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Identification
HMDB Protein ID HMDBP00292
Secondary Accession Numbers
  • 5527
  • HMDBP03821
Name Aldehyde dehydrogenase, dimeric NADP-preferring
Synonyms
  1. ALDHIII
  2. Aldehyde dehydrogenase 3
  3. Aldehyde dehydrogenase family 3 member A1
Gene Name ALDH3A1
Protein Type Unknown
Biological Properties
General Function Involved in oxidoreductase activity
Specific Function ALDHs play a major role in the detoxification of alcohol-derived acetaldehyde. They are involved in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation. This protein preferentially oxidizes aromatic aldehyde substrates. It may play a role in the oxidation of toxic aldehydes.
Pathways
  • Alkaptonuria
  • beta-Alanine metabolism
  • Chemical carcinogenesis
  • Cyclophosphamide Action Pathway
  • Cyclophosphamide Metabolism Pathway
  • D-glyceric acidura
  • Disulfiram Action Pathway
  • Dopamine beta-hydroxylase deficiency
  • Drug metabolism - cytochrome P450
  • Familial lipoprotein lipase deficiency
  • Felbamate Metabolism Pathway
  • Glycerol Kinase Deficiency
  • Glycerolipid Metabolism
  • Glycolysis / Gluconeogenesis
  • Hawkinsinuria
  • Histidine Metabolism
  • Histidine metabolism
  • Histidinemia
  • Ifosfamide Action Pathway
  • Ifosfamide Metabolism Pathway
  • Metabolism of xenobiotics by cytochrome P450
  • Monoamine oxidase-a deficiency (MAO-A)
  • Phenylalanine metabolism
  • Tyrosine Metabolism
  • Tyrosine metabolism
  • Tyrosinemia Type I
  • Tyrosinemia, transient, of the newborn
Reactions
An aldehyde + NAD(P)(+) + Water → a carboxylate + NAD(P)H details
Acetaldehyde + NADP + Water → Acetic acid + NADPH + Hydrogen Ion details
3-Aminopropionaldehyde + NAD + Water → beta-Alanine + NADH + Hydrogen Ion details
Phenylacetaldehyde + NAD + Water → Phenylacetic acid + NADH + Hydrogen Ion details
Phenylacetaldehyde + NADP + Water → Phenylacetic acid + NADPH + Hydrogen Ion details
4-Hydroxyphenylacetaldehyde + NAD + Water → p-Hydroxyphenylacetic acid + NADH + Hydrogen Ion details
4-Hydroxyphenylacetaldehyde + NADP + Water → p-Hydroxyphenylacetic acid + NADPH + Hydrogen Ion details
3,4-Dihydroxyphenylacetaldehyde + NAD + Water → 3,4-Dihydroxybenzeneacetic acid + NADH + Hydrogen Ion details
3,4-Dihydroxyphenylacetaldehyde + NADP + Water → 3,4-Dihydroxybenzeneacetic acid + NADPH + Hydrogen Ion details
3,4-Dihydroxymandelaldehyde + NAD + Water → 3,4-Dihydroxymandelic acid + NADH + Hydrogen Ion details
3,4-Dihydroxymandelaldehyde + NADP + Water → 3,4-Dihydroxymandelic acid + NADPH + Hydrogen Ion details
Homovanillin + NAD + Water → Homovanillic acid + NADH + Hydrogen Ion details
Homovanillin + NADP + Water → Homovanillic acid + NADPH + Hydrogen Ion details
3-Methoxy-4-hydroxyphenylglycolaldehyde + NAD + Water → Vanillylmandelic acid + NADH + Hydrogen Ion details
