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PROSITE documentation PDOC00538Histidine acid phosphatases signatures
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Acid phosphatases (EC 3.1.3.2) 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 3.1.3.10) (gene agp).
- Yeast constitutive and repressible acid phosphatases (genes PHO3 and PHO5).
- Fission yeast acid phosphatase (gene pho1).
- Aspergillus phytases A and B (EC 3.1.3.8) (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.
April 2006 / Pattern revised.
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PROSITE methods (with tools and information) covered by this documentation:
| 1 | Authors | van Etten R.L. Davidson R. Stevis P.E. MacArthur H. Moore D.L. |
| Source | J. Biol. Chem. 266:2313-2319(1991). |
| 2 | Authors | Ostanin K. Harms E.H. Stevis P.E. Kuciel R. Zhou M.-M. Van Etten R.L. |
| Title | Overexpression, site-directed mutagenesis, and mechanism of Escherichia coli acid phosphatase. | |
| Source | J. Biol. Chem. 267:22830-22836(1992). | |
| PubMed ID | 1429631 |
| 3 | Authors | Schneider G. Lindqvist Y. Vihko P. |
| Title | Three-dimensional structure of rat acid phosphatase. | |
| Source | EMBO J. 12:2609-2615(1993). | |
| PubMed ID | 8334986 |
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