Q99JT9 · MTND_MOUSE

  • Protein
    Acireductone dioxygenase
  • Gene
    Adi1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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 (PubMed:26858196).
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 (PubMed:26858196).
Ni-containing acireductone dioxygenase (Ni-ARD) produces methylthiopropionate, carbon monoxide and formate, and does not lie on the methionine recycle pathway (PubMed:26858196).
Also down-regulates cell migration mediated by MMP14 (By similarity).

Catalytic activity

Cofactor

Fe2+ (UniProtKB | Rhea| CHEBI:29033 )

Ni2+ (UniProtKB | Rhea| CHEBI:49786 )

Note: Binds either 1 Fe or Ni cation per monomer (PubMed:26858196).
Iron-binding promotes an acireductone dioxygenase reaction producing 2-keto-4-methylthiobutyrate, while nickel-binding promotes an acireductone dioxygenase reaction producing 3-(methylsulfanyl)propanoate (PubMed:26858196).

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
0.123 mM1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-oneusing iron as cofactor
0.44 mM1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-oneusing cobalt as cofactor
0.302 mM1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-oneusing nickel as cofactor
kcat is 114.3 sec-1 with 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one as substrate (using iron as cofactor) (PubMed:26858196).
kcat is 7.55 sec-1 with 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one as substrate (using cobalt as cofactor) (PubMed:26858196).
kcat is 17.7 sec-1 with 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one as substrate (using nickel as cofactor) (PubMed:26858196).

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 site88Fe2+ (UniProtKB | ChEBI); for iron-dependent acireductone dioxygenase activity
Binding site88Ni2+ (UniProtKB | ChEBI); for nickel-dependent acireductone dioxygenase activity
Binding site90Fe2+ (UniProtKB | ChEBI); for iron-dependent acireductone dioxygenase activity
Binding site90Ni2+ (UniProtKB | ChEBI); for nickel-dependent acireductone dioxygenase activity
Binding site94Fe2+ (UniProtKB | ChEBI); for iron-dependent acireductone dioxygenase activity
Binding site94Ni2+ (UniProtKB | ChEBI); for nickel-dependent acireductone dioxygenase activity
Binding site133Fe2+ (UniProtKB | ChEBI); for iron-dependent acireductone dioxygenase activity
Binding site133Ni2+ (UniProtKB | ChEBI); for nickel-dependent acireductone dioxygenase activity

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentnucleus
Cellular Componentplasma membrane
Molecular Functionacireductone dioxygenase (Ni2+-requiring) activity
Molecular Functionacireductone dioxygenase [iron(II)-requiring] activity
Molecular Functioniron ion binding
Molecular Functionnickel cation binding
Molecular Functionoxidoreductase activity
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)
    • Membrane-type 1 matrix metalloproteinase cytoplasmic tail-binding protein 1
      (MTCBP-1
      )

Gene names

    • Name
      Adi1
    • Synonyms
      Mtcbp1

Organism names

  • Taxonomic identifier
  • Strain
    • FVB/N
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q99JT9

Proteomes

Organism-specific databases

Subcellular Location

Cytoplasm
Nucleus
Cell membrane
; Peripheral membrane protein
Note: Localizes to the plasma membrane when complexed to MMP14.

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001629431-179Acireductone dioxygenase

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Monomer. Interacts with MMP14.

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region1-24Disordered

Sequence similarities

Belongs to the acireductone dioxygenase (ARD) family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    179
  • Mass (Da)
    21,524
  • Last updated
    2001-06-01 v1
  • MD5 Checksum
    E0AB4BD648265928C9E72570E2236939
MVQAWYMDESTADPRKPHRAQPDRPVSLEQLRTLGVLYWKLDADKYENDPELEKIRKMRNYSWMDIITICKDTLPNYEEKIKMFFEEHLHLDEEIRYILEGSGYFDVRDKEDKWIRISMEKGDMITLPAGIYHRFTLDEKNYVKAMRLFVGEPVWTPYNRPADHFDARVQYMSFLEGTA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AK145831
EMBL· GenBank· DDBJ
BAE26682.1
EMBL· GenBank· DDBJ
mRNA
BC005695
EMBL· GenBank· DDBJ
AAH05695.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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