Information on EC 3.6.3.14 - H+-transporting two-sector ATPase

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

EC NUMBER
COMMENTARY hide
3.6.3.14
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RECOMMENDED NAME
GeneOntology No.
H+-transporting two-sector 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 phosphoric ester
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transmembrane transport
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
adenosine ribonucleotides de novo biosynthesis
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Metabolic pathways
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Oxidative phosphorylation
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Photosynthesis
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (H+-transporting)
A multisubunit non-phosphorylated ATPase that is involved in the transport of ions. Large enzymes of mitochondria, chloroplasts and bacteria with a membrane sector (Fo, Vo, Ao) and a cytoplasmic-compartment sector (F1, V1, A1). The F-type enzymes of the inner mitochondrial and thylakoid membranes act as ATP synthases. All of the enzymes included here operate in a rotational mode, where the extramembrane sector (containing 3 alpha- and 3 beta-subunits) is connected via the delta-subunit to the membrane sector by several smaller subunits. Within this complex, the gamma- and epsilon-subunits, as well as the 9-12 c subunits rotate by consecutive 120_degree_ angles and perform parts of ATP synthesis. This movement is driven by the H+ electrochemical potential gradient. The V-type (in vacuoles and clathrin-coated vesicles) and A-type (archebacterial) enzymes have a similar structure but, under physiological conditions, they pump H+ rather than synthesize ATP.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain NASF-1, strain ATCC33020
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Manually annotated by BRENDA team
Asian tiger mosquito
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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
epsilon-subunit
UniProt
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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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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Manually annotated by BRENDA team
DSM 13
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Manually annotated by BRENDA team
DSM 13
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Manually annotated by BRENDA team
strain NRLL B939 and KM
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Manually annotated by BRENDA team
strain QM B1551
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Manually annotated by BRENDA team
gene atpZ
UniProt
Manually annotated by BRENDA team
gene atpZ
UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
Bacillus thuringiensis Al Hakam
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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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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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Manually annotated by BRENDA team
strain DSM7308
SwissProt
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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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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Manually annotated by BRENDA team
strain DK8
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Manually annotated by BRENDA team
strain SWM1 and JM109
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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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Manually annotated by BRENDA team
gene VHA-A encoding the catalytic subunit A
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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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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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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
a part of the F1F0-ATPase; IOB84
UniProt
Manually annotated by BRENDA team
a part of the F1F0-ATPase; IOB84
UniProt
Manually annotated by BRENDA team
Paracoccus denitrificans Pd 1222
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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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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
strain DK8
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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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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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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
additional information
goat
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
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
2'-deoxy-ATP + H2O
2'-deoxy-ADP + phosphate + H+/out
show the reaction diagram
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?
ADP + phosphate + H+
ATP + H2O
show the reaction diagram
ADP + phosphate + H+/out
ATP + H2O + H+/in
show the reaction diagram
ADP + phosphate + H+out
ATP + H2O + H+in
show the reaction diagram
ATP + H2O + Fe2+/in
ADP + phosphate + Fe2+/out
show the reaction diagram
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the enzyme transports Fe2+ and contributes to the iron uptake into rat heart. The activity of ATPase and ATP synthase may be associated with iron uptake in a different manner, probably via antiport of H+
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?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
ATP + H2O + Na+/in
ADP + phosphate + Na+/out
show the reaction diagram
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?
ATP + phosphate + H+/in
ADP + phosphate + H+/out
show the reaction diagram
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the enzyme couples the hydrolysis of ATP to the translocation of H+ across the membrane with generation of an electrochemical potential for H+. In fermentative bacteria the ATPase functions physiologically as an ATP-utilizing, electrogenic H+ pump, the electrochemical potential of H+ generated is ultilized as a driving force for transport and mobility, in facultative anaerobes the ATPase can function physiologically in either direction, depending upon the presence or the absence of oxygen
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r
ATPgammaS + H2O + H+/in
ADP + thiophosphate + H+/out
show the reaction diagram
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r
CTP + H2O + H+/in
CDP + 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
ITP + H2O + H+/in
IDP + phosphate + H+/out
show the reaction diagram
UTP + H2O + H+/in
UDP + phosphate + H+/out
show the reaction diagram
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
ADP + phosphate + H+
ATP + H2O
show the reaction diagram
ADP + phosphate + H+/out
ATP + H2O + H+/in
show the reaction diagram
ADP + phosphate + H+out
ATP + H2O + H+in
show the reaction diagram
ATP + H2O + Fe2+/in
ADP + phosphate + Fe2+/out
show the reaction diagram
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the enzyme transports Fe2+ and contributes to the iron uptake into rat heart. The activity of ATPase and ATP synthase may be associated with iron uptake in a different manner, probably via antiport of H+
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?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
ATP + phosphate + H+/in
ADP + phosphate + H+/out
show the reaction diagram
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the enzyme couples the hydrolysis of ATP to the translocation of H+ across the membrane with generation of an electrochemical potential for H+. In fermentative bacteria the ATPase functions physiologically as an ATP-utilizing, electrogenic H+ pump, the electrochemical potential of H+ generated is ultilized as a driving force for transport and mobility, in facultative anaerobes the ATPase can function physiologically in either direction, depending upon the presence or the absence of oxygen
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r
additional information
?
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