Information on EC 3.6.3.6 - H+-exporting ATPase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
3.6.3.6
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RECOMMENDED NAME
GeneOntology No.
H+-exporting ATPase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + H+/in = ADP + phosphate + H+/out
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphate bond
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transmembrane transport
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Oxidative phosphorylation
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (H+-exporting)
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme occurs in protozoa, fungi and plants, and generates an electrochemical potential gradient of protons across the plasma membrane.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Automatic Mining of ENzyme DAta
animal
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archaebacterium
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B subunit; strains strain NB and 306
UniProt
Manually annotated by BRENDA team
var. marathon
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Manually annotated by BRENDA team
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Candida albicans ATCC 96901
a fluconazole-resistant strain, gene PMA1
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Manually annotated by BRENDA team
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variety Caturra susceptible to pathogen Hemileia vastatrix and variety Colombia, resitant to Hemileia vastatrix
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Manually annotated by BRENDA team
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cv. Amiga
SwissProt
Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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SwissProt
Manually annotated by BRENDA team
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gene PMA1b, protein sequence idetical to PMA1a; differenial expression during asexual development, with a more than 10fold increase in expression in germinated cysts
SwissProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
gene PMA1
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Manually annotated by BRENDA team
gene PMA1
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Manually annotated by BRENDA team
strain NY13
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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yeasts
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Zea mays Pioneer 3906
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
dATP + H2O + H+/in
dADP + phosphate + H+/out
show the reaction diagram
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?
GTP + H2O + H+/in
GDP + phosphate + H+/out
show the reaction diagram
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6.5% of the activity with ATP
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ITP + H2O + H+/in
IDP + phosphate + H+/out
show the reaction diagram
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9.5% of the activity with ATP
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UTP + H2O + H+/in
UDP + phosphate + H+/out
show the reaction diagram
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9.5% of the activity with ATP
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?
additional information
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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19% of the activity with Mg2+
CaSO4
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in plants grown with 5 mM CaSO4 supply, Vmax of plasma membrane ATPase increases
Iron
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the process of H+secretion, driven by PM-H+-ATPase, is enhanced in iron-deficient rice roots
NaCl
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in plants grown with 100 mM NaCl supply, ATPase activity increases with salinity in a non-competitive way for 7 d and 21 d. In plants grown with 10 mM K2SO4 plus 100 mM NaCl supply, activity decreases competitively with Na+, after 21 d of salinity, with different effects on Km and Vmax
Zn2+
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33% of the activity with Mg2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,3-Butanedione
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2-(3-pyridinyl)-1,2-benzisoselenazol-3(2H)-one
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an ebselen analogue
2-phenyl-1,2-benzisoselenazol-3(2H)-one
2-phenyl-1,2-benzisoselenazol-3(2H)-one 1-oxide
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an ebselen analogue
adenosine 5'-(beta,gamma-imido)-triphosphate
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5 mM, 60% inhibition
adenosine 5'-monophosphate
decreases the interaction between the phosphorylated Vha2 and the 14-3-3 protein, followed by a reduction of the H+-ATPase activity and citrate exudation under Al stress conditions
ADP
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5 mM, 60% inhibition, Kd value 0.8 mM
Al3+
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inhibition of H+-ATPase activity, Mg2+ partly prevents
ATP
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competitive inhibitor, the enzyme activity decreases in the presence of Mg2+-free ATP. ATP inhibition also occurs at pH 7.5. Upon increasing Mg2+ concentration from 5 mM to 15 mM, the decrease in ATPase activity at high ATP concentration is prevented
bafilomycin A1
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Cd2+
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complete loss of ATP hydrolysis and proton transport. Exposure does not enhance the lipid peroxidation in plasma membrane, but causes an increase in the saturation of plasma membrane fatty acids and a decrease of the fatty acid chain length
Dicyclohexylcarbodiimide
diethylstilbestrol
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Dio-9
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distilbestrol
fluoroaluminates
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Mg2+ is an essential cofactor for inhibition, biphasic inhibitory process at pH 7.5 with a preference for AlF4- species
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Hemileia vastatrix
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treatment with soluble fraction of urediospores induces specific inhibition of of the resistant variety's Colombia H+-ATPase and proton pump activities, while the inhibition of the Caturra variety's proton-pump acitivy is only 16.5%
