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Information on EC 7.1.3.2 - Na+-exporting diphosphatase
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7.1.3.2 Na+-exporting diphosphataseIUBMB Comments
Requires Na+ and K+. This enzyme, found in some bacteria and archaea, couples the energy from diphosphate hydrolysis to active sodium translocation across the membrane. The enzyme is electrogenic, as the Na+ transport results in generation of a positive potential in the inner side of the membrane.
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The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
HppA, HppA1, K(+)-stimulated pyrophosphate-energized sodium pump, Na+-translocating membrane pyrophosphatase, sodium-translocating pyrophosphatase, TM_0174, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
HppA
HppA1
K(+)-stimulated pyrophosphate-energized sodium pump
Na+-translocating membrane pyrophosphatase
-
-
-
-
sodium-translocating pyrophosphatase
-
-
-
-
TM_0174
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
diphosphate + H2O + Na+[side 1] = 2 phosphate + Na+[side 2]
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-
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-
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SYSTEMATIC NAME
IUBMB Comments
diphosphate phosphohydrolase (Na+-transporting)
Requires Na+ and K+. This enzyme, found in some bacteria and archaea, couples the energy from diphosphate hydrolysis to active sodium translocation across the membrane. The enzyme is electrogenic, as the Na+ transport results in generation of a positive potential in the inner side of the membrane.
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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
diphosphate + H2O + Na+(side1)
H+ + Na+(side2) + 2 phosphate
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-
-
?
diphosphate + H2O + Na+(side1)
H+ + Na+(side2) + 2 phosphate
-
-
-
?
diphosphate + H2O + Na+[side 1]
2 phosphate + Na+[side 2]
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-
-
-
?
diphosphate + H2O + Na+[side 1]
2 phosphate + Na+[side 2]
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-
-
?
diphosphate + H2O + Na+[side 1]
2 phosphate + Na+[side 2]
-
-
-
?
diphosphate + H2O + Na+[side 1]
2 phosphate + Na+[side 2]
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-
-
?
diphosphate + H2O + Na+[side 1]
2 phosphate + Na+[side 2]
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-
-
?
additional information
?
-
enzyme does not catalyze oxygen exchange between phosphate and water. Solubilized HppA exhibits low but measurable PPi-synthesizing activity, which also requires Na+ but is inhibited by K+
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-
-
additional information
?
-
enzyme exhibits an absolute requirement for Na+ but displays the highest activity in the presence of millimolar levels of both Na+ and K+. Two Na+ binding sites and one K+ binding site are involved in enzyme activation. In the absence of K+, Li+ may substitute for Na+
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-
-
additional information
?
-
enzyme does not catalyze oxygen exchange between phosphate and water. Solubilized HppA exhibits low but measurable PPi-synthesizing activity, which also requires Na+ but is inhibited by K+
-
-
-
additional information
?
-
enzyme exhibits an absolute requirement for Na+ but displays the highest activity in the presence of millimolar levels of both Na+ and K+. Two Na+ binding sites and one K+ binding site are involved in enzyme activation. In the absence of K+, Li+ may substitute for Na+
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-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
not inhibitory: protonophore carbonyl cyanide m-chlorophenylhydrazone
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additional information
not inhibitory: protonophore carbonyl cyanide m-chlorophenylhydrazone
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additional information
not inhibitory: protonophore carbonyl cyanide m-chlorophenylhydrazone
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
K+
enzyme exhibits an absolute requirement for Na+ but displays the highest activity in the presence of millimolar levels of both Na+ and K+. Two Na+ binding sites and one K+ binding site are involved in enzyme activation
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
metabolism
enzyme catalyzes Na+ rather than H+ transport into Escherichia coli inner membrane vesicles. When assayed in uncoupled inner membrane vesicles, enzyme exhibits an absolute requirement for Na+ but displays the highest hydrolyzing activity in the presence of both Na+ and K+. Two Na+ binding sites are present in the protein. One of these sites can also bind K+, resulting in a 10fold increase in the affinity of the other site for Na+ and a 2fold increase in maximal velocity. The Na+ transport is accompanied by the generation of a positive inside membrane potential
metabolism
enzyme catalyzes Na+ rather than H+ transport into Escherichia coli inner membrane vesicles. When assayed in uncoupled inner membrane vesicles, enzyme exhibits an absolute requirement for Na+ but displays the highest hydrolyzing activity in the presence of both Na+ and K+. Two Na+ binding sites are present in the protein. One of these sites can also bind K+, resulting in a 10fold increase in the affinity of the other site for Na+ and a 2fold increase in maximal velocity. The Na+ transport is accompanied by the generation of a positive inside membrane potential
metabolism
enzyme catalyzes Na+ rather than H+ transport into Escherichia coli inner membrane vesicles. When assayed in uncoupled inner membrane vesicles, enzyme exhibits an absolute requirement for Na+ but displays the highest hydrolyzing activity in the presence of both Na+ and K+. Two Na+ binding sites are present in the protein. One of these sites can also bind K+, resulting in a 10fold increase in the affinity of the other site for Na+ and a 2fold increase in maximal velocity. The Na+ transport is accompanied by the generation of a positive inside membrane potential
