NADP-dependent isopropanol dehydrogenase

Name	NADP-dependent isopropanol dehydrogenase
Synonyms	1.1.1.80
Gene Name	adh
Organism	Thermoanaerobacter brockii
Amino acid sequence	>lcl\|BSEQ0011356\|NADP-dependent isopropanol dehydrogenase MKGFAMLSIGKVGWIEKEKPAPGPFDAIVRPLAVAPCTSDIHTVFEGAIGERHNMILGHE AVGEVVEVGSEVKDFKPGDRVVVPAITPDWRTSEVQRGYHQHSGGMLAGWKFSNVKDGVF GEFFHVNDADMNLAHLPKEIPLEAAVMIPDMMTTGFHGAELADIELGATVAVLGIGPVGL MAVAGAKLRGAGRIIAVGSRPVCVDAAKYYGATDIVNYKDGPIESQIMNLTEGKGVDAAI IAGGNADIMATAVKIVKPGGTIANVNYFGEGEVLPVPRLEWGCGMAHKTIKGGLCPGGRL RMERLIDLVFYKRVDPSKLVTHVFRGFDNIEKAFMLMKDKPKDLIKPVVILA
Number of residues	None
Molecular Weight	37646.685
Theoretical pI	6.86
GO Classification	Functions zinc ion binding isopropanol dehydrogenase (NADP+) activity Processes Components
General Function	Zinc ion binding
Specific Function	Alcohol dehydrogenase with a preference for medium chain secondary alcohols, such as 2-butanol and isopropanol. Has very low activity with primary alcohols, such as ethanol. Under physiological conditions, the enzyme reduces aldehydes and 2-ketones to produce secondary alcohols. Is also active with acetaldehyde and propionaldehyde.
Transmembrane Regions
GenBank Protein ID
UniProtKB ID	P14941
UniProtKB Entry Name
Cellular Location	None
Gene sequence	>lcl\|BSEQ0003747\|1059 bp ATGAAAGGTTTTGCAATGCTCAGTATCGGTAAAGTTGGCTGGATTGAGAAGGAAAAGCCT GCTCCTGGCCCATTTGATGCTATTGTAAGACCTCTAGCTGTGGCCCCTTGCACTTCGGAC ATTCATACCGTTTTTGAAGGCGCCATTGGCGAAAGACATAACATGATACTCGGTCACGAA GCTGTAGGTGAAGTAGTTGAAGTAGGTAGTGAGGTAAAAGATTTTAAACCTGGTGATCGC GTTGTTGTGCCAGCTATTACCCCTGATTGGCGGACCTCTGAAGTACAAAGAGGATATCAC CAGCACTCCGGTGGAATGCTGGCAGGCTGGAAATTTTCGAATGTAAAAGATGGTGTTTTT GGTGAATTTTTTCATGTGAATGATGCTGATATGAATTTAGCACATCTGCCTAAAGAAATT CCATTGGAAGCTGCAGTTATGATTCCCGATATGATGACCACTGGTTTTCACGGAGCTGAA CTGGCAGATATAGAATTAGGTGCGACGGTAGCAGTTTTGGGTATTGGCCCAGTAGGTCTT ATGGCAGTCGCTGGTGCCAAATTGCGTGGAGCCGGAAGAATTATTGCCGTAGGCAGTAGA CCAGTTTGTGTAGATGCTGCAAAATACTATGGAGCTACTGATATTGTAAACTATAAAGAT GGTCCTATCGAAAGTCAGATTATGAATCTAACTGAAGGCAAAGGTGTCGATGCTGCCATC ATCGCTGGAGGAAATGCTGACATTATGGCTACAGCAGTTAAGATTGTTAAACCTGGTGGC ACCATCGCTAATGTAAATTATTTTGGCGAAGGAGAGGTTTTGCCTGTTCCTCGTCTTGAA TGGGGTTGCGGCATGGCTCATAAAACTATAAAAGGCGGGCTATGCCCCGGTGGACGTCTA AGAATGGAAAGACTGATTGACCTTGTTTTTTATAAGCGTGTCGATCCTTCTAAGCTCGTC ACTCACGTTTTCCGGGGATTTGACAATATTGAAAAAGCCTTTATGTTGATGAAAGACAAA CCAAAAGACCTAATCAAACCTGTTGTAATATTAGCATAA
GenBank Gene ID
GeneCard ID	None
GenAtlas ID
HGNC ID
Chromosome Location	None
Locus	None
References	Peretz M, Burstein Y: Amino acid sequence of alcohol dehydrogenase from the thermophilic bacterium Thermoanaerobium brockii. Biochemistry. 1989 Aug 8;28(16):6549-55. [2790012 ] Korkhin Y, Kalb(Gilboa) AJ, Peretz M, Bogin O, Burstein Y, Frolow F: NADP-dependent bacterial alcohol dehydrogenases: crystal structure, cofactor-binding and cofactor specificity of the ADHs of Clostridium beijerinckii and Thermoanaerobacter brockii. J Mol Biol. 1998 May 22;278(5):967-81. [9836873 ] Goihberg E, Peretz M, Tel-Or S, Dym O, Shimon L, Frolow F, Burstein Y: Biochemical and structural properties of chimeras constructed by exchange of cofactor-binding domains in alcohol dehydrogenases from thermophilic and mesophilic microorganisms. Biochemistry. 2010 Mar 9;49(9):1943-53. doi: 10.1021/bi901730x. [20102159 ]

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