CATH Classification

Domain Context

CATH Clusters

Superfamily 1.20.150.20
Functional Family ATP synthase subunit alpha

Enzyme Information

3.6.3.14
H(+)-transporting two-sector ATPase.
based on mapping to UniProt P09219
ATP + H(2)O + H(+)(In) = ADP + phosphate + H(+)(Out).
-!- 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.

UniProtKB Entries (1)

P09219
ATPA_BACP3
Bacillus sp. PS3
ATP synthase subunit alpha

PDB Structure

PDB 1SKY
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
The crystal structure of the nucleotide-free alpha 3 beta 3 subcomplex of F1-ATPase from the thermophilic Bacillus PS3 is a symmetric trimer.
Shirakihara, Y., Leslie, A.G., Abrahams, J.P., Walker, J.E., Ueda, T., Sekimoto, Y., Kambara, M., Saika, K., Kagawa, Y., Yoshida, M.
Structure