GT-CORE (public beta v1)

Glycosyltransferase Curated Online Resource for Enzymology

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

KRE2

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) · Glycolipid 2-alpha-mannosyltransferase (EC 2.4.1.-)

GT15Model organism · annotation ≥ 4Fold GT-ARetaining3 PDB structure(s)

External resources

Identification and annotation

CAZy familyGT15 · CAZy entry
Gene symbolKRE2
Synonyms / alternate names
  • MNT1
  • Alpha-1,2-mannosyltransferase
UniProt accessionP27809
NCBI Gene ID852094
Source speciesSaccharomyces cerevisiae (strain ATCC 204508 / S288c)
Taxonomic domainEukaryota
UniProt annotation level5

Function and localisation

Enzyme functionGlycolipid 2-alpha-mannosyltransferase (EC 2.4.1.-)
Subcellular locationGolgi apparatus membrane

Structure and mechanism

Fold typeGT-A
Catalytic mechanismRetaining
Cation dependenceYes (Mn2+)
Oligomeric statenot curated
PDB structures1S4N, 1S4O, 1S4P

Donor and acceptor specificity

Sugar nucleotide donornot curated
Donor CCD code(s)not curated
Acceptor substrate(s)not curated
Acceptor CCD / GlycoCTnot curated

Protein sequences

Full protein sequence

442 aa
MALFLSKRLLRFTVIAGAVIVLLLTLNSNSRTQQYIPSSISAAFDFTSGSISPEQQVISEENDAKKLEQSALNSEASEDSEAMDEESKALKAAAEKADAPIDTKTTMDYITPSFANKAGKPKACYVTLVRNKELKGLLSSIKYVENKINKKFPYPWVFLNDEPFTEEFKEAVTKAVSSEVKFGILPKEHWSYPEWINQTKAAEIRADAATKYIYGGSESYRHMCRYQSGFFWRHELLEEYDWYWRVEPDIKLYCDINYDVFKWMQENEKVYGFTVSIHEYEVTIPTLWQTSMDFIKKNPEYLDENNLMSFLSNDNGKTYNLCHFWSNFEIANLNLWRSPAYREYFDTLDHQGGFFYERWGDAPVHSIAAALFLPKDKIHYFSDIGYHHPPYDNCPLDKEVYNSNNCECDQGNDFTFQGYSCGKEYYDAQGLVKPKNWKKFRE

Catalytic domain sequence

348 aa
AMDEESKALKAAAEKADAPIDTKTTMDYITPSFANKAGKPKACYVTLVRNKELKGLLSSIKYVENKINKKFPYPWVFLNDEPFTEEFKEAVTKAVSSEVKFGILPKEHWSYPEWINQTKAAEIRADAATKYIYGGSESYRHMCRYQSGFFWRHELLEEYDWYWRVEPDIKLYCDINYDVFKWMQENEKVYGFTVSIHEYEVTIPTLWQTSMDFIKKNPEYLDENNLMSFLSNDNGKTYNLCHFWSNFEIANLNLWRSPAYREYFDTLDHQGGFFYERWGDAPVHSIAAALFLPKDKIHYFSDIGYHHPPYDNCPLDKEVYNSNNCECDQGNDFTFQGYSCGKEYYDAQ