{PDOC00105}
{PS00114; PRPP_SYNTHASE}
{BEGIN}
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* Phosphoribosyl pyrophosphate synthase signature *
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Phosphoribosyl pyrophosphate  synthase  (EC 2.7.6.1) (PRPP synthase) catalyzes
the formation  of  PRPP  from ATP and ribose 5-phosphate. PRPP is then used in
various biosynthetic  pathways,  as  for  example in the formation of purines,
pyrimidines, histidine   and  tryptophan.  PRPP  synthase  requires  inorganic
phosphate and magnesium ions for its stability and activity.

In mammals,  three  isozymes of PRPP synthase are found; in yeast there are at
least four isozymes.

As a  signature  pattern  for this enzyme, we selected a very conserved region
that has  been  suggested to be involved in binding divalent cations [1]. This
region contains  two  conserved aspartic acid residues as well as a histidine,
which are all potential ligands for a cation such as magnesium.

-Consensus pattern: D-[LIM]-H-[SANDT]-x-[QS]-[IMSTAVF]-[QMLPH]-[GA]-[FY]-F-
                    x(2)-P-[LIVMFCT]-D
                    [The 2 D's and the H are  magnesium ligands]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: April 2006 / Pattern revised.

[ 1] Bower S.G., Harlow K.W., Switzer R.L., Hove-Jensen B.
     "Characterization of the Escherichia coli prsA1-encoded mutant
     phosphoribosylpyrophosphate synthetase identifies a divalent
     cation-nucleotide binding site."
     J. Biol. Chem. 264:10287-10291(1989).
     PubMed=2542328

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