{PDOC00359}
{PS00375; UDPGT}
{BEGIN}
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* UDP-glycosyltransferases signature *
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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-beta-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-beta-
   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.

-Consensus pattern: [FW]-x(2)-[QL]-x(2)-[LIVMYA]-[LIMV]-x(4,6)-[LVGAC]-
                    [LVFYAHM]-[LIVMF]-[STAGCM]-[HNQ]-[STAGC]-G-x(2)-[STAG]-
                    x(3)-[STAGL]-[LIVMFA]-x(4,5)-[PQR]-[LIVMTA]-x(3)-[PA]-
                    x(2,3)-[DES]-[QEHNR]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: December 2004 / Pattern and text revised.

[ 1] Dutton G.J.
     (In) Glucoronidation of drugs and other compounds, Dutton G.J., Ed.,
     pp 1-78, CRC Press, Boca Raton, (1980).
[ 2] Burchell 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.
     DNA Cell Biol. 10:487-494(1991).
[ 3] Schulte S., Stoffel W.
     "Ceramide UDPgalactosyltransferase from myelinating rat brain:
     purification, cloning, and expression."
     Proc. Natl. Acad. Sci. U.S.A. 90:10265-10269(1993).
     PubMed=7694285
[ 4] Furtek D., Schiefelbein J.W., Johnston F., Nelson O.E. Jr.
     Plant Mol. Biol. 11:473-481(1988).
[ 5] O'Reilly D.R., Miller L.K.
     Science 245:1110-1112(1989).
[ 6] Hernandez C., Olano C., Mendez C., Salas J.A.
     "Characterization of a Streptomyces antibioticus gene cluster encoding
     a glycosyltransferase involved in oleandomycin inactivation."
     Gene 134:139-140(1993).
     PubMed=8244027

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