A0A6P4CL16 · A0A6P4CL16_ARADU

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 site262Nucleophile; for N-glycosylase activity
Site281Important for catalytic activity
Binding site337[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site344[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site347[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site353[4Fe-4S] cluster (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentchloroplast nucleoid
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
      LOC107476774
    • Synonyms
      NTH1

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Fabales > Fabaceae > Papilionoideae > 50 kb inversion clade > dalbergioids sensu lato > Dalbergieae > Pterocarpus clade > Arachis

Accessions

  • Primary accession
    A0A6P4CL16

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for compositional bias, region, domain.

TypeIDPosition(s)Description
Compositional bias25-49Polar residues
Region25-88Disordered
Compositional bias74-88Basic and acidic residues
Domain179-335HhH-GPD
Region357-378Disordered

Sequence similarities

Belongs to the Nth/MutY family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    378
  • Mass (Da)
    41,660
  • Last updated
    2020-12-02 v1
  • Checksum
    FFBC50B4CA5EA287
MLVFSVTPRSFGLGRIKVSFLMTQTTPSLPSNSNTDTPTSDSSSHAASVSKARVFVRRSKRPKTTLVALQQKELEPPTRDHDKSSGLPEIEDFAYSGANNAFTQSSKSELGLDATLVESEATSPRHSGELPAHWERVLEGIRRMRCSAEAPVDTMGCEKAGDTLPPKERRFAVLVSSLLSSQTKDHVTHGAIQRLLENGLLTPDAINNADEETIKKMLYPVGFYTRKATNLKKIANICLMKYDGDIPSTIEQLLLLPGIGPKMAHLVMNVGWNNVQGICVDTHVHRICNRLGWVSRPSTKQKTLTPEETREALQRWLPREEWVPINPLLVGFGQTICTPLRPRCGECGISHLCPSAFKEASNSSPSSKPKKSGPNKKR

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias25-49Polar residues
Compositional bias74-88Basic and acidic residues

Keywords

Sequence databases

Genome annotation databases

Similar Proteins

Disclaimer

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