Q1DZA6 · KYNU_COCIM
- ProteinKynureninase
- GeneBNA5
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids478 (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
- H2O + L-kynurenine = anthranilate + 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 | 138 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 139 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 166-169 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: FPSD | ||||||
Binding site | 252 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 255 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 277 | 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 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
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Onygenales > Onygenaceae > Coccidioides
Accessions
- Primary accessionQ1DZA6
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000360868 | 1-478 | Kynureninase | |||
Sequence: MVDSSKAPLPFRDSALSFKREYAESLDAQDPLREFRNQFIIPSKADLKRKSLAVAEGESPSSDCIYLCGNSLGLQPKNARMYIDRFLQTWATKAVLGHFTKLEDSPFPPYMDYDDVTSKLMAQVVGALPSEVAVMSTLTGNLHLLMASFYRPTKEKYKIILEGKAFPSDHYAVESQIRHHGFDPKDAMVLIEPKDLKEPVLPTERILKTIDEHASSTALILLPGIQYYSGQYLDIPTITAHAHSKGLLIGWDCAHAAGNVELKLHDWDVDFAAWCTYKYVNSGPGSMGALFVHEKHGQVNLENKEDPYRHRLTGWWGGDKSLRFLMDNNFVPRPGAAGFQLSNPSVLDMTAVLSSLDIFDKATMPALRKKSLELTAYLEHLLLNSPEGVRPSDDPFSIITPSDPEARGAQLSVLLKPGLLDSVFSHLVDNGVILDERKPDVIRVAPAPLYNTFTDVWDFVQIFFDACRKAAQEKDTTS | ||||||
Modified residue | 278 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K |
Interaction
Structure
Sequence
- Sequence statusComplete
- Length478
- Mass (Da)53,331
- Last updated2013-01-09 v2
- Checksum6F5C91D5D94E8873
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
GG704914 EMBL· GenBank· DDBJ | EAS33333.2 EMBL· GenBank· DDBJ | Genomic DNA |