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Information on EC 7.1.3.1 - H+-exporting diphosphatase and Organism(s) Arabidopsis thaliana and UniProt Accession P31414
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7.1.3.1 H+-exporting diphosphataseIUBMB Comments
This enzyme, found in plants and fungi, couples the energy from diphosphate hydrolysis to active proton translocation across the tonoplast into the vacuole. The enzyme acts cooperatively with cytosolic soluble diphosphatases to regulate the cytosolic diphosphate level.
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Word Map
- 7.1.3.1
- vacuole
- h+-ppases
-
tonoplasts
- acidocalcisomes
- v-atpase
- ppases
- pyrophosphatases
- imidodiphosphate
-
3.6.1.1
- v-h+-atpase
- aminomethylenediphosphonate
-
h+-pumping
-
ppi-dependent
- medicine
- drug development
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
h(+)-pyrophosphatase, vacuolar h+ -atpase, proton pyrophosphatase, vacuolar h+-ppase, v-h+-ppase, h+ -ppase, proton-pumping pyrophosphatase, proton pumping pyrophosphatase, proton-pyrophosphatase, vp1-1, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AVP1
H+-PPase
hydrogen-translocating pyrophosphatase
-
-
-
-
proton-pumping dihosphatase
-
-
-
-
proton-pumping pyrophosphatase
V-PPase
vacuolar H+-pyrophosphatase
proton-pumping pyrophosphatase
-
-
-
-
vacuolar H+-pyrophosphatase
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
diphosphate phosphohydrolase (H+-transporting)
This enzyme, found in plants and fungi, couples the energy from diphosphate hydrolysis to active proton translocation across the tonoplast into the vacuole. The enzyme acts cooperatively with cytosolic soluble diphosphatases to regulate the cytosolic diphosphate level.
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
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
-
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
important for energy metabolism, provides energy for biosynthetic reactions, proton translocation through membrane provides a source of energy
-
-
?
additional information
?
-
proton-translocation activities are assayed by monitoring the fluorescence quenching of 9-amino-6-chloro-2-methoxyacridine
-
-
?
additional information
?
-
-
proton-translocation activities are assayed by monitoring the fluorescence quenching of 9-amino-6-chloro-2-methoxyacridine
-
-
?
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
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
-
-
-
?
diphosphate + H2O + H+[side 1]
2 phosphate + H+[side 2]
-
important for energy metabolism, provides energy for biosynthetic reactions, proton translocation through membrane provides a source of energy
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
malfunction
metabolism
-
implication of H+-PPase in postgerminative oilseed metabolism, overview
physiological function
additional information
physiological function
vacuolar H+ -ATPases are a specific class of multisubunit pumps that play an essential role in the generation of proton gradients across eukaryotic endomembranes. The plant proton-pumping inorganic pyrophosphatase functionally complements the vacuolar ATPase transport activity and confers bafilomycin resistance when recombinantly expressed in yeast
physiological function
enzyme overexpression confers enhanced tolerance to abiotic stresses, including heat shock and H2O2, as well as NaCl, Cd, Mn, Zn, Ca, and Al. Enzyme overexpression results in hypersensitivity to menadione and cobalt
malfunction
-
defects in PPase activity cause severe developmental defects and/or growth arrest in several organisms. The fugu5 mutant phenotype, caused by a defect in H+-PPase activity, shows a postgerminative growth phenotype, but is rescued by complementation with the yeast cytosolic PPase IPP1, overview. Increased cytosolic PPi levels Impaired postgerminative development in fugu5 by inhibiting gluconeogenesis
malfunction
the fugu5 mutant is defective in AVP1, i.e. vacuolar H+-pyrophosphatase, due to point mutations A709T, A553T, or E272K, and fails to support heterotrophic growth after germination. Exogenous supplementation of succinate or the specific removal of the cytosolic diphosphate by the heterologous expression of the cytosolic inorganic diphosphatase1, IPP1, gene from Saccharomyces cerevisiae rescues fugu5 phenotypes. Compared with the wild-type and AVP1Pro:IPP1 transgenic lines, hypocotyl elongation in the fugu5 mutant is severely compromised in the dark but recovers upon exogenous supply of succinate to the growth media. The peroxisomal beta-oxidation activity, dry seed contents of storage lipids, and their mobilization are unaffected in fugu5