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iejimalide A
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a macrolide that is cytostatic or cytotoxic against a wide range of cancer cells at low nanomolar concentrations, inhibits vacuolar H+-ATPase in the context of epithelial tumor cells leading to a lysosome-initiated cell death process, overview
iejimalide B
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a macrolide that is cytostatic or cytotoxic against a wide range of cancer cells at low nanomolar concentrations, inhibits vacuolar H+-ATPase in the context of epithelial tumor cells leading to a lysosome-initiated cell death process, overview
K+
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K+ is an intrinsic uncoupler of the proton pump. Binding of K+ to the cytoplasmic phosphorylation domain can induce dephosphorylation of the phosphorylated E1P reaction cycle intermediate by a mechanism involving residue E184 in the conserved TGEs motif
K-252a
K2SO4
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in plants grown with 10 mM K2SO4 plus 100 mM NaCl supply, activity decreases competitively with Na+, after 21 d of salinity, with different effects on Km and Vmax
lansoprazole
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miconazole
molybdate
N-(Ethoxycarbonyl)-2-ethoxy-1,2-dihydroquinoline
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no protection by MgADP-, protection by MgATP2- or Mg-vanadate
N-ethylmaleimide
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2 mM, 26% inhibition
Na2MO4
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weak
Na3VO4
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0.1 mM
NEM
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pseudo-first order kinetics, inhibition is prevented either by MgADP- and MgATP2-
oxidized glutathione
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p-hydroxymercuribenzoate
Phenylglyoxal
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pseudo-first order kinetics, inhibition is prevented either by MgADP- and MgATP2-
SidK
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a protein of Legionella pneumophila, an intracellular pathogen, specifically targets host v-ATPase. SidK interacts via an N-terminal portion with VatA, a key component of the proton pump leading to the inhibition of ATP hydrolysis and proton translocation. SidK inhibits vacuole acidification and impairs the ability of the cells to digest non-pathogenic Escherichia coli
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Triton X-100
Trypsin
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85% inhibition of the enzyme in plasma membrane vesicles in absence of MgATP2-, no inhibition in presence of MgATP2-
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vanadate
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
AlK(SO4)2
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treatment of cells results in increase in vandate-sensitive H+-transport and in enzymatic activity, whereas yeast-hypha transition is inhibited
D-glucose
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activates, brings about a global conformational change in H+-ATPase
dithiothreitol
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2 mM, 26% stimulation
fusicoccin
iodoacetic acid
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in roots in low-phosphorus nutrient solution, iodoacetic acid stimulates the activity of plasma membrane H+-ATPase and phosphorus uptake. The effect is blocked by naphthylphthalamic acid
lysophosphatidylcholine
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stimulates
Mg-ATP
Phospholipid
proton pump interactor
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proton pump interactor, isoform 1 (PPI1) is unable to suppress the auto-inhibitory action of the enzyme C-terminus, but further enhances the activity of the enzyme whose C-terminus has been displaced by low pH or by fusicoccin-induced binding of 14-3-3 proteins
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spermine
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about 2fold stimulation due to an increase in regulatory protein 14-3-3 levels associated with the enzyme. Stimulation has an S50 value of 0.07 mM, and spermine induces 14-3-3 protein association with the unphosphorylated C-terminal domain of the enzyme. The effect is stronger and additive to that of Mg2+
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.161 - 2.8
ATP
0.6 - 1.5
MgATP2-
0.05 - 0.064
vanadate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3 - 56.7
ATP
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.001 - 0.01
vanadate
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0067
2-(3-pyridinyl)-1,2-benzisoselenazol-3(2H)-one
Saccharomyces cerevisiae
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pH 6.5, 30C
0.0025 - 0.006
2-phenyl-1,2-benzisoselenazol-3(2H)-one
0.004
2-phenyl-1,2-benzisoselenazol-3(2H)-one 1-oxide
Saccharomyces cerevisiae
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pH 6.5, 30C
0.0013 - 0.0042
vanadate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.4
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mutants G793A, G793E
5.6
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mutant L797A
6.3
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wild type enzyme
6.4
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mutants D684N, D617A/D684N
6.6
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histidine-tagged enzyme
6.9 - 7
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assay at
7
5 hours after light start; 5 hours after light start; 5 hours after light start
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.4 - 7
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about 45% of maximal activity at pH 5.4 and at pH 7.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
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enzyme from both variety Caturra susceptible to pathogen Hemileia vastatrix and variety Colombia, resitant to Hemileia vastatrix
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
and flower, high abundance of transcripts; and flower, high abundance of transcripts
Manually annotated by BRENDA team
and bark, high abundance of transcripts; and bark, high abundance of transcripts
Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
plant
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plant
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information