GT-CORE (public beta v1)

Glycosyltransferase Curated Online Resource for Enzymology

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

bre-3

Caenorhabditis elegans · Beta-1,4-mannosyltransferase bre-3 (EC 2.4.1.-)

GT2Model organism · annotation ≥ 4Fold GT-AInverting

External resources

Identification and annotation

CAZy familyGT2 · CAZy entry
Gene symbolbre-3
Synonyms / alternate namesBacillus thuringiensis toxin-resistant protein 3
UniProt accessionQ03562
NCBI Gene ID176332
Source speciesCaenorhabditis elegans
Taxonomic domainEukaryota
UniProt annotation level4

Function and localisation

Enzyme functionBeta-1,4-mannosyltransferase bre-3 (EC 2.4.1.-)
Subcellular locationCytoplasm

Structure and mechanism

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

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

455 aa
MNCEVKHALHCAVLVAWIVCFAYFCGVFTEPVEGSVPESPVASYGLIWTVCLYLLRFTALLVLPQCLCNLGGLMMFNAFREKVQLKAAPLLSPFVCFRVVTKGNFPLLVKENIDTNMKTCFEAGMENFIFEVVTDKAINLPPNPRVREVVVPTVYKTKSGAKFKARALQYCLEDDVNILQPTDWIVHLDEETLLTTNAICGILNFCEDGKHQFGQGVITYANGDIVNWLTTLSDSFRVADDMGKLRFQFKLFHKPLFGWKGSYVVTQVEAERDVSYDHGMEGSIAEDCFFSMVAMKHGYSFDFIEGEMHEKSPFTMWDFLQQRKRWLQGILLTVHSSKIAVVHKALLALSLYAWATMPLTSLQVFLCPLFPLPRCLPFDFLLSFVGALNLYMYIFGVVKSFSHKYRNSLLRLAMYLAGALMTIPFNILIENAAVLVGMFGRKDQFYIVNKDIQTV

Catalytic domain sequence

211 aa
WIVHLDEETLLTTNAICGILNFCEDGKHQFGQGVITYANGDIVNWLTTLSDSFRVADDMGKLRFQFKLFHKPLFGWKGSYVVTQVEAERDVSYDHGMEGSIAEDCFFSMVAMKHGYSFDFIEGEMHEKSPFTMWDFLQQRKRWLQGILLTVHSSKIAVVHKALLALSLYAWATMPLTSLQVFLCPLFPLPRCLPFDFLLSFVGALNLYMYI