The domain within your query sequence starts at position 1 and ends at position 90; the E-value for the PAP2 domain shown below is 8.1e-13.



PFAM accession number:PF01569
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.

This is a PFAM domain. For full annotation and more information, please see the PFAM entry PAP2