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Identification
HMDB Protein ID HMDBP00786
Secondary Accession Numbers
  • 6066
  • HMDBP03825
Name Alcohol dehydrogenase 1C
Synonyms
  1. Alcohol dehydrogenase subunit gamma
Gene Name ADH1C
Protein Type Unknown
Biological Properties
General Function Involved in zinc ion binding
Specific Function Not Available
Pathways
  • Chemical carcinogenesis
  • 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
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
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
xenobiotic metabolic process
ethanol oxidation
Cellular Component
cytosol
Function
ion binding
cation binding
metal ion binding
binding
catalytic activity
transition metal ion binding
zinc ion binding
oxidoreductase activity
Molecular Function
alcohol dehydrogenase (NAD) activity
metal ion binding
zinc ion binding
nucleotide binding
Process
metabolic process
oxidation reduction
Cellular Location
  1. Cytoplasm
Gene Properties
Chromosome Location 4
Locus 4q23
SNPs ADH1C
Gene Sequence
>1128 bp
ATGAGCACAGCAGGAAAAGTAATCAAATGCAAAGCAGCTGTGCTATGGGAGTTAAAGAAA
CCCTTTTCCATTGAGGAGGTAGAGGTTGCACCTCCTAAGGCTCATGAAGTTCGCATTAAG
ATGGTGGCTGCAGGAATCTGTCGTTCAGATGAGCATGTGGTTAGTGGCAACCTGGTGACC
CCCCTTCCTGTGATTTTAGGCCATGAGGCAGCCGGCATCGTGGAAAGTGTTGGAGAAGGG
GTGACTACAGTCAAACCAGGTGATAAAGTCATCCCGCTCTTTACTCCTCAGTGTGGAAAA
TGCAGAATTTGCAAAAACCCAGAAAGCAACTACTGCTTGAAAAATGATCTAGGCAATCCT
CGGGGGACCCTGCAGGATGGCACCAGGAGGTTCACCTGCAGCGGGAAGCCCATCCACCAC
TTCGTCGGCGTCAGCACCTTCTCCCAGTACACAGTGGTGGATGAGAATGCAGTAGCCAAA
ATTGATGCAGCCTCGCCCCTGGAGAAAGTCTGCCTCATTGGCTGTGGATTTTCGACTGGT
TATGGGTCTGCAGTCAAAGTTGCCAAGGTCACCCCAGGGTCTACCTGTGCTGTGTTTGGC
CTGGGAGGGGTCGGCCTATCTGTTGTTATGGGCTGTAAAGCAGCTGGAGCAGCCAGAATC
ATTGCTGTGGACATCAACAAGGACAAATTTGCAAAGGCTAAAGAGTTGGGTGCCACTGAA
TGCATCAACCCTCAAGACTACAAGAAACCCATTCAGGAAGTGCTAAAGGAAATGACTGAT
GGAGGTGTGGATTTTTCGTTTGAAGTCATCGGTCAGCTTGACACCATGATGGCTTCCCTG
TTATGTTGTCATGAGGCATGTGGCACAAGTGTCATTGTAGGGGTACCTCCTGATTCCCAG
AACCTCTCAATAAACCCTATGCTGCTACTGACTGGACGCACGTGGAAAGGAGCTATTTTT
GGAGGCTTTAAGAGTAAAGAATCTGTCCCCAAACTTGTGGCTGACTTTATGGCTAAGAAG
TTTTCACTGGATGCATTAATAACAAATGTTTTACCTTTTGAAAAAATAAATGAAGGATTT
GACCTGCTTCGCTCTGGAAAGAGTATCCGTACCGTCCTGACGTTTTGA
Protein Properties
Number of Residues 375
Molecular Weight 39867.27
Theoretical pI 8.291
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Alcohol dehydrogenase 1C
MSTAGKVIKCKAAVLWELKKPFSIEEVEVAPPKAHEVRIKMVAAGICRSDEHVVSGNLVT
PLPVILGHEAAGIVESVGEGVTTVKPGDKVIPLFTPQCGKCRICKNPESNYCLKNDLGNP
RGTLQDGTRRFTCSGKPIHHFVGVSTFSQYTVVDENAVAKIDAASPLEKVCLIGCGFSTG
YGSAVKVAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIAVDINKDKFAKAKELGATE
CINPQDYKKPIQEVLKEMTDGGVDFSFEVIGRLDTMMASLLCCHEACGTSVIVGVPPDSQ
NLSINPMLLLTGRTWKGAIFGGFKSKESVPKLVADFMAKKFSLDALITNILPFEKINEGF
DLLRSGKSIRTVLTF
GenBank ID Protein 28404
UniProtKB/Swiss-Prot ID P00326
UniProtKB/Swiss-Prot Entry Name ADH1G_HUMAN
PDB IDs
GenBank Gene ID X04299
GeneCard ID ADH1C
GenAtlas ID ADH1C
HGNC ID HGNC:251
References
General References
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  3. Ikuta T, Szeto S, Yoshida A: Three human alcohol dehydrogenase subunits: cDNA structure and molecular and evolutionary divergence. Proc Natl Acad Sci U S A. 1986 Feb;83(3):634-8. [PubMed:2935875 ]
  4. Niederhut MS, Gibbons BJ, Perez-Miller S, Hurley TD: Three-dimensional structures of the three human class I alcohol dehydrogenases. Protein Sci. 2001 Apr;10(4):697-706. [PubMed:11274460 ]
  5. Gibbons BJ, Hurley TD: Structure of three class I human alcohol dehydrogenases complexed with isoenzyme specific formamide inhibitors. Biochemistry. 2004 Oct 5;43(39):12555-62. [PubMed:15449945 ]
  6. Hoog JO, Heden LO, Larsson K, Jornvall H, von Bahr-Lindstrom H: The gamma 1 and gamma 2 subunits of human liver alcohol dehydrogenase. cDNA structures, two amino acid replacements, and compatibility with changes in the enzymatic properties. Eur J Biochem. 1986 Sep 1;159(2):215-8. [PubMed:3758060 ]
  7. Yokoyama S, Matsuo Y, Rajasekharan S, Yokoyama R: Molecular structure of the human alcohol dehydrogenase 3 gene. Jpn J Genet. 1992 Apr;67(2):167-71. [PubMed:1524834 ]
  8. Buhler R, Hempel J, Kaiser R, de Zalenski C, von Wartburg JP, Jornvall H: Human liver alcohol dehydrogenase. 2. The primary structure of the gamma 1 protein chain. Eur J Biochem. 1984 Dec 17;145(3):447-53. [PubMed:6391921 ]