Vitamin K epoxide reductase (IPR012932)

Short name: VKOR

Domain relationships



Vitamin K epoxide reductase (VKOR) recycles vitamin K 2,3-epoxide to vitamin K hydroquinone, a co-factor that is essential for the posttranslational gamma-carboxylation of several blood coagulation factors [PMID: 14765194]. VKORC1, the catalytic subunit of the VKOR complex, is a member of a large family of predicted enzymes that are present in vertebrates, Drosophila, plants, bacteria and archaea [PMID: 15276181]. Bacterial VKOR homologues catalyse disulphide bridge formation in secreted proteins by cooperating with a periplasmic, Trx-like redox partner [PMID: 18413314, PMID: 18695247]. In fact, in some plant and bacterial homologues the VKORC1 homologous domain is fused with domains of the thioredoxin family of oxidoreductases [PMID: 15276181]. VKOR is part of a disulphide bond formation pathway that uses electrons from cysteines of newly synthesized proteins to reduce a quinone [PMID: 20110994].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.