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
- V-type ATP synthase catalytic alpha chain
- ATPase, F1/V1 complex, beta/alpha subunit, C-terminal
- ATPase, alpha/beta subunit, nucleotide-binding domain, active site
- ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain
- ATPsynthase alpha/beta subunit, N-terminal extension
- ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain
- ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain superfamily
2 more domains
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Endonuclease PI-Pho2 (preferred)
PDBe Complex ID:
PDB-CPX-129601 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endonuclease PI-Pho2
Molecule details ›
Chain: A
Length: 588 amino acids
Theoretical weight: 65.72 KDa
Source organism: Pyrococcus horikoshii
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 588 amino acids
Theoretical weight: 65.72 KDa
Source organism: Pyrococcus horikoshii
Expression system: Escherichia coli
UniProt:
- Canonical:
O57728 (Residues: 1-964; Coverage: 61%)
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
- C-terminal domain of V and A type ATP synthase
