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CAZyme Information: MGYG000000210_01915

You are here: Home > Sequence: MGYG000000210_01915

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; Actinobacteriota; Coriobacteriia; Coriobacteriales; Coriobacteriaceae; Collinsella;
CAZyme ID MGYG000000210_01915
CAZy Family GT2
CAZyme Description 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
520 MGYG000000210_44|CGC1 56150.37 6.7886
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000210 2261186 Isolate China Asia
Gene Location Start: 7835;  End: 9397  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000210_01915.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT2 199 321 6.8e-32 0.7294117647058823

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK09677 PRK09677 2.55e-52 1 182 3 184
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
cd04647 LbH_MAT_like 2.43e-42 66 179 2 109
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.
COG0110 WbbJ 6.13e-34 12 183 17 180
Acetyltransferase (isoleucine patch superfamily) [General function prediction only].
cd03357 LbH_MAT_GAT 4.31e-31 68 179 65 169
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).
cd03349 LbH_XAT 4.75e-30 53 182 9 128
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
ATP53428.1 6.82e-44 195 510 3 312
CAI33841.1 1.43e-41 197 428 3 236
SBT85362.1 1.43e-41 197 428 3 236
ARO10976.1 2.90e-41 195 439 3 246
QNU66608.1 3.93e-41 196 439 3 246

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5HEA_A 2.45e-27 190 413 1 230
CgTstructure in hexamer [Streptococcus parasanguinis FW213],5HEA_B CgT structure in hexamer [Streptococcus parasanguinis FW213],5HEA_C CgT structure in hexamer [Streptococcus parasanguinis FW213],5HEC_A CgT structure in dimer [Streptococcus parasanguinis FW213],5HEC_B CgT structure in dimer [Streptococcus parasanguinis FW213]
3BCV_A 1.75e-19 196 315 5 124
Crystalstructure of a putative glycosyltransferase from Bacteroides fragilis [Bacteroides fragilis NCTC 9343],3BCV_B Crystal structure of a putative glycosyltransferase from Bacteroides fragilis [Bacteroides fragilis NCTC 9343]
1KQA_A 2.69e-13 63 182 73 185
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]
6P61_A 2.55e-12 194 321 11 139
Structureof a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197],6P61_B Structure of a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197],6P61_C Structure of a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197],6P61_D Structure of a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197]
2Z87_A 2.87e-12 194 293 372 471
Crystalstructure of chondroitin polymerase from Escherichia coli strain K4 (K4CP) complexed with UDP-GalNAc and UDP [Escherichia coli],2Z87_B Crystal structure of chondroitin polymerase from Escherichia coli strain K4 (K4CP) complexed with UDP-GalNAc and UDP [Escherichia coli]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P37750 1.83e-34 4 182 8 186
Putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ OS=Escherichia coli (strain K12) OX=83333 GN=wbbJ PE=3 SV=2
A0A0H2UR96 1.82e-28 198 429 5 260
Glycosyltransferase GlyG OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=glyG PE=1 SV=1
A0A0H2URH7 8.55e-25 197 406 6 223
Glycosyltransferase GlyA OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=glyA PE=3 SV=1
P71059 2.37e-22 196 417 3 232
Uncharacterized glycosyltransferase EpsJ OS=Bacillus subtilis (strain 168) OX=224308 GN=epsJ PE=2 SV=1
P71057 3.59e-18 194 312 2 119
Putative glycosyltransferase EpsH OS=Bacillus subtilis (strain 168) OX=224308 GN=epsH PE=2 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
0.999967 0.000078 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000210_01915.