| UniProt functional annotation for C7QJ42 | |||
| UniProt code: C7QJ42. |
| Organism: | Catenulispora acidiphila (strain DSM 44928 / JCM 14897 / NBRC 102108 / NRRL B-24433 / ID139908). | |
| Taxonomy: | Bacteria; Actinobacteria; Catenulisporales; Catenulisporaceae; Catenulispora. | |
| Function: | Alpha-ketoglutarate-dependent dioxygenase that in vitro catalyzes the regio- and stereoselective hydroxylation of L-lysine, leading to (3S)-3-hydroxy-L-lysine. Can also use (5R)-5-hydroxy-L- lysine as substrate, but neither D-lysine nor L-ornithine. {ECO:0000269|Ref.2}. | |
| Catalytic activity: | Reaction=2-oxoglutarate + L-lysine + O2 = (3S)-3-hydroxy-L-lysine + CO2 + succinate; Xref=Rhea:RHEA:40747, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:32551, ChEBI:CHEBI:77409; Evidence={ECO:0000269|Ref.2}; | |
| Cofactor: | Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:Q9Z4Z5}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9Z4Z5}; | |
| Biotechnology: | Being totally regio- and stereoselective, this enzyme is of interest for biocatalytic purposes to produce chiral scaffolds that are of synthetic value in the preparation of more complex functionalized chiral molecules such as natural products and analogs. {ECO:0000305|Ref.2}. | |
| Similarity: | Belongs to the clavaminate synthase family. {ECO:0000305}. | |
Annotations taken from UniProtKB at the EBI.