Function and Biology Details
Reaction catalysed:
ATP + H(2)O + n Na(+)(Side 1) = ADP + phosphate + n Na(+)(Side 2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- V-type ATP synthase regulatory subunit B/beta
- P-loop containing nucleoside triphosphate hydrolase
- 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
- V-type ATP synthase catalytic alpha chain
- ATPase, F1/V1 complex, beta/alpha subunit, C-terminal
- ATPsynthase alpha/beta subunit, N-terminal extension
2 more domains
Structure analysis Details
Assembly composition:
hetero hexamer (preferred)
Assembly name:
V-type sodium ATPase (preferred)
PDBe Complex ID:
PDB-CPX-170667 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
V-type sodium ATPase catalytic subunit A
Molecule details ›
Chains: A, B, C
Length: 600 amino acids
Theoretical weight: 67.47 KDa
Source organism: Enterococcus hirae
Expression system: Cell free synthesis
UniProt:
Sequence domains:
Length: 600 amino acids
Theoretical weight: 67.47 KDa
Source organism: Enterococcus hirae
Expression system: Cell free synthesis
UniProt:
- Canonical:
Q08636 (Residues: 1-593; Coverage: 100%)
Sequence domains:
- ATP synthase alpha/beta family, beta-barrel domain
- ATPsynthase alpha/beta subunit N-term extension
- ATP synthase alpha/beta family, nucleotide-binding domain
V-type sodium ATPase subunit B
Molecule details ›
Chains: D, E, F
Length: 465 amino acids
Theoretical weight: 52.42 KDa
Source organism: Enterococcus hirae
Expression system: Cell free synthesis
UniProt:
Sequence domains:
Length: 465 amino acids
Theoretical weight: 52.42 KDa
Source organism: Enterococcus hirae
Expression system: Cell free synthesis
UniProt:
- Canonical: Q08637 (Residues: 1-458; Coverage: 100%)
Sequence domains:
- ATP synthase alpha/beta family, beta-barrel domain
- ATP synthase alpha/beta family, nucleotide-binding domain
