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Information on EC 3.1.3.4 - phosphatidate phosphatase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9FMN2
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3.1.3.4 phosphatidate phosphataseIUBMB Comments
This enzyme catalyses the Mg2+-dependent dephosphorylation of a 1,2-diacylglycerol-3-phosphate, yielding a 1,2-diacyl-sn-glycerol (DAG), the substrate for de novo lipid synthesis via the Kennedy pathway and for the synthesis of triacylglycerol. In lipid signalling, the enzyme generates a pool of DAG to be used for protein kinase C activation. The mammalian enzymes are known as lipins.
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Word Map
- 3.1.3.4
- phospholipid
- triacylglycerols
- phospholipase
-
lipins
- phosphatidylcholine
- triglyceride
- propranolol
- adipose
-
lysophosphatidic
- glycerolipids
- acyltransferase
- adipocyte
-
lipogenesis
-
lipogenic
- sphingosine
- pkc
- steatosis
- lipodystrophy
- rhabdomyolysis
- cytidylyltransferase
-
mg2+-independent
- sphingosine-1-phosphate
- phosphatidylethanol
-
diradylglycerol
-
bromoenol
-
transphosphatidylation
-
kennedy
- cdp-diacylglycerol
- sn-glycerol
-
argonaut
- 1,2-diacylglycerol
-
sphingoid
-
srebf1
-
dgats
-
pirnas
- glycerolphosphate
- pc-plc
-
plectonema
-
ctp:phosphocholine
-
plasticity-related
- acaca
-
prophenoloxidase
-
cholinephosphotransferase
-
phosphatidylcholine-specific
- sn-glycerol-3-phosphate
- medicine
- analysis
- drug development
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
phosphatidate phosphohydrolase, lipin-1, lpin1, pap-1, lipin1, phosphatidate phosphatase, lipin 1, prg-1, phosphatidic acid phosphohydrolase, pa phosphatase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acid phosphatidyl phosphatase
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-
-
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ecto-PAPase
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-
-
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ecto-phosphatidic acid phosphohydrolase
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-
-
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Germ cell guidance factor
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-
-
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lipid phosphate phosphatase
PA phosphatase
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-
-
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pah1
PAH2
PAP
phosphatidate phosphohydrolase
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-
-
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phosphatidic acid phosphatase
phosphatidic acid phosphohydrolase
Wunen protein
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-
-
-
additional information
PAP
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-
-
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phosphatidic acid phosphatase
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-
-
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phosphatidic acid phosphohydrolase
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-
-
-
additional information
-
plastidic PAPs in Arabidopsis belong to a distinct lipid phosphate phosphatase LPP subfamily with prokaryotic origin
additional information
plastidic PAPs in Arabidopsis belong to a distinct lipid phosphate phosphatase LPP subfamily with prokaryotic origin
additional information
plastidic PAPs in Arabidopsis belong to a distinct lipid phosphate phosphatase LPP subfamily with prokaryotic origin
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
diacylglycerol-3-phosphate phosphohydrolase
This enzyme catalyses the Mg2+-dependent dephosphorylation of a 1,2-diacylglycerol-3-phosphate, yielding a 1,2-diacyl-sn-glycerol (DAG), the substrate for de novo lipid synthesis via the Kennedy pathway and for the synthesis of triacylglycerol. In lipid signalling, the enzyme generates a pool of DAG to be used for protein kinase C activation. The mammalian enzymes are known as lipins.
CAS REGISTRY NUMBER
COMMENTARY
9025-77-8
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
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-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
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both PAH1 and PAH2 have two domains, the amino-terminal lipin and carboxy-terminal lipin domains. PAH1 and PAH2 may supply diacylglycerol as a substrate of galactolipid synthesis, and phosphatidic acid hydrolyzed by PAH1 and PAH2 may be derived from phosphatidylcholine and phosphatidylethanolamine
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-
?
phosphatidic acid + H2O
1,2-sn-diacylglycerol + phosphate
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-
-
?
phosphatidic acid + H2O
1,2-sn-diacylglycerol + phosphate
the plastidic phosphatidic acid phosphatase dephosphorylates phosphatidic acid to yield diacylglycerol, which is a precursor for galactolipids, a primary and indispensable component of photosynthetic membranes
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
-
-
?
phosphatidic acid + H2O
1,2-sn-diacylglycerol + phosphate
-
-
-
?
