Component of the dihydroxyacetone kinase complex, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaM serves as the phosphoryl donor. Is phosphorylated by phosphoenolpyruvate in an EI- and HPr-dependent reaction, and a phosphorelay system on histidine residues finally leads to phosphoryl transfer to DhaL and dihydroxyacetone. dihydroxyacetone + phosphoenolpyruvate = dihydroxyacetone phosphate + pyruvate kcat is 2.8 sec(-1). Values measured with the DhaKLM complex. Polyol metabolism; glycerol degradation. Homodimer (PubMed:11350937). The dihydroxyacetone kinase complex is composed of a homodimer of DhaM, a homodimer of DhaK and the subunit DhaL. Consists of three domains. The N-terminal dimerization domain has the same fold as the IIA domain of the mannose transporter of the bacterial phosphoenolpyruvate:sugar phosphotransferase system (PTS). The middle domain is similar to HPr and the C-terminus is similar to the N-terminal domain of enzyme I (EI) of the PTS. The IIA domain of DhaM (via phospho-His-9), instead of ATP, is the phosphoryl donor to dihydroxyacetone (Dha). The phosphoryl flow likely involves HPr ('His-15') -> DhaM (His-430 -> His-169 -> His-9) -> DhaL-ADP -> Dha. The HPr-like domain of DhaM cannot efficiently substitute for the general carrier protein HPr. Unlike the carbohydrate-specific transporters of the PTS, the complex DhaKLM has no transport activity. Belongs to the PEP-utilizing enzyme family. Was reported to be a protein deacetylase that removes acetyl groups on specific lysine residues in target proteins (PubMed:26716769). However, later experiments demonstrate that this protein does not have any protein deacetylase activity; the discrepancy observed seems to be due to contaminants having proteolytic activity (PubMed:29939131).