Q9L7T2 · FPG_PSEAE
- ProteinFormamidopyrimidine-DNA glycosylase
- GenemutM
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids270 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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 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 | 110 | DNA (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 151 | DNA (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Active site | 260 | 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 | DNA-(apurinic or apyrimidinic site) endonuclease activity | |
Molecular Function | hydrolase activity | |
Molecular Function | zinc ion binding | |
Biological Process | base-excision repair | |
Biological Process | DNA 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
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas
Accessions
- Primary accessionQ9L7T2
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for initiator methionine, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000170852 | 2-270 | Formamidopyrimidine-DNA glycosylase | |||
Sequence: PELPEVETTRRGIAPYLEGQRVERVIVRERRLRWPIPEDLDVRLSGQRIVSVERRAKYLLLGAEAGTLISHLGMSGSLRLVESGTPASRHEHVDIELASGMALRYTDPRRFGAMLWSLAPLEHELLRNLGPEPLTDAFAGQRLFELSRGRSMAVKPFIMDNAVVVGVGNIYASEALFAAGIDPRKPAGSISKARYLRLAEEIKRILAIAIERGGTTLRDFVGGDGQPGYFQQELFVYGRGGEFCKVCGSTLREIRLGQRASVYCPRCQR |
Proteomic databases
Interaction
Structure
Family & Domains
Features
Showing features for zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Zinc finger | 236-270 | FPG-type | ||||
Sequence: FVYGRGGEFCKVCGSTLREIRLGQRASVYCPRCQR |
Sequence similarities
Belongs to the FPG family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length270
- Mass (Da)30,047
- Last updated2007-01-23 v3
- ChecksumB1DCC6944E9B3E1E
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF220059 EMBL· GenBank· DDBJ | AAF42853.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE004091 EMBL· GenBank· DDBJ | AAG03746.1 EMBL· GenBank· DDBJ | Genomic DNA |