Q9L7T2 · FPG_PSEAE

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

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Features

Showing features for active site, binding site.

TypeIDPosition(s)Description
Active site2Schiff-base intermediate with DNA
Active site3Proton donor
Active site58Proton donor; for beta-elimination activity
Binding site91DNA (UniProtKB | ChEBI)
Binding site110DNA (UniProtKB | ChEBI)
Binding site151DNA (UniProtKB | ChEBI)
Active site260Proton donor; for delta-elimination activity

GO annotations

AspectTerm
Molecular Function8-oxo-7,8-dihydroguanine DNA N-glycosylase activity
Molecular Functionclass I DNA-(apurinic or apyrimidinic site) endonuclease activity
Molecular Functiondamaged DNA binding
Molecular FunctionDNA-(apurinic or apyrimidinic site) endonuclease activity
Molecular Functionhydrolase activity
Molecular Functionzinc ion binding
Biological Processbase-excision repair
Biological ProcessDNA repair

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Formamidopyrimidine-DNA glycosylase
  • EC number
  • Short names
    Fapy-DNA glycosylase
  • Alternative names
    • DNA-(apurinic or apyrimidinic site) lyase MutM
      (AP lyase MutM
      ) (EC:4.2.99.18
      ) . EC:4.2.99.18 (UniProtKB | ENZYME | Rhea)

Gene names

    • Name
      mutM
    • Synonyms
      fpg
    • Ordered locus names
      PA0357

Organism names

Accessions

  • Primary accession
    Q9L7T2

Proteomes

Organism-specific databases

PTM/Processing

Features

Showing features for initiator methionine, chain.

TypeIDPosition(s)Description
Initiator methionine1Removed
ChainPRO_00001708522-270Formamidopyrimidine-DNA glycosylase

Proteomic databases

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for zinc finger.

TypeIDPosition(s)Description
Zinc finger236-270FPG-type

Sequence similarities

Belongs to the FPG family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    270
  • Mass (Da)
    30,047
  • Last updated
    2007-01-23 v3
  • Checksum
    B1DCC6944E9B3E1E
MPELPEVETTRRGIAPYLEGQRVERVIVRERRLRWPIPEDLDVRLSGQRIVSVERRAKYLLLGAEAGTLISHLGMSGSLRLVESGTPASRHEHVDIELASGMALRYTDPRRFGAMLWSLAPLEHELLRNLGPEPLTDAFAGQRLFELSRGRSMAVKPFIMDNAVVVGVGNIYASEALFAAGIDPRKPAGSISKARYLRLAEEIKRILAIAIERGGTTLRDFVGGDGQPGYFQQELFVYGRGGEFCKVCGSTLREIRLGQRASVYCPRCQR

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF220059
EMBL· GenBank· DDBJ
AAF42853.1
EMBL· GenBank· DDBJ
Genomic DNA
AE004091
EMBL· GenBank· DDBJ
AAG03746.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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