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CAZyme Information: MGYG000000609_01379

You are here: Home > Sequence: MGYG000000609_01379

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
Lineage Bacteria; Firmicutes_A; Clostridia; TANB77; UBA1234; UBA1234;
CAZyme ID MGYG000000609_01379
CAZy Family GT2
CAZyme Description D-alanine--poly(phosphoribitol) ligase subunit 1
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1039 119875.33 5.6677
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000609 1535020 MAG Madagascar Africa
Gene Location Start: 106;  End: 3225  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000609_01379.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd05930 A_NRPS 0.0 94 574 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 7.16e-178 87 578 4 490
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.
PRK10252 entF 3.19e-169 8 614 388 1001
enterobactin non-ribosomal peptide synthetase EntF.
cd17646 A_NRPS_AB3403-like 1.61e-167 84 574 2 488
Peptide Synthetase. 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.
PRK12467 PRK12467 8.75e-164 8 596 1502 2102
peptide synthase; Provisional

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BAZ00088.1 3.21e-119 19 658 518 1179
BAZ75991.1 3.21e-119 19 658 518 1179
AFZ04852.1 3.83e-113 13 657 517 1183
BAY30132.1 1.66e-110 18 657 2646 3294
BAY90071.1 1.34e-109 18 657 2635 3283

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6MFZ_A 1.82e-137 7 654 1151 1794
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 1.62e-134 7 581 1151 1719
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]
1AMU_A 5.86e-122 70 596 29 547
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]
6P1J_A 1.97e-117 9 574 395 964
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]
5ES5_A 1.83e-115 77 657 200 764
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q9R9I9 4.12e-155 13 654 195 838
Mycosubtilin synthase subunit C OS=Bacillus subtilis OX=1423 GN=mycC PE=3 SV=1
Q7BQ71 4.20e-140 82 574 5 498
Zwittermicin A synthase ZmaJ OS=Bacillus cereus OX=1396 GN=zmaJ PE=1 SV=1
Q70LM6 1.77e-136 12 654 391 1031
Linear gramicidin synthase subunit B OS=Brevibacillus parabrevis OX=54914 GN=lgrB PE=1 SV=1
Q70LM7 1.34e-135 7 654 1148 1791
Linear gramicidin synthase subunit A OS=Brevibacillus parabrevis OX=54914 GN=lgrA PE=1 SV=1
P94459 4.58e-132 18 657 1431 2068
Plipastatin synthase subunit D OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsD PE=1 SV=2

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
1.000078 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000609_01379.