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Showing Protein Alcohol dehydrogenase class-3 (HMDBP00780)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 37 metabolites
Identification
HMDB Protein ID HMDBP00780
Secondary Accession Numbers
  • 6060
  • HMDBP03827
Name Alcohol dehydrogenase class-3
Synonyms
  1. Alcohol dehydrogenase 5
  2. Alcohol dehydrogenase class chi chain
  3. Alcohol dehydrogenase class-III
  4. FALDH
  5. FDH
  6. GSH-FDH
  7. Glutathione-dependent formaldehyde dehydrogenase
  8. S-(hydroxymethyl)glutathione dehydrogenase
Gene Name ADH5
Protein Type Unknown
Biological Properties
General Function Involved in zinc ion binding
Specific Function Class-III ADH is remarkably ineffective in oxidizing ethanol, but it readily catalyzes the oxidation of long-chain primary alcohols and the oxidation of S-(hydroxymethyl) glutathione.
Pathways
  • Chemical carcinogenesis - DNA adducts
  • Drug metabolism - cytochrome P450
  • fatty acid metabolism
  • Glycolysis / Gluconeogenesis
  • Metabolism of xenobiotics by cytochrome P450
  • Retinol metabolism
  • Tyrosine metabolism
Reactions
An alcohol + NAD → an aldehyde or ketone + NADH details
S-Hydroxymethylglutathione + NAD(P)(+) → S-Formylglutathione + NAD(P)H details
Primary alcohol + NAD → Aldehyde + NADH + Hydrogen Ion details
Ethanol + NAD → Acetaldehyde + NADH + Hydrogen Ion details
Vitamin A + NAD → Retinal + NADH + Hydrogen Ion details
3,4-Dihydroxyphenylglycol + NAD → 3,4-Dihydroxymandelaldehyde + NADH + Hydrogen Ion details
trans-3-Chloro-2-propene-1-ol + NAD → trans-3-Chloroallyl aldehyde + NADH + Hydrogen Ion details
cis-3-Chloro-2-propene-1-ol + NAD → cis-3-Chloroallyl aldehyde + NADH + Hydrogen Ion details
1-Hydroxymethylnaphthalene + NAD → 1-Naphthaldehyde + NADH + Hydrogen Ion details
(2-Naphthyl)methanol + NAD → 2-Naphthaldehyde + NADH + Hydrogen Ion details
S-Hydroxymethylglutathione + NAD → S-Formylglutathione + NADH + Hydrogen Ion details
Chloral hydrate + NADH + Hydrogen Ion → 2,2,2-Trichloroethanol + NAD + Water details
Aldophosphamide + NADH + Hydrogen Ion → Alcophosphamide + NAD details
2-Phenyl-1,3-propanediol monocarbamate + NAD → 3-Carbamoyl-2-phenylpropionaldehyde + NADH + Hydrogen Ion details
4-Hydroxy-5-phenyltetrahydro-1,3-oxazin-2-one + NAD → 5-Phenyl-1,3-oxazinane-2,4-dione + NADH + Hydrogen Ion details
GO Classification
Biological Process
ethanol catabolic process
retinoid metabolic process
formaldehyde catabolic process
peptidyl-cysteine S-nitrosylation
positive regulation of blood pressure
respiratory system process
response to lipopolysaccharide
response to nitrosative stress
response to redox state
ethanol oxidation
aging
Cellular Component
mitochondrion
nucleus
Function
ion binding
cation binding
metal ion binding
binding
catalytic activity
transition metal ion binding
zinc ion binding
oxidoreductase activity, acting on the ch-oh group of donors, nad or nadp as acceptor
oxidoreductase activity, acting on ch-oh group of donors
oxidoreductase activity
s-(hydroxymethyl)glutathione dehydrogenase activity
Molecular Function
electron carrier activity
alcohol dehydrogenase (NAD) activity
metal ion binding
formaldehyde dehydrogenase activity
S-(hydroxymethyl)glutathione dehydrogenase activity
fatty acid binding
zinc ion binding
nucleotide binding
Process
metabolic process
small molecule metabolic process
alcohol metabolic process
oxidation reduction
monohydric alcohol metabolic process
ethanol metabolic process
ethanol oxidation
Cellular Location
  1. Cytoplasm
Gene Properties
Chromosome Location 4
Locus 4q23
SNPs ADH5
Gene Sequence 