3-Methoxy-4-hydroxyphenylglycolaldehyde + NADP + Water → Vanillylmandelic acid + NADPH + Hydrogen Ion details
Methylimidazole acetaldehyde + NAD + Water → Methylimidazoleacetic acid + NADH + Hydrogen Ion details
Chloral hydrate + NAD → Trichloroacetic acid + NADH + Hydrogen Ion details
Aldophosphamide + NAD + Water → Carboxyphosphamide + NADH + Hydrogen Ion details
Aldophosphamide + NADP + Water → Carboxyphosphamide + NADPH + Hydrogen Ion details
3-Carbamoyl-2-phenylpropionaldehyde + NAD + Water → 3-Carbamoyl-2-phenylpropionic acid + NADH + Hydrogen Ion details
GO Classification
Biological Process
cellular aldehyde metabolic process
positive regulation of cell proliferation
response to drug
response to nutrient
response to glucocorticoid stimulus
aging
response to hypoxia
response to cAMP
Cellular Component
cytosol
endoplasmic reticulum
Function
catalytic activity
aldehyde dehydrogenase [nad(p)+] activity
oxidoreductase activity
oxidoreductase activity, acting on the aldehyde or oxo group of donors
oxidoreductase activity, acting on the aldehyde or oxo group of donors, nad or nadp as acceptor
Molecular Function
aldehyde dehydrogenase (NAD) activity
3-chloroallyl aldehyde dehydrogenase activity
aldehyde dehydrogenase [NAD(P)+] activity
alcohol dehydrogenase (NADP+) activity
Process
metabolic process
cellular aldehyde metabolic process
cellular metabolic process
oxidation reduction
Cellular Location
  1. Cytoplasm
Gene Properties
Chromosome Location 17
Locus 17p11.2
SNPs ALDH3A1
Gene Sequence
>1362 bp
ATGAGCAAGATCAGCGAGGCCGTGAAGCGCGCCCGCGCCGCCTTCAGCTCGGGCAGGACC
CGTCCGCTGCAGTTCCGGATCCAGCAGCTGGAGGCGCTGCAGCGCCTGATCCAGGAGCAG
GAGCAGGAGCTGGTGGGCGCGCTGGCCGCAGACCTGCACAAGAATGAATGGAACGCCTAC
TATGAGGAGGTGGTGTACGTCCTAGAGGAGATCGAGTACATGATCCAGAAGCTCCCTGAG
TGGGCCGCGGATGAGCCCGTGGAGAAGACGCCCCAGACTCAGCAGGACGAGCTCTACATC
CACTCGGAGCCACTGGGCGTGGTCCTCGTCATTGGCACCTGGAACTACCCCTTCAACCTC
ACCATCCAGCCCATGGTGGGCGCCATCGCTGCAGGGAACTCAGTGGTCCTCAAGCCCTCG
GAGCTGAGTGAGAACATGGCGAGCCTGCTGGCTACCATCATCCCCCAGTACCTGGACAAG
GATCTGTACCCAGTAATCAATGGGGGTGTCCCTGAGACCACGGAGCTGCTCAAGGAGAGG
TTCGACCATATCCTGTACACGGGCAGCACGGGGGTGGGGAAGATCATCATGACGGCTGCT
GCCAAGCACCTGACCCCTGTCACGCTGGAGCTGGGAGGGAAGAGTCCCTGCTACGTGGAC
AAGAACTGTGACCTGGACGTGGCCTGCCGACGCATCGCCTGGGGGAAATTCATGAACAGT
GGCCAGACCTGCGTGGCCCCTGACTACATCCTCTGTGACCCCTCGATCCAGAACCAAATT
GTGGAGAAGCTCAAGAAGTCACTGAAAGAGTTCTACGGGGAAGATGCTAAGAAATCCCGG
GACTATGGAAGAATCATTAGTGCCCGGCACTTCCAGAGGGTGATGGGCCTGATTGAGGGC
CAGAAGGTGGCTTATGGGGGCACCGGGGATGCCGCCACTCGCTACATAGCCCCCACCATC
CTCACGGACGTGGACCCCCAGTCCCCGGTGATGCAAGAGGAGATCTTCGGGCCTGTGCTG
CCCATCGTGTGCGTGCGCAGCCTGGAGGAGGCCATCCAGTTCATCAACCAGCGTGAGAAG
CCCCTGGCCCTCTACATGTTCTCCAGCAACGACAAGGTGATTAAGAAGATGATTGCAGAG
ACATCCAGTGGTGGGGTGGCGGCCAACGATGTCATCGTCCACATCACCTTGCACTCTCTG
CCCTTCGGGGGCGTGGGGAACAGCGGCATGGGATCCTACCATGGCAAGAAGAGCTTCGAG
ACTTTCTCTCACCGCCGCTCTTGCCTGGTGAGGCCTCTGATGAATGATGAAGGCCTGAAG
GTCAGATACCCCCCGAGCCCGGCCAAGATGACCCAGCACTGA
Protein Properties
Number of Residues 453
