A0A0L0TBY1 · A0A0L0TBY1_ALLM3
- Protein3-hydroxyanthranilate 3,4-dioxygenase
- GeneBNA1
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids170 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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
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 | 45 | O2 (UniProtKB | ChEBI) | |||
Binding site | 49 | Fe cation (UniProtKB | ChEBI); catalytic | |||
Binding site | 55 | Fe cation (UniProtKB | ChEBI); catalytic | |||
Binding site | 55 | substrate | |||
Binding site | 94 | Fe cation (UniProtKB | ChEBI); catalytic | |||
Binding site | 98 | substrate | |||
Binding site | 108 | substrate | |||
Binding site | 123 | a divalent metal cation (UniProtKB | ChEBI) | |||
Binding site | 126 | a divalent metal cation (UniProtKB | ChEBI) | |||
Binding site | 160 | a divalent metal cation (UniProtKB | ChEBI) | |||
Binding site | 163 | a divalent metal cation (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
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
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Fungi incertae sedis > Blastocladiomycota > Blastocladiomycetes > Blastocladiales > Blastocladiaceae > Allomyces
Accessions
- Primary accessionA0A0L0TBY1
Proteomes
Organism-specific databases
Subcellular Location
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length170
- Mass (Da)19,391
- Last updated2015-11-11 v1
- Checksum703208BDAC40B403
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
GG745378 EMBL· GenBank· DDBJ | KNE72226.1 EMBL· GenBank· DDBJ | Genomic DNA |