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	PROSITE documentation PDOC00538

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.

Last update:

April 2006 / Pattern revised.

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 in UniProtKB/Swiss-Prot known to belong to this class: 79
  • detected by PS00616: 72 (true positives)
  • undetected by PS00616: 7 (7 false negatives and 0 'partial')
• Other sequence(s) in UniProtKB/Swiss-Prot detected by PS00616:
  5 false positives.
• Retrieve an alignment of UniProtKB/Swiss-Prot true positive hits:
  Clustal format, color, condensed view  /  Clustal format, color  /  Clustal format, plain text  /  Fasta format
• Retrieve the sequence logo from the alignment
• Taxonomic distribution of all UniProtKB (Swiss-Prot + TrEMBL) entries matching PS00616
• Retrieve a list of all UniProtKB (Swiss-Prot + TrEMBL) entries matching PS00616
• Scan UniProtKB (Swiss-Prot and/or TrEMBL) entries against PS00616
• View ligand binding statistics of PS00616
• 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 in UniProtKB/Swiss-Prot known to belong to this class: 78
  • detected by PS00778: 45 (true positives)
  • undetected by PS00778: 33 (32 false negatives and 1 'partial')
• Other sequence(s) in UniProtKB/Swiss-Prot detected by PS00778:
  43 false positives.
• Retrieve an alignment of UniProtKB/Swiss-Prot true positive hits:
  Clustal format, color, condensed view  /  Clustal format, color  /  Clustal format, plain text  /  Fasta format
• Retrieve the sequence logo from the alignment
• Taxonomic distribution of all UniProtKB (Swiss-Prot + TrEMBL) entries matching PS00778
• Retrieve a list of all UniProtKB (Swiss-Prot + TrEMBL) entries matching PS00778
• Scan UniProtKB (Swiss-Prot and/or TrEMBL) entries against PS00778
• View ligand binding statistics of PS00778
• Matching PDB structures: 1CVI 1DKL 1DKM 1DKN ... [ALL]

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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