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Identification
HMDB Protein ID HMDBP00291
Secondary Accession Numbers
  • 5526
  • HMDBP03798
Name 4-trimethylaminobutyraldehyde dehydrogenase
Synonyms
  1. Aldehyde dehydrogenase E3 isozyme
  2. Aldehyde dehydrogenase family 9 member A1
  3. Gamma-aminobutyraldehyde dehydrogenase
  4. R-aminobutyraldehyde dehydrogenase
  5. TMABADH
Gene Name ALDH9A1
Protein Type Unknown
Biological Properties
General Function Involved in oxidoreductase activity
Specific Function Converts gamma-trimethylaminobutyraldehyde into gamma-butyrobetaine. Catalyzes the irreversible oxidation of a broad range of aldehydes to the corresponding acids in an NAD-dependent reaction.
Pathways
  • Arginine and proline metabolism
  • Ascorbate and aldarate metabolism
  • beta-Alanine metabolism
  • carnitine biosynthesis
  • Carnitine Synthesis
  • fatty acid metabolism
  • Glycerolipid metabolism
  • Glycolysis / Gluconeogenesis
  • Histidine metabolism
  • Lysine degradation
  • Propanoate metabolism
  • Pyruvate metabolism
  • Tryptophan metabolism
  • Valine, leucine and isoleucine degradation
Reactions
4-Trimethylammoniobutanal + NAD + Water → 4-Trimethylammoniobutanoic acid + NADH details
An aldehyde + NAD + Water → a carboxylate + NADH details
4-Aminobutyraldehyde + NAD + Water → gamma-Aminobutyric acid + NADH details
Aldehyde + NAD + Water → Fatty acid + NADH + Hydrogen Ion details
Acetaldehyde + NAD + Water → Acetic acid + NADH + Hydrogen Ion details
3-Aminopropionaldehyde + NAD + Water → beta-Alanine + NADH + Hydrogen Ion details
Glyceraldehyde + NAD + Water → Glyceric acid + NADH + Hydrogen Ion details
4-Aminobutyraldehyde + NADP + Water → gamma-Aminobutyric acid + NADPH + Hydrogen Ion details
4-Aminobutyraldehyde + NAD + Water → gamma-Aminobutyric acid + NADH + Hydrogen Ion details
Indoleacetaldehyde + NAD + Water → Indoleacetic acid + NADH + Hydrogen Ion details
2-Propyn-1-al + NAD + Water → Propynoic acid + NADH + Hydrogen Ion details
D-Glucurono-6,3-lactone + NAD + Water → Glucaric acid + NADH + Hydrogen Ion details
4-Trimethylammoniobutanal + NAD + Water → 4-Trimethylammoniobutanoic acid + NADH + Hydrogen Ion details
(S)-Methylmalonic acid semialdehyde + NAD + Water → Methylmalonic acid + NADH + Hydrogen Ion details
Imidazole-4-acetaldehyde + NAD + Water → Imidazoleacetic acid + NADH + Hydrogen Ion details
3a,7a-Dihydroxy-5b-cholestan-26-al + NAD + Water → 17alpha,20alpha-Dihydroxypregn-4-en-3-one + NADH + Hydrogen Ion details
5-Hydroxyindoleacetaldehyde + NAD + Water → 5-Hydroxyindoleacetic acid + Hydrogen Ion + NADH details
N4-Acetylaminobutanal + NAD + Water → 4-Acetamidobutanoic acid + NADH + Hydrogen Ion details
GO Classification
Biological Process
hormone metabolic process
cellular aldehyde metabolic process
neurotransmitter biosynthetic process
liver development
kidney development
carnitine biosynthetic process
Cellular Component
cytosol
mitochondrion
plasma membrane
Function
catalytic activity
oxidoreductase activity
Molecular Function
1-pyrroline dehydrogenase activity
4-trimethylammoniobutyraldehyde dehydrogenase activity
amine binding
aminobutyraldehyde dehydrogenase activity
NAD binding
3-chloroallyl aldehyde dehydrogenase activity
Process
metabolic process
oxidation reduction
Cellular Location
  1. Cytoplasm
Gene Properties
Chromosome Location 1
Locus 1q23.1
SNPs ALDH9A1
Gene Sequence
>1485 bp
ATGAGCACTGGCACCTTCGTCGTGTCGCAGCCGCTCAATTACCGCGGCGGGGCCCGCGTG
GAGCCGGCGGACGCCTCCGGTACCGAGAAAGCTTTCGAGCCAGCAACCGGCCGAGTGATA
GCTACTTTCACATGTTCAGGAGAAAAGGAAGTAAATTTGGCTGTTCAAAATGCAAAGGCT
GCTTTTAAAATATGGAGTCAAAAATCTGGCATGGAGCGTTGCCGAATCCTTTTGGAGGCT
