A0A7R7ZQ62 · A0A7R7ZQ62_ASPCH

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 site81Fe2+ (UniProtKB | ChEBI); for iron-dependent acireductone dioxygenase activity
Binding site81Ni2+ (UniProtKB | ChEBI); for nickel-dependent acireductone dioxygenase activity
Binding site83Fe2+ (UniProtKB | ChEBI); for iron-dependent acireductone dioxygenase activity
Binding site83Ni2+ (UniProtKB | ChEBI); for nickel-dependent acireductone dioxygenase activity
Binding site87Fe2+ (UniProtKB | ChEBI); for iron-dependent acireductone dioxygenase activity
Binding site87Ni2+ (UniProtKB | ChEBI); for nickel-dependent acireductone dioxygenase activity
Binding site126Fe2+ (UniProtKB | ChEBI); for iron-dependent acireductone dioxygenase activity
Binding site126Ni2+ (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
      ACHE_50180S

Organism names

  • Taxonomic identifier
  • Strain
    • M1
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Aspergillus

Accessions

  • Primary accession
    A0A7R7ZQ62

Proteomes

Subcellular Location

Keywords

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region1-21Disordered

Sequence similarities

Belongs to the acireductone dioxygenase (ARD) family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    178
  • Mass (Da)
    20,880
  • Last updated
    2021-06-02 v1
  • Checksum
    6008E7468A1399BF
MKAYWYDNQPGDQRLPHDSGRPVTESYLESIGVFYRHCPTIDLVDALAAERGYKNRDEVCVSPQTMGDVYEEKVKTFFSEHLHEDEEIRYIRDGEGYFDVRGQEDEWVRIRLSKDDLIILPAGIYHRFTTDDKNYVKAMRLFQEEPKWTPLNRGPEVDVNPHRKTYLETVHSPAVAVN

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP024420
EMBL· GenBank· DDBJ
BCR88982.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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