Function and Biology Details
Reaction catalysed:
ATP + H(2)O + 4 H(+)(Side 1) = ADP + phosphate + 4 H(+)(Side 2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- ATP synthase, F0 complex, subunit C
- P-loop containing nucleoside triphosphate hydrolase
- ATP synthase, F1 complex, alpha subunit
- ATP synthase, F0 complex, subunit C, DCCD-binding site
- V-ATPase proteolipid subunit C-like domain
- F/V-ATP synthase subunit C superfamily
- F1F0 ATP synthase subunit C superfamily
- ATP synthase, F1 complex, gamma subunit
16 more domains
Structure analysis Details
Assembly composition:
hetero nonadecamer (preferred)
PDBe Complex ID:
PDB-CPX-165660 (preferred)
Entry contents:
6 distinct polypeptide molecules
Macromolecules (6 distinct):
ATP synthase subunit alpha, mitochondrial
Molecule details ›
Chains: A, B, C
Length: 536 amino acids
Theoretical weight: 58.15 KDa
Source organism: Yarrowia lipolytica
UniProt:
Sequence domains:
Length: 536 amino acids
Theoretical weight: 58.15 KDa
Source organism: Yarrowia lipolytica
UniProt:
- Canonical:
Q6C326 (Residues: 1-536; Coverage: 100%)
Sequence domains:
- ATP synthase alpha/beta family, beta-barrel domain
- ATP synthase alpha/beta family, nucleotide-binding domain
- ATP synthase alpha/beta chain, C terminal domain
ATP synthase subunit beta, mitochondrial
Molecule details ›
Chains: D, E, F
Length: 509 amino acids
Theoretical weight: 54.59 KDa
Source organism: Yarrowia lipolytica
UniProt:
Sequence domains:
Length: 509 amino acids
Theoretical weight: 54.59 KDa
Source organism: Yarrowia lipolytica
UniProt:
- Canonical: Q6CFT7 (Residues: 1-509; Coverage: 100%)
Sequence domains:
- ATP synthase alpha/beta family, beta-barrel domain
- ATP synthase alpha/beta family, nucleotide-binding domain
- C-terminal domain of V and A type ATP synthase
ATP synthase subunit gamma, mitochondrial
ATP synthase subunit delta, mitochondrial
ATP synthase subunit 9, mitochondrial
