A0A2L2XSK2 · A0A2L2XSK2_9CHRO
- ProteinAcireductone dioxygenase
- GenemtnD
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids183 (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 binding site, site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 99 | Fe2+ (UniProtKB | ChEBI) | |||
Binding site | 99 | Ni2+ (UniProtKB | ChEBI) | |||
Binding site | 101 | Fe2+ (UniProtKB | ChEBI) | |||
Binding site | 101 | Ni2+ (UniProtKB | ChEBI) | |||
Site | 104 | May play a role in transmitting local conformational changes | |||
Binding site | 105 | Fe2+ (UniProtKB | ChEBI) | |||
Binding site | 105 | Ni2+ (UniProtKB | ChEBI) | |||
Site | 107 | Important to generate the dianion | |||
Binding site | 144 | Fe2+ (UniProtKB | ChEBI) | |||
Binding site | 144 | 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 > Cyanobacteriota > Cyanophyceae > Oscillatoriophycideae > Chroococcales > Microcystaceae > Microcystis
Accessions
- Primary accessionA0A2L2XSK2
Proteomes
Interaction
Subunit
Monomer.
Structure
Sequence
- Sequence statusComplete
- Length183
- Mass (Da)20,888
- Last updated2018-04-25 v1
- ChecksumF785F895547294D1
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BDSM01000043 EMBL· GenBank· DDBJ | GBF54998.1 EMBL· GenBank· DDBJ | Genomic DNA |