The domain within your query sequence starts at position 85 and ends at position 214; the E-value for the acidPPc domain shown below is 3.98e-13.
WARNING!
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 | |||
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Position | Amino acid | Present? | |
Domain | Protein | ||
64 | 148 | H | Yes |
120 | 204 | H | Yes |
N/A | N/A | D | No |
ACLAASLALALNGVFTNIIKLIVGRPRPDFFYRCFPDGLAHSDLTCTGDEDVVNEGRKSF PSGHSSFAFAGLAFASFYLAGKLHCFTPQGRGKSWRLCAFLSPLLFAAVIALSRTCDYKH HWQGWYKDMH
acidPPcAcid phosphatase homologues |
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SMART accession number: | SM00014 |
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Description: | - |
Interpro abstract (IPR000326): | This entry represents type 2 phosphatidic acid phosphatase (PAP2; EC 3.1.3.4 ) enzymes, such as phosphatidylglycerophosphatase B EC 3.1.3.27 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: |
There are 60557 acidPPc domains in 60341 proteins in SMART's nrdb database.
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- Evolution (species in which this domain is found)
- Disease (disease genes where sequence variants are found in this domain)
- Metabolism (metabolic pathways involving proteins which contain this domain)
- Structure (3D structures containing this domain)
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