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  Domain Name: sulfite_reductase_li
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural similarity to ferredoxin reductase and sequence similarity to dihydroorotate dehydrogenases. Clostridium pasteurianum inducible dissimilatory type sulfite reductase is linked to ferredoxin and reduces NH2OH and SeO3 at a lesser rate than it's normal substate SO3(2-). Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+.
No pairwise interactions are available for this conserved domain.

Total Mutations Found: 13
Total Disease Mutations Found: 8
This domain occurred 6 times on human genes (8 proteins).



  METHEMOGLOBINEMIA, TYPE I
  METHEMOGLOBINEMIA, TYPE II


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Range on the Protein:  

   Protein ID            Protein Position

Domain Position:  


Feature Name:Total Found:
FAD binding pocket
NAD binding pocket
Iron coordination center
FAD binding motif
phosphate binding motif
beta-alpha-beta structure

















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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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