GT-CORE (public beta v1)

Glycosyltransferase Curated Online Resource for Enzymology

Family-organised sequence, structure, mechanism and substrate-specificity records for the CAZy glycosyltransferases

DPM1

Homo sapiens · Dolichol-phosphate mannosyltransferase subunit 1 (EC 2.4.1.83)

GT2Model organism · annotation ≥ 4Fold GT-AInverting

External resources

Identification and annotation

CAZy familyGT2 · CAZy entry
Gene symbolDPM1
Synonyms / alternate names
  • Dolichol-phosphate mannose synthase subunit 1
  • Dolichyl-phosphate beta-D-mannosyltransferase subunit 1
  • Mannose-P-dolichol synthase subunit 1
UniProt accessionO60762
NCBI Gene ID8813
Source speciesHomo sapiens
Taxonomic domainEukaryota
UniProt annotation level5

Function and localisation

Enzyme functionDolichol-phosphate mannosyltransferase subunit 1 (EC 2.4.1.83)
Subcellular locationEndoplasmic reticulum

Structure and mechanism

Fold typeGT-A
Catalytic mechanismInverting
Cation dependenceYes (Mg2+, Mn2+, Ca2+)
Oligomeric stateComponent of the dolichol-phosphate mannose (DPM) synthase c
PDB structuresnot curated

Donor and acceptor specificity

Sugar nucleotide donorGDP-alpha-D-mannose
Donor CCD code(s)GDD
Acceptor substrate(s)
  • a di-trans
  • poly-cis-dolichyl phosphate
Acceptor CCD / GlycoCTnot curated

Protein sequences

Full protein sequence

260 aa
MASLEVSRSPRRSRRELEVRSPRQNKYSVLLPTYNERENLPLIVWLLVKSFSESGINYEIIIIDDGSPDGTRDVAEQLEKIYGSDRILLRPREKKLGLGTAYIHGMKHATGNYIIIMDADLSHHPKFIPEFIRKQKEGNFDIVSGTRYKGNGGVYGWDLKRKIISRGANFLTQILLRPGASDLTGSFRLYRKEVLEKLIEKCVSKGYVFQMEMIVRARQLNYTIGEVPISFVDRVYGESKLGGNEIVSFLKGLLTLFATT

Catalytic domain sequence

228 aa
VLLPTYNERENLPLIVWLLVKSFSESGINYEIIIIDDGSPDGTRDVAEQLEKIYGSDRILLRPREKKLGLGTAYIHGMKHATGNYIIIMDADLSHHPKFIPEFIRKQKEGNFDIVSGTRYKGNGGVYGWDLKRKIISRGANFLTQILLRPGASDLTGSFRLYRKEVLEKLIEKCVSKGYVFQMEMIVRARQLNYTIGEVPISFVDRVYGESKLGGNEIVSFLKGLLTL