B0JUK9 · MTND_MICAN

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

Protein has several cofactor binding sites:
Fe2+ (UniProtKB | Rhea| CHEBI:29033 )

Note: Binds 1 Fe2+ cation per monomer.
Ni2+ (UniProtKB | Rhea| CHEBI:49786 )

Note: Binds 1 nickel ion per monomer.

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, site.

TypeIDPosition(s)Description
Binding site99Fe2+ (UniProtKB | ChEBI)
Binding site99Ni2+ (UniProtKB | ChEBI)
Binding site101Fe2+ (UniProtKB | ChEBI)
Binding site101Ni2+ (UniProtKB | ChEBI)
Site104May play a role in transmitting local conformational changes
Binding site105Fe2+ (UniProtKB | ChEBI)
Binding site105Ni2+ (UniProtKB | ChEBI)
Site107Important to generate the dianion
Binding site144Fe2+ (UniProtKB | ChEBI)
Binding site144Ni2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
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
Biological ProcessL-methionine salvage from S-adenosylmethionine

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Acireductone dioxygenase
  • Alternative names
    • 1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase
      (DHK-MTPene dioxygenase
      )
    • 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
      mtnD
    • Ordered locus names
      MAE_46350

Organism names

Accessions

  • Primary accession
    B0JUK9

Proteomes

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003592111-183Acireductone dioxygenase

Proteomic databases

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the acireductone dioxygenase (ARD) family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    183
  • Mass (Da)
    20,819
  • Last updated
    2008-03-18 v1
  • Checksum
    F780422554778590
MAILRLENGTTYTQLADISLELAKLNVTLNYWPIENEATRQLLKQASLTDEEKEIVLTSLDGYFEQLKQEAGYQARDLIVLHPEIANLDTLLAKFERCHTHADDEVRYIIDGEGVFGFVFADGSQGELTIQPQEYINVPAHSEHWFHLTASKRVKAVRYFTSTAGWVPEYTETVIRFPSLTAV

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP009552
EMBL· GenBank· DDBJ
BAG04457.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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