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  Domain Name: NOX_Duox_like_FAD_NA
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as superoxide and hydrogen peroxide. ROS were originally identified as bactericidal agents in phagocytes, but are now also implicated in cell signaling and metabolism. NOX has a 6-alpha helix heme-binding transmembrane domain fused to a flavoprotein with the nucleotide binding domain located in the cytoplasm. Duox enzymes link a peroxidase domain to the NOX domain via a single transmembrane and EF-hand Ca2+ binding sites. The flavoprotein module has a ferredoxin like FAD/NADPH binding domain. In classical phagocytic NOX2, electron transfer occurs from NADPH to FAD to the heme of cytb to oxygen leading to superoxide formation.
No pairwise interactions are available for this conserved domain.

Total Mutations Found: 25
Total Disease Mutations Found: 14
This domain occurred 11 times on human genes (19 proteins).



  GRANULOMATOUS DISEASE, CHRONIC, X-LINKED
  GRANULOMATOUS DISEASE, CHRONIC, X-LINKED, VARIANT
  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
FAD binding motif
beta-alpha-beta stucture
NAD pyrophosphate binding
NADP ribose binding motif




























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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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