A0A5E8B471 · A0A5E8B471_9ASCO
- ProteinKynureninase
- GeneBNA5
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids458 (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
- 3-hydroxy-L-kynurenine + H2O = 3-hydroxyanthranilate + 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 | 126 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 127 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 154-157 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 210 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 241 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 244 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 266 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 296 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 324 | 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
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Dipodascaceae > Saprochaete
Accessions
- Primary accessionA0A5E8B471
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Modified residue | 267 | N6-(pyridoxal phosphate)lysine | |||
Interaction
Subunit
Homodimer.
Structure
Sequence
- Sequence statusComplete
- Length458
- Mass (Da)50,271
- Last updated2019-11-13 v1
- MD5 Checksum398412E097C7783C3F7438F0701F36CF
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CABVLU010000001 EMBL· GenBank· DDBJ | VVT44125.1 EMBL· GenBank· DDBJ | Genomic DNA |