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Information on EC 7.1.2.2 - H+-transporting two-sector ATPase

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EC Tree
IUBMB Comments
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 (archaeal) enzymes have a similar structure but, under physiological conditions, they pump H+ rather than synthesize ATP.
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UNIPROT: P69447
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Word Map
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
atp synthase, v-atpase, f1-atpase, h+-atpase, mitochondrial atpase, vacuolar h(+)-atpase, vacuolar atpase, lipid-binding protein, vacuolar h+-atpase, f0f1-atpase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
chloroplast ATP synthase
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proton translocating chloroplast ATP synthase
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15 kDa mediatophore protein
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-
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32 kDa accessory protein
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-
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59 kDa membrane-associated GTP-binding protein
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-
-
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A6L
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-
-
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ATP synthase
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-
-
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ATP synthase proteolipid P1
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-
-
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ATP synthase proteolipid P2
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-
-
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ATP synthase proteolipid P3
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-
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bacterial Ca2+/Mg2+ ATPase
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-
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BN59
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-
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C7-1 protein
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-
-
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CGI-11
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-
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chloroplast ATPase
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-
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coupling factors (F0,F1 and CF1)
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-
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Dicyclohexylcarbodiimide-binding protein
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-
-
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Ductin
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-
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DVA41
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-
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F0F1-ATPase
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-
-
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F1-ATPase
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-
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F1F0 ATPase
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-
-
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F1F0H+-ATPase
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-
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H+-ATPase
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-
-
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H+-translocating ATPase
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-
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H+-transporting ATPase
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-
-
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HATPL
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-
-
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HO57
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-
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Invasion protein invC
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-
-
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Isoform HO68
-
-
-
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Isoform VA68
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-
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Lipid-binding protein
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-
-
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M40
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-
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mitochondrial ATPase
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-
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My032 protein
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-
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Oligomycin sensitivity conferral protein
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-
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OSCP
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-
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P31
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-
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P39
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-
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Physophilin
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-
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PKIWI505
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-
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Protein bellwether
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-
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Sul-ATPase alpha
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-
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Sul-ATPase beta
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-
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SUL-ATPase epsilon
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-
-
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Sul-ATPase gamma
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-
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UV-inducible PU4 protein
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-
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V-ATPase 28 kDa accessory protein
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-
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V-ATPase 40 kDa accessory protein
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V-ATPase 41 KDa accessory protein
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V-ATPase 9.2 kDa membrane accessory protein
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V-ATPase S1 accessory protein
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VEG100
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-
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VEG31
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Vegetative protein 100
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Vegetative protein 31
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VHA16K
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YOPS secretion ATPase
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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-
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transmembrane transport
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PATHWAY SOURCE
PATHWAYS
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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 (archaeal) 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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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
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-
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r
additional information
?
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NATURAL SUBSTRATE
NATURAL 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
-
-
-
r
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ATPH_SPIOL
81
0
7974
Swiss-Prot
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified native chloroplast enzyme, hanging drop vapour diffusion method, 0.002 ml protein solution containing 10 mg/ml protein is mixed at 15°C with 0.002 ml crystallization buffer containing 30% v/v PEG 400, 100 mM sodium acetate, pH 4.6, 100 mM cadmium chloride, and 100 mM lithium chloride, and 1 mM ADP to stabilize the F1F0 complex, X-ray diffraction structure determination and analysis at 3.8-4.0 A resolution
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme from thylakoid membranes by ammonium sulfate fractionation, sucrose density centrifugation, and anion exchange chromatography
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Vollmar, M.; Schlieper, D.; Winn, M.; Buechner, C.; Groth, G.
Structure of the c14 rotor ring of the proton translocating chloroplast ATP synthase
J. Biol. Chem.
284
18228-18235
2009
Spinacia oleracea (P69447), Spinacia oleracea
Manually annotated by BRENDA team