The domain within your query sequence starts at position 1 and ends at position 98; the E-value for the Acylphosphatase domain shown below is 6e-26.



PFAM accession number:PF00708
Interpro abstract (IPR001792):

Acylphosphatase ( EC ) is an enzyme of approximately 98 amino acid residues that specifically catalyses the hydrolysis of the carboxyl-phosphate bond of acylphosphates [ (PUBMED:1664426) ], its substrates including 1,3-diphosphoglycerate and carbamyl phosphate [ (PUBMED: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 [ (PUBMED:2538623) ]: it may, however, play a part in the regulation of the glycolytic pathway and pyrimidine biosynthesis [ (PUBMED: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 [ (PUBMED:9799289) (PUBMED:12206761) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Acylphosphatase