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| PROSITE documentation PDOC00538 |
Histidine acid phosphatases signatures
Description:
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.
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) |
| Consensus pattern: |
[LIVM]-x(2)-[LIVMA]-x(2)-[LIVM]-x-R-H-[GN]-x-R-x-[PAS]
H is the phosphohistidine residue |
| Sequences known to belong to this class detected by the pattern: |
ALL |
| Other sequence(s) detected in Swiss-Prot: |
2. |
|
|
|
| Matching PDB structures:
1CVI 1DKL 1DKM 1DKN ... [ALL] |
| HIS_ACID_PHOSPHAT_2, PS00778; Histidine acid phosphatases active site signature (PATTERN) |
| Consensus pattern: |
[LIVMF]-x-[LIVMFAG]-{T}-x-[STAGI]-H-D-[STANQ]-{V}-[LIVM]-x(2)-[LIVMFY]-x(2)-[STA]
H is an active site residue |
| Sequences known to belong to this class detected by the pattern: |
ALL, except for rat prostatic acid phosphatase which seems to have Tyr instead of the active site His |
| Other sequence(s) detected in Swiss-Prot: |
14. |
|
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|
| Matching PDB structures:
1CVI 1DKL 1DKM 1DKN ... [ALL] |
References:
| 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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