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

for references in articles please use BRENDA:EC7.1.2.2

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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 α- and 3 β-subunits) is connected via the δ-subunit to the membrane sector by several smaller subunits. Within this complex, the γ- and ε-subunits, as well as the 9–12 c subunits rotate by consecutive 120° 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.

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