An iron-dependent alcohol dehydrogenase required for optimal 1,2-propanediol (1,2-PD) degradation. NAD(+) and NADH are regenerated internally within the bacterial microcompartment (BMC) dedicated to 1,2-PD degradation by the PduP and PduQ enzymes, which reduce NAD(+) and oxidize NADH respectively, although there must also be cofactor transport across the BMC. The 1,2-PD-specific bacterial microcompartment (BMC) concentrates low levels of 1,2-PD catabolic enzymes, concentrates volatile reaction intermediates thus enhancing pathway flux and keeps the level of toxic, mutagenic propionaldehyde low. 1-propanol + NAD(+) = H(+) + NADH + propanal Enzyme is oxygen sensitive. Optimum pH is 7.0 for propionaldehyde reduction and 9.0 for 1-propanol dehydrogenase. Polyol metabolism; 1,2-propanediol degradation. Interacts with PduP, probably via the N-terminus of PduQ. Probably located inside the BMC shell. BMC production is induced by growth on 1,2-PD vitamin B12 medium. Loss of NADH-dependent reduction of propionaldehyde in BMCs. BMCs appear to be normal, cells grow more slowly on 1,2-PD with limiting or saturating CN-B12. Bacterial microcompartments (BMC) 100-200 nm in cross section are formed during aerobic growth on minimal 1,2-PD-B12 or anaerobic growth on 1,2-PD-tetrathionate medium, but not during aerobic growth on glucose, anerobic growth on glucose or pyruvate-tetrathionate (PubMed:10498708). BMCs can constitute up to 10% of total cell protein (PubMed:12923081). Belongs to the iron-containing alcohol dehydrogenase family.