GT-CORE (public beta v1)

Glycosyltransferase Curated Online Resource for Enzymology

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

UGT79T1

Saponaria officinalis · UDP-glucosyl transferase 79T1 (EC 2.4.1.-)

GT1Non-model organism · annotation 4–5Fold GT-BInverting

External resources

Identification and annotation

CAZy familyGT1 · CAZy entry
Gene symbolUGT79T1
Synonyms / alternate namesSaoffv11049136m
UniProt accessionA0AAW1IQ05
NCBI Gene IDnot curated
Source speciesSaponaria officinalis
Taxonomic domainEukaryota
UniProt annotation level4

Function and localisation

Enzyme functionUDP-glucosyl transferase 79T1 (EC 2.4.1.-)
Subcellular locationnot curated

Structure and mechanism

Fold typeGT-B
Catalytic mechanismInverting
Cation dependenceNo
Oligomeric statenot curated
PDB structuresnot curated

Donor and acceptor specificity

Sugar nucleotide donorUDP-beta-L-rhamnose
Donor CCD code(s)AWU
Acceptor substrate(s)3-O-{beta-D-Xyl-(1->3)-[beta-D-Gal-(1->2)]-beta-D-GlcA}-quillaic acid beta-D-Fuc ester
Acceptor CCD / GlycoCTnot curated

Protein sequences

Full protein sequence

447 aa
MSAKMLHVVMYPWFAYGHMIPFLHLSNKLAETGHKVTYILPPKALTRLQNLNLNPTQITFRTITVPRVDGLPAGAENVTDIPDITLHTHLATALDRTRPEFETIVELIKPDVIMYDVAYWVPEVAVKYGAKSVAYSVVSAASVSLSKTVVDRMTPLEKPMTEEERKKKFAQYPHLIQLYGPFGEGITMYDRLTGMLSKCDAIACRTCREIEGKYCQYLSTQYEKKVTLTGPVLPEPEVGATLEAPWSEWLSRFKLGSVLFCAFGSQFYLDKDQFQEIILGLEMTNLPFLMAVQPPKGCATIEEAYPEGFAERVKDRGVVTSQWVQQLVILAHPAVGCFVNHCAFGTMWEALLSEKQLVMIPQLGDQILNTKMLADELKVGVEVERGIGGWVSKENLCKAIKSVMDEDSEIGKDVKQSHEKWRATLSSKDLMSTYIDSFIKDLQALVE

Catalytic domain sequence

403 aa
LHVVMYPWFAYGHMIPFLHLSNKLAETGHKVTYILPPKALTRLQNLNLNPTQITFRTITVPRVDGLPAGAENVTDIPDITLHTHLATALDRTRPEFETIVELIKPDVIMYDVAYWVPEVAVKYGAKSVAYSVVSAASVSLSKTVVDRMTPLEKPMTEEERKKKFAQYPHLIQLYGPFGEGITMYDRLTGMLSKCDAIACRTCREIEGKYCQYLSTQYEKKVTLTGPVLPEPEVGATLEAPWSEWLSRFKLGSVLFCAFGSQFYLDKDQFQEIILGLEMTNLPFLMAVQPPKGCATIEEAYPEGFAERVKDRGVVTSQWVQQLVILAHPAVGCFVNHCAFGTMWEALLSEKQLVMIPQLGDQILNTKMLADELKVGVEVERGIGGWVSKENLCKAIKSVMDEDS