Q1LCS4 · 3HAO_CUPMC
- Protein3-hydroxyanthranilate 3,4-dioxygenase
- GenenbaC
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids174 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate.
Catalytic activity
- 3-hydroxyanthranilate + O2 = (2Z,4Z)-2-amino-3-carboxymuconate 6-semialdehyde
Cofactor
Note: Binds 2 Fe2+ ions per subunit.
Activity regulation
Inhibited by 4-chloro-3-hydroxyanthranilate. Mechanism of inactivation involves the oxidation of the catalytic active site Fe2+ to the catalytically inactive Fe3+ oxidation state, superoxide production, and formation of two disulfide bonds between Cys-125 and Cys-128, and Cys-162 and Cys-165. Enzyme can be reactivated under reducing conditions.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
22.4 μM | 3-hydroxyanthranilate |
Pathway
Cofactor biosynthesis; NAD+ biosynthesis; quinolinate from L-kynurenine: step 3/3.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 47 | O2 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 51 | Fe cation 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 57 | Fe cation 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 57 | substrate | ||||
Sequence: E | ||||||
Binding site | 95 | Fe cation 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 99 | substrate | ||||
Sequence: R | ||||||
Binding site | 110 | substrate | ||||
Sequence: E | ||||||
Binding site | 125 | Fe cation 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 128 | Fe cation 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 162 | Fe cation 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 165 | Fe cation 2 (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 3-hydroxyanthranilate 3,4-dioxygenase activity | |
Molecular Function | ferrous iron binding | |
Biological Process | 'de novo' NAD biosynthetic process from tryptophan | |
Biological Process | anthranilate metabolic process | |
Biological Process | quinolinate biosynthetic process | |
Biological Process | tryptophan catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name3-hydroxyanthranilate 3,4-dioxygenase
- EC number
- Alternative names
Gene names
Encoded on
- Plasmid megaplasmid
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Burkholderiaceae > Cupriavidus
Accessions
- Primary accessionQ1LCS4
Proteomes
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 47 | Increases KM for 3-hydroxyanthranilate 7-fold. Decreases activity 1000-fold. | ||||
Sequence: R → A | ||||||
Mutagenesis | 99 | Increases KM for 3-hydroxyanthranilate 40-fold. Decreases activity 5000-fold. | ||||
Sequence: R → A | ||||||
Mutagenesis | 110 | Decreases KM for 3-hydroxyanthranilate 2-fold. Decreases activity 2000-fold. | ||||
Sequence: E → A |
Chemistry
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000245477 | 1-174 | 3-hydroxyanthranilate 3,4-dioxygenase | |||
Sequence: MLTYGAPFNFPRWIDEHAHLLKPPVGNRQVWQDSDFIVTVVGGPNHRTDYHDDPLEEFFYQLRGNAYLNLWVDGRRERADLKEGDIFLLPPHVRHSPQRPEAGSACLVIERQRPAGMLDGFEWYCDACGHLVHRVEVQLKSIVTDLPPLFESFYASEDKRRCPHCGQVHPGRAA |
Interaction
Subunit
Homodimer.
Structure
Sequence
- Sequence statusComplete
- Length174
- Mass (Da)20,028
- Last updated2006-05-30 v1
- Checksum385F2E3DEB3947B8
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000353 EMBL· GenBank· DDBJ | ABF12052.1 EMBL· GenBank· DDBJ | Genomic DNA |