B0Y9Z9 · 3HAO1_ASPFC
- Protein3-hydroxyanthranilate 3,4-dioxygenase 1
- Genebna1-1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids192 (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 | 50 | O2 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 54 | Fe cation (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 60 | Fe cation (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 60 | substrate | ||||
Sequence: E | ||||||
Binding site | 102 | Fe cation (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 106 | substrate | ||||
Sequence: R | ||||||
Binding site | 116 | substrate | ||||
Sequence: E | ||||||
Binding site | 131 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 134 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 168 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 171 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: C |
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 1
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Fumigati
Accessions
- Primary accessionB0Y9Z9
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000361976 | 1-192 | 3-hydroxyanthranilate 3,4-dioxygenase 1 | |||
Sequence: MLPPALNIPKWLEENSHLLQPPVNNYCVYHPSSPATAGYTVMIVGGPNARTDYHINTTPEFFYQYRGSMLLKTVDTSVSPPVFQDIPIHEGSIFLLPANTPHCPVRFKDTVGVVMEQPRPKDAVDTMLWFCKKCGEVVWEKRFVCTDLGTQVKEVVEEFAADQEKRTCKACGTIAETRYQEGEVVQPPRFLE |
Structure
Sequence
- Sequence statusComplete
- Length192
- Mass (Da)21,705
- Last updated2008-04-08 v1
- Checksum148D406C365727F7
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
DS499600 EMBL· GenBank· DDBJ | EDP48842.1 EMBL· GenBank· DDBJ | Genomic DNA |