|SMART accession number:||SM00756|
|Description:||Family of likely enzymes that includes the catalytic subunit of vitamin K epoxide reductase. Bacterial homologues are fused to members of the thioredoxin family of oxidoreductases.|
|Interpro abstract (IPR012932):|
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 [(PUBMED: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 [(PUBMED:15276181)]. Bacterial VKOR homologues catalyse disulphide bridge formation in secreted proteins by cooperating with a periplasmic, Trx-like redox partner [(PUBMED:18413314), (PUBMED:18695247)]. In fact, in some plant and bacterial homologues the VKORC1 homologous domain is fused with domains of the thioredoxin family of oxidoreductases [(PUBMED:15276181)]. VKOR is part of a disulphide bond formation pathway that uses electrons from cysteines of newly synthesized proteins to reduce a quinone [(PUBMED:20110994)].
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- Evolution (species in which this domain is found)
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- Structure (3D structures containing this domain)
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