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

Candida albicans (strain SC5314 / ATCC MYA-2876) · Dolichol-phosphate mannosyltransferase subunit 1 (EC 2.4.1.83)

GT2Non-model organism · annotation 4–5Fold GT-AInverting

External resources

Identification and annotation

CAZy familyGT2 · CAZy entry
Gene symbolDPM1
Synonyms / alternate namesnot curated
UniProt accessionA0A1D8PEA2
NCBI Gene ID3640700
Source speciesCandida albicans (strain SC5314 / ATCC MYA-2876)
Taxonomic domainEukaryota
UniProt annotation level4

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 (Ca2+, Mg2+, Mn2+)
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

239 aa
MTQNKYSVILPTYNEKRNLPILIYLLNKTFTANKLDWEVIIVDDNSPDGTQEIAKKLIDIFGPEHIQLRPRAGKLGLGTAYVHGLQFVTGNFVIIMDADFSHHPEAIPEFIAKQKSQDYDIVTGTRYAGDGGVFGWDFKRKLISRGANFLASVVLRPHVSDLTGSFRLYKTDVLRKIIDVTQSKGYVFQMEMMVRAKAMGFTVGEVPISFVDRLYGESKLGGDEIVQYAKGVWTLFTSV

Catalytic domain sequence

171 aa
SVILPTYNEKRNLPILIYLLNKTFTANKLDWEVIIVDDNSPDGTQEIAKKLIDIFGPEHIQLRPRAGKLGLGTAYVHGLQFVTGNFVIIMDADFSHHPEAIPEFIAKQKSQDYDIVTGTRYAGDGGVFGWDFKRKLISRGANFLASVVLRPHVSDLTGSFRLYKTDVLRKI