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PROSITE documentation PDOC00538

Histidine acid phosphatases signatures


Acid phosphatases (EC are a heterogeneous group of proteins that hydrolyze phosphate esters, optimally at low pH. It has been shown [1] that a number of acid phosphatases, from both prokaryotes and eukaryotes, share two regions of sequence similarity, each centered around a conserved histidine residue. These two histidines seem to be involved in the enzymes' catalytic mechanism [2,3]. The first histidine is located in the N-terminal section and forms a phosphohistidine intermediate while the second is located in the C-terminal section and possibly acts as proton donor. Enzymes belonging to this family are called 'histidine acid phosphatases' and are listed below:

  • Escherichia coli pH 2.5 acid phosphatase (gene appA).
  • Escherichia coli glucose-1-phosphatase (EC (gene agp).
  • Yeast constitutive and repressible acid phosphatases (genes PHO3 and PHO5).
  • Fission yeast acid phosphatase (gene pho1).
  • Aspergillus phytases A and B (EC (gene phyA and phyB).
  • Mammalian lysosomal acid phosphatase.
  • Mammalian prostatic acid phosphatase.
  • Caenorhabditis elegans hypothetical proteins B0361.7, C05C10.1, C05C10.4 and F26C11.1.
Last update:

April 2006 / Pattern revised.

Technical section

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

HIS_ACID_PHOSPHAT_1, PS00616; Histidine acid phosphatases phosphohistidine signature  (PATTERN)

HIS_ACID_PHOSPHAT_2, PS00778; Histidine acid phosphatases active site signature  (PATTERN)


1Authorsvan Etten R.L., Davidson R., Stevis P.E., MacArthur H., Moore D.L.
SourceJ. Biol. Chem. 266:2313-2319(1991).

2AuthorsOstanin K., Harms E.H., Stevis P.E., Kuciel R., Zhou M.-M., Van Etten R.L.
TitleOverexpression, site-directed mutagenesis, and mechanism of Escherichia coli acid phosphatase.
SourceJ. Biol. Chem. 267:22830-22836(1992).
PubMed ID1429631

3AuthorsSchneider G., Lindqvist Y., Vihko P.
TitleThree-dimensional structure of rat acid phosphatase.
SourceEMBO J. 12:2609-2615(1993).
PubMed ID8334986

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