A0A171KNC4 · A0A171KNC4_9BURK

  • Protein
    Formamidopyrimidine-DNA glycosylase
  • Gene
    mutM
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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.

Caution

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 site58Proton donor; for beta-elimination activity
Binding site91DNA (UniProtKB | ChEBI)
Binding site109DNA (UniProtKB | ChEBI)
Binding site154DNA (UniProtKB | ChEBI)
Active site264Proton 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
      AAV32_16815
      , EV679_3056

Organism names

  • Taxonomic identifier
  • Organism
  • Strains
    • CG1
    • DSM 16618
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Alcaligenaceae > Kerstersia

Accessions

  • Primary accession
    A0A171KNC4

Proteomes

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain2-112Formamidopyrimidine-DNA glycosylase catalytic
Domain240-274FPG-type

Sequence similarities

Belongs to the FPG family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    275
  • Mass (Da)
    30,540
  • Last updated
    2016-07-06 v1
  • Checksum
    CF066882D9444140
MPELPEVETTRRGIAPLVSGKPLREFVVREPRLRWPVPAELPAILPGHTLLECGRRGKYLLLRFDHGVQIVHLGMSGALRVVARDAFLRPHDHVEWDFGDTILRLHDPRRFGAVLWHPDGGTPVEQHPLLAHLGIEPFDPRFDGNWLHRHFTGKSQAIKQALLAGQAVVGVGNIYASESLFRARIHPATPAGKLSLPRCKRLAAAITATLTDALASGGSTLRDYVNPDSQPGAYFDIHAAVYDREGQPCRICSTAIKRIVQGQRATYYCPRCQRS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LBNE01000016
EMBL· GenBank· DDBJ
KKO70391.1
EMBL· GenBank· DDBJ
Genomic DNA
SGWZ01000006
EMBL· GenBank· DDBJ
RZS65268.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp