Corynebacterium glutamicum is a Gram-positive soil bacterium that is widely used for the industrial production of amino acids. It also produces organic acids including lactate, succinate, and acetate under oxygen limitation. Under oxygen-deprived conditions, the key enzymes of the glycolytic and organic acid production pathways are upregulated. Of the enzymes upregulated, NAD-linked L-lactate dehydrogenase, encoded by the ldhA gene, is responsible for L-lactate production from pyruvate. To reveal a regulatory mechanism involved in upregulation of ldhA in C. glutamicum, we performed DNA affinity purification, and identified SugR, a global repressor of genes involved in sugar uptake and glycolysis, as a protein binding to the ldhA promoter region. Whereas ldhA gene expression and ldhA promoter activity were completely repressed during growth of wild type cells in the absence of sugar, no such repression was observed in sugR mutant cells, indicating that SugR represses ldhA transcription. Electrophoretic mobility shift assays and DNase I footprint analyses revealed that two direct repeats, centered at position -17 with respect to the transcriptional start point, are required for SugR binding to the ldhA promoter, and that fructose-1-phosphate is the strongest negative effector of repressor activity of SugR. Therefore, it is likely that SugR plays an important role in the coordinated expression of genes involved in conversion of sugars to organic acids in C. glutamicum. This work was partially supported by a grant from the New Energy and Industrial Technology Development Organization (NEDO).