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CAZyme Information: MGYG000001641_02051

You are here: Home > Sequence: MGYG000001641_02051

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 CAG-485 sp900760815
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-485; CAG-485 sp900760815
CAZyme ID MGYG000001641_02051
CAZy Family GT2
CAZyme Description Gramicidin S synthase 2
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
2418 266118.3 4.616
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001641 2823092 MAG United States North America
Gene Location Start: 7680;  End: 14936  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001641_02051.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK12316 PRK12316 0.0 5 2003 1558 3620
peptide synthase; Provisional
PRK12467 PRK12467 0.0 21 2002 68 2160
peptide synthase; Provisional
PRK05691 PRK05691 0.0 24 2003 697 2773
peptide synthase; Validated
cd05930 A_NRPS 4.91e-150 1454 1922 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 3.56e-149 442 903 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QND46664.1 7.66e-195 4 1992 564 2649
ACX49739.1 2.86e-116 5 1716 11 1846
BAY90071.1 7.66e-82 922 2008 2138 3286
BAY30132.1 2.96e-81 25 963 2269 3270
BAZ00088.1 2.51e-78 25 963 2267 3268

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6MFZ_A 1.84e-201 439 2005 216 1797
Crystalstructure of dimodular LgrA in a condensation state [Brevibacillus parabrevis],6MFZ_B Crystal structure of dimodular LgrA in a condensation state [Brevibacillus parabrevis]
6MFY_A 4.43e-188 439 1925 216 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]
6MFX_A 3.26e-100 439 1400 216 1178
Crystalstructure of a 4-domain construct of a mutant of LgrA in the substrate donation state [Brevibacillus parabrevis]
6MFW_A 3.26e-100 439 1400 216 1178
Crystalstructure of a 4-domain construct of LgrA in the substrate donation state [Brevibacillus parabrevis]
5U89_A 3.23e-89 1440 2007 24 604
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 5.86e-227 5 2007 1673 3731
Bacitracin synthase 1 OS=Bacillus licheniformis OX=1402 GN=bacA PE=3 SV=1
P0C064 7.06e-226 5 2005 1063 3122
Gramicidin S synthase 2 OS=Brevibacillus brevis OX=1393 GN=grsB PE=1 SV=2
P0C063 1.44e-222 5 2005 1063 3123
Gramicidin S synthase 2 OS=Aneurinibacillus migulanus OX=47500 GN=grsB PE=3 SV=2
O30409 6.18e-214 5 2006 1057 3112
Tyrocidine synthase 3 OS=Brevibacillus parabrevis OX=54914 GN=tycC PE=1 SV=1
O68007 1.95e-213 5 2005 77 2129
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
1.000056 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001641_02051.