PROSITE documentation PDOC00631
7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase signature


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 (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.

Last update:

July 1999 / Pattern and text revised.


Technical section

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

HPPK, PS00794; 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase signature  (PATTERN)


1AuthorsTalarico T.L. Ray P.H. Dev I.K. Merrill B.M. Dallas W.S.
TitleCloning, sequence analysis, and overexpression of Escherichia coli folK, the gene coding for 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase.
SourceJ. Bacteriol. 174:5971-5977(1992).
PubMed ID1325970

2AuthorsVolpes F. Dyer M. Scaife J.G. Darby G. Stammers D.K. Delves C.J.
SourceGene 112:213-218(1992).

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