S9VGF7 · S9VGF7_9TRYP
- ProteinKynureninase
- GeneKYNU
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids469 (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 + H+ + L-alanine
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 | 122 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 123 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 150-153 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: FPSD | ||||||
Binding site | 241 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 244 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 266 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 298 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 326 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: T |
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 |
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 > Discoba > Euglenozoa > Kinetoplastea > Metakinetoplastina > Trypanosomatida > Trypanosomatidae > Strigomonadinae > Strigomonas
Accessions
- Primary accessionS9VGF7
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 267 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K |
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 71-368 | Aminotransferase class V | ||||
Sequence: AMNDFLMKWQDQAVEGHFMQPDPWFEIDDVLRADMGKIVGASKREVVVMNALTVNLHLMLSAFYRPEGKRKKILMESHGFPSDTHCMASHLEVCGMSAEEDLLFVAAPGHEDWRAPAVPVTTKLFLDAIEKHADEVAVVLLTAVHFLTGQLFDIPTIVKAAHAKGMVVGVDAAHAVGNVPLKLHEWDVDFACWCTYKYLNSGPGNVGGAFVHSKHTDGASKLKYFKGWWGHDRKNRFSMHHNFEPADGAAAFQMSTPPSGSLTMLAPSLKLMASIGMPKLREKSLLLTAYMELLLHEL |
Sequence similarities
Belongs to the kynureninase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length469
- Mass (Da)51,343
- Last updated2013-10-16 v1
- Checksum53443E1BB1546A60
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
ATMH01008295 EMBL· GenBank· DDBJ | EPY22210.1 EMBL· GenBank· DDBJ | Genomic DNA |