NADPH-dependent oxidoreductase which catalyzes the reduction of a variety of compounds bearing carbonyl groups including ketosteroids, alpha-dicarbonyl compounds, aldehydes, aromatic ketones and quinones. Reduces 3-ketosteroids and benzil into 3beta-hydroxysteroids and R-benzoin, respectively, in contrast to the stereoselectivity of non-primate DHRS4s which produce 3alpha-hydroxysteroids and S-benzoin. Diplays low activity toward all-trans-retinal and no activity toward 9-cis-retinal as compared to non-primate mammals. In the reverse reaction, catalyze the NAD-dependent oxidation of 3beta-hydroxysteroids and alcohol, but with much lower efficiency. Involved in the metabolism of 3beta-hydroxysteroids, isatin and xenobiotic carbonyl compounds. a secondary alcohol + NADP(+) = a ketone + H(+) + NADPH 3beta-hydroxy-5beta-pregnane-20-one + NADP(+) = 5beta-pregnan-3,20-dione + H(+) + NADPH 5beta-dihydrotestosterone + H(+) + NADPH = 5beta-androstane-3beta,17beta-diol + NADP(+) 5beta-androstane-3,17-dione + H(+) + NADPH = 3beta-hydroxy-5beta-androstane-17-one + NADP(+) H(+) + isatin + NADPH = 3-hydroxyindolin-2-one + NADP(+) lithocholate + NADP(+) = 3-oxo-5beta-cholan-24-oate + H(+) + NADPH 3-oxo-5beta-cholan-24-oate + H(+) + NADPH = isolithocholate + NADP(+) Homotetramer. The C-terminus peroxisomal targeting signal tripeptide is important for peroxisomal import. Once in the peroxisome, it is involved in intersubunit interactions. Three specific residues, Ser-176, Phe-179 and Thr-195 are conserved between primates whereas the respective residues are phenylalanine, leucine, and asparagine in the other mammal enzymes. The two residues at positions 176 and 179 are molecular determinants responsible for the stereoselective reduction of 3-ketosteroids and benzil. The presence of an asparagine at position 195 is important for the maintenance of the quaternary structure and stability at cold temperature. The absence of an asparagine at position 195 destabilizes the quaternary structure, thereby affecting catalytic efficiency toward some substrates and decreasing stability at cold temperature. Primate DHRS4s display different stereoselectivity and catalytic efficiency in the oxidoreduction of some substrates as compared to other mammal DHRS4s due to a difference in conserved amino acid residues. Belongs to the short-chain dehydrogenases/reductases (SDR) family.