Bifunctional enzyme with both malic and malolactic enzyme activities (PubMed:33824210). In the absence of NADPH, catalyzes the reversible decarboxylation of malate to pyruvate (PubMed:16788182, PubMed:33824210). Can use NAD and NADP, but with a very strong preference for NADP (PubMed:16788182). In the presence of excess NADPH, catalyzes the non-oxidative decarboxylation of malate to lactate (PubMed:33824210). During growth on glucose, contributes to NADPH balancing via oxidation of the NADPH produced in excess by other enzymatic reactions (PubMed:33824210). Can also catalyze the decarboxylation of oxaloacetate (PubMed:16788182). (S)-malate + NADP(+) = CO2 + NADPH + pyruvate H(+) + oxaloacetate = CO2 + pyruvate (S)-malate + H(+) = (S)-lactate + CO2 Divalent metal cations. NADPH is a strong modulator that switches activity from a pyruvate-producing malic enzyme to a lactate-generating malolactic enzyme. Interacts with BrxC. Transcribed at a high level under all of the conditions tested. Mutant shows wild-type growth on glucose but a much slower growth rate on malate, fumarate, or succinate plus glutamate (PubMed:16788182). Overexpression of the other three malic enzymes, mleA, maeA or malS cannot compensate for the ytsJ deletion (PubMed:16788182). The ATP concentrations in the mutant grown in minimal medium with glucose are similar to the wild-type level. ATP concentrations decrease by about 20% in malate minimal medium (PubMed:23136871). NADPH overproduction is virtually abolished in the deletion mutant (PubMed:33824210). Belongs to the malic enzymes family.