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CAZyme Information: MGYG000003520_00453

You are here: Home > Sequence: MGYG000003520_00453

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 RC9 sp900769145
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; UBA932; RC9; RC9 sp900769145
CAZyme ID MGYG000003520_00453
CAZy Family GT2
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
401 43916.1 7.7773
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003520 2768956 MAG Fiji Oceania
Gene Location Start: 38695;  End: 39900  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003520_00453.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT2 19 132 3.2e-20 0.6882352941176471

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd04179 DPM_DPG-synthase_like 2.23e-38 20 193 1 183
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.
pfam09835 DUF2062 8.11e-21 269 385 14 130
Uncharacterized protein conserved in bacteria (DUF2062). This domain, found in various prokaryotic proteins, has no known function.
pfam00535 Glycos_transf_2 4.30e-18 19 130 1 115
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.
COG0463 WcaA 2.37e-17 20 266 7 243
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
cd06442 DPM1_like 2.81e-17 20 208 1 198
DPM1_like represents putative enzymes similar to eukaryotic DPM1. Proteins similar to eukaryotic DPM1, including enzymes from bacteria and archaea; 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. This protein family belongs to Glycosyltransferase 2 superfamily.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUR44619.1 1.43e-148 13 391 14 394
QNL40921.1 2.87e-148 13 391 14 394
SCV08080.1 8.17e-148 13 391 14 394
QRQ55492.1 8.17e-148 13 391 14 394
ALJ48662.1 8.17e-148 13 391 14 394

PDB Hits      help

has no PDB hit.

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
A0QZ12 1.06e-16 5 208 14 225
Polyprenol monophosphomannose synthase OS=Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) OX=246196 GN=ppm1 PE=1 SV=1
D4GYG3 1.40e-13 19 224 8 211
Glycosyltransferase AglJ OS=Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) OX=309800 GN=aglJ PE=1 SV=1
Q9LM93 7.79e-13 20 210 17 218
Dolichol-phosphate mannosyltransferase subunit 1 OS=Arabidopsis thaliana OX=3702 GN=DPMS1 PE=1 SV=1
B3VA58 3.79e-12 20 211 8 220
UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminyltransferase OS=Methanococcus voltae OX=2188 GN=aglK PE=1 SV=1
Q57964 5.77e-11 21 218 4 209
Uncharacterized protein MJ0544 OS=Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) OX=243232 GN=MJ0544 PE=4 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
1.000069 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      download full data without filtering help

start end
225 244
278 300
313 335
366 388