CATH Classification

Domain Context

CATH Clusters

Superfamily 2.30.30.650
Functional Family

Enzyme Information

3.1.-.-
Acting on ester bonds.
based on mapping to UniProt O57728
7.1.2.2
H(+)-transporting two-sector ATPase.
based on mapping to UniProt O57728
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)

O57728
VATA_PYRHO
Pyrococcus horikoshii OT3
V-type ATP synthase alpha chain

PDB Structure

PDB 3SDZ
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Engineered tryptophan in the adenine-binding pocket of catalytic subunit A of A-ATP synthase demonstrates the importance of aromatic residues in adenine binding, forming a tool for steady-state and time-resolved fluorescence spectroscopy.
Tadwal, V.S., Manimekalai, M.S., Gruber, G.
Acta Crystallogr.,Sect.F