InterPro domain: IPR012734

This family consists of examples of the single chain form of dihydroxyacetone kinase (also called glycerone kinase) that uses ATP ( 2.7.1.29 ) as the phosphate donor, rather than a phosphoprotein as in Escherichia coli. This form has separable domains homologous to the K and L subunits of the E. coli enzyme, and is found in yeasts and other eukaryotes and in some bacteria, including Citrobacter freundii [ 1 , 2 ].

The member from tomato has been shown to phosphorylate dihydroxyacetone, 3,4-dihydroxy-2-butanone, and some other aldoses and ketoses [ 3 ]. Members from mammals have been shown to catalyse both the phosphorylation of dihydroxyacetone and the splitting of ribonucleoside diphosphate-X compounds among which FAD is the best substrate [ 4 ]. In yeast there are two isozymes of dihydroxyacetone kinase (Dak1 and Dak2). They are required for detoxification of dihydroxyacetone (DHA) [ 5 ].

1. Biochemical and molecular characterization of the oxidative branch of glycerol utilization by Citrobacter freundii. J. Bacteriol. 177, 4392-401
2. Crystal structure of the Citrobacter freundii dihydroxyacetone kinase reveals an eight-stranded alpha-helical barrel ATP-binding domain. J. Biol. Chem. 278, 48236-44
3. A tomato enzyme catalyzing the phosphorylation of 3,4-dihydroxy-2-butanone. Phytochemistry 60, 3-11
4. Identification of human and rat FAD-AMP lyase (cyclic FMN forming) as ATP-dependent dihydroxyacetone kinases. Biochem. Biophys. Res. Commun. 338, 1682-9
5. Cloning and overexpression in Escherichia coli of the gene encoding dihydroxyacetone kinase isoenzyme I from Schizosaccharomyces pombe, and its application to dihydroxyacetone phosphate production. Appl. Microbiol. Biotechnol. 51, 193-200