PROSITE documentation PDOC00359

UDP-glycosyltransferases signature




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-glucoronosyl transferases (EC 2.4.1.17) (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 carcinogens.
  • A large number of putative UDPGT from Caenorhabditis elegans.
  • Mammalian 2-hydroxyacylsphingosine 1-β-galactosyltransferase [3] (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 [4] 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.
  • Plants limonoid glucosyltransferase (EC 2.4.1.210).
  • Baculoviruses ecdysteroid UDP-glucosyltransferase (EC 2.4.1.-) [5] (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- diglucoside.
  • Streptomyces macrolide glycosyltransferases (EC 2.4.1.-) [6]. 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 and from which a pattern has been extracted to detect them.

Last update:

December 2004 / Pattern and text revised.

Technical section

PROSITE method (with tools and information) covered by this documentation:

UDPGT, PS00375; UDP-glycosyltransferases signature  (PATTERN)


References

1AuthorsDutton G.J.
Source(In) Glucoronidation of drugs and other compounds, Dutton G.J., Ed., pp 1-78, CRC Press, Boca Raton, (1980).

2AuthorsBurchell B., Nebert D.W., Nelson D.R., Bock K.W., Iyanagi T., Jansen P.L., Lancet D., Mulder G.J., Chowdhury J.R., Siest G., Tephly T.R., Mackenzie P.I.
SourceDNA Cell Biol. 10:487-494(1991).

3AuthorsSchulte S., Stoffel W.
TitleCeramide UDPgalactosyltransferase from myelinating rat brain: purification, cloning, and expression.
SourceProc. Natl. Acad. Sci. U.S.A. 90:10265-10269(1993).
PubMed ID7694285

4AuthorsFurtek D., Schiefelbein J.W., Johnston F., Nelson O.E. Jr.
SourcePlant Mol. Biol. 11:473-481(1988).

5AuthorsO'Reilly D.R., Miller L.K.
SourceScience 245:1110-1112(1989).

6AuthorsHernandez C., Olano C., Mendez C., Salas J.A.
TitleCharacterization of a Streptomyces antibioticus gene cluster encoding a glycosyltransferase involved in oleandomycin inactivation.
SourceGene 134:139-140(1993).
PubMed ID8244027



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
Prosite License or see: prosite_license.html.

Miscellaneous

View entry in original PROSITE document format
View entry in raw text format (no links)