phosphatidic acid + H2O
1,2-sn-diacylglycerol + phosphate
the plastidic phosphatidic acid phosphatase dephosphorylates phosphatidic acid to yield diacylglycerol, which is a precursor for galactolipids, a primary and indispensable component of photosynthetic membranes
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Mg2+
about 75% inhibition at 20 mM, isozyme LPPgamma
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 10
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
the homolog of cyanobacterial LPP, isozyme LPPepsilon1, is localized to chloroplasts and contains a plastidic transit peptide
the homolog of cyanobacterial LPP, isozyme LPPepsilon2, is localized to chloroplasts and contains a plastidic transit peptide
the homolog of cyanobacterial LPP, isozyme LPPgamma, is localized to chloroplasts and contains a plastidic transit peptide
additional information
-
isozyme LPPbeta contains no plastidic transit peptide
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additional information
isozyme LPPbeta contains no plastidic transit peptide
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additional information
isozyme LPPbeta contains no plastidic transit peptide
-
additional information
isozyme LPPbeta contains no plastidic transit peptide
-
additional information
isozyme LPPbeta contains no plastidic transit peptide
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additional information
-
isozyme LPPdelta contains no plastidic transit peptide
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additional information
isozyme LPPdelta contains no plastidic transit peptide
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additional information
isozyme LPPdelta contains no plastidic transit peptide
-
additional information
isozyme LPPdelta contains no plastidic transit peptide
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additional information
isozyme LPPdelta contains no plastidic transit peptide
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
the enzyme regulates phosphatidylcholine biosynthesis in Arabidopsis by phosphatidic acid-mediated activation of CTP:phosphocholine cytidylyltransferase activity
malfunction
metabolism
the enzyme regulates phosphatidylcholine biosynthesis in Arabidopsis by phosphatidic acid-mediated activation of CTP:phosphocholine cytidylyltransferase activity
physiological function
malfunction
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double mutant pah1pah2 plants have decreased phosphatidic acid hydrolysis, thus affecting the eukaryotic pathway of galactolipid synthesis. Upon phosphate starvation, pah1pah2 plants are severely impaired in growth and membrane lipid remodeling. PAP activity in the supernatant fraction of pah1pah2 mutant leaves is decreased by approximately 40% as compared to that in wild-type leaves. Defect in PAP activity in vivo in rosette leaves of pah1pah2 mutants. Relative amount of phosphatidic acid increases to 1.61fold in pah1pah2 double mutants as compared to the wild-type. 26% increase in phosphatidic acid levels in pah1pah2 plants as compared to wild-type plants. The transgenic plants (35S::PAH1-GFP, pah1pah2 and 35S::PAH2-GFP, pah1pah2) recover the phenotype observed in pah1pah2 mutant. Endoplasmic reticulum-localized eukaryotic pathway of membrane lipid metabolism is compromised in pah1pah2 double mutants
malfunction
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partitioning of substrate between the prokaryotic and eukaryotic pathways is perturbed in the pah1 pah2-1 double mutant. Both the total lipid content and the phospholipid content of pah1 pah2-1 mutant leaves and roots is greater than wild type on a per unit fresh weight basis
malfunction
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the inhibition of stomatal opening is less sensitive to abscisic acid in lipid phosphate phosphatase 2-deficient plants than in wild type plants. Lipid phosphate phosphatase 2-deficient plants accumulate more phosphatidic acid than wild type and have a higher phosphatidic acid kinase activity
physiological function
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PAH1 and PAH2 are the phosphatidate phosphatase responsible for the eukaryotic pathway of galactolipid synthesis. Membrane lipid remodeling mediated by these two enzymes is an essential adaptation mechanism to cope with phosphate starvation. Complements yeast DELTAdpp1DELTAlpp1DELTApah1 in vivo
physiological function
-
lipid phosphate phosphatase 2 is a part of abscisic acid signalling and participates to the regulation of stomatal movements
physiological function
-
phosphatidic acid phosphatase enzymes, PAH1 and PAH2, are capable of repressing phospholipid biosynthesis at the endoplasmic reticulum in Arabidopsis thaliana. PAH1/2 play a role in the provision of eukaryotic substrate for galactolipid synthesis in leaves
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PAH2_ARATH
930
0
101218
Swiss-Prot
Mitochondrion (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
23371
x * 23371, isozyme LPPdelta, sequence calculation
25736
x * 25736, isozyme LPPgamma, sequence calculation
30578
x * 30578, isozyme LPPepsilon1, sequence calculation
31512
x * 31512, isozyme LPPepsilon2, sequence calculation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 23371, isozyme LPPdelta, sequence calculation
?
x * 25736, isozyme LPPgamma, sequence calculation
?
x * 30578, isozyme LPPepsilon1, sequence calculation
?
