Q99JT9 · MTND_MOUSE
- ProteinAcireductone dioxygenase
- GeneAdi1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids179 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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
- 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2 = 4-methylsulfanyl-2-oxobutanoate + formate + 2 H+
Cofactor
Ni2+ (UniProtKB | Rhea| CHEBI:49786 )
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.123 mM | 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one | using iron as cofactor | ||||
0.44 mM | 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one | using cobalt as cofactor | ||||
0.302 mM | 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one | using 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).
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.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 88 | Fe2+ (UniProtKB | ChEBI); for iron-dependent acireductone dioxygenase activity | |||
Binding site | 88 | Ni2+ (UniProtKB | ChEBI); for nickel-dependent acireductone dioxygenase activity | |||
Binding site | 90 | Fe2+ (UniProtKB | ChEBI); for iron-dependent acireductone dioxygenase activity | |||
Binding site | 90 | Ni2+ (UniProtKB | ChEBI); for nickel-dependent acireductone dioxygenase activity | |||
Binding site | 94 | Fe2+ (UniProtKB | ChEBI); for iron-dependent acireductone dioxygenase activity | |||
Binding site | 94 | Ni2+ (UniProtKB | ChEBI); for nickel-dependent acireductone dioxygenase activity | |||
Binding site | 133 | Fe2+ (UniProtKB | ChEBI); for iron-dependent acireductone dioxygenase activity | |||
Binding site | 133 | Ni2+ (UniProtKB | ChEBI); for nickel-dependent acireductone dioxygenase activity | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Cellular Component | plasma membrane | |
Molecular Function | acireductone dioxygenase (Ni2+-requiring) activity | |
Molecular Function | acireductone dioxygenase [iron(II)-requiring] activity | |
Molecular Function | iron ion binding | |
Molecular Function | nickel cation binding | |
Molecular Function | oxidoreductase activity | |
Biological Process | L-methionine salvage from methylthioadenosine |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAcireductone dioxygenase
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ99JT9
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Note: Localizes to the plasma membrane when complexed to MMP14.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000162943 | 1-179 | Acireductone dioxygenase | ||
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-24 | Disordered | |||
Sequence similarities
Belongs to the acireductone dioxygenase (ARD) family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length179
- Mass (Da)21,524
- Last updated2001-06-01 v1
- MD5 ChecksumE0AB4BD648265928C9E72570E2236939
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK145831 EMBL· GenBank· DDBJ | BAE26682.1 EMBL· GenBank· DDBJ | mRNA | ||
BC005695 EMBL· GenBank· DDBJ | AAH05695.1 EMBL· GenBank· DDBJ | mRNA |