Catalyzes the NAD(P)(+)-dependent oxidation of D-glucose to D-gluconate via gluconolactone. Displays broad substrate specificity since it is able to catalyze the oxidation of a number of alternative aldose sugars, such as D-galactose, D-xylose and L-arabinose, to the corresponding glyconate. Can utilize both NAD(+) and NADP(+) as electron acceptor. Physiologically, seems to be involved in the degradation of both glucose and galactose through a non-phosphorylative variant of the Entner-Doudoroff pathway. D-glucose + NAD(+) = D-glucono-1,5-lactone + H(+) + NADH D-glucose + NAD(+) = D-glucono-1,5-lactone + H(+) + NADH D-glucose + NADP(+) = D-glucono-1,5-lactone + H(+) + NADPH D-glucose + NADP(+) = D-glucono-1,5-lactone + H(+) + NADPH D-galactose + NAD(+) = D-galactono-1,4-lactone + H(+) + NADH D-galactose + NADP(+) = D-galactono-1,5-lactone + H(+) + NADPH D-galactose + NADP(+) = D-galactono-1,5-lactone + H(+) + NADPH an aldopyranose + NAD(+) = aldono-1,5-lactone + H(+) + NADH an aldopyranose + NADP(+) = aldono-1,5-lactone + H(+) + NADPH Binds 2 Zn(2+) ions per subunit. One of the zinc atoms is essential for catalytic activity while the other has a structural function. Inhibited by EDTA in vitro. Optimum pH is 9. Optimum temperature is 77 degrees Celsius. At 37 degrees Celsius, shows about 20% activity as compared with the maximal value. Homotetramer. Belongs to the zinc-containing alcohol dehydrogenase family. Glucose 1-dehydrogenase subfamily.