EC 7.1.2.2 - H+-transporting two-sector ATPase

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IntEnz Enzyme Nomenclature
EC 7.1.2.2

Names

Accepted name:
H+-transporting two-sector ATPase
Other names:
ATP synthase
F1-ATPase
FoF1-ATPase
H+-transporting ATPase
bacterial Ca2+/Mg2+ ATPase
chloroplast ATPase
coupling factors (Fo, F1 and CF1)
mitochondrial ATPase
F0F1-ATPase
H+-transporting ATP synthase
Systematic name:
ATP phosphohydrolase (two-sector, H+-transporting)

Reaction

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 (archeal) enzymes have a similar structure but, under physiological conditions, they pump H+ rather than synthesize ATP.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00137 , PROSITE:PDOC00138 , PROSITE:PDOC00327 , PROSITE:PDOC00420 , PROSITE:PDOC00526
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot: (2162) [show] [UniProt]

References

  1. Boyer, P.D.
    The binding change mechanism for ATP synthase - some probabilities and possibilities.
    Biochim. Biophys. Acta 1140: 215-250 (1993). [PMID: 8417777]
  2. Abrahams, J.P., Leslie, A.G.W., Lutter, R. and Walker, J.F.
    Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria.
    Nature 375: 621-628 (1994). [PMID: 8065448]
  3. Blair, A., Ngo, L., Park, J., Paulsen, I.T. and Saier, M.H., Jr.
    Phylogenetic analyses of the homologous transmembrane channel-forming proteins of the FoF1-ATPases of bacteria, chloroplasts and mitochondria.
    Microbiology 142: 17-32 (1996). [PMID: 8581162]
  4. Noji, H., Yasuda, R., Yoshida, M. and Kinosita, K., Jr.
    Direct observation of the rotation of F1-ATPase.
    Nature 386: 299-302 (1997). [PMID: 9069291]
  5. Perlin, D. S., San Francisco, M. J., Slayman, C. W., Rosen, B. P.
    H+/ATP stoichiometry of proton pumps from Neurospora crassa and Escherichia coli.
    Arch. Biochem. Biophys. 248: 53-61 (1986). [PMID: 2425739]
  6. Turina, P., Samoray, D., Graber, P.
    H+/ATP ratio of proton transport-coupled ATP synthesis and hydrolysis catalysed by CF0F1-liposomes.
    EMBO J. 22: 418-426 (2003). [PMID: 12554643]

[EC 7.1.2.2 created 1984 as EC 3.6.1.34, transferred 2000 to EC 3.6.3.14, transferred 2018 to EC 7.1.2.2]