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  Domain Name: ALDH_F8_HMSADH
Human aldehyde dehydrogenase family 8 member A1-like. In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.
No pairwise interactions are available for this conserved domain.

Total Mutations Found: 62
Total Disease Mutations Found: 28
This domain occurred 18 times on human genes (32 proteins).



  EPILEPSY, PYRIDOXINE-DEPENDENT
  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:
NAD binding site
catalytic residues




















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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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