CATH Classification
Domain Context
CATH Clusters
| Superfamily | 2.40.50.100 |
| Functional Family | V-type proton ATPase catalytic subunit A |
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 | 5X09 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Crystallographic and enzymatic insights into the mechanisms of Mg-ADP inhibition in the A1 complex of the A1AO ATP synthase
J. Struct. Biol.
|