logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000000012_03330

You are here: Home > Sequence: MGYG000000012_03330

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 Bacillus subtilis
Lineage Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; Bacillus subtilis
CAZyme ID MGYG000000012_03330
CAZy Family GT2
CAZyme Description Tyrocidine synthase 3
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
889 100061.21 5.0447
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000012 4053580 Isolate United Kingdom Europe
Gene Location Start: 100608;  End: 103277  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000012_03330.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd17655 A_NRPS_Bac 0.0 273 768 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 0.0 282 765 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.
cd12117 A_NRPS_Srf_like 8.51e-161 272 765 1 483
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C). 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 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. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
PRK12467 PRK12467 7.05e-159 18 860 236 1104
peptide synthase; Provisional
COG1020 EntF 1.76e-151 56 690 1 641
Non-ribosomal peptide synthetase component F [Secondary metabolites biosynthesis, transport and catabolism].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BAZ00088.1 4.41e-131 22 850 318 1175
BAZ75991.1 4.41e-131 22 850 318 1175
BAY90071.1 2.72e-130 7 850 299 1174
BAY30132.1 1.41e-128 22 850 318 1177
AFZ04852.1 1.24e-120 22 856 323 1186

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6MFZ_A 1.94e-116 65 850 1005 1794
Crystalstructure of dimodular LgrA in a condensation state [Brevibacillus parabrevis],6MFZ_B Crystal structure of dimodular LgrA in a condensation state [Brevibacillus parabrevis]
2VSQ_A 7.55e-116 15 853 194 1039
Structureof surfactin A synthetase C (SrfA-C), a nonribosomal peptide synthetase termination module [Bacillus subtilis]
1AMU_A 1.80e-109 246 797 18 555
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]
6MFY_A 2.12e-106 65 768 1005 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]
5U89_A 1.22e-104 248 853 5 602
Crystalstructure of a cross-module fragment from the dimodular NRPS DhbF [Geobacillus sp. Y4.1MC1]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
O68006 1.64e-141 15 827 2876 3704
Bacitracin synthase 1 OS=Bacillus licheniformis OX=1402 GN=bacA PE=3 SV=1
Q9R9J0 6.33e-140 200 860 3216 3879
Mycosubtilin synthase subunit B OS=Bacillus subtilis OX=1423 GN=mycB PE=3 SV=1
O30409 8.46e-138 18 857 3305 4150
Tyrocidine synthase 3 OS=Brevibacillus parabrevis OX=54914 GN=tycC PE=1 SV=1
P27206 1.11e-134 18 850 194 1039
Surfactin synthase subunit 1 OS=Bacillus subtilis (strain 168) OX=224308 GN=srfAA PE=1 SV=4
P0C064 6.53e-130 18 856 3316 4163
Gramicidin S synthase 2 OS=Brevibacillus brevis OX=1393 GN=grsB PE=1 SV=2

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
1.000048 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000012_03330.