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CAZyme Information: MGYG000001514_01534

You are here: Home > Sequence: MGYG000001514_01534

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_A ihumii
Lineage Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_A; Paenibacillus_A ihumii
CAZyme ID MGYG000001514_01534
CAZy Family GT2
CAZyme Description Tyrocidine synthase 2
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1565 MGYG000001514_11|CGC15 175945.41 5.0648
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001514 5923787 Isolate not provided not provided
Gene Location Start: 590842;  End: 595539  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001514_01534.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK12316 PRK12316 0.0 98 1087 4149 5144
peptide synthase; Provisional
PRK12467 PRK12467 0.0 97 1078 2692 3668
peptide synthase; Provisional
PRK12467 PRK12467 0.0 4 1354 9 1373
peptide synthase; Provisional
PRK12467 PRK12467 0.0 16 1565 1082 2644
peptide synthase; Provisional
cd17651 A_NRPS_VisG_like 0.0 513 998 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BAY30132.1 1.48e-212 31 1083 2228 3295
BAZ00088.1 6.76e-212 34 1083 2228 3293
BAZ75991.1 6.76e-212 34 1083 2228 3293
BAY90071.1 2.91e-209 34 1057 2219 3257
QND46664.1 6.69e-198 41 1100 1605 2687

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6P1J_A 1.81e-196 52 997 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]
6OYF_A 6.15e-176 51 908 3 873
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 1.01e-170 51 908 3 873
Thestructure of condensation and adenylation domains of teixobactin-producing nonribosomal peptide synthetase Txo1 serine module in complex with Mg [Eleftheria terrae]
6MFZ_A 1.20e-168 57 1078 792 1793
Crystalstructure of dimodular LgrA in a condensation state [Brevibacillus parabrevis],6MFZ_B Crystal structure of dimodular LgrA in a condensation state [Brevibacillus parabrevis]
6MFX_A 2.48e-152 504 1534 202 1194
Crystalstructure of a 4-domain construct of a mutant 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
P27206 0.0 39 1557 2089 3583
Surfactin synthase subunit 1 OS=Bacillus subtilis (strain 168) OX=224308 GN=srfAA PE=1 SV=4
Q04747 0.0 52 1565 2098 3579
Surfactin synthase subunit 2 OS=Bacillus subtilis (strain 168) OX=224308 GN=srfAB PE=1 SV=3
O30408 0.0 34 1557 2081 3583
Tyrocidine synthase 2 OS=Brevibacillus parabrevis OX=54914 GN=tycB PE=1 SV=1
P39847 3.96e-319 52 1562 1059 2553
Plipastatin synthase subunit C OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsC PE=1 SV=2
Q70LM5 1.70e-318 42 1556 3646 5175
Linear gramicidin synthase subunit C OS=Brevibacillus parabrevis OX=54914 GN=lgrC 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
1.000071 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001514_01534.