| UniProt functional annotation for Q1LK00 | |||
| UniProt code: Q1LK00. |
| Organism: | Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34) (Ralstonia metallidurans). | |
| Taxonomy: | Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Burkholderiaceae; Cupriavidus. | |
| 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. {ECO:0000255|HAMAP-Rule:MF_01972, ECO:0000269|PubMed:17198384}. | |
| Catalytic activity: | Reaction=L-tryptophan + O2 = N-formyl-L-kynurenine; Xref=Rhea:RHEA:24536, ChEBI:CHEBI:15379, ChEBI:CHEBI:57912, ChEBI:CHEBI:58629; EC=1.13.11.11; Evidence={ECO:0000255|HAMAP- Rule:MF_01972, ECO:0000269|PubMed:14700627, ECO:0000269|PubMed:17198384}; | |
| Cofactor: | Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000255|HAMAP-Rule:MF_01972}; Note=Binds 1 heme group per subunit. {ECO:0000255|HAMAP-Rule:MF_01972}; | |
| Biophysicochemical properties: | Kinetic parameters: KM=350 uM for tryptophan {ECO:0000269|PubMed:14700627}; | |
| Pathway: | Amino-acid degradation; L-tryptophan degradation via kynurenine pathway; L-kynurenine from L-tryptophan: step 1/2. {ECO:0000255|HAMAP-Rule:MF_01972}. | |
| Subunit: | Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01972, ECO:0000269|PubMed:17198384}. | |
| Similarity: | Belongs to the tryptophan 2,3-dioxygenase family. {ECO:0000255|HAMAP-Rule:MF_01972}. | |
Annotations taken from UniProtKB at the EBI.