UDP-glycosyltransferase family, conserved site (IPR035595)

Short name: UDP_glycos_trans_CS

Overlapping homologous superfamilies


Domain relationships



UDP glycosyltransferases (UGT) are a superfamily of enzymes that catalyzes the addition of the glycosyl group from a UTP-sugar to a small hydrophobic molecule. This family currently consist of:

  • Mammalian UDP-glucuronosyl transferases (EC: (UDPGT) [PMID: 1909870]. A large family of membrane-bound microsomal enzymes which catalyze the transfer of glucuronic acid to a wide variety of exogenous and endogenous lipophilic substrates. These enzymes are of major importance in the detoxification and subsequent elimination of xenobiotics such as drugs and carcinogens.
  • A large number of putative UDPGT from Caenorhabditis elegans.
  • Mammalian 2-hydroxyacylsphingosine 1-beta-galactosyltransferase [PMID: 7694285] (EC: (also known as UDP-galactose-ceramide galactosyltransferase). This enzyme catalyzes the transfer of galactose to ceramide, a key enzymatic step in the biosynthesis of galactocerebrosides, which are abundant sphingolipids of the myelin membrane of the central nervous system and peripheral nervous system.
  • Plants flavonol O(3)-glucosyltransferase (EC: An enzyme that catalyzes the transfer of glucose from UDP-glucose to a flavanol. This reaction is essential and one of the last steps in anthocyanin pigment biosynthesis.
  • Baculoviruses ecdysteroid UDP-glucosyltransferase (EC:2.4.1) [PMID: 2505387] (egt). This enzyme catalyzes the transfer of glucose from UDP-glucose to ectysteroids which are insect molting hormones. The expression of egt in the insect host interferes with the normal insect development by blocking the molting process.
  • Prokaryotic zeaxanthin glucosyltransferase (EC:2.4.1) (gene crtX), an enzyme involved in carotenoid biosynthesis and that catalyses the glycosylation reaction which converts zeaxanthin to zeaxanthin-beta-diglucoside.
  • Streptomyces macrolide glycosyltransferases (EC:2.4.1) [PMID: 8244027]. These enzymes specifically inactivates macrolide anitibiotics via 2'-O-glycosylation using UDP-glucose.

These enzymes share a conserved domain of about 50 amino acid residues located in their C-terminal section.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE patterns