A0A0M9FWC8 · A0A0M9FWC8_LEPPY

Function

function

Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base excision repair (BER), the primary repair pathway for the repair of oxidative DNA damage. The DNA N-glycosylase activity releases the damaged DNA base from DNA by cleaving the N-glycosidic bond, leaving an AP site. The AP lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination. Primarily recognizes and repairs oxidative base damage of pyrimidines.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Cofactor

[4Fe-4S] cluster (UniProtKB | Rhea| CHEBI:49883 )

Note: Binds 1 [4Fe-4S] cluster. The cluster does not appear to play a role in catalysis, but is probably involved in the proper positioning of the enzyme along the DNA strand.

Features

Showing features for active site, site, binding site.

TypeIDPosition(s)Description
Active site140Nucleophile; for N-glycosylase activity
Site159Important for catalytic activity
Binding site210[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site217[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site220[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site226[4Fe-4S] cluster (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentmitochondrion
Cellular Componentnucleus
Molecular Function4 iron, 4 sulfur cluster binding
Molecular Functionclass I DNA-(apurinic or apyrimidinic site) endonuclease activity
Molecular FunctionDNA binding
Molecular Functionendonuclease activity
Molecular Functionmetal ion binding
Molecular Functionoxidized pyrimidine nucleobase lesion DNA N-glycosylase activity
Biological Processbase-excision repair, AP site formation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Endonuclease III homolog
  • EC number
  • Alternative names
    • Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase
      (DNA glycosylase/AP lyase
      )

Gene names

    • Name
      NTH1
    • ORF names
      ABB37_06827

Organism names

Accessions

  • Primary accession
    A0A0M9FWC8

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain58-208HhH-GPD
Region236-272Disordered
Compositional bias252-272Basic and acidic residues

Sequence similarities

Belongs to the Nth/MutY family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    272
  • Mass (Da)
    30,430
  • Last updated
    2015-12-09 v1
  • Checksum
    0FC6FF884319574B
MKRMAFVPPSDWAKLYARLEDYRMTLKAPVDTIGCHMLRDRTASKETQRFHTLVALMLSAQTKDGVTAVAMQTLMQRGLTPQSVQAMTESELDSCICKVGFHNTKAKHIKQVADIIVRDYNGNVPREYSELIAFPGVGPKMANLFFQDADHRIIGIGVDTHVHRISQRFGWVPSTVKTPEDTRKALESWLPREHWGTVNHLLVGLGQTICTPLRPKCDACKLSDVCPNAFKETKAAGEPKLSTLRSPKKKPRAAAGPSDDVAENPTRKREKR

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias252-272Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LGTL01000016
EMBL· GenBank· DDBJ
KPA77425.1
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.
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