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InterPro: IPR020456 Acylphosphatase

Protein matches Help

UniProtKB

Matches:

621 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR020456 Acylphosphatase

Type

Region

Signatures Help

Database	ID	Name	Proteins
PRINTS	PR00112	ACYLPHPHTASE	621
Signatures in BioMart

InterPro Relationships Help

Parent

IPR001792 Acylphosphatase-like

Contains

IPR017968 Acylphosphatase, conserved site

GO Term annotation Help

Function

GO:0003998 acylphosphatase activity

InterPro annotation

Entry Details in BioMart

Abstract

Acylphosphatase (EC:3.6.1.7) is an enzyme of approximately 98 amino acid residues that specifically catalyses the hydrolysis of the carboxyl-phosphate bond of acylphosphates [1], its substrates including 1,3-diphosphoglycerate and carbamyl phosphate [2]. The enzyme has a mainly beta-sheet structure with 2 short alpha-helical segments. It is distributed in a tissue-specific manner in a wide variety of species, although its physiological role is as yet unknown [2]: it may, however, play a part in the regulation of the glycolytic pathway and pyrimidine biosynthesis [3]. There are two known isozymes. One seems to be specific to muscular tissues, the other, called 'organ-common type', is found in many different tissues. While bacterial and archebacterial hypothetical proteins that are highly similar to that enzyme and that probably possess the same activity.

These proteins include:

Escherichia coli putative acylphosphatase (EC:3.6.1.7) (acylphosphate phosphohydrolase) (gene yccX).
Bacillus subtilis putative acylphosphatase (EC:3.6.1.7) (acylphosphate phosphohydrolase) (gene yflL).
Archaeoglobus fulgidus putative acylphosphatase (EC:3.6.1.7) (acylphosphate phosphohydrolase) (O29440).

Structural links Help

PDB - click here

SCOP: d.58.10.1

CATH: 3.30.70.100

Database links Help

Enzyme: EC:3.6.1.7

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR020456

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O35031 Acylphosphatase

P00818 Acylphosphatase-2

P07311 Acylphosphatase-1

P56375 Acylphosphatase-2

Q9VF36 Acylphosphatase-2

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR001792	Acylphosphatase-like
IPR017968	Acylphosphatase, conserved site
IPR020456	Acylphosphatase
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Mizuno Y, Kanesaka Y, Fujita H, Minowa O, Shiokawa H. The primary structure of two molecular species of porcine organ-common type acylphosphatase. J. Biochem. 110 790-4 1991 [PubMed: 1664426] http://jb.oxfordjournals.org/cgi/content/abstract/110/5/790
2.	Saudek V, Atkinson RA, Williams RJ, Ramponi G. Identification and description of alpha-helical regions in horse muscle acylphosphatase by 1H nuclear magnetic resonance spectroscopy. J. Mol. Biol. 205 229-39 1989 [PubMed: 2538623] http://dx.doi.org/10.1016/0022-2836(89)90377-X
3.	Minowa O, Ohba Y, Mizuno Y, Shiokawa H. The primary structure of chicken muscle acylphosphatase isozyme Ch1. J. Biochem. 102 1213-20 1987 [PubMed: 2830253] http://jb.oxfordjournals.org/cgi/content/abstract/102/5/1213

Additional Reading Open in usermanual
	Cheung YY, Allen MD, Bycroft M, Wong KB. Crystallization and preliminary crystallographic analysis of an acylphosphatase from the hyperthermophilic archaeon Pyrococcus horikoshii. Acta Crystallogr. D Biol. Crystallogr. 60 2004 1308-10 [PubMed: 15213401] http://dx.doi.org/10.1107/S0907444904010996
	Cheung YY, Lam SY, Chu WK, Allen MD, Bycroft M, Wong KB. Crystal structure of a hyperthermophilic archaeal acylphosphatase from Pyrococcus horikoshii--structural insights into enzymatic catalysis, thermostability, and dimerization. Biochemistry 44 2005 4601-11 [PubMed: 15779887] http://dx.doi.org/10.1021/bi047832k
	Thunnissen MM, Taddei N, Liguri G, Ramponi G, Nordlund P. Crystal structure of common type acylphosphatase from bovine testis. Structure 5 1997 69-79 [PubMed: 9016712] http://dx.doi.org/10.1016/S0969-2126(97)00167-6
	Zuccotti S, Rosano C, Ramazzotti M, Degl'Innocenti D, Stefani M, Manao G, Bolognesi M. Three-dimensional structural characterization of a novel Drosophila melanogaster acylphosphatase. Acta Crystallogr. D Biol. Crystallogr. 60 2004 1177-9 [PubMed: 15159593] http://dx.doi.org/10.1107/S0907444904006808
	Pastore A, Saudek V, Ramponi G, Williams RJ. Three-dimensional structure of acylphosphatase. Refinement and structure analysis. J. Mol. Biol. 224 1992 427-40 [PubMed: 1313885] http://dx.doi.org/10.1016/0022-2836(92)91005-A

InterPro 23.1