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PRISE-like Rossmann-fold domain
This NAD(P)-binding Rossmann-fold-like domain is found in a number of enzymes with oxidoreductase activity. Amongst them are the PRISEs (Progesterone 5beta-reductase and/or iridoid synthase-like 1,4-enone reductases) that are involved in cardenolide and iridoid biosynthesis. This domain is also found in the short chain dehydrogenase ausT, involved in the terpenoid biosynthesis pathway. (from Pfam)
NAD-dependent epimerase/dehydratase family protein
This family of proteins utilise NAD as a cofactor. The proteins in this family use nucleotide-sugar substrates for a variety of chemical reactions. [1]. 9174344. Structural analysis of UDP-sugar binding to UDP-galactose 4-epimerase from Escherichia coli. Thoden JB, Hegeman AD, Wesenberg G, Chapeau MC, Frey PA, Holden HM;. Biochemistry 1997;36:6294-6304. (from Pfam)
SDR family oxidoreductase
atypical-extended SDR (short-chain dehydrogenase/reductase) family NAD(P)-dependent oxidoreductase shares the structure of an extended SDR, but has a different glycine-rich nucleotide binding motif (GXXGXXG) and lacks the YXXXK active site motif of classical and extended SDRs, similar to Arabidopsis thaliana 3-oxo-Delta(4,5)-steroid 5-beta-reductase that catalyzes the stereospecific conversion of progesterone to 5-beta-pregnane-3,20-dione
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