LMPD Database

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LMP007360

UniProt Annotations

Entry Information
Gene Namedolichyl-phosphate beta-D-mannosyltransferase
Protein EntryDPM1_YEAST
UniProt IDP14020
SpeciesYeast (S288c)
Comments
Comment typeDescription
Biophysicochemical PropertiesKinetic parameters: KM=1.2 uM for GDP-mannose {ECO:0000269|PubMed:15548536}; Vmax=25.1 nmol/min/mg enzyme for GDP-mannose {ECO:0000269|PubMed:15548536}; Note=For the phosphorylated protein, the Vmax increases to 146.7 nmol/min/mg enzyme, whereas the KM stays at 1.1 uM for GDP- mannose, increasing the catalytic efficiency 6-fold.;
Biophysicochemical PropertiesKinetic parameters: KM=1.2 uM for GDP-mannose ; Vmax=25.1 nmol/min/mg enzyme for GDP-mannose ; Note=For the phosphorylated protein, the Vmax increases to 146.7 nmol/min/mg enzyme, whereas the KM stays at 1.1 uM for GDP- mannose, increasing the catalytic efficiency 6-fold.;
Catalytic ActivityGDP-mannose + dolichyl phosphate = GDP + dolichyl D-mannosyl phosphate.
FunctionTransfers mannose from GDP-mannose to dolichol monophosphate to form dolichol phosphate mannose (Dol-P-Man) which is the mannosyl donor in pathways leading to N-glycosylation, glycosyl phosphatidylinositol membrane anchoring, and O- mannosylation of proteins.
MiscellaneousPresent with 1885 molecules/cell in log phase SD medium
MiscellaneousPresent with 1885 molecules/cell in log phase SD medium. {ECO:0000269|PubMed:14562106}.
PathwayProtein modification; protein glycosylation.
SimilarityBelongs to the glycosyltransferase 2 family
SimilarityBelongs to the glycosyltransferase 2 family. {ECO:0000305}.
Subcellular LocationEndoplasmic reticulum membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15657391}; Single-pass type IV membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15657391}.
Subcellular LocationEndoplasmic reticulum membrane ; Single-pass type IV membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15657391}.
SubunitInteracts with the C-terminus of SAC1, thereby sequestering it to the endoplasmic reticulum in exponentially growing cells. Under nutrient limitation conditions, this interaction is rapidly abolished
SubunitInteracts with the C-terminus of SAC1, thereby sequestering it to the endoplasmic reticulum in exponentially growing cells. Under nutrient limitation conditions, this interaction is rapidly abolished. {ECO:0000269|PubMed:15657391}.