A0A7W7GDT4 · A0A7W7GDT4_9ACTN
- ProteinKynureninase
- GenekynU
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids394 (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 | 97 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 98 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 125-128 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 194 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 197 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 219 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 249 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 275 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
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
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Streptosporangiales > Streptosporangiaceae > Sphaerisporangium
Accessions
- Primary accessionA0A7W7GDT4
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Modified residue | 220 | N6-(pyridoxal phosphate)lysine | |||
Interaction
Subunit
Homodimer.
Structure
Sequence
- Sequence statusComplete
- Length394
- Mass (Da)42,426
- Last updated2021-06-02 v1
- Checksum548386A8CB8DFC73
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JACHND010000001 EMBL· GenBank· DDBJ | MBB4705967.1 EMBL· GenBank· DDBJ | Genomic DNA |