A0AA38Y293 · A0AA38Y293_9EURO
- ProteinMultifunctional fusion protein
- GeneBNA5
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1555 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
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.
Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid.
Catalytic activity
- 3-hydroxy-L-kynurenine + H2O = 3-hydroxyanthranilate + L-alanine + H+
Cofactor
Protein has several cofactor binding sites:
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 1/3.
Cofactor biosynthesis; NAD+ biosynthesis; quinolinate from L-kynurenine: step 2/3.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 105 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 106 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 218 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 221 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 243 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 274 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 302 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial outer membrane | |
Molecular Function | DNA binding | |
Molecular Function | FAD binding | |
Molecular Function | kynureninase activity | |
Molecular Function | kynurenine 3-monooxygenase activity | |
Molecular Function | metal ion binding | |
Molecular Function | pyridoxal phosphate binding | |
Molecular Function | single-stranded DNA 3'-5' DNA exonuclease activity | |
Biological Process | 'de novo' NAD biosynthetic process from tryptophan | |
Biological Process | anthranilate metabolic process | |
Biological Process | DNA repair | |
Biological Process | L-kynurenine catabolic process | |
Biological Process | quinolinate biosynthetic process | |
Biological Process | tryptophan catabolic process to kynurenine |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameMultifunctional fusion protein
Including 2 domains:
- Recommended nameKynureninase
- EC number
- Alternative names
- Recommended nameKynurenine 3-monooxygenase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Chaetothyriomycetidae > Chaetothyriales > Trichomeriaceae > Knufia
Accessions
- Primary accessionA0AA38Y293
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Modified residue | 244 | N6-(pyridoxal phosphate)lysine | |||
Interaction
Subunit
Homodimer.
Monomer. Interacts with ssb (via C-terminus); this interaction stimulates the exonuclease activity by recruiting the enzyme to its substrate.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 1053-1208 | ExoI SH3-like | |||
Domain | 1211-1333 | ExoI C-terminal | |||
Sequence similarities
Belongs to the aromatic-ring hydroxylase family. KMO subfamily.
Belongs to the kynureninase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,555
- Mass (Da)175,574
- Last updated2024-01-24 v1
- MD5 ChecksumCE0FB8BDAB4036F1EA4AD87064DF3889
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JAPDRN010000049 EMBL· GenBank· DDBJ | KAJ9633084.1 EMBL· GenBank· DDBJ | Genomic DNA |