A0AA43QKY2 · A0AA43QKY2_9LECA
- Protein3-hydroxyanthranilate 3,4-dioxygenase
- GeneBNA1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids175 (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 | 44 | O2 (UniProtKB | ChEBI) | |||
Binding site | 48 | Fe cation (UniProtKB | ChEBI); catalytic | |||
Binding site | 54 | Fe cation (UniProtKB | ChEBI); catalytic | |||
Binding site | 54 | substrate | |||
Binding site | 92 | Fe cation (UniProtKB | ChEBI); catalytic | |||
Binding site | 96 | substrate | |||
Binding site | 106 | substrate | |||
Binding site | 121 | a divalent metal cation (UniProtKB | ChEBI) | |||
Binding site | 124 | a divalent metal cation (UniProtKB | ChEBI) | |||
Binding site | 158 | a divalent metal cation (UniProtKB | ChEBI) | |||
Binding site | 161 | 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
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Lecanoromycetes > OSLEUM clade > Lecanoromycetidae > Lecanorales > Lecanorineae > Ramalinaceae > Ramalina
Accessions
- Primary accessionA0AA43QKY2
Proteomes
Subcellular Location
Structure
Sequence
- Sequence statusComplete
- Length175
- Mass (Da)20,044
- Last updated2024-01-24 v1
- ChecksumFEDFDFFB83FBC6F6
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JAPUFD010000007 EMBL· GenBank· DDBJ | MDI1488391.1 EMBL· GenBank· DDBJ | Genomic DNA |