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CAZyme Information: MGYG000003687_05732

You are here: Home > Sequence: MGYG000003687_05732

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 Paenibacillus polymyxa
Lineage Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus polymyxa
CAZyme ID MGYG000003687_05732
CAZy Family GT2
CAZyme Description Gramicidin S synthase 2
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1301 145292.32 4.5922
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003687 5656034 Isolate China Asia
Gene Location Start: 4522;  End: 8427  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003687_05732.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK12316 PRK12316 0.0 433 1286 51 850
peptide synthase; Provisional
PRK12467 PRK12467 0.0 11 1286 692 1917
peptide synthase; Provisional
PRK12316 PRK12316 0.0 11 1285 2182 3387
peptide synthase; Provisional
PRK12467 PRK12467 0.0 433 1286 51 853
peptide synthase; Provisional
cd19531 LCL_NRPS-like 0.0 431 843 1 427
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity. LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. 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). In addition to the LCL-type, there are various subtypes of C-domains such as 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 epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QND46664.1 6.06e-211 22 1277 1206 2411
ACX49739.1 1.51e-170 7 1202 653 1833
BAY90071.1 3.56e-145 342 1285 2133 3039
BAY30132.1 4.81e-145 342 1285 2144 3050
BAZ00088.1 2.89e-144 342 1285 2142 3048

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6MFY_A 4.07e-223 11 1282 381 1558
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]
6MFZ_A 2.55e-222 11 1282 381 1558
Crystalstructure of dimodular LgrA in a condensation state [Brevibacillus parabrevis],6MFZ_B Crystal structure of dimodular LgrA in a condensation state [Brevibacillus parabrevis]
5U89_A 5.03e-168 27 862 222 1071
Crystalstructure of a cross-module fragment from the dimodular NRPS DhbF [Geobacillus sp. Y4.1MC1]
2JGP_A 3.81e-164 338 853 3 520
Structureof the TycC5-6 PCP-C bidomain of the tyrocidine synthetase TycC [Brevibacillus brevis]
6MFW_A 1.12e-155 11 836 381 1184
Crystalstructure of a 4-domain construct of LgrA in the substrate donation state [Brevibacillus parabrevis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
O30409 0.0 27 1282 3766 4950
Tyrocidine synthase 3 OS=Brevibacillus parabrevis OX=54914 GN=tycC PE=1 SV=1
P39845 0.0 24 1275 647 1832
Plipastatin synthase subunit A OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsA PE=1 SV=2
P0C064 0.0 27 1280 1697 2878
Gramicidin S synthase 2 OS=Brevibacillus brevis OX=1393 GN=grsB PE=1 SV=2
P0C063 0.0 27 1280 1697 2880
Gramicidin S synthase 2 OS=Aneurinibacillus migulanus OX=47500 GN=grsB PE=3 SV=2
O68007 0.0 24 1281 706 1887
Bacitracin synthase 2 OS=Bacillus licheniformis OX=1402 GN=bacB PE=3 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
1.000053 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003687_05732.