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CAZyme Information: MGYG000003138_00792

You are here: Home > Sequence: MGYG000003138_00792

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 Streptococcus pseudopneumoniae_O
Lineage Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; Streptococcus; Streptococcus pseudopneumoniae_O
CAZyme ID MGYG000003138_00792
CAZy Family GT8
CAZyme Description Glycosyltransferase stabilizing protein Gtf2
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
292 MGYG000003138_5|CGC2 32955.48 5.3468
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003138 1796209 MAG United States North America
Gene Location Start: 97308;  End: 98186  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003138_00792.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd04647 LbH_MAT_like 3.72e-40 181 280 1 101
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, galactoside O-acetyltransferase (GAT), xenobiotic acyltransferase (XAT) and similar proteins. MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively while GAT specifically acetylates galactopyranosides. XAT catalyzes the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients. Members of this family contain a a left-handed parallel beta-helix (LbH) domain with at least 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). They are trimeric in their active form.
cd03357 LbH_MAT_GAT 1.20e-29 174 285 54 164
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively at the C6 position of the nonreducing end glucosyl moiety. GAT specifically acetylates galactopyranosides. Furthermore, MAT shows higher affinity toward artificial substrates containing an alkyl or hydrophobic chain as well as a glucosyl unit. Active MAT and GAT are homotrimers, with each subunit consisting of an N-terminal alpha-helical region and a C-terminal left-handed parallel alpha-helix (LbH) subdomain with 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).
COG0110 WbbJ 2.59e-26 139 291 26 178
Acetyltransferase (isoleucine patch superfamily) [General function prediction only].
PRK09677 PRK09677 4.41e-21 156 291 41 184
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
cd03349 LbH_XAT 2.60e-17 200 280 20 116
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of a large number of microbial enzymes that catalyze the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. Members of this class of enzymes include Enterococcus faecium streptogramin A acetyltransferase and Pseudomonas aeruginosa chloramphenicol acetyltransferase. They contain repeated copies of a six-residue hexapeptide repeat sequence motif (X-[STAV]-X-[LIV]-[GAED]-X) and adopt a left-handed parallel beta helix (LbH) structure. The active enzyme is a trimer with CoA and substrate binding sites at the interface of two separate LbH subunits. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BCJ11248.1 5.39e-194 1 291 1 291
CBJ22900.1 1.30e-185 1 291 1 291
VFH90022.1 3.72e-185 1 291 1 291
VGM73422.1 3.72e-185 1 291 1 291
QJS37518.1 7.50e-185 1 291 1 291

