A0A1J7J0Q0 · A0A1J7J0Q0_9PEZI
- ProteinKynureninase
- GeneBNA5
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids473 (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 | 133 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 134 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 162-165 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: FPSD | ||||||
Binding site | 248 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 251 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 273 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 315 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 343 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: N |
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
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Sordariomycetidae > Coniochaetales > Coniochaetaceae > Coniochaeta
Accessions
- Primary accessionA0A1J7J0Q0
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 274 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K |
Interaction
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-21 | Basic and acidic residues | ||||
Sequence: MASSHRRDRARQLDREDPLAS | ||||||
Region | 1-25 | Disordered | ||||
Sequence: MASSHRRDRARQLDREDPLASTRSE | ||||||
Domain | 61-284 | Aminotransferase class V | ||||
Sequence: YLCGNSLGLQPKRTVTRLQQYLSTWATQGVQGHFKPLDDSPLPTWLDADARAAELIAPVVGADKSEVAVMQTLTANLHFLMSAFYRPDINGRHKIILESKAFPSDHFAVETQLRHHGLSPETSMITLKSPHSEDNVLTTDDITSAIAEHADSTALILLPGIQYYTGQLLDIRTITAFAHKHGIFIIWDLAHAVGNVPLALHDWDVDAAAWCTYKYLNGGPGCIG |
Sequence similarities
Belongs to the kynureninase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length473
- Mass (Da)51,765
- Last updated2017-02-15 v1
- Checksum44FCA4DD74C69129
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-21 | Basic and acidic residues | ||||
Sequence: MASSHRRDRARQLDREDPLAS |
Keywords
- Technical term