A0A397Y599 · A0A397Y599_BRACM

Function

function

Catalyzes 2 different reactions between oxygen and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site. Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4-methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine in the methionine recycle pathway. Ni-containing acireductone dioxygenase (Ni-ARD) produces methylthiopropionate, carbon monoxide and formate, and does not lie on the methionine recycle pathway.

Catalytic activity

Cofactor

Fe2+ (UniProtKB | Rhea| CHEBI:29033 )

Ni2+ (UniProtKB | Rhea| CHEBI:49786 )

Note: Binds either 1 Fe or Ni cation per monomer. Iron-binding promotes an acireductone dioxygenase reaction producing 2-keto-4-methylthiobutyrate, while nickel-binding promotes an acireductone dioxygenase reaction producing 3-(methylsulfanyl)propanoate.

Pathway

Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 5/6.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site89Fe2+ (UniProtKB | ChEBI); for iron-dependent acireductone dioxygenase activity
Binding site89Ni2+ (UniProtKB | ChEBI); for nickel-dependent acireductone dioxygenase activity
Binding site91Fe2+ (UniProtKB | ChEBI); for iron-dependent acireductone dioxygenase activity
Binding site91Ni2+ (UniProtKB | ChEBI); for nickel-dependent acireductone dioxygenase activity
Binding site95Fe2+ (UniProtKB | ChEBI); for iron-dependent acireductone dioxygenase activity
Binding site95Ni2+ (UniProtKB | ChEBI); for nickel-dependent acireductone dioxygenase activity
Binding site134Fe2+ (UniProtKB | ChEBI); for iron-dependent acireductone dioxygenase activity
Binding site134Ni2+ (UniProtKB | ChEBI); for nickel-dependent acireductone dioxygenase activity

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentnucleus
Molecular Functionacireductone dioxygenase (Ni2+-requiring) activity
Molecular Functionacireductone dioxygenase [iron(II)-requiring] activity
Molecular Functioniron ion binding
Molecular Functionnickel cation binding
Biological ProcessL-methionine salvage from methylthioadenosine

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Acireductone dioxygenase
  • Alternative names
    • Acireductone dioxygenase (Fe(2+)-requiring)
      (ARD'
      ; Fe-ARD
      ) (EC:1.13.11.54
      ) . EC:1.13.11.54 (UniProtKB | ENZYME | Rhea)
    • Acireductone dioxygenase (Ni(2+)-requiring)
      (ARD
      ; Ni-ARD
      ) (EC:1.13.11.53
      ) . EC:1.13.11.53 (UniProtKB | ENZYME | Rhea)

Gene names

    • ORF names
      BRARA_I01800

Organism names

  • Taxonomic identifier
  • Strain
    • cv. B-3
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Brassiceae > Brassica

Accessions

  • Primary accession
    A0A397Y599

Proteomes

Subcellular Location

Keywords

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region1-20Disordered

Sequence similarities

Belongs to the acireductone dioxygenase (ARD) family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    187
  • Mass (Da)
    22,401
  • Last updated
    2018-12-05 v1
  • MD5 Checksum
    7E6ADC04DBEC306EFEB0AC59A40835ED
MALEAWLMDDSNEDQRLPHHPNPKELLTMDYLAELGVLYWKLNPDNYENDSELGKIRDERGYDYMDMLDLCPEKVSNYEEKLKNFFTEHIHKDEEIRYCLAGSGYFDVRDKDDRWIRIWMKPGDLIVLPAGIYHRFTLDTSNYIKLMRLFVGEPVWTPYNRPQEEHPVRKEYIKSLTHKFGESIQAH

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CM010636
EMBL· GenBank· DDBJ
RID45043.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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