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CAZyme Information: MGYG000003203_03943

You are here: Home > Sequence: MGYG000003203_03943

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 Butyricimonas sp900759925
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Marinifilaceae; Butyricimonas; Butyricimonas sp900759925
CAZyme ID MGYG000003203_03943
CAZy Family GT2
CAZyme Description Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
242 28273.63 6.6383
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003203 5334161 MAG United States North America
Gene Location Start: 3369;  End: 4097  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003203_03943.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT2 5 152 8.4e-19 0.8588235294117647

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd04188 DPG_synthase 3.25e-65 6 221 1 211
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.
cd04179 DPM_DPG-synthase_like 1.17e-42 6 194 1 184
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.
PTZ00260 PTZ00260 2.32e-32 6 242 74 317
dolichyl-phosphate beta-glucosyltransferase; Provisional
cd04187 DPM1_like_bac 8.51e-21 6 173 1 159
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.
pfam00535 Glycos_transf_2 4.97e-18 5 173 1 164
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
QRO49018.1 2.43e-143 1 242 1 242
AZS28989.1 9.44e-141 1 242 1 242
QNM87048.1 8.97e-77 1 241 1 242
BBM87585.1 2.36e-75 6 241 5 237
AXY77483.1 6.70e-74 1 241 80 320

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5MLZ_A 1.27e-08 3 237 24 246
Dolichylphosphate mannose synthase in complex with GDP and Mg2+ [Pyrococcus furiosus DSM 3638],5MM0_A Dolichyl phosphate mannose synthase in complex with GDP-mannose and Mn2+ (donor complex) [Pyrococcus furiosus DSM 3638],5MM1_A Dolichyl phosphate mannose synthase in complex with GDP and dolichyl phosphate mannose [Pyrococcus furiosus DSM 3638]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
A2ELE6 1.91e-26 7 237 81 313
Dolichyl-phosphate beta-glucosyltransferase ALG5C OS=Trichomonas vaginalis OX=5722 GN=ALG5C PE=1 SV=1
A2DZE8 1.56e-24 4 237 75 307
Dolichyl-phosphate beta-glucosyltransferase ALG5A OS=Trichomonas vaginalis OX=5722 GN=ALG5A PE=1 SV=1
A2DSR8 1.60e-23 7 237 78 307
Dolichyl-phosphate beta-glucosyltransferase ALG5E OS=Trichomonas vaginalis OX=5722 GN=ALG5E PE=1 SV=1
A2EK20 2.39e-21 7 237 78 310
Dolichyl-phosphate beta-glucosyltransferase ALG5B OS=Trichomonas vaginalis OX=5722 GN=ALG5B PE=1 SV=1
A2E3C6 1.12e-20 4 237 76 311
Dolichyl-phosphate beta-glucosyltransferase ALG5D OS=Trichomonas vaginalis OX=5722 GN=ALG5D 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
1.000063 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003203_03943.