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InterPro: IPR000560 Histidine acid phosphatase

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1608 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
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Accession List
Matches in BioMart

Accession

IPR000560 Histidine_acid_Pase

Type

Family

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00328	Acid_phosphat_A	1581
PROSITE pattern	PS00616	HIS_ACID_PHOSPHAT_1	893
PROSITE pattern	PS00778	HIS_ACID_PHOSPHAT_2	494
Signatures in BioMart

InterPro Relationships Help

Children

IPR016274 Histidine acid phosphatase, eukaryotic

GO Term annotation Help

Function

GO:0003993 acid phosphatase activity

InterPro annotation

Entry Details in BioMart

Abstract

Acid phosphatases (EC:3.1.3.2) are a heterogeneous group of proteins that hydrolyse 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 centred 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 include:

Escherichia coli pH 2.5 acid phosphatase (gene appA).
E. coli glucose-1-phosphatase (EC:3.1.3.10) (gene agp).
Yeast constitutive and repressible acid phosphatases (genes PHO3 and PHO5).
Schizosaccharomyces pombe acid phosphatase (gene pho1).
Aspergillus awamori phytases A and B (EC:3.1.3.8) (gene phyA and phyB).
Mammalian lysosomal and prostatic acid phosphatase.
Several Caenorhabditis elegans hypothetical proteins.

Structural links Help

PDB - click here

SCOP: c.60.1.2

CATH: 3.40.50.1240

Database links Help

PDBe-motif: PS00616 , PS00778

Enzyme: EC:3

PROSITE doc: PDOC00538

PANDIT: PF00328

Blocks: IPB000560

Pfam Clan: CL0071.8

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR000560

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

A2ARP1 Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1

P00635 Repressible acid phosphatase

P15309 Prostatic acid phosphatase

P91309 Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase

Q9VR59 Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR016274	Histidine acid phosphatase, eukaryotic
IPR000560	Histidine acid phosphatase
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Van Etten RL, Davidson R, Stevis PE, MacArthur H, Moore DL. Covalent structure, disulfide bonding, and identification of reactive surface and active site residues of human prostatic acid phosphatase. J. Biol. Chem. 266 2313-9 1991 [PubMed: 1989985] http://intl.jbc.org/cgi/reprint/266/4/2313.pdf
2.	Schneider G, Lindqvist Y, Vihko P. Three-dimensional structure of rat acid phosphatase. EMBO J. 12 2609-15 1993 [PubMed: 8334986] http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=8334986
3.	Ostanin K, Harms EH, Stevis PE, Kuciel R, Zhou MM, Van Etten RL. Overexpression, site-directed mutagenesis, and mechanism of Escherichia coli acid phosphatase. J. Biol. Chem. 267 22830-6 1992 [PubMed: 1429631] http://intl.jbc.org/cgi/reprint/267/32/22830.pdf

Additional Reading Open in usermanual
	Kostrewa D, Wyss M, D'Arcy A, van Loon AP. Crystal structure of Aspergillus niger pH 2.5 acid phosphatase at 2. 4 A resolution. J. Mol. Biol. 288 1999 965-74 [PubMed: 10329192] http://dx.doi.org/10.1006/jmbi.1999.2736
	Xiang T, Liu Q, Deacon AM, Koshy M, Kriksunov IA, Lei XG, Hao Q, Thiel DJ. Crystal structure of a heat-resilient phytase from Aspergillus fumigatus, carrying a phosphorylated histidine. J. Mol. Biol. 339 2004 437-45 [PubMed: 15136045] http://dx.doi.org/10.1016/j.jmb.2004.03.057
	Liu Q, Huang Q, Lei XG, Hao Q. Crystallographic snapshots of Aspergillus fumigatus phytase, revealing its enzymatic dynamics. Structure 12 2004 1575-83 [PubMed: 15341723] http://dx.doi.org/10.1016/j.str.2004.06.015
	Jakob CG, Lewinski K, Kuciel R, Ostrowski W, Lebioda L. Crystal structure of human prostatic acid phosphatase . Prostate 42 2000 211-8 [PubMed: 10639192]
	Lee DC, Cottrill MA, Forsberg CW, Jia Z. Functional insights revealed by the crystal structures of Escherichia coli glucose-1-phosphatase. J. Biol. Chem. 278 2003 31412-8 [PubMed: 12782623] http://dx.doi.org/10.1074/jbc.M213154200
	Ortlund E, LaCount MW, Lebioda L. Crystal structures of human prostatic acid phosphatase in complex with a phosphate ion and alpha-benzylaminobenzylphosphonic acid update the mechanistic picture and offer new insights into inhibitor design. Biochemistry 42 2003 383-9 [PubMed: 12525165] http://dx.doi.org/10.1021/bi0265067

InterPro 23.1