ABSTRACT Transporters of the dicarboxylate amino acid-cation symporter family often mediate uptake of C ₄ -dicarboxylates, such as succinate or l -malate, in bacteria. A member of this family, dicarboxylate transporter A (DctA) from Corynebacterium glutamicum , was characterized to catalyze uptake of the C ₄ -dicarboxylates succinate, fumarate, and l -malate, which was inhibited by oxaloacetate, 2-oxoglutarate, and glyoxylate. DctA activity was not affected by sodium availability but was dependent on the electrochemical proton potential. Efficient growth of C. glutamicum in minimal medium with succinate, fumarate, or l -malate as the sole carbon source required high dctA expression levels due either to a promoter-up mutation identified in a spontaneous mutant or to ectopic overexpression. Mutant analysis indicated that DctA and DccT, a C ₄ -dicarboxylate divalent anion/sodium symporter-type transporter, are the only transporters for succinate, fumarate, and l -malate in C. glutamicum .