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CAZyme Information: MGYG000000272_01087

You are here: Home > Sequence: MGYG000000272_01087

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 Prevotella hominis
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella hominis
CAZyme ID MGYG000000272_01087
CAZy Family GT2
CAZyme Description PGL/p-HBAD biosynthesis glycosyltransferase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
258 MGYG000000272_10|CGC2 29416.96 8.463
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000272 3991064 Isolate China Asia
Gene Location Start: 43737;  End: 44513  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000272_01087.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT2 5 164 1.7e-23 0.9235294117647059

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06433 GT_2_WfgS_like 7.31e-68 5 219 1 199
WfgS and WfeV are involved in O-antigen biosynthesis. Escherichia coli WfgS and Shigella dysenteriae WfeV are glycosyltransferase 2 family enzymes involved in O-antigen biosynthesis. GT-2 enzymes have 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. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.
cd00761 Glyco_tranf_GTA_type 5.11e-24 6 109 1 98
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.
pfam00535 Glycos_transf_2 6.71e-24 5 164 1 156
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.
PRK10063 PRK10063 8.86e-23 5 225 4 207
colanic acid biosynthesis glycosyltransferase WcaE.
COG0463 WcaA 5.18e-22 1 257 2 247
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QNT67007.1 6.46e-153 1 258 1 258
BCS85605.1 3.44e-125 1 258 1 259
VEH14708.1 5.39e-122 1 258 1 259
ALO49442.1 1.76e-118 1 256 1 256
QUB47200.1 8.82e-118 1 256 1 256

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3BCV_A 4.41e-07 3 102 6 99
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]
5HEA_A 1.43e-06 5 98 8 95
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]
1H7L_A 5.28e-06 3 152 2 152
dTDP-MAGNESIUMCOMPLEX OF SPSA FROM BACILLUS SUBTILIS [Bacillus subtilis],1H7Q_A dTDP-MANGANESE COMPLEX OF SPSA FROM BACILLUS SUBTILIS [Bacillus subtilis],1QG8_A Native (Magnesium-Containing) Spsa From Bacillus Subtilis [Bacillus subtilis],1QGQ_A Udp-manganese Complex Of Spsa From Bacillus Subtilis [Bacillus subtilis],1QGS_A Udp-Magnesium Complex Of Spsa From Bacillus Subtilis [Bacillus subtilis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P9WMX6 3.79e-23 4 219 6 206
PGL/p-HBAD biosynthesis glycosyltransferase MT3031 OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=MT3031 PE=3 SV=1
P0A5A0 3.79e-23 4 219 6 206
PGL/p-HBAD biosynthesis glycosyltransferase Mb2981 OS=Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) OX=233413 GN=BQ2027_MB2981 PE=3 SV=1
P9WMX7 3.79e-23 4 219 6 206
PGL/p-HBAD biosynthesis glycosyltransferase Rv2957 OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=Rv2957 PE=1 SV=1
A5U6W5 3.79e-23 4 219 6 206
PGL/p-HBAD biosynthesis glycosyltransferase MRA_2984 OS=Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra) OX=419947 GN=MRA_2984 PE=3 SV=2
A1KMV1 3.79e-23 4 219 6 206
PGL/p-HBAD biosynthesis glycosyltransferase BCG_2978 OS=Mycobacterium bovis (strain BCG / Pasteur 1173P2) OX=410289 GN=BCG_2978 PE=3 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
1.000066 0.000001 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000272_01087.