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CAZyme Information: MGYG000004748_01875

You are here: Home > Sequence: MGYG000004748_01875

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; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides;
CAZyme ID MGYG000004748_01875
CAZy Family GT2
CAZyme Description Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
345 40374.73 8.386
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004748 4696076 MAG China Asia
Gene Location Start: 169058;  End: 170095  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004748_01875.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT2 4 134 5.7e-37 0.7529411764705882

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK10073 PRK10073 8.68e-31 2 246 7 245
putative glycosyl transferase; Provisional
pfam00535 Glycos_transf_2 1.27e-26 4 129 1 123
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 1.25e-25 5 90 1 83
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.
COG0463 WcaA 2.80e-22 1 297 3 279
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
cd04179 DPM_DPG-synthase_like 5.01e-18 5 133 1 128
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily. DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. The UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate. This protein family belongs to Glycosyltransferase 2 superfamily.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUT68157.1 1.69e-156 1 342 1 341
QUT63141.1 2.40e-156 1 342 1 341
QQA31497.1 2.76e-156 1 342 5 345
BBK88593.1 7.89e-156 1 345 5 348
QUT36883.1 5.59e-155 1 342 1 341

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5HEA_A 1.73e-27 3 236 7 251
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 1.44e-26 2 215 6 231
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 5.06e-21 2 245 21 262
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 7.43e-18 3 111 377 481
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 7.43e-18 3 111 376 480
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
P71059 3.37e-31 3 219 5 222
Uncharacterized glycosyltransferase EpsJ OS=Bacillus subtilis (strain 168) OX=224308 GN=epsJ PE=2 SV=1
P11290 8.63e-28 2 249 7 252
Uncharacterized glycosyltransferase YibD OS=Escherichia coli (strain K12) OX=83333 GN=yibD PE=3 SV=2
A0A0H2URH7 2.07e-26 2 217 6 224
Glycosyltransferase GlyA OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=glyA PE=3 SV=1
P71057 3.56e-23 3 248 6 251
Putative glycosyltransferase EpsH OS=Bacillus subtilis (strain 168) OX=224308 GN=epsH PE=2 SV=1
A0A0H2UR96 6.64e-23 3 217 5 223
Glycosyltransferase GlyG OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=glyG PE=1 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
1.000087 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004748_01875.