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zinc-binding dehydrogenase
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)
NAD(P)H-quinone oxidoreductase
NAD(P)H-quinone oxidoreductase catalyzes the NADPH-dependent reduction of quinones; similar to quinone oxidoreductase PIG3, a medium chain dehydrogenase/reductase family member which acts in the apoptotic pathway
putative NAD(P)H quinone oxidoreductase, PIG3 family
Members of this family are putative quinone oxidoreductases that belong to the broader superfamily (modeled by Pfam PF00107) of zinc-dependent alcohol (of medium chain length) dehydrogenases and quinone oxiooreductases. The alignment shows no motif of conserved Cys residues as are found in zinc-binding members of the superfamily, and members are likely to be quinone oxidoreductases instead. A member of this family in Homo sapiens, PIG3, is induced by p53 but is otherwise uncharacterized.
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