acidPPcAcid phosphatase homologues
|SMART accession number:||SM00014|
|Interpro abstract (IPR000326):|
This entry represents type 2 phosphatidic acid phosphatase (PAP2; EC 126.96.36.199) enzymes, such as phosphatidylglycerophosphatase B EC 188.8.131.52 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.
|GO component:||membrane (GO:0016020)|
|GO function:||catalytic activity (GO:0003824)|
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