A0A5S6PWW5 · A0A5S6PWW5_BRUMA
- ProteinKynureninase
- GeneBma-kynu-1
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids808 (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 | 474 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 475 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 502-505 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: FPSD | ||||||
Binding site | 558 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 590 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 612 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 642 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 670 | 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 | metal ion binding | |
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 > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Spirurina > Spiruromorpha > Filarioidea > Onchocercidae > Brugia
Accessions
- Primary accessionA0A5S6PWW5
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 613 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K |
Interaction
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 103-161 | FLYWCH-type | ||||
Sequence: RSKKGFEKLAYDGFLYNLDKRHQKYVLWRCEMSKKPGYKCSGRVRMTEDSLEMYSSHSH | ||||||
Region | 227-251 | Disordered | ||||
Sequence: LLEESLNPTSSSYDSSSITSTSTSN | ||||||
Compositional bias | 229-251 | Polar residues | ||||
Sequence: EESLNPTSSSYDSSSITSTSTSN |
Sequence similarities
Belongs to the kynureninase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length808
- Mass (Da)91,568
- Last updated2020-02-26 v1
- Checksum657F8A28924E5D71
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A5S6PWD9 | A0A5S6PWD9_BRUMA | Bma-kynu-1 | 654 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 229-251 | Polar residues | ||||
Sequence: EESLNPTSSSYDSSSITSTSTSN |
Keywords
- Technical term