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5E9U_B 4.98e-13 2 131 280 412
Crystalstructure of GtfA/B complex bound to UDP and GlcNAc [Streptococcus gordonii],5E9U_D Crystal structure of GtfA/B complex bound to UDP and GlcNAc [Streptococcus gordonii],5E9U_F Crystal structure of GtfA/B complex bound to UDP and GlcNAc [Streptococcus gordonii],5E9U_H Crystal structure of GtfA/B complex bound to UDP and GlcNAc [Streptococcus gordonii]
5E9T_B 4.99e-13 2 131 280 412
Crystalstructure of GtfA/B complex [Streptococcus gordonii],5E9T_D Crystal structure of GtfA/B complex [Streptococcus gordonii]
3ECT_A 6.05e-13 175 280 69 175
CrystalStructure of the Hexapeptide-Repeat Containing-Acetyltransferase VCA0836 from Vibrio cholerae [Vibrio cholerae],3NZ2_A Crystal Structure of Hexapeptide-Repeat containing-Acetyltransferase VCA0836 Complexed with Acetyl Co Enzyme A from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],3NZ2_B Crystal Structure of Hexapeptide-Repeat containing-Acetyltransferase VCA0836 Complexed with Acetyl Co Enzyme A from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],3NZ2_C Crystal Structure of Hexapeptide-Repeat containing-Acetyltransferase VCA0836 Complexed with Acetyl Co Enzyme A from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],3NZ2_D Crystal Structure of Hexapeptide-Repeat containing-Acetyltransferase VCA0836 Complexed with Acetyl Co Enzyme A from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],3NZ2_E Crystal Structure of Hexapeptide-Repeat containing-Acetyltransferase VCA0836 Complexed with Acetyl Co Enzyme A from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],3NZ2_F Crystal Structure of Hexapeptide-Repeat containing-Acetyltransferase VCA0836 Complexed with Acetyl Co Enzyme A from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],3NZ2_G Crystal Structure of Hexapeptide-Repeat containing-Acetyltransferase VCA0836 Complexed with Acetyl Co Enzyme A from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],3NZ2_H Crystal Structure of Hexapeptide-Repeat containing-Acetyltransferase VCA0836 Complexed with Acetyl Co Enzyme A from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],3NZ2_I Crystal Structure of Hexapeptide-Repeat containing-Acetyltransferase VCA0836 Complexed with Acetyl Co Enzyme A from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],3NZ2_J Crystal Structure of Hexapeptide-Repeat containing-Acetyltransferase VCA0836 Complexed with Acetyl Co Enzyme A from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],3NZ2_K Crystal Structure of Hexapeptide-Repeat containing-Acetyltransferase VCA0836 Complexed with Acetyl Co Enzyme A from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],3NZ2_L Crystal Structure of Hexapeptide-Repeat containing-Acetyltransferase VCA0836 Complexed with Acetyl Co Enzyme A from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961]
5GVW_A 2.14e-11 13 131 283 405
Crystalstructure of the apo-form glycosyltransferase GlyE in Streptococcus pneumoniae TIGR4 [Streptococcus pneumoniae],5GVW_B Crystal structure of the apo-form glycosyltransferase GlyE in Streptococcus pneumoniae TIGR4 [Streptococcus pneumoniae],5GVW_C Crystal structure of the apo-form glycosyltransferase GlyE in Streptococcus pneumoniae TIGR4 [Streptococcus pneumoniae],5GVW_D Crystal structure of the apo-form glycosyltransferase GlyE in Streptococcus pneumoniae TIGR4 [Streptococcus pneumoniae]
1KQA_A 4.10e-11 202 290 96 184
GalactosideAcetyltransferase In Complex With Coenzyme A [Escherichia coli],1KQA_B Galactoside Acetyltransferase In Complex With Coenzyme A [Escherichia coli],1KQA_C Galactoside Acetyltransferase In Complex With Coenzyme A [Escherichia coli],1KRR_A Galactoside Acetyltransferase in Complex with Acetyl-Coenzyme A [Escherichia coli],1KRR_B Galactoside Acetyltransferase in Complex with Acetyl-Coenzyme A [Escherichia coli],1KRR_C Galactoside Acetyltransferase in Complex with Acetyl-Coenzyme A [Escherichia coli],1KRU_A Galactoside Acetyltransferase in Complex with IPTG and Coenzyme A [Escherichia coli],1KRU_B Galactoside Acetyltransferase in Complex with IPTG and Coenzyme A [Escherichia coli],1KRU_C Galactoside Acetyltransferase in Complex with IPTG and Coenzyme A [Escherichia coli],1KRV_A Galactoside Acetyltransferase in Complex with CoA and PNP-beta-Gal [Escherichia coli],1KRV_B Galactoside Acetyltransferase in Complex with CoA and PNP-beta-Gal [Escherichia coli],1KRV_C Galactoside Acetyltransferase in Complex with CoA and PNP-beta-Gal [Escherichia coli]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
A0A0H2URA3 1.14e-18 7 133 277 404
Glycosyltransferase GlyB OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=glyB PE=3 SV=1
Q3S2Y1 2.08e-15 2 141 278 420
UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase stabilizing protein GtfB OS=Streptococcus agalactiae OX=1311 GN=gtfB PE=1 SV=1
Q9AEU2 1.68e-14 11 129 284 404
Probable glycosyl transferase Gly OS=Streptococcus gordonii OX=1302 GN=gly PE=3 SV=2
A0A0H2UR90 2.52e-13 2 134 278 413
UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase stabilizing protein GtfB OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=gtfB PE=1 SV=1
Q86A05 5.01e-13 164 289 64 190
Putative acetyltransferase DDB_G0275507 OS=Dictyostelium discoideum OX=44689 GN=DDB_G0275507 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
1.000075 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003138_00792.