Acylphosphatase-like domain (IPR001792)

Short name: Acylphosphatase-like_dom

Overlapping homologous superfamilies

Domain relationships



Acylphosphatase (EC: is an enzyme of approximately 98 amino acid residues that specifically catalyses the hydrolysis of the carboxyl-phosphate bond of acylphosphates [PMID: 1664426], its substrates including 1,3-diphosphoglycerate and carbamyl phosphate [PMID: 2538623]. 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 [PMID: 2538623]: it may, however, play a part in the regulation of the glycolytic pathway and pyrimidine biosynthesis [PMID: 2830253]. 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. A number of bacterial and archebacterial hypothetical proteins are highly similar to that enzyme and that probably possess the same activity.

An acylphosphatase-like domain is also found in some prokaryotic hydrogenase maturation HypF carbamoyltransferases [PMID: 9799289, PMID: 12206761].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE profiles