physiological function
-
proton-translocating vacuolar PPase, H+-PPase, uses the energy of diphosphate hydrolysis to acidify the vacuole in higher plants. H+-PPase is a master regulator of cytosolic diphosphate homeostasis, another role of H+-PPase in plants is vacuolar acidification, the role of H+-PPase as a proton-pump is negligible
physiological function
vacuolar H+-diphosphatase, AVP1, is a key enzyme in phosphate hydrolysis
physiological function
-
co-expression of the enzyme and a vacuolar Na+/H+ antiporter gene from Pennisetum glaucum confers enhanced salt tolerance to the transformed tomato compared with the single gene transgenic plants and the wild type. Co-expression of the enzymes improves the osmoregulatory capacity of double transgenic lines by enhanced sequestration of ions into the vacuole by increasing the availability of protons and thus alleviating the toxic effect of Na+
physiological function
-
enzyme overexpression markedly stimulates growth and increase stolerance to biotic and abiotic stresses
physiological function
-
enzyme overexpression mediates enhanced phloem loading and long-distance transport leading to growth enhancement
physiological function
-
heterologous expression of the enzyme at the fungal vacuolar membrane alleviates growth inhibition by tridemorph, reduces apoptosis levels in yeast and increases resistance to amine fungicides
physiological function
-
the enzyme catalyzes a coupled reaction of diphosphate hydrolysis and active proton translocation across the tonoplast. Additional enzyme expression improves plant growth by increasing cell number, predominantly as a consequence of the diphosphate hydrolyzing activity of the enzyme
physiological function
-
the enzyme is required for pyrophosphate metabolism and photosynthate partitioning in phloem function
physiological function
-
the enzyme regulates root and shoot development via facilitation of auxin flux, and enhances plant resistance to salt and drought stresses. Perennial creeping bentgrass plants over-expressing the enzyme exhibit improved resistance to salinity (100-300 mM naCl) than wild type controls
additional information
vacuolar proteases are involved in the processing of native AVP1 and its chimaeric derivatives targeted to the vacuolar membrane
additional information
-
vacuolar proteases are involved in the processing of native AVP1 and its chimaeric derivatives targeted to the vacuolar membrane
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). AVP1_ARATH
770
14
80820
Swiss-Prot
Secretory Pathway (Reliability: 1)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
vacuolar proteases are involved in the processing of native AVP1 and its chimaeric derivatives targeted to the vacuolar membrane
phosphoprotein
-
phosphorylation or poly-phosphorylation at S46, S47, S48, K55, Y61, T129, Y130, Y170, T576, T618, T633, and Y700
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A553T
naturally occuring point mutation A553T plus deletion of residues from Leu554 to Ala558 in the transmembrane domain 12. The mutant fails to support heterotrophic growth after germination. Exogenous supplementation of succinate or the specific removal of the cytosolic diphosphate by the heterologous expression of the cytosolic inorganic pyrophosphatase 1, IPP1, gene from Saccharomyces cerevisiae rescues fugu5 phenotypes. Compared with the wild-type and AVP1Pro:IPP1 transgenic lines, hypocotyl elongation in the fugu5 mutant is severely compromised in the dark but recovers upon exogenous supply of succinate to the growth media. The peroxisomal beta-oxidation activity, dry seed contents of storage lipids, and their mobilization are unaffected in fugu5
A709T
the naturally occuring fugu5 mutant is defective in AVP1, i.e. vacuolar H+-pyrophosphatase, due to a point mutation A709T and fails to support heterotrophic growth after germination. Cell division is almost totally inhibited in cotyledons postembryonically, phenotype, overview, fails to support heterotrophic growth after germination. Exogenous supplementation of succinate or the specific removal of the cytosolic diphosphate by the heterologous expression of the cytosolic inorganic pyrophosphatase 1, IPP1, gene from Saccharomyces cerevisiae rescues fugu5 phenotypes. Compared with the wild-type and AVP1Pro:IPP1 transgenic lines, hypocotyl elongation in the fugu5 mutant is severely compromised in the dark but recovers upon exogenous supply of succinate to the growth media. The peroxisomal beta-oxidation activity, dry seed contents of storage lipids, and their mobilization are unaffected in fugu5
