Function and Biology Details
Reaction catalysed:
Hydrolyzes free adenine bases from 7,8-dihydro-8-oxoguanine:adenine mismatched double-stranded DNA, leaving an apurinic site.
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
- HhH-GPD domain
- Endonuclease III-like, iron-sulphur cluster loop motif
- Endonuclease III, iron-sulphur binding site
- Endonuclease III-like, conserved site-2
- Helix-hairpin-helix motif
- Helix-hairpin-helix, base-excision DNA repair, C-terminal
- A/G-specific adenine glycosylase MutY
- Adenine/Thymine-DNA glycosylase
1 more domain
Structure domain:
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
Adenine DNA glycosylase (preferred)
PDBe Complex ID:
PDB-CPX-148181 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Adenine DNA glycosylase
Molecule details ›
Chain: A
Length: 225 amino acids
Theoretical weight: 25.05 KDa
Source organism: Escherichia coli
UniProt:
Sequence domains:
Length: 225 amino acids
Theoretical weight: 25.05 KDa
Source organism: Escherichia coli
UniProt:
- Canonical:
P17802 (Residues: 1-225; Coverage: 64%)
Sequence domains:
- HhH-GPD superfamily base excision DNA repair protein
- Helix-hairpin-helix motif
- Iron-sulfur binding domain of endonuclease III
