Q1IGF3 · FPG_PSEE4

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.

Type
IDPosition(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 Functionzinc ion binding
Biological Processbase-excision 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
      PSEEN0287

Organism names

Accessions

  • Primary accession
    Q1IGF3

Proteomes

PTM/Processing

Features

Showing features for initiator methionine, chain.

Type
IDPosition(s)Description
Initiator methionine1Removed
ChainPRO_10000087432-270Formamidopyrimidine-DNA glycosylase

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)
    30,051
  • Last updated
    2006-06-13 v1
  • MD5 Checksum
    52B5AE17D7FEC36022E41B64881A8DE8
MPELPEVETTRRGIAPHLVGQRVSRVVVRDRRLRWPIPEDLDVRLSGQCIVSVERRAKYLLINAEVGTLISHLGMSGNLRLVELGLPAAKHEHVDIELESGLMLRYTDPRRFGAMLWSLDPLNHELLIRLGPEPLTDLFDGERLFQLSRGRSMAVKPFIMDNAVVVGVGNIYATEALFAAGIDPRREAGGISRARYLKLAIEIKRVLAAAIEQGGTTLRDFIGGDGQPGYFQQELFVYGRGGQPCKVCGTELREVKLGQRASVFCPKCQR

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CT573326
EMBL· GenBank· DDBJ
CAK13249.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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