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CAZyme Information: MGYG000003142_00511

You are here: Home > Sequence: MGYG000003142_00511

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 Clostridium_J sp900547625
Lineage Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium_J; Clostridium_J sp900547625
CAZyme ID MGYG000003142_00511
CAZy Family GT2
CAZyme Description Gramicidin S synthase 2
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
2534 MGYG000003142_2|CGC3 293722.93 5.4445
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003142 3709509 MAG United States North America
Gene Location Start: 211511;  End: 219115  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003142_00511.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK12316 PRK12316 0.0 1086 2110 43 1087
peptide synthase; Provisional
cd05930 A_NRPS 0.0 512 987 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 0.0 1551 2023 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.
PRK12316 PRK12316 0.0 1 1380 6 1391
peptide synthase; Provisional
PRK12467 PRK12467 0.0 44 1256 2639 3753
peptide synthase; Provisional

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QND46664.1 0.0 47 2083 554 2636
BAY90071.1 2.57e-267 221 2104 306 3280
BAY30132.1 1.35e-259 221 2104 307 3291
BAZ75991.1 1.15e-258 221 2104 307 3289
BAZ00088.1 1.15e-258 221 2104 307 3289

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6MFY_A 0.0 495 2027 202 1716
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 0.0 495 2104 202 1794
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 7.26e-208 478 1523 5 1071
Crystalstructure of a cross-module fragment from the dimodular NRPS DhbF [Geobacillus sp. Y4.1MC1]
6MFW_A 7.30e-205 495 1518 202 1205
Crystalstructure of a 4-domain construct of LgrA in the substrate donation state [Brevibacillus parabrevis]
6MFX_A 3.64e-204 495 1518 202 1205
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
P45745 0.0 54 2107 9 2107
Dimodular nonribosomal peptide synthase OS=Bacillus subtilis (strain 168) OX=224308 GN=dhbF PE=1 SV=4
Q70LM4 0.0 52 2525 2580 5070
Linear gramicidin synthase subunit D OS=Brevibacillus parabrevis OX=54914 GN=lgrD PE=1 SV=1
Q04747 0.0 42 2107 1046 3104
Surfactin synthase subunit 2 OS=Bacillus subtilis (strain 168) OX=224308 GN=srfAB PE=1 SV=3
P94459 0.0 34 2104 1037 3101
Plipastatin synthase subunit D OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsD PE=1 SV=2
Q70LM5 0.0 52 2108 9 2113
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
1.000046 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003142_00511.