E272K
naturally occuring point mutation, fails to support heterotrophic growth after germination. Exogenous supplementation of succinate or the specific removal of the cytosolic diphosphate by the heterologous expression of the cytosolic inorganic pyrophosphatase 1, IPP1, gene from Saccharomyces cerevisiae rescues fugu5 phenotypes. Compared with the wild-type and AVP1Pro:IPP1 transgenic lines, hypocotyl elongation in the fugu5 mutant is severely compromised in the dark but recovers upon exogenous supply of succinate to the growth media. The peroxisomal beta-oxidation activity, dry seed contents of storage lipids, and their mobilization are unaffected in fugu5
additional information
additional information
expression of a chimaeric derivative of the Arabidopsis thaliana H+ -PPase AVP1, which is preferentially targeted to internal membranes of yeast, alleviates the phenotypes associated with V-ATPase deficiency. Phenotypic complementation was achieved both with a yeast strain with its V-ATPase specifically inhibited by bafilomycin A1 and with a vma1-null mutant lacking a catalytic V-ATPase subunit. Cells expressing the different AVP1 chimaeras show a somewhat smaller sensitivity to this CaCl2. In the presence of Zn2+ , only those cells transformed with plasmids pTcAVP1 and pTcGFPAVP1 expressing internal membrane-targeted chimaeras grows after 4 days, particularly the latter. Phenotypes, overview. In yeast strain YPC4, the presence of GFP at the N-terminus of AVP1 increased the specific activity of the resulting protein 3-4-fold with respect to AVP1 and TcAVP1
additional information
-
expression of a chimaeric derivative of the Arabidopsis thaliana H+ -PPase AVP1, which is preferentially targeted to internal membranes of yeast, alleviates the phenotypes associated with V-ATPase deficiency. Phenotypic complementation was achieved both with a yeast strain with its V-ATPase specifically inhibited by bafilomycin A1 and with a vma1-null mutant lacking a catalytic V-ATPase subunit. Cells expressing the different AVP1 chimaeras show a somewhat smaller sensitivity to this CaCl2. In the presence of Zn2+ , only those cells transformed with plasmids pTcAVP1 and pTcGFPAVP1 expressing internal membrane-targeted chimaeras grows after 4 days, particularly the latter. Phenotypes, overview. In yeast strain YPC4, the presence of GFP at the N-terminus of AVP1 increased the specific activity of the resulting protein 3-4-fold with respect to AVP1 and TcAVP1
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, phylogenetic tree and sequence comparisons, overview
expressed in Escherichia coli BL21 (DE3) cells and Saccharomyces cerevisiae BY4741 cells
expression of AVP1, preferentially targeted to internal membranes, in Saccharomyces cerevisiae YPC3 mutant strain, generated from haploid strain W303-1A, and YPC4 mutant strain, generated from strain RS-1144
DNA and amino acid sequence determination and analysis, phylogenetic tree and sequence comparisons, overview
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
McIntosh, M.T.; Vaidya, A.B.
Vacuolar type H+ pumping pyrophosphatases of parasitic protozoa
Int. J. Parasitol.
32
1-14
2002
Arabidopsis thaliana, Vigna radiata, Plasmodium falciparum, Pyrobaculum aerophilum, Rhodospirillum rubrum, Thermotoga maritima, Toxoplasma gondii, Trypanosoma cruzi, Zea mays
Serrano, A.; Perez-Castineira, J.R.; Baltscheffsky, H.; Baltscheffsky, M.
Proton-pumping inorganic pyrophosphatases in some archaea and other extremophilic prokaryotes
J. Bioenerg. Biomembr.
36
127-133
2004
Chlorobaculum tepidum, Chloroflexus aurantiacus, Novosphingobium aromaticivorans, Thermobifida fusca, Caldanaerobacter subterraneus subsp. tengcongensis, Rhodospirillum rubrum (O68460), Arabidopsis thaliana (P31414), Arabidopsis thaliana (Q56ZN6), Pyrobaculum aerophilum (Q8ZWI8), Trypanosoma cruzi (Q9NDF0), Thermotoga maritima (Q9S5X0), Streptomyces coelicolor (Q9X913)
Perez-Castineira, J.R.; Hernandez, A.; Drake, R.; Serrano, A.
A plant proton-pumping inorganic pyrophosphatase functionally complements the vacuolar ATPase transport activity and confers bafilomycin resistance in yeast
Biochem. J.
437
269-278
2011
Arabidopsis thaliana (P31414), Arabidopsis thaliana
Ferjani, A.; Segami, S.; Horiguchi, G.; Muto, Y.; Maeshima, M.; Tsukaya, H.
Keep an eye on PPi: the vacuolar-type H+-pyrophosphatase regulates postgerminative development in Arabidopsis
Plant Cell
23
2895-2908
2011
Arabidopsis thaliana (A8MQH1)
Ferjani, A.; Segami, S.; Horiguchi, G.; Sakata, A.; Maeshima, M.; Tsukaya, H.
