B0XS72 · KYNU1_ASPFC
- ProteinKynureninase 1
- Genebna5-1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids509 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively.
Catalytic activity
- L-kynurenine + H2O = anthranilate + L-alanine + H+
Cofactor
Pathway
Amino-acid degradation; L-kynurenine degradation; L-alanine and anthranilate from L-kynurenine: step 1/1.
Cofactor biosynthesis; NAD+ biosynthesis; quinolinate from L-kynurenine: step 2/3.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 169 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 170 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 197-200 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 283 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 286 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 308 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 349 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 377 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 3-hydroxykynureninase activity | |
Molecular Function | kynureninase activity | |
Molecular Function | pyridoxal phosphate binding | |
Biological Process | 'de novo' NAD biosynthetic process from tryptophan | |
Biological Process | anthranilate metabolic process | |
Biological Process | L-kynurenine catabolic process | |
Biological Process | quinolinate biosynthetic process | |
Biological Process | tryptophan catabolic process to kynurenine |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameKynureninase 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 accessionB0XS72
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000356963 | 1-509 | Kynureninase 1 | ||
Modified residue | 309 | N6-(pyridoxal phosphate)lysine | |||
Interaction
Subunit
Homodimer.
Structure
Sequence
- Sequence statusComplete
- Length509
- Mass (Da)57,148
- Last updated2008-04-08 v1
- MD5 Checksum06322C02C435E6FC96621F9A51837C79
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
DS499595 EMBL· GenBank· DDBJ | EDP54558.1 EMBL· GenBank· DDBJ | Genomic DNA |