<unk>  <unk>  is an enzyme () that reduces<unk> <unk>  after it has been oxidised in the carboxylation of glutamic acid residues in blood coagulation enzymes.<unk>  is a member of a large family of predicted enzymes that are present in vertebrates, Drosophila, plants, bacteria and archaea. In some plant and bacterial homologues, the<unk>  domain is fused with domains of the thioredoxin family of oxidoreductases. Four cysteine residues and one residue, which is either serine or threonine, are identified as likely active-site residues. Solved bacterial<unk>  structures has enabled more insights into the catalytic mechanism. All<unk> s are transmembrane proteins with at least three TM helices at the catalytic core. The quinone to be reduced is bound by a redox-active CXXC motif in the C-terminal helices, similar to the DsbB active site. Two other cysteines to the N-terminal are located in a loop outside of the transmembrane region; they relay electrons with a redox protein (or in the case of the bacterial homolog, its own fused domain). The human gene for<unk>  is called<unk> C1 <unk>  complex subunit 1). It is the target of anticoagulant warfarin. Its partner is a redox protein with an unknown identity. There is also a similar gene called<unk> C1L1.
Vitamin K epoxide reductase
Prothrombinase
Von Willebrand factor
UDP glucuronosyltransferase 1 family, polypeptide A1
Flavin-containing monooxygenase 3
Prostaglandin-endoperoxide synthase 2
Thrombin
Tenase