A0A171KNC4 · A0A171KNC4_9BURK
- ProteinFormamidopyrimidine-DNA glycosylase
- GenemutM
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids275 (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 DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). 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 | 58 | Proton donor; for beta-elimination activity | ||||
Sequence: K | ||||||
Binding site | 91 | DNA (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 109 | DNA (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 154 | DNA (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 264 | Proton donor; for delta-elimination activity | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 8-oxo-7,8-dihydroguanine DNA N-glycosylase activity | |
Molecular Function | class I DNA-(apurinic or apyrimidinic site) endonuclease activity | |
Molecular Function | damaged DNA binding | |
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 nameFormamidopyrimidine-DNA glycosylase
- EC number
- Short namesFapy-DNA glycosylase
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Alcaligenaceae > Kerstersia
Accessions
- Primary accessionA0A171KNC4
Proteomes
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 2-112 | Formamidopyrimidine-DNA glycosylase catalytic | ||||
Sequence: PELPEVETTRRGIAPLVSGKPLREFVVREPRLRWPVPAELPAILPGHTLLECGRRGKYLLLRFDHGVQIVHLGMSGALRVVARDAFLRPHDHVEWDFGDTILRLHDPRRFG | ||||||
Domain | 240-274 | FPG-type | ||||
Sequence: AVYDREGQPCRICSTAIKRIVQGQRATYYCPRCQR |
Sequence similarities
Belongs to the FPG family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length275
- Mass (Da)30,540
- Last updated2016-07-06 v1
- ChecksumCF066882D9444140
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LBNE01000016 EMBL· GenBank· DDBJ | KKO70391.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
SGWZ01000006 EMBL· GenBank· DDBJ | RZS65268.1 EMBL· GenBank· DDBJ | Genomic DNA |