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CAZyme Information: MGYG000001757_01290

You are here: Home > Sequence: MGYG000001757_01290

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 Ruminococcus sp900540005
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Ruminococcus; Ruminococcus sp900540005
CAZyme ID MGYG000001757_01290
CAZy Family GT2
CAZyme Description Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
322 MGYG000001757_30|CGC1 36147.94 7.7774
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001757 2373085 MAG Sweden Europe
Gene Location Start: 16568;  End: 17536  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001757_01290.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT2 7 165 5.6e-23 0.9529411764705882

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd04179 DPM_DPG-synthase_like 8.60e-50 5 184 1 185
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.
cd04187 DPM1_like_bac 5.36e-26 7 173 3 167
Bacterial DPM1_like enzymes are related to eukaryotic DPM1. A family of bacterial enzymes related to eukaryotic DPM1; Although the mechanism of eukaryotic enzyme is well studied, the mechanism of the bacterial enzymes is not well understood. The eukaryotic 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. 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. This protein family belongs to Glycosyltransferase 2 superfamily.
cd04188 DPG_synthase 5.36e-24 7 168 3 171
DPG_synthase is involved in protein N-linked glycosylation. 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.
cd06442 DPM1_like 5.33e-23 4 196 1 197
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.
pfam00535 Glycos_transf_2 2.56e-21 7 164 4 163
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QWT52101.1 1.00e-157 1 318 1 318
QUC68516.1 4.20e-154 1 312 1 312
AJA50424.1 3.43e-153 1 310 1 310
AOZ73870.1 3.43e-153 1 310 1 310
AOZ77667.1 3.43e-153 1 310 1 310

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5EKE_A 1.08e-09 1 305 26 321
Structureof the polyisoprenyl-phosphate glycosyltransferase GtrB (F215A mutant) [Synechocystis sp. PCC 6803 substr. Kazusa],5EKE_B Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (F215A mutant) [Synechocystis sp. PCC 6803 substr. Kazusa],5EKE_C Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (F215A mutant) [Synechocystis sp. PCC 6803 substr. Kazusa],5EKE_D Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (F215A mutant) [Synechocystis sp. PCC 6803 substr. Kazusa]
5EKP_A 1.94e-09 1 305 26 321
Structureof the polyisoprenyl-phosphate glycosyltransferase GtrB (WT) [Synechocystis sp. PCC 6803 substr. Kazusa],5EKP_B Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (WT) [Synechocystis sp. PCC 6803 substr. Kazusa],5EKP_C Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (WT) [Synechocystis sp. PCC 6803 substr. Kazusa],5EKP_D Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (WT) [Synechocystis sp. PCC 6803 substr. Kazusa]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
B3VA58 1.26e-22 7 198 10 218
UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminyltransferase OS=Methanococcus voltae OX=2188 GN=aglK PE=1 SV=1
Q58619 9.05e-18 2 198 18 214
Uncharacterized protein MJ1222 OS=Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) OX=243232 GN=MJ1222 PE=4 SV=1
C5CBV8 1.83e-14 1 196 1 201
Undecaprenyl-phosphate mannosyltransferase OS=Micrococcus luteus (strain ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 / NCIMB 9278 / NCTC 2665 / VKM Ac-2230) OX=465515 GN=Mlut_12000 PE=1 SV=1
A2E3C6 8.14e-12 7 199 80 289
Dolichyl-phosphate beta-glucosyltransferase ALG5D OS=Trichomonas vaginalis OX=5722 GN=ALG5D PE=1 SV=1
A2ELE6 9.37e-11 7 199 82 291
Dolichyl-phosphate beta-glucosyltransferase ALG5C OS=Trichomonas vaginalis OX=5722 GN=ALG5C 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
1.000086 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      download full data without filtering help

start end
234 256
266 288