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CAZyme Information: MGYG000001102_01423

You are here: Home > Sequence: MGYG000001102_01423

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 UBA7185 sp900756555
Lineage Bacteria; Firmicutes_B; Peptococcia; Peptococcales; Peptococcaceae; UBA7185; UBA7185 sp900756555
CAZyme ID MGYG000001102_01423
CAZy Family GT2
CAZyme Description Putative teichuronic acid biosynthesis glycosyltransferase TuaG
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
250 MGYG000001102_97|CGC1 28758.74 8.0052
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001102 2481411 MAG China Asia
Gene Location Start: 3832;  End: 4584  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001102_01423.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT2 5 160 9.6e-37 0.9588235294117647

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam00535 Glycos_transf_2 5.69e-39 5 158 1 160
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 2.25e-35 6 122 1 118
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.
cd04196 GT_2_like_d 1.96e-33 5 200 1 203
Subfamily of Glycosyltransferase Family GT2 of unknown function. GT-2 includes diverse families of glycosyltransferases 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. 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.
cd06433 GT_2_WfgS_like 3.44e-32 5 201 1 195
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.
cd04184 GT2_RfbC_Mx_like 7.40e-30 3 188 2 189
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis. The rfbC gene encodes a predicted protein of 1,276 amino acids, which is required for O-antigen biosynthesis in Myxococcus xanthus. It is a subfamily of Glycosyltransferase Family GT2, which 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. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AEV28907.1 3.88e-65 5 250 8 253
QSX09600.1 4.05e-62 5 250 6 251
BBM36550.1 9.92e-59 4 248 6 249
BBM57016.1 7.96e-58 4 248 6 249
BBM40863.1 1.59e-57 4 248 6 249

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5HEA_A 2.23e-25 3 151 6 142
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 4.41e-17 4 200 7 225
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]
6H1J_A 2.96e-14 1 183 19 207
ChainA, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H1J_B Chain B, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H1J_C Chain C, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H21_A Chain A, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H21_B Chain B, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H21_C Chain C, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H2N_A Chain A, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H2N_B Chain B, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H2N_C Chain C, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4F_A Chain A, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4F_B Chain B, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4F_C Chain C, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4F_D Chain D, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4F_E Chain E, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4F_F Chain F, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4F_G Chain G, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4F_H Chain H, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4F_I Chain I, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4F_O Chain O, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4F_P Chain P, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4F_Q Chain Q, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4M_A Chain A, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4M_B Chain B, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4M_C Chain C, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4M_D Chain D, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4M_E Chain E, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4M_F Chain F, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4M_G Chain G, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4M_H Chain H, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4M_I Chain I, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4M_O Chain O, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4M_P Chain P, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4M_Q Chain Q, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6HNQ_A Chain A, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6HNQ_B Chain B, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6HNQ_C Chain C, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6HNQ_D Chain D, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6HNQ_E Chain E, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6HNQ_F Chain F, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6HNQ_G Chain G, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6HNQ_H Chain H, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6HNQ_I Chain I, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6HNQ_O Chain O, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6HNQ_P Chain P, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6HNQ_Q Chain Q, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315]
2Z86_A 1.00e-12 3 133 376 506
Crystalstructure of chondroitin polymerase from Escherichia coli strain K4 (K4CP) complexed with UDP-GlcUA and UDP [Escherichia coli],2Z86_B Crystal structure of chondroitin polymerase from Escherichia coli strain K4 (K4CP) complexed with UDP-GlcUA and UDP [Escherichia coli],2Z86_C Crystal structure of chondroitin polymerase from Escherichia coli strain K4 (K4CP) complexed with UDP-GlcUA and UDP [Escherichia coli],2Z86_D Crystal structure of chondroitin polymerase from Escherichia coli strain K4 (K4CP) complexed with UDP-GlcUA and UDP [Escherichia coli]
2Z87_A 1.00e-12 3 133 375 505
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
O32268 8.06e-54 3 246 7 250
Putative teichuronic acid biosynthesis glycosyltransferase TuaG OS=Bacillus subtilis (strain 168) OX=224308 GN=tuaG PE=2 SV=1
Q57022 7.40e-42 1 249 3 250
Uncharacterized glycosyltransferase HI_0868 OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=HI_0868 PE=3 SV=1
B5L3F2 1.09e-34 3 247 5 244
UDP-Glc:alpha-D-GlcNAc-diphosphoundecaprenol beta-1,3-glucosyltransferase WfgD OS=Escherichia coli OX=562 GN=wfgD PE=1 SV=1
Q077R2 1.41e-24 1 212 1 207
UDP-Glc:alpha-D-GlcNAc-diphosphoundecaprenol beta-1,3-glucosyltransferase WfaP OS=Escherichia coli OX=562 GN=wfaP PE=1 SV=1
Q1RIM7 8.11e-22 4 131 293 418
Uncharacterized glycosyltransferase RBE_0706 OS=Rickettsia bellii (strain RML369-C) OX=336407 GN=RBE_0706 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
1.000051 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001102_01423.