>1125 bp
ATGGCGAACGAGGTTATCAAGTGCAAGGCTGCAGTTGCTTGGGAGGCTGGAAAGCCTCTC
TCCATAGAGGAGATAGAGGTGGCACCCCCAAAGGCTCATGAAGTTCGAATCAAGATCATT
GCCACTGCGGTTTGCCACACCGATGCCTATACCCTGAGTGGAGCTGATCCTGAGGGTTGT
TTTCCAGTGATCTTGGGACATGAAGGTGCTGGAATTGTGGAAAGTGTTGGTGAGGGAGTT
ACTAAGCTGAAGGCGGGTGACACTGTCATCCCACTTTACATCCCACAGTGTGGAGAATGC
AAATTTTGTCTAAATCCTAAAACTAACCTTTGCCAGAAGATAAGAGTCACTCAAGGGAAA
GGATTAATGCCAGATGGTACCAGCAGATTTACTTGCAAAGGAAAGACAATTTTGCATTAC
ATGGGAACCAGCACATTTTCTGAATACACAGTTGTGGCTGATATCTCTGTTGCTAAAATA
GATCCTTTAGCACCTTTGGATAAAGTCTGCCTTCTAGGTTGTGGCATTTCAACCGGTTAT
GGTGCTGCTGTGAACACTGCCAAGTTGGAGCCTGGCTCTGTTTGTGCCGTCTTTGGTCTG
GGAGGAGTCGGATTGGCAGTTATCATGGGCTGTAAAGTGGCTGGTGCTTCCCGGATCATT
GGTGTGGACATCAATAAAGATAAATTTGCAAGGGCCAAAGAGTTTGGAGCCACTGAATGT
ATTAACCCTCAGGATTTTAGTAAACCCATCCAGGAAGTGCTCATTGAGATGACCGATGGA
GGAGTGGACTATTCCTTTGAATGTATTGGTAATGTGAAGGTCATGAGAGCAGCACTTGAG
GCATGTCACAAGGGCTGGGGCGTCAGCGTCGTGGTTGGAGTAGCTGCTTCAGGTGAAGAA
ATTGCCACTCGTCCATTCCAGCTGGTAACAGGTCGCACATGGAAAGGCACTGCCTTTGGA
GGATGGAAGAGTGTAGAAAGTGTCCCAAAGTTGGTGTCTGAATATATGTCCAAAAAGATA
AAAGTTGATGAATTTGTGACTCACAATCTGTCTTTTGATGAAATCAACAAAGCCTTTGAA
CTGATGCATTCTGGAAAGAGCATTCGAACTGTTGTAAAGATTTAA
Protein Properties
Number of Residues 374
Molecular Weight 39723.945
Theoretical pI 7.488
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence 
>Alcohol dehydrogenase class-3
MANEVIKCKAAVAWEAGKPLSIEEIEVAPPKAHEVRIKIIATAVCHTDAYTLSGADPEGC
FPVILGHEGAGIVESVGEGVTKLKAGDTVIPLYIPQCGECKFCLNPKTNLCQKIRVTQGK
GLMPDGTSRFTCKGKTILHYMGTSTFSEYTVVADISVAKIDPLAPLDKVCLLGCGISTGY
GAAVNTAKLEPGSVCAVFGLGGVGLAVIMGCKVAGASRIIGVDINKDKFARAKEFGATEC
INPQDFSKPIQEVLIEMTDGGVDYSFECIGNVKVMRAALEACHKGWGVSVVVGVAASGEE
IATRPFQLVTGRTWKGTAFGGWKSVESVPKLVSEYMSKKIKVDEFVTHNLSFDEINKAFE
LMHSGKSIRTVVKI
GenBank ID Protein 178134
UniProtKB/Swiss-Prot ID P11766
UniProtKB/Swiss-Prot Entry Name ADHX_HUMAN
PDB IDs
GenBank Gene ID M30471
GeneCard ID ADH5
GenAtlas ID ADH5
HGNC ID HGNC:253
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. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  4. Sharma CP, Fox EA, Holmquist B, Jornvall H, Vallee BL: cDNA sequence of human class III alcohol dehydrogenase. Biochem Biophys Res Commun. 1989 Oct 31;164(2):631-7. [PubMed:2818582 ]
  5. Giri PR, Krug JF, Kozak C, Moretti T, O'Brien SJ, Seuanez HN, Goldman D: Cloning and comparative mapping of a human class III (chi) alcohol dehydrogenase cDNA. Biochem Biophys Res Commun. 1989 Oct 16;164(1):453-60. [PubMed:2679557 ]
  6. Hur MW, Edenberg HJ: Cloning and characterization of the ADH5 gene encoding human alcohol dehydrogenase 5, formaldehyde dehydrogenase. Gene. 1992 Nov 16;121(2):305-11. [PubMed:1446828 ]
  7. Kaiser R, Holmquist B, Hempel J, Vallee BL, Jornvall H: Class III human liver alcohol dehydrogenase: a novel structural type equidistantly related to the class I and class II enzymes. Biochemistry. 1988 Feb 23;27(4):1132-40. [PubMed:3365377 ]
  8. Holmquist B, Moulis JM, Engeland K, Vallee BL: Role of arginine 115 in fatty acid activation and formaldehyde dehydrogenase activity of human class III alcohol dehydrogenase. Biochemistry. 1993 May 18;32(19):5139-44. [PubMed:8494891 ]
  9. Engeland K, Hoog JO, Holmquist B, Estonius M, Jornvall H, Vallee BL: Mutation of Arg-115 of human class III alcohol dehydrogenase: a binding site required for formaldehyde dehydrogenase activity and fatty acid activation. Proc Natl Acad Sci U S A. 1993 Mar 15;90(6):2491-4. [PubMed:8460164 ]
  10. Yang ZN, Bosron WF, Hurley TD: Structure of human chi chi alcohol dehydrogenase: a glutathione-dependent formaldehyde dehydrogenase. J Mol Biol. 1997 Jan 24;265(3):330-43. [PubMed:9018047 ]