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  Domain Name: FNR_like
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation in many organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one- electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and 2 electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).
No pairwise interactions are available for this conserved domain.

Total Mutations Found: 60
Total Disease Mutations Found: 25
This domain occurred 18 times on human genes (36 proteins).



  ANTLEY-BIXLER SYNDROME WITH GENITAL ANOMALIES AND DISORDERED STEROIDOGENESIS
  DISORDERED STEROIDOGENESIS DUE TO CYTOCHRO
  DISORDERED STEROIDOGENESIS DUE TO CYTOCHROME P450 OXIDOREDUCTASE DEFICIENCY
  GRANULOMATOUS DISEASE, CHRONIC, X-LINKED
  GRANULOMATOUS DISEASE, CHRONIC, X-LINKED, VARIANT
  HOMOCYSTINURIA-MEGALOBLASTIC ANEMIA, CBLE COMPLEMENTATION TYPE
  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
conserved FAD binding mot
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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