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CAZyme Information: MGYG000001443_04863

You are here: Home > Sequence: MGYG000001443_04863

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 Streptomyces albus
Lineage Bacteria; Actinobacteriota; Actinomycetia; Streptomycetales; Streptomycetaceae; Streptomyces; Streptomyces albus
CAZyme ID MGYG000001443_04863
CAZy Family GT2
CAZyme Description D-alanine--poly(phosphoribitol) ligase subunit 1
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
954 101163.83 6.3706
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001443 7820353 Isolate not provided not provided
Gene Location Start: 2756266;  End: 2759130  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001443_04863.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd17643 A_NRPS_Cytc1-like 0.0 364 855 1 446
similar to adenylation domain of cytotrienin synthetase CytC1. This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. 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 1.49e-177 364 859 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.
PRK12467 PRK12467 6.12e-154 313 951 1537 2167
peptide synthase; Provisional
PRK12467 PRK12467 3.46e-150 22 954 101 1104
peptide synthase; Provisional
cd12117 A_NRPS_Srf_like 7.50e-150 358 859 5 483
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BAY30132.1 6.16e-130 282 952 512 1185
BAZ00088.1 5.12e-129 222 952 450 1183
BAZ75991.1 5.12e-129 222 952 450 1183
BAY90071.1 2.17e-126 313 947 541 1177
AFY93865.1 4.60e-121 363 948 344 930

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6N8E_A 2.11e-111 222 947 391 1066
Crystalstructure of holo-ObiF1, a five domain nonribosomal peptide synthetase from Burkholderia diffusa [Burkholderia diffusa]
6P1J_A 2.24e-103 250 855 369 960
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]
5N9W_A 2.04e-99 349 855 17 517
Structureof adenylation domain THR1 involved in the biosynthesis of 4-chlorothreonine in Streptomyces SP.OH-5093, apo structure [Streptomyces sp.],5N9W_B Structure of adenylation domain THR1 involved in the biosynthesis of 4-chlorothreonine in Streptomyces SP.OH-5093, apo structure [Streptomyces sp.],5N9X_A Structure of adenylation domain THR1 involved in the biosynthesis of 4-chlorothreonine in Streptomyces SP.OH-5093, ligand bound structure [Streptomyces sp.],5N9X_B Structure of adenylation domain THR1 involved in the biosynthesis of 4-chlorothreonine in Streptomyces SP.OH-5093, ligand bound structure [Streptomyces sp.]
3VNQ_A 8.49e-99 360 855 45 529
Co-crystalstructure of NRPS adenylation protein CytC1 with ATP from streptomyces [Streptomyces sp.],3VNR_A Co-crystal structure of NRPS adenylation protein CytC1 with aminobutyric acid and AMP from streptomyces [Streptomyces sp.],3VNS_A Co-crystal structure of NRPS adenylation protein CytC1 with D-valine and AMP from streptomyces [Streptomyces sp.]
6MFZ_A 2.87e-91 328 952 1203 1802
Crystalstructure of dimodular LgrA in a condensation state [Brevibacillus parabrevis],6MFZ_B Crystal structure of dimodular LgrA in a condensation 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 6.48e-136 315 924 1480 2084
Dimodular nonribosomal peptide synthase OS=Bacillus subtilis (strain 168) OX=224308 GN=dhbF PE=1 SV=4
Q52400 1.03e-128 345 922 16 581
Syringomycin synthase SyrB1 OS=Pseudomonas syringae pv. syringae OX=321 GN=syrB1 PE=1 SV=2
P39846 2.79e-119 270 944 1423 2073
Plipastatin synthase subunit B OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsB PE=1 SV=1
Q70LM6 4.68e-101 288 946 4032 4670
Linear gramicidin synthase subunit B OS=Brevibacillus parabrevis OX=54914 GN=lgrB PE=1 SV=1
Q70LM4 9.60e-96 251 947 1419 2093
Linear gramicidin synthase subunit D OS=Brevibacillus parabrevis OX=54914 GN=lgrD PE=1 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
1.000043 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001443_04863.