Alcohol dehydrogenase E chain

NameAlcohol dehydrogenase E chain
Synonyms
  • 1.1.1.1
Gene NameNot Available
OrganismHorse
Amino acid sequence
>lcl|BSEQ0013600|Alcohol dehydrogenase E chain
MSTAGKVIKCKAAVLWEEKKPFSIEEVEVAPPKAHEVRIKMVATGICRSDDHVVSGTLVT
PLPVIAGHEAAGIVESIGEGVTTVRPGDKVIPLFTPQCGKCRVCKHPEGNFCLKNDLSMP
RGTMQDGTSRFTCRGKPIHHFLGTSTFSQYTVVDEISVAKIDAASPLEKVCLIGCGFSTG
YGSAVKVAKVTQGSTCAVFGLGGVGLSVIMGCKAAGAARIIGVDINKDKFAKAKEVGATE
CVNPQDYKKPIQEVLTEMSNGGVDFSFEVIGRLDTMVTALSCCQEAYGVSVIVGVPPDSQ
NLSMNPMLLLSGRTWKGAIFGGFKSKDSVPKLVADFMAKKFALDPLITHVLPFEKINEGF
DLLRSGESIRTILTF
Number of residues375
Molecular Weight39935.22
Theoretical pINot Available
GO Classification
Functions
  • zinc ion binding
  • alcohol dehydrogenase (NAD) activity
Components
  • cytoplasm
General FunctionZinc ion binding
Specific FunctionNot Available
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein IDNot Available
UniProtKB IDP00327
UniProtKB Entry NameADH1E_HORSE
Cellular LocationCytoplasm
Gene sequence
>lcl|BSEQ0013601|Alcohol dehydrogenase E chain
ATGAGCACAGCAGGAAAAGTAATAAAATGCAAAGCGGCTGTGCTGTGGGAGGAAAAGAAA
CCATTTTCCATCGAGGAGGTGGAGGTTGCACCCCCGAAGGCCCATGAAGTCCGTATAAAG
ATGGTGGCCACAGGAATTTGTCGCTCAGATGACCACGTGGTTAGTGGAACCCTTGTCACA
CCTCTTCCTGTGATCGCAGGCCATGAGGCAGCGGGCATTGTGGAGAGCATTGGAGAAGGC
GTCACTACAGTAAGACCAGGTGATAAAGTCATCCCACTCTTTACTCCCCAGTGTGGAAAA
TGCAGGGTTTGTAAGCACCCTGAAGGCAACTTCTGCTTGAAAAATGATCTGAGCATGCCT
CGGGGAACCATGCAGGATGGTACCAGCAGGTTCACCTGCAGAGGGAAGCCCATCCACCAC
TTCCTTGGCACCAGCACCTTCTCCCAGTACACCGTGGTGGACGAGATCTCAGTGGCCAAG
ATCGATGCGGCCTCACCGCTGGAGAAAGTCTGTCTCATTGGCTGTGGATTTTCTACTGGT
TATGGGTCTGCAGTCAAGGTTGCCAAGGTCACCCAGGGCTCCACCTGTGCCGTGTTTGGC
CTTGGAGGAGTGGGCCTGTCTGTTATCATGGGCTGTAAAGCAGCCGGAGCGGCCAGGATC
ATTGGGGTGGACATCAACAAAGACAAGTTTGCAAAGGCCAAAGAAGTGGGTGCCACTGAG
TGTGTCAACCCTCAGGACTACAAGAAACCCATCCAGGAGGTGCTGACAGAAATGAGCAAT
GGAGGTGTGGATTTTTCCTTTGAAGTCATTGGTCGGCTCGACACTATGGTGACTGCCTTG
TCATGCTGTCAAGAAGCATATGGTGTGAGCGTCATTGTGGGAGTACCTCCTGATTCCCAA
AATCTCTCTATGAATCCTATGTTGCTACTGAGTGGACGTACCTGGAAAGGAGCTATTTTT
GGCGGTTTTAAGAGTAAAGATTCTGTCCCCAAACTTGTGGCCGATTTTATGGCTAAAAAG
TTTGCACTGGATCCTTTAATCACCCATGTTTTACCTTTTGAAAAAATAAATGAAGGATTT
GACCTGCTTCGCTCTGGAGAGAGTATCCGTACCATCCTGACGTTTTGA
GenBank Gene IDNot Available
GeneCard IDNot Available
GenAtlas IDNot Available
HGNC IDNot Available
Chromosome LocationNot Available
LocusNot Available
References
  1. Park DH, Plapp BV: Isoenzymes of horse liver alcohol dehydrogenase active on ethanol and steroids. cDNA cloning, expression, and comparison of active sites. J Biol Chem. 1991 Jul 15;266(20):13296-302. 1712777
  2. Jornvall H: Horse liver alcohol dehydrogenase. On the primary structures of the isoenzymes. Eur J Biochem. 1970 Sep;16(1):41-9. 5466062
  3. Eklund H, Nordstrom B, Zeppezauer E, Soderlund G, Ohlsson I, Boiwe T, Soderberg BO, Tapia O, Branden CI, Akeson A: Three-dimensional structure of horse liver alcohol dehydrogenase at 2-4 A resolution. J Mol Biol. 1976 Mar 25;102(1):27-59. 178875
  4. Eklund H, Samama JP, Jones TA: Crystallographic investigations of nicotinamide adenine dinucleotide binding to horse liver alcohol dehydrogenase. Biochemistry. 1984 Dec 4;23(25):5982-96. 6098306
  5. Al-Karadaghi S, Cedergren-Zeppezauer ES, Hovmoller S: Refined crystal structure of liver alcohol dehydrogenase-NADH complex at 1.8 A resolution. Acta Crystallogr D Biol Crystallogr. 1994 Nov 1;50(Pt 6):793-807. 15299346