Regulation of pyrophosphate levels by H+-PPase is central for proper resumption of early plant development
Plant Signal. Behav.
7
38-42
2012
Arabidopsis thaliana
Asaoka, M.M.; Segami, S.; Ferjani, A.; Maeshima, M.
Contribution of PPi-hydrolyzing function of vacuolar H+-pyrophosphatase in vegetative growth of Arabidopsis evidenced by expression of uncoupling mutated enzymes
Front. Plant Sci.
7
415
2016
Arabidopsis thaliana
Hernandez, A.; Herrera-Palau, R.; Madronal, J.M.; Albi, T.; Lopez-Lluch, G.; Perez-Castineira, J.R.; Navas, P.; Valverde, F.; Serrano, A.
Vacuolar H+-pyrophosphatase AVP1 is involved in amine fungicide tolerance in Arabidopsis thaliana and provides tridemorph resistance in yeast
Front. Plant Sci.
7
85
2016
Arabidopsis thaliana
Pizzio, G.A.; Hirschi, K.D.; Gaxiola, R.A.
Conjecture regarding posttranslational modifications to the Arabidopsis type I proton-pumping pyrophosphatase (AVP1)
Front. Plant Sci.
8
1572
2017
Arabidopsis thaliana
Yoon, H.S.; Kim, S.Y.; Kim, I.S.
Stress response of plant H+-PPase-expressing transgenic Escherichia coli and Saccharomyces cerevisiae a potentially useful mechanism for the development of stress-tolerant organisms
J. Appl. Genet.
54
129-133
2013
Arabidopsis thaliana (P31414), Oryza sativa (P93409)
Bhaskaran, S.; Savithramma, D.L.
Co-expression of Pennisetum glaucum vacuolar Na+/H+ antiporter and Arabidopsis H+-pyrophosphatase enhances salt tolerance in transgenic tomato
J. Exp. Bot.
62
5561-5570
2011
Arabidopsis thaliana
Li, Z.; Baldwin, C.M.; Hu, Q.; Liu, H.; Luo, H.
Heterologous expression of Arabidopsis H+-pyrophosphatase enhances salt tolerance in transgenic creeping bentgrass (Agrostis stolonifera L.)
Plant Cell Environ.
33
272-289
2010
Arabidopsis thaliana
Segami, S.; Asaoka, M.; Kinoshita, S.; Fukuda, M.; Nakanishi, Y.; Maeshima, M.
Biochemical, structural and physiological characteristics of vacuolar H+-pyrophosphatase
Plant Cell Physiol.
59
1300-1308
2018
Arabidopsis thaliana, Vigna radiata
Rea, P.A.; Britten, C.J.; Sarafian, V.
Common identity of substrate binding subunit of vacuolar H+-translocating inorganic pyrophosphatase of higher plant cells
Plant Physiol.
100
723-732
1992
Arabidopsis thaliana, Beta vulgaris, Vigna radiata, Zea mays
Pizzio, G.A.; Paez-Valencia, J.; Khadilkar, A.S.; Regmi, K.; Patron-Soberano, A.; Zhang, S.; Sanchez-Lares, J.; Furstenau, T.; Li, J.; Sanchez-Gomez, C.; Valencia-Mayoral, P.; Yadav, U.P.; Ayre, B.G.; Gaxiola, R.A.
Arabidopsis type I proton-pumping pyrophosphatase expresses strongly in phloem, where it is required for pyrophosphate metabolism and photosynthate partitioning
Plant Physiol.
167
1541-1553
2015
Arabidopsis thaliana
Khadilkar, A.S.; Yadav, U.P.; Salazar, C.; Shulaev, V.; Paez-Valencia, J.; Pizzio, G.A.; Gaxiola, R.A.; Ayre, B.G.
Constitutive and companion cell-specific overexpression of AVP1, encoding a proton-pumping pyrophosphatase, enhances biomass accumulation, phloem loading, and long-distance transport
Plant Physiol.
170
401-414
2016
Arabidopsis thaliana
EXTERNAL LINKS (specific for EC-Number 7.1.3.1)
Transporter Classification Database (TCDB): 3.A.10.3.1, 3.A.10.2.1, 3.A.10.1.1, 3.A.10.2.3, 3.A.10.1.8, 3.A.10.2.4, 3.A.10.1.17, 3.A.10.2.2, 3.A.10.3.3, 3.A.10.1.9, 3.A.10.1.2, 3.A.10.3.4, 3.A.10.3.5, 3.A.10.3.2, 3.A.10.1.16, 3.A.10.1.15
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