A0A2D7NNI8 · A0A2D7NNI8_UNCDE

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.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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 site59Proton donor; for beta-elimination activity
Binding site93DNA (UniProtKB | ChEBI)
Binding site112DNA (UniProtKB | ChEBI)
Active site262Proton 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
    • ORF names
      CL937_02140

Organism names

Accessions

  • Primary accession
    A0A2D7NNI8

Proteomes

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain2-115Formamidopyrimidine-DNA glycosylase catalytic
Domain238-272FPG-type

Sequence similarities

Belongs to the FPG family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    272
  • Mass (Da)
    31,323
  • Last updated
    2018-04-25 v1
  • Checksum
    3301CFB255B15972
MPELPEVETIVRGLDRELRGETIDSLEIFRSDPIIQGDPESFSEFLCGRKIKAVQRRAKFLLFHFXPVGGMVVHLRMTGKFTLTETKEPPGPHERIWFQLKSGRLLIYSDLRCFGTLECHESLDAWEDSKKLGPEPFSQDFNAKSLRKRLRESQREVKPLLLDQGLLAGLGNIYASEVLFRCGINPCRKGKRVKLREWEKLVDETRSVLNEAIEKNGTSISDFRRVDEKTGEFQNFLRVYEREGKPCVSCGMPVQRIVQQQRSSYFCPGCQV

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
NZHX01000031
EMBL· GenBank· DDBJ
MAJ48493.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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