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.

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.

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.

undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional

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.

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]

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]

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]

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]

Prophage bactoprenol glucosyl transferase homolog OS=Escherichia coli (strain K12) OX=83333 GN=yfdH PE=1 SV=1

SfII prophage-derived bactoprenol glucosyl transferase OS=Shigella flexneri OX=623 GN=gtrB PE=3 SV=1

Bactoprenol glucosyl transferase OS=Shigella phage SfII OX=66284 GN=gtrB PE=3 SV=1

Bactoprenol glucosyl transferase OS=Shigella phage SfX OX=10874 GN=gtrB PE=3 SV=1

Bactoprenol glucosyl transferase OS=Shigella phage SfV OX=55884 GN=gtrB PE=3 SV=1