Molecular Weight 50394.57
Theoretical pI 6.544
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Aldehyde dehydrogenase, dimeric NADP-preferring
MSKISEAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAY
YEEVVYVLEEIEYMIQKLPEWAADEPVEKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNL
TIQPMVGAIAAGNAVVLKPSELSENMASLLATIIPQYLDKDLYPVINGGVPETTELLKER
FDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNS
GQTCVAPDYILCDPSIQNQIVEKLKKSLKEFYGEDAKKSRDYGRIISARHFQRVMGLIEG
QKVAYGGTGDAATRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREK
PLALYMFSSNDKVIKKMIAETSSGGVAANDVIVHITLHSLPFGGVGNSGMGSYHGKKSFE
TFSHRRSCLVRPLMNDEGLKVRYPPSPAKMTQH
GenBank ID Protein 22907049
UniProtKB/Swiss-Prot ID P30838
UniProtKB/Swiss-Prot Entry Name AL3A1_HUMAN
PDB IDs
GenBank Gene ID NM_000691.4
GeneCard ID ALDH3A1
GenAtlas ID ALDH3A1
HGNC ID HGNC:405
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. 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 ]
  3. Zody MC, Garber M, Adams DJ, Sharpe T, Harrow J, Lupski JR, Nicholson C, Searle SM, Wilming L, Young SK, Abouelleil A, Allen NR, Bi W, Bloom T, Borowsky ML, Bugalter BE, Butler J, Chang JL, Chen CK, Cook A, Corum B, Cuomo CA, de Jong PJ, DeCaprio D, Dewar K, FitzGerald M, Gilbert J, Gibson R, Gnerre S, Goldstein S, Grafham DV, Grocock R, Hafez N, Hagopian DS, Hart E, Norman CH, Humphray S, Jaffe DB, Jones M, Kamal M, Khodiyar VK, LaButti K, Laird G, Lehoczky J, Liu X, Lokyitsang T, Loveland J, Lui A, Macdonald P, Major JE, Matthews L, Mauceli E, McCarroll SA, Mihalev AH, Mudge J, Nguyen C, Nicol R, O'Leary SB, Osoegawa K, Schwartz DC, Shaw-Smith C, Stankiewicz P, Steward C, Swarbreck D, Venkataraman V, Whittaker CA, Yang X, Zimmer AR, Bradley A, Hubbard T, Birren BW, Rogers J, Lander ES, Nusbaum C: DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage. Nature. 2006 Apr 20;440(7087):1045-9. [PubMed:16625196 ]
  4. Hsu LC, Chang WC, Shibuya A, Yoshida A: Human stomach aldehyde dehydrogenase cDNA and genomic cloning, primary structure, and expression in Escherichia coli. J Biol Chem. 1992 Feb 15;267(5):3030-7. [PubMed:1737758 ]
  5. Hsu LC, Yoshida A: Human stomach aldehyde dehydrogenase, ALDH3. Adv Exp Med Biol. 1993;328:141-52. [PubMed:8493892 ]
  6. Yin SJ, Vagelopoulos N, Wang SL, Jornvall H: Structural features of stomach aldehyde dehydrogenase distinguish dimeric aldehyde dehydrogenase as a 'variable' enzyme. 'Variable' and 'constant' enzymes within the alcohol and aldehyde dehydrogenase families. FEBS Lett. 1991 May 20;283(1):85-8. [PubMed:2037078 ]
  7. Eckey R, Timmann R, Hempel J, Agarwal DP, Goedde HW: Biochemical, immunological, and molecular characterization of a "high Km" aldehyde dehydrogenase. Adv Exp Med Biol. 1991;284:43-52. [PubMed:1905102 ]
  8. Tsukamoto N, Chang C, Yoshida A: Mutations associated with Sjogren-Larsson syndrome. Ann Hum Genet. 1997 May;61(Pt 3):235-42. [PubMed:9250352 ]