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-glucoronosyl transferases (EC 220.127.116.11) (UDPGT) [1,2]. 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
A large number of putative UDPGT from Caenorhabditis elegans.
Mammalian 2-hydroxyacylsphingosine 1-β-galactosyltransferase 
(EC 18.104.22.168) (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 22.214.171.124). 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
Baculoviruses ecdysteroid UDP-glucosyltransferase (EC 2.4.1.-)  (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 glucosyl transferase (EC 2.4.1.-) (gene crtX), an
enzyme involved in carotenoid biosynthesis and that catalyses the
glycosylation reaction which converts zeaxanthin to zeaxanthin-β-
Streptomyces macrolide glycosyltransferases (EC 2.4.1.-) . These enzymes
specifically inactivates macrolide anitibiotics via 2'-O-glycosylation
These enzymes share a conserved domain of about 50 amino acid residues located
in their C-terminal section and from which a pattern has been extracted to
December 2004 / Pattern and text revised.
PROSITE method (with tools and information) covered by this documentation:
(In) Glucoronidation of drugs and other compounds, Dutton G.J., Ed., pp 1-78, CRC Press, Boca Raton, (1980).
PROSITE is copyright. It is produced by the SIB Swiss Institute
Bioinformatics. There are no restrictions on its use by non-profit
institutions as long as its content is in no way modified. Usage by and
for commercial entities requires a license agreement. For information
about the licensing scheme send an email to
or see: prosite_license.html.