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{PDOC00631}
{PS00794; HPPK}
{BEGIN}
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* 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase signature *
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All organisms require reduced folate cofactors  for the synthesis of a variety
of metabolites.  Most  microorganisms  must synthesize folate  de novo because
they lack the  active transport system of higher vertebrate cells which allows
these organisms   to   use   dietary   folates.  Enzymes  involved  in  folate
biosynthesis are therefore targets for a variety of antimicrobial agents  such
as trimethoprim or sulfonamides.

7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase     (EC 2.7.6.3)    (HPPK)
catalyzes the attachment of pyrophosphate to 6-hydroxymethyl-7,8-dihydropterin
to form 6-hydroxymethyl-7,8-dihydropteridine pyrophosphate.  This is the first
step in a three-step pathway leading to 7,8-dihydrofolate.

Bacterial HPPK (gene folK or sulD) [1] is a  protein  of      160 to 270 amino
acids. In the lower eukaryote Pneumocystis carinii, HPPK is the central domain
of a multifunctional folate synthesis enzyme (gene fas) [2].

As a signature for HPPK, we selected a conserved region located in the central
section of these enzymes.

-Consensus pattern: [KRHD]-x-[GA]-[PSAE]-R-x(2)-D-[LIV]-D-[LIVM](2)
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: July 1999 / Pattern and text revised.

[ 1] Talarico T.L., Ray P.H., Dev I.K., Merrill B.M., Dallas W.S.
     "Cloning, sequence analysis, and overexpression of Escherichia coli
     folK, the gene coding for
     7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase."
     J. Bacteriol. 174:5971-5977(1992).
     PubMed=1325970
[ 2] Volpes F., Dyer M., Scaife J.G., Darby G., Stammers D.K., Delves C.J.
     Gene 112:213-218(1992).

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