<p>Acylphosphatase (<db_xref db="EC" dbkey="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 [<cite idref="PUB00002351"/>], its substrates including 1,3-diphosphoglycerate and carbamyl phosphate [<cite idref="PUB00003238"/>]. 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 [<cite idref="PUB00003238"/>]: it may, however, play a part in the regulation of the glycolytic pathway and pyrimidine biosynthesis [<cite idref="PUB00002331"/>]. 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.</p><p>These proteins include:<ul><li> <taxon tax_id="562">Escherichia coli</taxon> putative acylphosphatase (<db_xref db="EC" dbkey="3.6.1.7"/>) (acylphosphate phosphohydrolase) (gene yccX).</li><li> <taxon tax_id="1423">Bacillus subtilis</taxon> putative acylphosphatase (<db_xref db="EC" dbkey="3.6.1.7"/>) (acylphosphate phosphohydrolase) (gene yflL).</li><li> <taxon tax_id="2234">Archaeoglobus fulgidus</taxon> putative acylphosphatase (<db_xref db="EC" dbkey="3.6.1.7"/>) (acylphosphate phosphohydrolase) (<db_xref db="SWISSPROT" dbkey="O29440"/>).</li></ul> </p><p>This entry is also found in an acylphosphatase-like domain in some prokaryotic hydrogenase maturation HypF carbamoyltransferases [<cite idref="PUB00033805"/>, <cite idref="PUB00011085"/>].</p>