| Primary Identifier | IPR012736 | Type | Domain |
| Short Name | DhaK_1 |
| description | In bacteria, dihydroxyacetone is formed by the oxidation of glycerol or the aldol cleavage of fructose-6-phosphate. Dihydroxyacetone kinase converts this compound to the glycolytic intermediate dihydroxyacetone phosphate. Two forms of this enzyme have been shown to exist, using either ATP or a phosphoprotein of the phosphoenolpyruvate: sugar phosphotransferase system (PTS) as phosphate donor. The ATP-dependent kinases () are single-subunit enzymes that are composed of two domains []. The phosphoprotein-dependent kinases are composed of three subunits: DhaK and DhaL, which are homologous to the domains from the ATP-dependent enzyme; and DhaM which is a component of the PTS system [].This entry represents the DhaK subunit of phosphoprotein-dependent dihydroxyacetone kinase. The model excludes the DhaK paralog DhaK2 () encoded in the same operon as DhaK in the firmicutes, with which it sometimes exists as a DhaK/DhaK2 fusion. This subunit is a homodimer which contains the dihydroxyacetone-binding site []. The overall fold consists of two six-stranded mixed β-sheets surrounded by nine α-helices and a β-ribbon covering the exposed edge strand of one sheet. |
