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  Domain Name: SCAD_SBCAD
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA dehydrogenases. Short chain acyl-CoA dehydrogenase (SCAD). SCAD is a mitochondrial beta-oxidation enzyme. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of SCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. This subgroup also contains the eukaryotic short/branched chain acyl-CoA dehydrogenase(SBCAD), the bacterial butyryl-CoA dehydorgenase(BCAD) and 2-methylbutyryl-CoA dehydrogenase, which is involved in isoleucine catabolism. These enzymes are homotetramers.
No pairwise interactions are available for this conserved domain.

Total Mutations Found: 59
Total Disease Mutations Found: 48
This domain occurred 10 times on human genes (22 proteins).



  2-@METHYLBUTYRYL-COA DEHYDROGENASE DEFICIENCY
  ISOVALERIC ACIDEMIA
  ISOVALERIC ACIDEMIA, TYPE I
  SCAD DEFICIENCY
  SCAD DEFICIENCY, MILD
  VLCAD DEFICIENCY


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Range on the Protein:  

   Protein ID            Protein Position

Domain Position:  


Feature Name:Total Found:
FAD binding site
substrate binding pocket
homotetramer interface
catalytic base

















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Please Cite: Peterson, T.A., Adadey, A., Santana-Cruz ,I., Sun, Y., Winder A, Kann, M.G., (2010) DMDM: Domain Mapping of Disease Mutations. Bioinformatics 26 (19), 2458-2459.

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