A0A0L0SQ18 · A0A0L0SQ18_ALLM3

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 site91Fe2+ (UniProtKB | ChEBI); for iron-dependent acireductone dioxygenase activity
Binding site91Ni2+ (UniProtKB | ChEBI); for nickel-dependent acireductone dioxygenase activity
Binding site93Fe2+ (UniProtKB | ChEBI); for iron-dependent acireductone dioxygenase activity
Binding site93Ni2+ (UniProtKB | ChEBI); for nickel-dependent acireductone dioxygenase activity
Binding site97Fe2+ (UniProtKB | ChEBI); for iron-dependent acireductone dioxygenase activity
Binding site97Ni2+ (UniProtKB | ChEBI); for nickel-dependent acireductone dioxygenase activity
Binding site136Fe2+ (UniProtKB | ChEBI); for iron-dependent acireductone dioxygenase activity
Binding site136Ni2+ (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

    • Name
      ADI1
    • ORF names
      AMAG_10005

Organism names

Accessions

  • Primary accession
    A0A0L0SQ18

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Interaction

Protein-protein interaction databases

Family & Domains

Sequence similarities

Belongs to the acireductone dioxygenase (ARD) family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    186
  • Mass (Da)
    21,347
  • Last updated
    2015-11-11 v1
  • Checksum
    BA02BA249F418554
MVRIYYYDNDTTTDPRAPHVLPGHADLTERDLATTGVLYWRVPIAADGRAHLTEIDRISAERGYKNRDQICVAPGRLPEYETKIKSFFDEHLHEDEEIRYILGGSGFFDVRDDKDRWVRVAVQAGDLLVLPAGIYHRFTTDEKNYIEAMRLFKDEPKWTPLSRSIPATDKVPSRAEYLATIAPASH

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
GG745345
EMBL· GenBank· DDBJ
KNE64648.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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