x * 31512, isozyme LPPepsilon2, sequence calculation
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
a lppepsilon1lppepsilon2 double knock-out mutant shows no significant changes in lipid composition
additional information
a lppepsilon1lppepsilon2 double knock-out mutant shows no significant changes in lipid composition
additional information
a lppepsilon1lppepsilon2 double knock-out mutant shows no significant changes in lipid composition
additional information
a lppepsilon1lppepsilon2 double knock-out mutant shows no significant changes in lipid composition
additional information
a lppepsilon1lppepsilon2 double knock-out mutant shows no significant changes in lipid composition
additional information
-
a lppgamma homozygous mutant is isolated only under ectopic overexpression of LPPgamma, suggesting that loss of LPPgamma may cause lethal effect on plant viability
additional information
a lppgamma homozygous mutant is isolated only under ectopic overexpression of LPPgamma, suggesting that loss of LPPgamma may cause lethal effect on plant viability
additional information
a lppgamma homozygous mutant is isolated only under ectopic overexpression of LPPgamma, suggesting that loss of LPPgamma may cause lethal effect on plant viability
additional information
a lppgamma homozygous mutant is isolated only under ectopic overexpression of LPPgamma, suggesting that loss of LPPgamma may cause lethal effect on plant viability
additional information
a lppgamma homozygous mutant is isolated only under ectopic overexpression of LPPgamma, suggesting that loss of LPPgamma may cause lethal effect on plant viability
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
full-length coding sequence of PAH1 and PAH2 cloned into the pDO105 vector at NotI/MluI sites for PAH1 and NotI/PstI sites for PAH2. Vector constructs introduced into a Saccharomyces cerevisiae DELTAdpp1DELTAlpp1DELTApah1 mutant. Transgenic pah1pah2 plants that harbor either 35S::PAH1-GFP or 35S::PAH2-GFP transgenes
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isozyme LPPbeta, DNA and amino acid sequence determination and analysis, LPP subfamily phylogenetic tree
isozyme LPPepsilon1, DNA and amino acid sequence determination and analysis, LPP subfamily phylogenetic tree, functional complementation of a PAP-deficient yeast DELTAdpp1DELTAlpp1DELTApah1 by the plastidic LPP, phenotype rescue in vivo and in vitro, overview, expression of the isozyme in transgenic Arabidopsis thaliana plants using Agrobacterium tumefaciens-mediated transformation
isozyme LPPepsilon2, DNA and amino acid sequence determination and analysis, LPP subfamily phylogenetic tree, functional complementation of a PAP-deficient yeast DELTAdpp1DELTAlpp1DELTApah1 by the plastidic LPP, phenotype rescue in vivo and in vitro, overview, expression of the isozyme in transgenic ARabidopsis thaliana plants using Agrobacterium tumefaciens-mediated transformation
isozyme LPPgamma, DNA and amino acid sequence determination and analysis, LPP subfamily phylogenetic tree, functional complementation of a PAP-deficient yeast DELTAdpp1DELTAlpp1DELTApah1 by the plastidic LPP, phenotype rescue in vivo and in vitro, overview, expression of isozyme LPPgamma in transgenic Arabidopsis thaliana plants using Agrobacterium tumefaciens-mediated transformation
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
homozygous T-DNA-tagged mutants of PAH1 and PAH2 do not express their respective full-length mRNAs
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nakamura, Y.; Tsuchiya, M.; Ohta, H.
Plastidic phosphatidic acid phosphatases identified in a distinct subfamily of lipid phosphate phosphatases with prokaryotic origin
J. Biol. Chem.
282
29013-29021
2007
Arabidopsis thaliana, Arabidopsis thaliana (Q0WUC2), Arabidopsis thaliana (Q6NLA5), Arabidopsis thaliana (Q6NQL6), Arabidopsis thaliana (Q9SUW4)
Nakamura, Y.; Koizumi, R.; Shui, G.; Shimojima, M.; Wenk, M.R.; Ito, T.; Ohta, H.
Arabidopsis lipins mediate eukaryotic pathway of lipid metabolism and cope critically with phosphate starvation
Proc. Natl. Acad. Sci. USA
106
20978-20983
2009
Arabidopsis thaliana, Saccharomyces cerevisiae
Paradis, S.; Villasuso, A.L.; Aguayo, S.S.; Maldiney, R.; Habricot, Y.; Zalejski, C.; Machado, E.; Sotta, B.; Miginiac, E.; Jeannette, E.
Arabidopsis thaliana lipid phosphate phosphatase 2 is involved in abscisic acid signalling in leaves
Plant Physiol. Biochem.
49
357-362
2011
Arabidopsis thaliana
Eastmond, P.J.; Quettier, A.L.; Kroon, J.T.; Craddock, C.; Adams, N.; Slabas, A.R.
A phosphatidate phosphatase double mutant provides a new insight into plant membrane lipid homeostasis
Plant Signal. Behav.
6
526-527
2011
Arabidopsis thaliana
Craddock, C.P.; Adams, N.; Bryant, F.M.; Kurup, S.; Eastmond, P.J.
Phosphatidic acid phosphohydrolase regulates phosphatidylcholine biosynthesis in Arabidopsis by phosphatidic acid-mediated activation of CTP phosphocholine cytidylyltransferase activity
Plant Cell
27
1251-1264
2015
Arabidopsis thaliana (Q9FMN2), Arabidopsis thaliana (Q9SF47), Arabidopsis thaliana
EXTERNAL LINKS (specific for EC-Number 3.1.3.4)
Transporter Classification Database (TCDB): 9.B.105.3.2
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