E9FVX1 · E9FVX1_DAPPU
- ProteinKynureninase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids479 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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 | 153 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 154 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 181-184 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: FPSD | ||||||
Binding site | 237 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 266 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 269 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 291 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 321 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 349 | 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
- Organism
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Crustacea > Branchiopoda > Diplostraca > Cladocera > Anomopoda > Daphniidae > Daphnia
Accessions
- Primary accessionE9FVX1
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 292 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K |
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 132-391 | Aminotransferase class V | ||||
Sequence: KESLVKLVGAGHSDEVVCMNGLSVNIHLLLISFYRPTANRYKIMIEGHSFPSDRYAVVSQLKLHGYTEEDGLVILQTRTGEHLLRTEDILAAIQEHGQSVAVVFLSGVHYYTGQKFDIETITKSGQAQGCLVGWDLAHAAGNTELKLHDWSVDFACWCSYKYLNSGAGCIAGAFIHRKHHQDDRPRLCGWWSNREETRFDMQHSVDAAPGADAYRLCNPPPALVALHKAGLEIFEEAGMDRLLAKQYLLTGYLEYLMDHL |
Sequence similarities
Belongs to the kynureninase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length479
- Mass (Da)54,020
- Last updated2011-04-05 v1
- Checksum44A1FBB567E54F2F
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
GL732525 EMBL· GenBank· DDBJ | EFX89028.1 EMBL· GenBank· DDBJ | Genomic DNA |