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CAZyme Information: MGYG000000858_01123

You are here: Home > Sequence: MGYG000000858_01123

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 Collinsella sp900542155
Lineage Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Coriobacteriaceae; Collinsella; Collinsella sp900542155
CAZyme ID MGYG000000858_01123
CAZy Family GT2
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
353 MGYG000000858_11|CGC1 39970.97 5.4889
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000858 2197901 MAG China Asia
Gene Location Start: 8636;  End: 9697  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000858_01123.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT2 15 140 9.7e-29 0.7352941176470589

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam00535 Glycos_transf_2 1.14e-28 15 142 1 127
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 1.71e-24 16 126 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.
COG0463 WcaA 1.55e-22 14 256 5 248
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
cd04179 DPM_DPG-synthase_like 1.12e-21 16 127 1 113
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.
PRK10073 PRK10073 8.61e-20 10 154 4 151
putative glycosyl transferase; Provisional

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BAK44090.1 1.06e-103 14 350 10 335
AJC12297.1 1.33e-90 14 350 5 330
QKF06686.1 6.66e-88 14 350 6 331
BCV18572.1 3.63e-86 14 313 5 306
CDZ23680.1 4.95e-57 14 325 4 292

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5HEA_A 1.22e-14 14 229 7 223
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]
2Z86_A 5.35e-14 14 253 377 601
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 5.35e-14 14 253 376 600
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]
5TZE_C 5.67e-13 12 250 1 228
Crystalstructure of S. aureus TarS in complex with UDP-GlcNAc [Staphylococcus aureus],5TZE_E Crystal structure of S. aureus TarS in complex with UDP-GlcNAc [Staphylococcus aureus],5TZI_C Crystal structure of S. aureus TarS 1-349 [Staphylococcus aureus],5TZJ_A Crystal structure of S. aureus TarS 1-349 in complex with UDP-GlcNAc [Staphylococcus aureus],5TZJ_C Crystal structure of S. aureus TarS 1-349 in complex with UDP-GlcNAc [Staphylococcus aureus],5TZK_C Crystal structure of S. aureus TarS 1-349 in complex with UDP [Staphylococcus aureus]
5TZ8_A 9.20e-13 12 250 1 228
Crystalstructure of S. aureus TarS [Staphylococcus aureus],5TZ8_B Crystal structure of S. aureus TarS [Staphylococcus aureus],5TZ8_C Crystal structure of S. aureus TarS [Staphylococcus aureus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
A0A0H2URH7 3.79e-16 13 138 6 129
Glycosyltransferase GlyA OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=glyA PE=3 SV=1
P71059 1.86e-13 14 126 5 115
Uncharacterized glycosyltransferase EpsJ OS=Bacillus subtilis (strain 168) OX=224308 GN=epsJ PE=2 SV=1
Q8L0V4 3.08e-13 14 253 434 658
Chondroitin synthase OS=Escherichia coli OX=562 GN=kfoC PE=1 SV=1
A0A0H2UR96 7.94e-13 14 138 5 128
Glycosyltransferase GlyG OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=glyG PE=1 SV=1
P71057 8.28e-13 11 127 5 116
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
1.000076 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000858_01123.