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  Domain Name: ALDH_PADH_NahF
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like. NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.
No pairwise interactions are available for this conserved domain.

Total Mutations Found: 62
Total Disease Mutations Found: 29
This domain occurred 18 times on human genes (32 proteins).



  ALCOHOL DEPENDENCE, PROTECTION AGAINST, INCLUDED;;
  ALCOHOL SENSITIVITY, ACUTE
  EPILEPSY, PYRIDOXINE-DEPENDENT
  HANGOVER, SUSCEPTIBILITY TO, INCLUDED;;|
  HYPERPROLINEMIA, TYPE II
  METHYLMALONATE SEMIALDEHYDE DEHYDROGENASE DEFICIENCY
  MICROPHTHALMIA, ISOLATED 8
  SJOGREN-LARSSON SYNDROME
  SUCCINIC SEMIALDEHYDE DEHYDROGENASE DEFICIENCY


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Range on the Protein:  

   Protein ID            Protein Position

Domain Position:  


Feature Name:Total Found:
catalytic residues
NAD(P) binding site




















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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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