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CAZyme Information: MGYG000001647_00952

You are here: Home > Sequence: MGYG000001647_00952

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 UMGS1781 sp900553695
Lineage Bacteria; Firmicutes_A; Clostridia; TANB77; CAG-508; UMGS1781; UMGS1781 sp900553695
CAZyme ID MGYG000001647_00952
CAZy Family GT2
CAZyme Description D-alanine--poly(phosphoribitol) ligase subunit 1
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1446 MGYG000001647_26|CGC1 165807.9 6.7066
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001647 1184465 MAG United States North America
Gene Location Start: 5498;  End: 9838  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001647_00952.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd05930 A_NRPS 8.01e-165 472 946 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.
cd17655 A_NRPS_Bac 2.57e-159 462 946 1 486
bacitracin synthetase and related proteins. This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. 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.
cd12117 A_NRPS_Srf_like 4.06e-144 462 946 1 483
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C). 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 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. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
PRK12467 PRK12467 3.05e-142 8 1043 52 1111
peptide synthase; Provisional
PRK12467 PRK12467 3.34e-141 8 1026 1119 2160
peptide synthase; Provisional

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BAY90071.1 4.98e-113 8 1026 2238 3280
BAY30132.1 6.80e-112 8 1026 2249 3291
BAZ00088.1 2.17e-111 8 1026 2247 3289
BAZ75991.1 2.17e-111 8 1026 2247 3289
QND46664.1 7.04e-106 86 1040 1696 2671

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2VSQ_A 1.59e-113 3 1022 10 1032
Structureof surfactin A synthetase C (SrfA-C), a nonribosomal peptide synthetase termination module [Bacillus subtilis]
1AMU_A 2.34e-110 439 977 20 556
PhenylalanineActivating Domain Of Gramicidin Synthetase 1 In A Complex With Amp And Phenylalanine [Brevibacillus brevis],1AMU_B Phenylalanine Activating Domain Of Gramicidin Synthetase 1 In A Complex With Amp And Phenylalanine [Brevibacillus brevis]
5ES5_A 1.51e-108 462 1025 207 760
Crystalstructure of the initiation module of LgrA in the 'open' and 'closed ' adenylation states [Brevibacillus parabrevis],5ES5_B Crystal structure of the initiation module of LgrA in the 'open' and 'closed ' adenylation states [Brevibacillus parabrevis],5ES8_A Crystal structure of the initiation module of LgrA in the thiolation state [Brevibacillus parabrevis],5ES8_B Crystal structure of the initiation module of LgrA in the thiolation state [Brevibacillus parabrevis],5ES9_A Crystal structure of the LgrA initiation module in the formylation state [Brevibacillus parabrevis],5ES9_B Crystal structure of the LgrA initiation module in the formylation state [Brevibacillus parabrevis]
6MFZ_A 8.35e-106 6 1026 786 1794
Crystalstructure of dimodular LgrA in a condensation state [Brevibacillus parabrevis],6MFZ_B Crystal structure of dimodular LgrA in a condensation state [Brevibacillus parabrevis]
6MFW_A 7.72e-105 462 1025 209 762
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
P27206 3.78e-165 1 1027 1 1040
Surfactin synthase subunit 1 OS=Bacillus subtilis (strain 168) OX=224308 GN=srfAA PE=1 SV=4
P39845 5.89e-157 1 1087 1 1081
Plipastatin synthase subunit A OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsA PE=1 SV=2
P0C063 4.71e-145 2 1027 1058 2075
Gramicidin S synthase 2 OS=Aneurinibacillus migulanus OX=47500 GN=grsB PE=3 SV=2
Q70LM4 1.62e-144 2 1445 3635 5078
Linear gramicidin synthase subunit D OS=Brevibacillus parabrevis OX=54914 GN=lgrD PE=1 SV=1
P45745 1.38e-138 6 1026 9 1029
Dimodular nonribosomal peptide synthase OS=Bacillus subtilis (strain 168) OX=224308 GN=dhbF PE=1 SV=4

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
1.000052 0.000003 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001647_00952.