Dihydroxyacetone binding subunit of the dihydroxyacetone kinase, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone via a phosphoryl group transfer from DhaL-ATP (PubMed:15476397, PubMed:11350937). Binds covalently dihydroxyacetone in hemiaminal linkage (PubMed:15476397). DhaK acts also as corepressor of the transcription activator DhaR by binding to the sensor domain of DhaR (PubMed:24440518). In the presence of dihydroxyacetone, DhaL-ADP displaces DhaK and stimulates DhaR activity (PubMed:24440518). In the absence of dihydroxyacetone, DhaL-ADP is converted by the PTS to DhaL-ATP, which does not bind to DhaR (PubMed:24440518). dihydroxyacetone + phosphoenolpyruvate = dihydroxyacetone phosphate + pyruvate Inhibited by chloro-3-hydroxyacetone and D,L-glyceraldehyde. kcat is 2.8 sec(-1) with dihydroxyacetone as substrate. Values measured with the DhaKLM complex (PubMed:11350937). kcat is 290 min(-1) with dihydroxyacetone as substrate. kcat is 12.5 min(-1) with D,L-glyceraldehyde as substrate (PubMed:15476397). Polyol metabolism; glycerol degradation. Homodimer (PubMed:12813127, PubMed:15476397, PubMed:24440518). The dihydroxyacetone kinase complex is composed of a homodimer of DhaM, a homodimer of DhaK and the subunit DhaL (PubMed:12813127, PubMed:15476397). DhaL also forms a complex with DhaR (PubMed:24440518). Activated by DhaR. Unlike the carbohydrate-specific transporters of the PTS, the complex DhaKML has no transport activity.