Catalyzes both the phosphorylation of dihydroxyacetone and of glyceraldehyde, and the splitting of ribonucleoside diphosphate-X compounds among which FAD is the best substrate (PubMed:7831203). Represses IFIH1-mediated cellular antiviral response (By similarity). ATP + dihydroxyacetone = ADP + dihydroxyacetone phosphate + H(+) ATP + D-glyceraldehyde = ADP + D-glyceraldehyde 3-phosphate + H(+) FAD = AMP + H(+) + riboflavin cyclic-4',5'-phosphate Manganese or cobalt are requested for FAD-AMP lyase activity. Optimum pH is 7. Optimum temperature is 60 degrees Celsius. Homodimer (PubMed:7831203). Interacts with IFIH1 (via the CARD domains), the interaction is inhibited by viral infection (By similarity). Detected in kidney (at protein level). DhaK and DhaL domains have differential roles, individually DhaK is inactive and DhaL displays cyclase but not kinase activity. Belongs to the dihydroxyacetone kinase (DAK) family.