InterPro: IPR001792 Acylphosphatase-like

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).

An acylphosphatase-like domain is also found in some prokaryotic hydrogenase maturation HypF carbamoyltransferases [4, 5].