GCCAGGATAATAAGGGAACGGGAGGATGAAATTGCTACTATGGAGTGCATCAACAATGGC
AAGTCCATCTTTGAGGCCCGCTTGGACATTGACATTTCCTGGCAGTGCCTGGAGTATTAT
GCGGGCTTGGCTGCATCCATGGCTGGTGAACACATCCAGCTCCCAGGTGGATCGTTTGGT
TATACCAGAAGAGAACCACTTGGGGTATGTGTGGGAATAGGAGCATGGAACTACCCCTTT
CAGATTGCCTCTTGGAAGTCGGCTCCAGCATTAGCCTGTGGTAATGCCATGGTCTTTAAA
CCTTCTCCCTTTACACCTGTTTCTGCATTGCTACTGGCTGAAATCTACAGTGAGGCTGGT
GTACCTCCTGGGCTCTTCAATGTGGTGCAGGGAGGGGCTGCCACAGGCCAGTTTCTGTGT
CAGCATCCCGATGTGGCCAAAGTCTCCTTCACTGGAAGTGTGCCCACTGGCATGAAGATC
ATGGAGATGTCAGCTAAAGGAATCAAACCTGTTACCTTGGAACTTGGAGGCAAATCTCCA
CTCATCATCTTCTCAGACTGTGATATGAACAATGCTGTAAAGGGGGCGCTGATGGCCAAC
TTCCTCACACAAGGCCAGGTTTGCTGTAATGGCACAAGAGTATTTGTGCAGAAAGAAATT
CTTGATAAATTTACAGAGGAAGTGGTGAAACAGACCCAAAGGATTAAAATTGGAGATCCC
CTTCTGGAAGATACAAGGATGGGTCCACTCATCAACCGACCACACCTGGAGCGAGTCCTT
GGGTTTGTCAAAGTGGCAAAGGAGCAGGGTGCTAAAGTGTTATGTGGTGGAGATATATAT
GTACCTGAAGATCCCAAATTAAAGGATGGATATTACATGAGACCTTGTGTATTAACTAAT
TGCAGAGACGACATGACCTGTGTGAAGGAAGAGATCTTTGGGCCTGTTATGTCCATTTTA
TCATTTGACACTGAAGCTGAGGTTCTAGAAAGAGCCAATGATACCACTTTTGGACTAGCA
GCTGGCGTCTTTACCAGGGACATCCAACGGGCTCATAGAGTGGTAGCTGAGCTTCAGGCT
GGGACGTGCTTCATTAACAACTATAACGTCAGCCCAGTGGAGTTGCCCTTTGGTGGATAT
AAGAAGTCAGGATTTGGCAGAGAGAACGGCCGTGTGACAATCGAATATTATTCACAGCTG
AAGACTGTGTGTGTGGAGATGGGTGATGTGGAATCTGCTTTTTGA
Protein Properties
Number of Residues 494
Molecular Weight 56291.485
Theoretical pI 6.564
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>4-trimethylaminobutyraldehyde dehydrogenase
MSTGTFVVSQPLNYRGGARVEPADASGTEKAFEPATGRVIATFTCSGEKEVNLAVQNAKA
AFKIWSQKSGMERCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYY
AGLAASMAGEHIQLPGGSFGYTRREPLGVCVGIGAWNYPFQIASWKSAPALACGNAMVFK
PSPFTPVSALLLAEIYSEAGVPPGLFNVVQGGAATGQFLCQHPDVAKVSFTGSVPTGMKI
MEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEI
LDKFTEEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDIY
VPEDPKLKDGYYMRPCVLTNCRDDMTCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLA
AGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKSGFGRENGRVTIEYYSQL
KTVCVEMGDVESAF
GenBank ID Protein 7248636
UniProtKB/Swiss-Prot ID P49189
UniProtKB/Swiss-Prot Entry Name AL9A1_HUMAN
PDB IDs Not Available
GenBank Gene ID AF172093
GeneCard ID ALDH9A1
GenAtlas ID ALDH9A1
HGNC ID HGNC:412
References
General References
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  3. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  4. Lin SW, Chen JC, Hsu LC, Hsieh CL, Yoshida A: Human gamma-aminobutyraldehyde dehydrogenase (ALDH9): cDNA sequence, genomic organization, polymorphism, chromosomal localization, and tissue expression. Genomics. 1996 Jun 15;34(3):376-80. [PubMed:8786138 ]
  5. Vaz FM, Fouchier SW, Ofman R, Sommer M, Wanders RJ: Molecular and biochemical characterization of rat gamma-trimethylaminobutyraldehyde dehydrogenase and evidence for the involvement of human aldehyde dehydrogenase 9 in carnitine biosynthesis. J Biol Chem. 2000 Mar 10;275(10):7390-4. [PubMed:10702312 ]
  6. Kikonyogo A, Pietruszko R: Aldehyde dehydrogenase from adult human brain that dehydrogenates gamma-aminobutyraldehyde: purification, characterization, cloning and distribution. Biochem J. 1996 May 15;316 ( Pt 1):317-24. [PubMed:8645224 ]
  7. Kurys G, Shah PC, Kikonygo A, Reed D, Ambroziak W, Pietruszko R: Human aldehyde dehydrogenase. cDNA cloning and primary structure of the enzyme that catalyzes dehydrogenation of 4-aminobutyraldehyde. Eur J Biochem. 1993 Dec 1;218(2):311-20. [PubMed:8269919 ]
  8. Kurys G, Ambroziak W, Pietruszko R: Human aldehyde dehydrogenase. Purification and characterization of a third isozyme with low Km for gamma-aminobutyraldehyde. J Biol Chem. 1989 Mar 15;264(8):4715-21. [PubMed:2925663 ]