home *** CD-ROM | disk | FTP | other *** search
- ******************************************
- * Histidine acid phosphatases signatures *
- ******************************************
-
- 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.
-
- -Consensus pattern: [LIVM]-x(2)-[LIVMA]-x(2)-[LIVM]-x-R-H-[GN]-x-R-x-P
- [H is the phosphohistidine residue]
- -Sequences known to belong to this class detected by the pattern: ALL.
- -Other sequence(s) detected in SWISS-PROT: NONE.
-
- -Consensus pattern: [LIVM]-x-[LIVMFA]-x(2)-[STAG]-H-D-[STAN]-x-[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: human transducin beta chain 3.
-
- -Last update: June 1994 / Patterns and text revised.
-
- [ 1] van Etten R.L., Davidson R., Stevis P.E., MacArthur H., Moore D.L.
- J. Biol. Chem. 266:2313-2319(1991).
- [ 2] Ostanin K., Harms E.H., Stevis P.E., Kuciel R., Zhou M.-M.,
- van Etten R.L.
- J. Biol. Chem. 267:22830-22836(1992).
- [ 3] Schneider G., Lindqvist Y., Vihko P.
- EMBO J. 12:2609-2615(1993).
-