A0A103QPX8 · A0A103QPX8_9BURK
- ProteinTryptophan 2,3-dioxygenase
- GenekynA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids308 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Heme-dependent dioxygenase that catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring and converts L-tryptophan to N-formyl-L-kynurenine. Catalyzes the oxidative cleavage of the indole moiety.
Catalytic activity
- L-tryptophan + O2 = N-formyl-L-kynurenine
Cofactor
Note: Binds 1 heme group per subunit.
Pathway
Amino-acid degradation; L-tryptophan degradation via kynurenine pathway; L-kynurenine from L-tryptophan: step 1/2.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | heme binding | |
Molecular Function | metal ion binding | |
Molecular Function | tryptophan 2,3-dioxygenase activity | |
Biological Process | tryptophan catabolic process to acetyl-CoA | |
Biological Process | tryptophan catabolic process to kynurenine |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTryptophan 2,3-dioxygenase
- EC number
- Short namesTDO
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Burkholderiaceae > Burkholderia > Burkholderia cepacia complex
Accessions
- Primary accessionA0A103QPX8
Proteomes
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-36 | Disordered | ||||
Sequence: MQPPGSDAPAGCPFSGARTAAPAHEAPHVPGEAGEQ |
Sequence similarities
Belongs to the tryptophan 2,3-dioxygenase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length308
- Mass (Da)35,244
- Last updated2016-04-13 v1
- Checksum940A2CD4FA2A703E