metabolism
-
enzyme catalyzes Na+ rather than H+ transport into Escherichia coli inner membrane vesicles. When assayed in uncoupled inner membrane vesicles, enzyme exhibits an absolute requirement for Na+ but displays the highest hydrolyzing activity in the presence of both Na+ and K+. Two Na+ binding sites are present in the protein. One of these sites can also bind K+, resulting in a 10fold increase in the affinity of the other site for Na+ and a 2fold increase in maximal velocity. The Na+ transport is accompanied by the generation of a positive inside membrane potential
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metabolism
-
enzyme catalyzes Na+ rather than H+ transport into Escherichia coli inner membrane vesicles. When assayed in uncoupled inner membrane vesicles, enzyme exhibits an absolute requirement for Na+ but displays the highest hydrolyzing activity in the presence of both Na+ and K+. Two Na+ binding sites are present in the protein. One of these sites can also bind K+, resulting in a 10fold increase in the affinity of the other site for Na+ and a 2fold increase in maximal velocity. The Na+ transport is accompanied by the generation of a positive inside membrane potential
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physiological function
-
enzyme belongs to a monophyletic clade comprising Na+-transporting PPases within the K+-dependent subfamily. A specific Glu residue located in the cytoplasm-membrane interface of transmembrane helix 6 appears to be central in the transport mechanism
physiological function
-
enzyme belongs to a monophyletic clade comprising Na+-transporting PPases within the K+-dependent subfamily. A specific Glu residue located in the cytoplasm-membrane interface of transmembrane helix 6 appears to be central in the transport mechanism
physiological function
-
enzyme belongs to a monophyletic clade comprising Na+-transporting PPases within the K+-dependent subfamily. A specific Glu residue located in the cytoplasm-membrane interface of transmembrane helix 6 appears to be central in the transport mechanism
physiological function
-
enzyme belongs to a monophyletic clade comprising Na+-transporting PPases within the K+-dependent subfamily. A specific Glu residue located in the cytoplasm-membrane interface of transmembrane helix 6 appears to be central in the transport mechanism
physiological function
enzyme is able to complement a yeast mutant lacking cytosolic soluble diphosphatase IPP1 and acts also under salt stress. When yeast cells expressing HppA1 are grown in the presence of NaCl only a marginal increase in their internal PPi levels is observed with respect to control cells
physiological function
-
inverted membrane vesicles of Acetobacter woodii have a membrane-bound diphosphatase that catalyzes diphosphate hydrolysis. Hydrolysis of diphosphate is accompanied by Na+ transport into the lumen of the inverted membrane vesicles. Na+ transport is primary and electrogenic
physiological function
-
enzyme is able to complement a yeast mutant lacking cytosolic soluble diphosphatase IPP1 and acts also under salt stress. When yeast cells expressing HppA1 are grown in the presence of NaCl only a marginal increase in their internal PPi levels is observed with respect to control cells
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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). HPPA1_MOOTA
Moorella thermoacetica (strain ATCC 39073 / JCM 9320)
672
0
68449
Swiss-Prot
-
HPPA1_METMA
Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)
676
0
69221
Swiss-Prot
-
HPPA_THEMA
Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
726
0
77046
Swiss-Prot
-
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D190A
the Na+ dose dependencies closely resemble those of the wild-type enzyme
D190A/D703N
activation by alkali cations is similar to the D703N variant, but the maximum is shifted to 2fold higher Na+ and K+ concentrations
D703N
only one Na+ binding site (K+-dependent) and one K+ binding site are involved in activation of the variant
D190A
-
the Na+ dose dependencies closely resemble those of the wild-type enzyme
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D190A/D703N
-
activation by alkali cations is similar to the D703N variant, but the maximum is shifted to 2fold higher Na+ and K+ concentrations
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D703N
-
only one Na+ binding site (K+-dependent) and one K+ binding site are involved in activation of the variant
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Belogurov, G.; Malinen, A.; Turkina, M.; Jalonen, U.; Rytknen, K.; Baykov, A.; Lahti, R.
Membrane-bound pyrophosphatase of Thermotoga maritima requires sodium for activity
Biochemistry
44
2088-2096
2005
Thermotoga maritima (Q9S5X0), Thermotoga maritima DSM 3109 (Q9S5X0)
brenda
Malinen, A.; Belogurov, G.; Baykov, A.; Lahti, R.
Na+-pyrophosphatase A novel primary sodium pump
Biochemistry
46
8872-8878
2007
Moorella thermoacetica (Q2RIS7), Methanosarcina mazei (Q8PYZ8), Thermotoga maritima (Q9S5X0), Methanosarcina mazei DSM 3647 (Q8PYZ8), Thermotoga maritima DSM 3109 (Q9S5X0)
brenda
Perez-Castineira, J.R.; Serrano, A.
The H+-translocating inorganic pyrophosphatase from Arabidopsis thaliana is more sensitive to sodium than its Na+-translocating counterpart from Methanosarcina mazei
Front. Plant Sci.
11
1240
2020
Methanosarcina mazei (Q8PYZ8), Methanosarcina mazei DSM 3647 (Q8PYZ8)
brenda
Luoto, H.; Belogurov, G.; Baykov, A.; Lahti, R.; Malinen, A.
Na+-translocating membrane pyrophosphatases are widespread in the microbial world and evolutionarily precede H+-translocating pyrophosphatases
J. Biol. Chem.
286
21633-21642
2011
Chlorobium limicola, Clostridium tetani, Desulfuromonas acetoxidans, Anaerostipes caccae
brenda
Biegel, E.; Mueller, V.
A Na+-translocating pyrophosphatase in the acetogenic bacterium Acetobacterium woodii
J. Biol. Chem.
286
6080-6084
2011
Acetobacterium woodii
brenda
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