CATH Classification

Domain Context

CATH Clusters

Superfamily 2.40.50.100
Functional Family V-type proton ATPase catalytic subunit A

Enzyme Information

7.1.2.2
H(+)-transporting two-sector ATPase.
based on mapping to UniProt Q74MJ7
ATP + H(2)O + 4 H(+)(Side 1) = ADP + phosphate + 4 H(+)(Side 2).
-!- A multisubunit non-phosphorylated ATPase that is involved in the transport of ions. -!- Large enzymes of mitochondria, chloroplasts and bacteria with a membrane sector (F(o), V(o), A(o)) and a cytoplasmic-compartment sector (F(1), V(1), A(1)). -!- 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. -!- Formerly EC 3.6.1.34 and EC 3.6.3.14.

UniProtKB Entries (1)

Q74MJ7
VATA_NANEQ
Nanoarchaeum equitans Kin4-M
V-type ATP synthase alpha chain

PDB Structure

PDB 5BN3
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structural Basis for a Unique ATP Synthase Core Complex from Nanoarcheaum equitans
Mohanty, S., Jobichen, C., Chichili, V.P.R., Velazquez-Campoy, A., Low, B.C., Hogue, C.W.V., Sivaraman, J.
J.Biol.Chem.
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