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  Domain Name: ALDH_F9_TMBADH
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1. NAD+-dependent, 4-trimethylaminobutyraldehyde dehydrogenase (TMABADH, EC=1.2.1.47), also known as aldehyde dehydrogenase family 9 member A1 (ALDH9A1) in humans, is a cytosolic tetramer which catalyzes the oxidation of gamma-aminobutyraldehyde involved in 4-aminobutyric acid (GABA) biosynthesis and also oxidizes betaine aldehyde (gamma-trimethylaminobutyraldehyde) which is involved in carnitine biosynthesis.
No pairwise interactions are available for this conserved domain.

Total Mutations Found: 61
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
tetrameric interface
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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