Function and Biology Details
Reactions catalysed:
P(1),P(4)-bis(5'-adenosyl)tetraphosphate + H(2)O = ATP + AMP
8-oxo-GTP + H(2)O = 8-oxo-GDP + phosphate
Biochemical function:
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
Structure domain:
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nudix hydrolase DR_1025
Molecule details ›
Chains: A, B
Length: 159 amino acids
Theoretical weight: 17.59 KDa
Source organism: Deinococcus radiodurans
Expression system: Escherichia coli
UniProt:
Sequence domains: NUDIX domain
Structure domains: Nucleoside Triphosphate Pyrophosphohydrolase
Length: 159 amino acids
Theoretical weight: 17.59 KDa
Source organism: Deinococcus radiodurans
Expression system: Escherichia coli
UniProt:
- Canonical:
Q9RVK2 (Residues: 1-159; Coverage: 100%)
Sequence domains: NUDIX domain
Structure domains: Nucleoside Triphosphate Pyrophosphohydrolase
