A0A6C1BUC0 · A0A6C1BUC0_9AQUI
- ProteinAcireductone dioxygenase
- GenemtnD
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids184 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes 2 different reactions between oxygene 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
- 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2 = 3-(methylsulfanyl)propanoate + CO + formate + 2 H+
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 Fe2+ cation per monomer.
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 site, binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Site | 94 | May play a role in metal incorporation in vivo | |||
Binding site | 95 | Fe2+ (UniProtKB | ChEBI) | |||
Binding site | 95 | Ni2+ (UniProtKB | ChEBI) | |||
Binding site | 97 | Fe2+ (UniProtKB | ChEBI) | |||
Binding site | 97 | Ni2+ (UniProtKB | ChEBI) | |||
Binding site | 101 | Fe2+ (UniProtKB | ChEBI) | |||
Binding site | 101 | Ni2+ (UniProtKB | ChEBI) | |||
Site | 103 | Important to generate the dianion | |||
Binding site | 139 | Fe2+ (UniProtKB | ChEBI) | |||
Binding site | 139 | Ni2+ (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
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 | |
Biological Process | L-methionine salvage from methylthioadenosine | |
Biological Process | L-methionine salvage from S-adenosylmethionine |
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 lineageBacteria > Aquificota > Aquificia > Aquificales > Aquificaceae > Hydrogenobacter
Accessions
- Primary accessionA0A6C1BUC0
Proteomes
Interaction
Subunit
Monomer.
Structure
Sequence
- Sequence statusComplete
- Length184
- Mass (Da)21,509
- Last updated2020-06-17 v1
- Checksum610645CEC134EBA4
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP048795 EMBL· GenBank· DDBJ | QID33390.1 EMBL· GenBank· DDBJ | Genomic DNA |