The domain within your query sequence starts at position 59 and ends at position 180; the E-value for the acidPPc domain shown below is 1.31e-13.

Some of the required catalytic sites were not detected in this domain. It is probably inactive! Check the literature (PubMed 10835340 ) for details.

Catalytic residues
PositionAmino acidPresent?


Acid phosphatase homologues
SMART accession number:SM00014
Description: -
Interpro abstract (IPR000326):

This entry represents type 2 phosphatidic acid phosphatase (PAP2; EC enzymes, such as phosphatidylglycerophosphatase B EC from Escherichia coli. PAP2 enzymes have a core structure consisting of a 5-helical bundle, where the beginning of the third helix binds the cofactor [(PUBMED:10835340)]. PAP2 enzymes catalyse the dephosphorylation of phosphatidate, yielding diacylglycerol and inorganic phosphate [(PUBMED:17079146)]. In eukaryotic cells, PAP activity has a central role in the synthesis of phospholipids and triacylglycerol through its product diacylglycerol, and it also generates and/or degrades lipid-signalling molecules that are related to phosphatidate.

Other related enzymes have a similar core structure, including haloperoxidases such as bromoperoxidase (contains one core bundle, but forms a dimer), chloroperoxidases (contains two core bundles arranged as in other family dimers), bacitracin transport permease from Bacillus licheniformis, glucose-6-phosphatase from rat. The vanadium-dependent haloperoxidases exclusively catalyse the oxidation of halides, and act as histidine phosphatases, using histidine for the nucleophilic attack in the first step of the reaction [(PUBMED:12447906)]. Amino acid residues involved in binding phosphate/vanadate are conserved between the two families, supporting a proposal that vanadium passes through a tetrahedral intermediate during the reaction mechanism.

Family alignment:
View or

There are 60557 acidPPc domains in 60341 proteins in SMART's nrdb database.

Click on the following links for more information.