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:
- P-loop containing nucleoside triphosphate hydrolase
- ATP synthase, F1 complex, alpha subunit
- ATP synthase, F1 complex, beta subunit
- ATP synthase, alpha subunit, C-terminal
- ATPase, alpha/beta subunit, nucleotide-binding domain, active site
- ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain
- ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain
- ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain superfamily
5 more domains
Structure analysis Details
Assemblies composition:
Assembly name:
ATP synthase chloroplastic (preferred)
PDBe Complex ID:
PDB-CPX-133605 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
ATP synthase subunit alpha, chloroplastic
Molecule details ›
Chain: A
Length: 507 amino acids
Theoretical weight: 55.51 KDa
Source organism: Spinacia oleracea
UniProt:
Sequence domains:
Length: 507 amino acids
Theoretical weight: 55.51 KDa
Source organism: Spinacia oleracea
UniProt:
- Canonical:
P06450 (Residues: 1-507; 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, chloroplastic
Molecule details ›
Chain: B
Length: 498 amino acids
Theoretical weight: 53.92 KDa
Source organism: Spinacia oleracea
UniProt:
Sequence domains:
Length: 498 amino acids
Theoretical weight: 53.92 KDa
Source organism: Spinacia oleracea
UniProt:
- Canonical: P00825 (Residues: 1-498; Coverage: 100%)
Sequence domains:
- ATP synthase alpha/beta family, beta-barrel domain
- ATP synthase alpha/beta family, nucleotide-binding domain
