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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-dependent alcohol dehydrogenase family protein
zinc-dependent alcohol dehydrogenase family protein which may be a zinc-binding alcohol dehydrogenase and catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones, or may be a medium chain reductase/dehydrogenase
zinc-binding alcohol dehydrogenase family protein
Members of this model form a distinct subset of the larger family of oxidoreductases that includes zinc-binding alcohol dehydrogenases and NADPH:quinone reductases (PF00107). The gene neighborhood of members of this family is not conserved and it appears that no members are characterized. The sequence of the family includes 6 invariant cysteine residues and one invariant histidine. It appears that no member is characterized.
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