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CAZyme Information: MGYG000002490_03757

You are here: Home > Sequence: MGYG000002490_03757

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 Paenibacillus_B thiaminolyticus
Lineage Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_B; Paenibacillus_B thiaminolyticus
CAZyme ID MGYG000002490_03757
CAZy Family GT2
CAZyme Description 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
494 55618.34 5.2745
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002490 6537383 Isolate Japan Asia
Gene Location Start: 84424;  End: 85908  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002490_03757.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT2 205 332 7e-24 0.7470588235294118

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd04647 LbH_MAT_like 2.72e-29 60 171 2 108
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.
pfam00535 Glycos_transf_2 6.85e-21 205 331 1 126
Glycosyl transferase family 2. Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.
cd00761 Glyco_tranf_GTA_type 4.95e-20 206 318 1 111
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold. Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.
cd03349 LbH_XAT 6.68e-19 74 169 10 121
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.
COG0110 WbbJ 7.25e-19 62 171 70 174
Acetyltransferase (isoleucine patch superfamily) [General function prediction only].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QDM42457.1 0.0 1 494 8 501
BBI32702.1 1.64e-264 1 493 1 473
QJD82898.1 1.13e-239 30 491 4 465
AJS57572.1 6.10e-163 3 489 2 489
BBI33988.1 2.25e-158 1 489 1 489

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4MZU_A 2.96e-07 61 189 30 164
Crystalstructure of FdtD, a bifunctional ketoisomerase/N-acetyltransferase from Shewanella denitrificans [Shewanella denitrificans OS217],4MZU_B Crystal structure of FdtD, a bifunctional ketoisomerase/N-acetyltransferase from Shewanella denitrificans [Shewanella denitrificans OS217],4MZU_C Crystal structure of FdtD, a bifunctional ketoisomerase/N-acetyltransferase from Shewanella denitrificans [Shewanella denitrificans OS217],4MZU_D Crystal structure of FdtD, a bifunctional ketoisomerase/N-acetyltransferase from Shewanella denitrificans [Shewanella denitrificans OS217],4MZU_E Crystal structure of FdtD, a bifunctional ketoisomerase/N-acetyltransferase from Shewanella denitrificans [Shewanella denitrificans OS217],4MZU_F Crystal structure of FdtD, a bifunctional ketoisomerase/N-acetyltransferase from Shewanella denitrificans [Shewanella denitrificans OS217],4MZU_G Crystal structure of FdtD, a bifunctional ketoisomerase/N-acetyltransferase from Shewanella denitrificans [Shewanella denitrificans OS217],4MZU_H Crystal structure of FdtD, a bifunctional ketoisomerase/N-acetyltransferase from Shewanella denitrificans [Shewanella denitrificans OS217],4MZU_I Crystal structure of FdtD, a bifunctional ketoisomerase/N-acetyltransferase from Shewanella denitrificans [Shewanella denitrificans OS217],4MZU_J Crystal structure of FdtD, a bifunctional ketoisomerase/N-acetyltransferase from Shewanella denitrificans [Shewanella denitrificans OS217],4MZU_K Crystal structure of FdtD, a bifunctional ketoisomerase/N-acetyltransferase from Shewanella denitrificans [Shewanella denitrificans OS217],4MZU_L Crystal structure of FdtD, a bifunctional ketoisomerase/N-acetyltransferase from Shewanella denitrificans [Shewanella denitrificans OS217]
6YV7_B 1.11e-06 200 263 40 103
MannosyltransferasePcManGT from Pyrobaculum calidifontis [Pyrobaculum calidifontis JCM 11548],6YV8_B Mannosyltransferase PcManGT from Pyrobaculum calidifontis in complex with GDP and Mn2+ [Pyrobaculum calidifontis JCM 11548],6YV9_A Mannosyltransferase PcManGT from Pyrobaculum calidifontis in complex with GDP-Man and Mn2+ [Pyrobaculum calidifontis JCM 11548]
6YV7_A 1.11e-06 200 263 41 104
MannosyltransferasePcManGT from Pyrobaculum calidifontis [Pyrobaculum calidifontis JCM 11548],6YV8_A Mannosyltransferase PcManGT from Pyrobaculum calidifontis in complex with GDP and Mn2+ [Pyrobaculum calidifontis JCM 11548],6YV9_B Mannosyltransferase PcManGT from Pyrobaculum calidifontis in complex with GDP-Man and Mn2+ [Pyrobaculum calidifontis JCM 11548]
3EEV_A 1.38e-06 113 169 103 159
CrystalStructure of Chloramphenicol Acetyltransferase VCA0300 from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],3EEV_B Crystal Structure of Chloramphenicol Acetyltransferase VCA0300 from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],3EEV_C Crystal Structure of Chloramphenicol Acetyltransferase VCA0300 from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],6PUA_A The 2.0 A Crystal Structure of the Type B Chloramphenicol Acetyltransferase from Vibrio cholerae [Vibrio cholerae O1 biovar El Tor str. N16961],6PUA_B The 2.0 A Crystal Structure of the Type B Chloramphenicol Acetyltransferase from Vibrio cholerae [Vibrio cholerae O1 biovar El Tor str. N16961],6PUA_C The 2.0 A Crystal Structure of the Type B Chloramphenicol Acetyltransferase from Vibrio cholerae [Vibrio cholerae O1 biovar El Tor str. N16961],6PUB_A Crystal Structure of the Type B Chloramphenicol Acetyltransferase from Vibrio cholerae in the Complex with Crystal Violet [Vibrio cholerae O1 biovar El Tor str. N16961],6U9C_A The 2.2 A Crystal Structure of the Type B Chloramphenicol Acetyltransferase from Vibrio cholerae in the complex with Acetyl CoA [Vibrio cholerae O1 biovar El Tor str. N16961],6U9C_B The 2.2 A Crystal Structure of the Type B Chloramphenicol Acetyltransferase from Vibrio cholerae in the complex with Acetyl CoA [Vibrio cholerae O1 biovar El Tor str. N16961],6U9C_C The 2.2 A Crystal Structure of the Type B Chloramphenicol Acetyltransferase from Vibrio cholerae in the complex with Acetyl CoA [Vibrio cholerae O1 biovar El Tor str. N16961]
6MFK_A 1.95e-06 114 169 111 166
ChainA, Chloramphenicol acetyltransferase [Elizabethkingia anophelis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P26401 3.53e-15 203 382 2 203
Abequosyltransferase RfbV OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=rfbV PE=1 SV=2
P37750 2.89e-10 60 182 68 193
Putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ OS=Escherichia coli (strain K12) OX=83333 GN=wbbJ PE=3 SV=2
P9WMX7 4.36e-08 202 328 4 131
PGL/p-HBAD biosynthesis glycosyltransferase Rv2957 OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=Rv2957 PE=1 SV=1
P0A5A0 4.36e-08 202 328 4 131
PGL/p-HBAD biosynthesis glycosyltransferase Mb2981 OS=Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) OX=233413 GN=BQ2027_MB2981 PE=3 SV=1
P9WMX6 4.36e-08 202 328 4 131
PGL/p-HBAD biosynthesis glycosyltransferase MT3031 OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=MT3031 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
1.000046 0.000001 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002490_03757.