A0A855JMR4 · A0A855JMR4_9PSED
- ProteinKynurenine formamidase
- GenekynB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids216 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the kynurenine pathway of tryptophan degradation.
Catalytic activity
- N-formyl-L-kynurenine + H2O = L-kynurenine + formate + H+
Cofactor
Note: Binds 2 zinc ions per subunit.
Pathway
Amino-acid degradation; L-tryptophan degradation via kynurenine pathway; L-kynurenine from L-tryptophan: step 2/2.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 21 | substrate | ||||
Sequence: W | ||||||
Binding site | 51 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 55 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 57 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 57 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 61 | Proton donor/acceptor | ||||
Sequence: H | ||||||
Binding site | 163 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 175 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 175 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | arylformamidase activity | |
Molecular Function | formamidase activity | |
Molecular Function | zinc ion binding | |
Biological Process | tryptophan catabolic process to kynurenine |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameKynurenine formamidase
- EC number
- Short namesKFA ; KFase
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas
Accessions
- Primary accessionA0A855JMR4
Proteomes
Interaction
Subunit
Homodimer.
Structure
Sequence
- Sequence statusComplete
- Length216
- Mass (Da)23,621
- Last updated2021-09-29 v1
- Checksum55DAA5DF929A1624