NADP-dependent isopropanol dehydrogenase

NameNADP-dependent isopropanol dehydrogenase
Synonyms
  • 1.1.1.80
Gene Nameadh
OrganismThermoanaerobacter brockii
Amino acid sequence
>lcl|BSEQ0011356|NADP-dependent isopropanol dehydrogenase
MKGFAMLSIGKVGWIEKEKPAPGPFDAIVRPLAVAPCTSDIHTVFEGAIGERHNMILGHE
AVGEVVEVGSEVKDFKPGDRVVVPAITPDWRTSEVQRGYHQHSGGMLAGWKFSNVKDGVF
GEFFHVNDADMNLAHLPKEIPLEAAVMIPDMMTTGFHGAELADIELGATVAVLGIGPVGL
MAVAGAKLRGAGRIIAVGSRPVCVDAAKYYGATDIVNYKDGPIESQIMNLTEGKGVDAAI
IAGGNADIMATAVKIVKPGGTIANVNYFGEGEVLPVPRLEWGCGMAHKTIKGGLCPGGRL
RMERLIDLVFYKRVDPSKLVTHVFRGFDNIEKAFMLMKDKPKDLIKPVVILA
Number of residues352
Molecular Weight37646.685
Theoretical pI6.86
GO Classification
Functions
  • zinc ion binding
  • isopropanol dehydrogenase (NADP+) activity
General FunctionZinc ion binding
Specific FunctionAlcohol 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.
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein ID1771791
UniProtKB IDP14941
UniProtKB Entry NameADH_THEBR
Cellular LocationNot Available
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 IDX64841
GeneCard IDNot Available
GenAtlas IDNot Available
HGNC IDNot Available
Chromosome LocationNot Available
LocusNot Available
References
  1. 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
  2. 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
  3. 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