A0A6P4APH7 · A0A6P4APH7_ZIZJJ
- ProteinAcireductone dioxygenase
- GeneLOC107423094
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids200 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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. 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
Ni2+ (UniProtKB | Rhea| CHEBI:49786 )
Note: Binds either 1 Fe or Ni cation per monomer. Iron-binding promotes an acireductone dioxygenase reaction producing 2-keto-4-methylthiobutyrate, while nickel-binding promotes an acireductone dioxygenase reaction producing 3-(methylsulfanyl)propanoate.
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 | 99 | Fe2+ (UniProtKB | ChEBI); for iron-dependent acireductone dioxygenase activity | ||||
Sequence: H | ||||||
Binding site | 99 | Ni2+ (UniProtKB | ChEBI); for nickel-dependent acireductone dioxygenase activity | ||||
Sequence: H | ||||||
Binding site | 101 | Fe2+ (UniProtKB | ChEBI); for iron-dependent acireductone dioxygenase activity | ||||
Sequence: H | ||||||
Binding site | 101 | Ni2+ (UniProtKB | ChEBI); for nickel-dependent acireductone dioxygenase activity | ||||
Sequence: H | ||||||
Binding site | 105 | Fe2+ (UniProtKB | ChEBI); for iron-dependent acireductone dioxygenase activity | ||||
Sequence: E | ||||||
Binding site | 105 | Ni2+ (UniProtKB | ChEBI); for nickel-dependent acireductone dioxygenase activity | ||||
Sequence: E | ||||||
Binding site | 144 | Fe2+ (UniProtKB | ChEBI); for iron-dependent acireductone dioxygenase activity | ||||
Sequence: H | ||||||
Binding site | 144 | Ni2+ (UniProtKB | ChEBI); for nickel-dependent acireductone dioxygenase activity | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
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 |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAcireductone dioxygenase
- Alternative names
Gene names
Organism names
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Rosales > Rhamnaceae > Paliureae > Ziziphus
Accessions
- Primary accessionA0A6P4APH7
Proteomes
Structure
Family & Domains
Sequence similarities
Belongs to the acireductone dioxygenase (ARD) family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length200
- Mass (Da)23,664
- Last updated2020-12-02 v1
- Checksum4E7287321F8434C2
Keywords
- Technical term