Q8SRB8 · NTH_ENCCU

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.

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 site149Nucleophile; for N-glycosylase activity
Site168Important for catalytic activity
Binding site217[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site224[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site227[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site233[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 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
    • Ordered locus names
      ECU08_0880

Organism names

Accessions

  • Primary accession
    Q8SRB8

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003829191-238Endonuclease III homolog

Expression

Developmental stage

Expressed in late sporogonial stages.

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain129-155HhH

Sequence similarities

Belongs to the Nth/MutY family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    238
  • Mass (Da)
    26,755
  • Last updated
    2002-06-01 v1
  • Checksum
    3D9D7B774187F35B
MGSASGEEREGPLGLYLEIKMQRKDIVSPVDTMGCSITPSCRTEEERRFHILVSLLLSSQTKDEVTYEAMARLRKLLPESAATDGEARGGLTIERVANSDVKHINECIKKVGFHNRKAANLKKIAEILREKGLPREMKDLISLPGIGNKMALLYMSHACNRTVGISVDTHVHRISNRIGLVRTRDVESTRRELERVVPRKEWKTINNILVGFGQTICVAKRPRCEECCIRGRCPSSLF

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AL590448
EMBL· GenBank· DDBJ
CAD26394.1
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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