Family

UDP-glucuronosyl/UDP-glucosyltransferase (IPR002213)

Short name: UDP_glucos_trans

Family relationships

Description

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:2.4.1.17) (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:2.4.1.45) (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:2.4.1.91). 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.

GO terms

Biological Process

GO:0008152 metabolic process

Molecular Function

GO:0016758 transferase activity, transferring hexosyl groups

Cellular Component

No terms assigned in this category.

Contributing signatures

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