Enzymes from the LDHD subfamily can be found in bacteria and some lower eukaryotes, such as protists, fungi and green algae. Bacterial proteins initially annotated as ᴅ-lactate dehydrogenases (LDHD, or ᴅ-LDH) act at the last step of glycolysis in anaerobic conditions by catalyzing the reduction of pyruvate to ᴅ-lactate, allowing regeneration of NAD+ from NADH. They may also play a role in other processes, as demonstrated for VanH, which is responsible for vancomycin resistance in Enterococcus faecium. The only eukaryotic ᴅ-LDH studied so far, the Chlamydomonas reinhardtii enzyme, was shown to reduce pyruvate in fermentation pathways in chloroplasts.