{PDOC00538} {PS00616; HIS_ACID_PHOSPHAT_1} {PS00778; HIS_ACID_PHOSPHAT_2} {BEGIN} ****************************************** * 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. - Caenorhabditis elegans hypothetical proteins B0361.7, C05C10.1, C05C10.4 and F26C11.1. -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. -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. -Last update: April 2006 / Pattern 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. "Overexpression, site-directed mutagenesis, and mechanism of Escherichia coli acid phosphatase." J. Biol. Chem. 267:22830-22836(1992). PubMed=1429631 [ 3] Schneider G., Lindqvist Y., Vihko P. "Three-dimensional structure of rat acid phosphatase." EMBO J. 12:2609-2615(1993). PubMed=8334986 -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}