Psychrophilic alcohol dehydrogenase that exhibits a wide range of substrate specificity, oxidizing mainly primary and secondary aliphatic alcohols, utilizing NAD(+) as a cosubstrate. In vitro, shows highest reaction rates for ethanol as a substrate and gradually decreases its reaction rates as the length and branching of the carbon chain of the alcohol substrates increase. To a lesser extent, is also able to reduce aldehydes and ketones. Do not catalyze the further oxidation of aldehydes to carboxylic acids. Cannot use NADP(+) instead of NAD(+). a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH a secondary alcohol + NAD(+) = a ketone + H(+) + NADH ethanol + NAD(+) = acetaldehyde + H(+) + NADH 1-propanol + NAD(+) = H(+) + NADH + propanal butan-1-ol + NAD(+) = butanal + H(+) + NADH NAD(+) + propan-2-ol = acetone + H(+) + NADH Binds 2 Zn(2+) ions per subunit. One metal ion is located at the active-site region and has been termed catalytic, while the second metal ion has been termed structural. kcat is 549.1 min(-1) for the oxidation of ethanol (at pH 7.4 and 30 degrees Celsius). kcat is 488.8 min(-1) for the oxidation of propan-1-ol (at pH 7.4 and 30 degrees Celsius). kcat is 486.7 min(-1) for the oxidation of butan-1-ol (at pH 7.4 and 30 degrees Celsius). kcat is 382.7 min(-1) for the oxidation of propan-2-ol (at pH 7.4 and 30 degrees Celsius). kcat is 409.8 min(-1) for the reduction of acetone (at pH 6.0 and 30 degrees Celsius) (PubMed:9660191). kcat is 9.4 sec(-1) for the oxidation of ethanol (at pH 7.4 and 30 degrees Celsius) (PubMed:32596590). Optimum pH is 7.4 and 6.0 for the oxidation of ethanol and reduction of acetone, respectively. Is a very thermostable, cold-adapted enzyme. Is active from 10 to at least 53 degrees Celsius and unfolds at 89 degrees Celsius. Homotetramer. Each subunit comprises two distinct structural domains: the catalytic domain (residues 1-150 and 288-340/345) and the nucleotide-binding domain (residues 151-287). Belongs to the zinc-containing alcohol dehydrogenase family. The protein characterized in PubMed:9660191 corresponds to this sequence and not to the fragment sequence described in this article.