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CAZyme Information: MGYG000000227_04867

You are here: Home > Sequence: MGYG000000227_04867

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 sonorensis
Lineage Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; Bacillus sonorensis
CAZyme ID MGYG000000227_04867
CAZy Family GT2
CAZyme Description Plipastatin synthase subunit C
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1445 163606.8 5.5944
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000227 4782975 Isolate China Asia
Gene Location Start: 75;  End: 4412  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000227_04867.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK12316 PRK12316 0.0 9 1445 2687 4099
peptide synthase; Provisional
PRK12316 PRK12316 0.0 10 1434 1645 3045
peptide synthase; Provisional
PRK12316 PRK12316 0.0 18 960 4199 5136
peptide synthase; Provisional
cd19534 E_NRPS 0.0 978 1412 1 428
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family. Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
PRK12316 PRK12316 0.0 5 1439 134 1547
peptide synthase; Provisional

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QND46664.1 1.11e-194 12 977 1708 2674
BAZ00088.1 4.52e-164 6 966 2334 3295
BAZ75991.1 4.52e-164 6 966 2334 3295
BAY30132.1 8.22e-164 6 966 2336 3297
BAY90071.1 1.49e-163 6 966 2325 3286

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6P1J_A 5.24e-195 25 880 106 964
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]
6MFZ_A 4.56e-189 1 963 860 1797
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 4.02e-177 6 964 103 1040
Structureof surfactin A synthetase C (SrfA-C), a nonribosomal peptide synthetase termination module [Bacillus subtilis]
6OYF_A 2.59e-171 6 794 88 873
Thestructure of condensation and adenylation domains of teixobactin-producing nonribosomal peptide synthetase Txo1 serine module [Eleftheria terrae],6OZV_A The structure of condensation and adenylation domains of teixobactin-producing nonribosomal peptide synthetase Txo1 serine module in complex with AMP [Eleftheria terrae],6P4U_A The structure of condensation and adenylation domains of teixobactin-producing nonribosomal peptide synthetase Txo1 serine module in complex with Mg and AMP [Eleftheria terrae]
6P3I_A 6.44e-165 6 794 88 873
Thestructure of condensation and adenylation domains of teixobactin-producing nonribosomal peptide synthetase Txo1 serine module in complex with Mg [Eleftheria terrae]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P39845 0.0 3 1445 1127 2561
Plipastatin synthase subunit A OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsA PE=1 SV=2
P94459 0.0 3 1442 2163 3600
Plipastatin synthase subunit D OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsD PE=1 SV=2
P27206 0.0 12 1438 2184 3583
Surfactin synthase subunit 1 OS=Bacillus subtilis (strain 168) OX=224308 GN=srfAA PE=1 SV=4
Q04747 0.0 12 1444 2180 3580
Surfactin synthase subunit 2 OS=Bacillus subtilis (strain 168) OX=224308 GN=srfAB PE=1 SV=3
P39846 0.0 1 1445 1128 2560
Plipastatin synthase subunit B OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsB PE=1 SV=1

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
1.000055 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000227_04867.