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alcohol dehydrogenase catalytic domain-containing protein
This is the catalytic domain of alcohol dehydrogenases. Many of them contain an inserted zinc binding domain. This domain has a GroES-like structure [1-2]. [1]. 8804825. Structural classification of proteins: new superfamilies. Murzin AG;. Curr Opin Struct Biol 1996;6:386-394. [2]. 10556240. Conserved structural features and sequence patterns in the GroES fold family. Taneja B, Mande SC;. Protein Eng 1999;12:815-818. (from Pfam)
zinc-binding dehydrogenase
MDR family oxidoreductase
MDR (medium chain dehydrogenase/reductase) family oxidoreductase similar to acrylyl-CoA reductase AcuI, which catalyzes the NADPH-dependent reduction of acrylyl-CoA to propanoyl-CoA
acryloyl-CoA reductase
This model represents a subfamily of PF00107 as defined by Pfam, a superfamily in which some members are zinc-binding medium-chain alcohol dehydrogenases while others are quinone oxidoreductases with no bound zinc. This subfamily includes proteins studied crystallographically for insight into function: YhdH from Escherichia coli and YhfP from Bacillus subtilis. Members bind NADPH or NAD, but not zinc.
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