Schultz et al. (1998) Proc. Natl. Acad. Sci. USA 95, 5857-5864
Letunic et al. (2012) Nucleic Acids Res , doi:10.1093/nar/gkr931

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acidPPc Acid phosphatase homologues

SMART accession number:	SM00014
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.
GO component:	membrane (GO:0016020)
GO function:	catalytic activity (GO:0003824)
Family alignment:	View or CHROMA formatCLUSTALW formatMSF formatFASTA formatPIR format

There are 4706 acidPPc domains in 4699 proteins in SMART's nrdb database.

Click on the following links for more information.

• Evolution (species in which this domain is found)

• Click on to expand nodes. To display all proteins with a acidPPc domain in a specific node, click on it.

  This tree shows only several representative species. The complete taxonomic breakdown of all proteins with acidPPc domain is also avaliable.

  Useful shortcuts: Expand all nodes or Collapse tree
  Go to specific node: Anopheles gambiae, Arabidopsis thaliana, Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens, Mus musculus, Rattus norvegicus, Saccharomyces cerevisiae, Takifugu rubripes

• Disease (disease genes where sequence variants are found in this domain)

• SwissProt sequences and OMIM curated human diseases associated with missense mutations within the acidPPc domain.

  Protein	Disease
  UNKNOWN (SMART)	OMIM:232200: Glycogen storage disease I

• Metabolism (metabolic pathways involving proteins which contain this domain)

• Click the image to view the interactive version of the map in iPath

  % proteins involved KEGG pathway ID Description 27.27 map00564 Glycerophospholipid metabolism 12.73 map00600 Sphingolipid metabolism 10.00 map00561 Glycerolipid metabolism 9.70 map00740 Riboflavin metabolism 6.97 map00361 gamma-Hexachlorocyclohexane degradation 5.15 map00510 N-Glycan biosynthesis 2.73 map00760 Nicotinate and nicotinamide metabolism 2.73 map00530 Aminosugars metabolism 2.73 map04070 Phosphatidylinositol signaling system 2.73 map00730 Thiamine metabolism 2.73 map00051 Fructose and mannose metabolism 2.42 map04920 Adipocytokine signaling pathway 2.42 map00052 Galactose metabolism 2.42 map04910 Insulin signaling pathway 2.42 map00500 Starch and sucrose metabolism 2.42 map00010 Glycolysis / Gluconeogenesis 2.12 map02020 Two-component system - General 0.30 map00550 Peptidoglycan biosynthesis This information is based on mapping of SMART genomic protein database to KEGG orthologous groups. Percentage points are related to the number of proteins with acidPPc domain which could be assigned to a KEGG orthologous group, and not all proteins containing acidPPc domain. Please note that proteins can be included in multiple pathways, ie. the numbers above will not always add up to 100%.

• Structure (3D structures containing this domain)

• 3D Structures of acidPPc domains in PDB

  PDB code	Main view	Title
  1d2t		Crystal structure of acid phosphatase from escherichia blattae
  1eoi		Crystal structure of acid phosphatase from escherichia blattae complexed with the transition state analog molybdate
  1iw8		Crystal structure of a mutant of acid phosphatase from escherichia blattae (g74d/i153t)
  2a96		Crystal structure of phosphate tethered phon of s. typhimurium
  2akc		Crystal structure of tungstate complex of the phon protein from s. typhimurium
  2ipb		Crystal structure of t159d mutant of s. typhimurium phon protein

• Links (links to other resources describing this domain)

• INTERPRO	IPR000326

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