Mitochondrial phosphatidylglycerophosphatase (PGP phosphatase) () dephosphorylates phosphatidylglycerolphosphate to generate phosphatidylglycerol in cardiolipin biosynthesis. Cardiolipin is a unique dimeric phosphoglycerolipid predominantly present in mitochondrial membranes. The inverted phosphatase motif includes the highly conserved DKD triad [, ]. In Saccharomyces cerevisiae, Gep4 is required for the stability of respiratory chain supercomplexes and for growth at elevated temperature, in presence of ethidium bromide or in absence of prohibitins []. Chloroplastic phosphatidylglycerophosphate phosphatase is involved in the biosynthesis of phosphatidylglycerol (PG), a phosphoglycerolipid present in chloroplastic thylakoid membranes and has a photosynthetic function [].
This entry represents a short conserved region carrying a PGP motif that is repeated in the eukaryotic sperm tail protein, outer dense fibre protein 3 []. Orthologues from some species may include up to 40 Pro-Gly-Pro repeats.
This family represents 2-phosphoglycolate phosphatase (PGP) and is limited to prokaryotes. PGP is an essential enzyme in the glycolate salvage pathway in higher organisms (photorespiration in plants). Phosphoglycolate results from the oxidase activity of RubisCO in the Calvin cycle when concentrations of carbon dioxide are low relative to oxygen. In Ralstonia eutropha and Rhodobacter sphaeroides, the PGP gene (CbbZ) is located on an operon along with other Calvin cycle enzymes including RubisCO [, ]. In E. coli, however, there does not appear to be a functional Calvin cycle (RubisCO is absent), although the E. coli PGP gene (gph) is on the same operon (dam) with ribulose-5-phosphate-3-epimerase (rpe), a gene in the pentose-phosphate pathway (along with other, unrelated genes) []. The E. coli enzyme catalyzes the dephosphorylation of 2-phosphoglycolate and it is involved in salvage in the metabolism of a two-carbon compound generated by the cellular DNA repair machinery [].This enzyme is a member of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolase enzymes.
Phosphoglycolate phosphatase (PGP) is an essential enzyme in the glycolate salvage pathway in higher organisms (photorespiration in plants). Phosphoglycolate results from the oxidase activity of RubisCO in the Calvin cycle when concentrations of carbon dioxide are low relative to oxygen. In Ralstonia eutropha and Rhodobacter sphaeroides, the PGP gene (CbbZ) is located on an operon along with other Calvin cycle enzymes including RubisCO [, ]. In E. coli, however, there does not appear to be a functional Calvin cycle (RubisCO is absent), although the E. coli PGP gene (gph) is on the same operon (dam) with ribulose-5-phosphate-3-epimerase (rpe), a gene in the pentose-phosphate pathway (along with other, unrelated genes). This enzyme is a member of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolase enzymes.This entry represents an α-helical orthogonal bundle found towards the N terminus of phosphoglycolate phosphatase and related proteins.
CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase (), also known as phosphatidylglycerophosphate synthase, glycerophosphate phosphatidyltransferase and PGP synthase, catalyses the conversion of CDP-diacylglycerol and glycerol-3-phosphate to CMP and 3-(3-phosphatidyl)-glycerol 1-phosphate in the committed step to the synthesis of acidic phospholipids. It is an integral membrane protein. A number of related enzymes are quite similar in both sequence and catalytic activity, including Saccharomyces cerevisiae (Baker's yeast) YDL142c, now known to be a cardiolipin synthase. There may be problems with incorrect transitive annotation of near homologues as authentic CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase.
This family represents 2-phosphoglycolate phosphatase (PGP) and is limited to prokaryotes. PGP is an essential enzyme in the glycolate salvage pathway in higher organisms (photorespiration in plants). Phosphoglycolate results from the oxidase activity of RubisCO in the Calvin cycle when concentrations of carbon dioxide are low relative to oxygen. In Ralstonia eutropha and Rhodobacter sphaeroides, the PGP gene (CbbZ) is located on an operon along with other Calvin cycle enzymes including RubisCO [, ]. In E. coli, however, there does not appear to be a functional Calvin cycle (RubisCO is absent), although the E. coli PGP gene (gph) is on the same operon (dam) with ribulose-5-phosphate-3-epimerase (rpe), a gene in the pentose-phosphate pathway (along with other, unrelated genes) []. The E. coli enzyme catalyzes the dephosphorylation of 2-phosphoglycolate and it is involved in salvage in the metabolism of a two-carbon compound generated by the cellular DNA repair machinery [].This enzyme is a member of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolase enzymes.This entry also includes N-acetylmuramic acid 6-phosphate phosphatase from Pseudomonas putida, which catalyses the dephosphorylation of N-acetylmuramate 6-phosphate during recycling of peptidoglycan from the cell wall [].
CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase (), also known as phosphatidylglycerophosphate synthase, glycerophosphate phosphatidyltransferase and PGP synthase, catalyses the conversion of CDP-diacylglycerol and glycerol-3-phosphate to CMP and 3-(3-phosphatidyl)-glycerol 1-phosphate in the committed step to the synthesis of acidic phospholipids. It is an integral membrane protein. A number of related enzymes are quite similar in both sequence and catalytic activity, including Saccharomyces cerevisiae (Baker's yeast) YDL142c, now known to be a cardiolipin synthase. There may be problems with incorrect transitive annotation of near homologues as authentic CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase.This entry represents a family of bacterial CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferases [].
This family of sequences represent 2-phosphoglycolate phosphatase which is limited to the eukaryotic lineage. PGP is an essential enzyme in the glycolate salvage pathway in higher organisms (photorespiration in plants). Phosphoglycolate results from the oxidase activity of RubisCO in the Calvin cycle when concentrations of carbon dioxide are low relative to oxygen. In mammals, PGP (also known as Glycerol-3-phosphate phosphatase) []is found in many tissues, notably in red blood cells where P-glycolate is and important activator of the hydrolysis of 2,3-bisphosphoglycerate, a major modifier of the oxygen affinity of hemoglobin. The PGPase enzyme described here is a member of the Haloacid dehalogenase superfamily of hydrolase enzymes. Unlike the bacterial PGP equivalog (), which is a member of class (subfamily) I, this enzyme is a member of class (subfamily) II []. These two enzymes have almost certainly arisen from convergent evolution (although these two ancestors may themselves have diverged from a more distant HAD superfamily progenitor). One of the sequences in the group comes from Chlamydomonas reinhardtii, a photosynthetic alga. The enzyme has been purified and characterised and these data are fully consistent with the assignment of function as a PGPase involved in photorespiration []. Another, from Homo sapiens (Human), is supported as a member of the family indirectly. Biochemical characterisation of partially purified PGP's from various tissues including red blood cells []have been performed while one gene for PGP has been localized to chromosome 16p13.3 []. The Homo sapiens (Human) sequence maps to chromosome 22. There is indeed a related gene on chromosome 16 (and it is expressed, since EST's are found) which shows 46% identity and 59% positives by BLAST2 (E=1e-66). Presumably, these two genes are isoforms and have the same catalytic function while being expressed in different tissues and may be differently regulated. The sequence from Caenorhabditis elegans, is only supported by sequence similarity. This family is closely related to a family of bacterial sequences including the Escherichia coli NagD and Bacillus subtilis AraL genes which are characterised by the ability to hydrolyze para-nitrophenylphosphate (pNPPases or NPPases). The Chlamydomonas reinhardtii PGPase does not catalyze this reaction and so presumably these two groups have different functions and substrate specificities. Many of the genes in this family have been annotated as pNPPases due to this association.
