E1W9M1 · END8_SALTS
- ProteinEndonuclease 8
- Genenei
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids263 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as a DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized pyrimidines, such as thymine glycol, 5,6-dihydrouracil and 5,6-dihydrothymine. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.
Catalytic activity
- 2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-phospho-2'-deoxyribonucleoside-DNA + H+
Cofactor
Note: Binds 1 zinc ion per subunit.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 2 | Schiff-base intermediate with DNA | ||||
Sequence: P | ||||||
Active site | 3 | Proton donor | ||||
Sequence: E | ||||||
Active site | 53 | Proton donor; for beta-elimination activity | ||||
Sequence: K | ||||||
Binding site | 70 | DNA (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 125 | DNA (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 169 | DNA (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Active site | 253 | Proton donor; for delta-elimination activity | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | class I DNA-(apurinic or apyrimidinic site) endonuclease activity | |
Molecular Function | damaged DNA binding | |
Molecular Function | oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity | |
Molecular Function | zinc ion binding | |
Biological Process | base-excision repair |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameEndonuclease 8
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Salmonella
Accessions
- Primary accessionE1W9M1
- Secondary accessions
Proteomes
PTM/Processing
Features
Showing features for initiator methionine, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000405416 | 2-263 | Endonuclease 8 | |||
Sequence: PEGPEIRRAADNLEAAIKGKPLTDVWFAFAQLKPYESQLTGQLVTRIETRGKALLTHFSNGLTLYSHNQLYGVWRVIDTGEIPQTTRILRVRLQTADKTILLYSASDIEMLTAEQLTTHPFLQRVGPDVLDARLTPEEVKARLLSPRFRNRQFSGLLLDQSFLAGLGNYLRVEILWQVGLTGQHKAKDLNEAQLNALSHALLDIPRLSYTTRGQADENKHHGALFRFKLFHRDGEACERCGGIIEKTTLSSRPFYWCPHCQK |
Structure
Family & Domains
Features
Showing features for zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Zinc finger | 229-263 | FPG-type | ||||
Sequence: KLFHRDGEACERCGGIIEKTTLSSRPFYWCPHCQK |
Sequence similarities
Belongs to the FPG family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length263
- Mass (Da)29,863
- Last updated2010-11-30 v1
- Checksum0BA96E876F2F19FE
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
FQ312003 EMBL· GenBank· DDBJ | CBW16808.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF300989 EMBL· GenBank· DDBJ | AAG28771.1 EMBL· GenBank· DDBJ | Genomic DNA |