InterPro domain: IPR018485

FGGY carbohydrate kinases carry out ATP-dependent phosphorylation on one out of at least nine distinct sugar substrates [ 1 ]. These enzymes include L-ribulokinase ( 2.7.1.16 ) (gene araB); Erythriol kinase ( 2.7.1.27 ) (gene eryA); L-fucolokinase ( 2.7.1.51 ) (gene fucK); gluconokinase ( 2.7.1.12 ) (gene gntK); glycerol kinase ( 2.7.1.30 ) (gene glpK); xylulokinase ( 2.7.1.17 ) (gene xylB); L-xylulose kinase ( 2.7.1.53 ) (gene lyxK), D-ribulokinase ( 2.7.1.47 ) (gene rbtK); and rhamnulokinase ( 2.7.1.5 ) (gene rhaB). This family also contains a divergent subfamily functioning in quorum sensing, which phosphorylates AI-2, a bacterial signaling molecule derived from 4,5-dihydroxy-2,3-pentanedione (DPD) [ 2 ].

This entry represents the C-terminal domain of these proteins. It adopts a ribonuclease H-like fold and is structurally related to the N-terminal domain [ 3 , 4 ].

All described members of this enzyme family are composed of two homologous actin-like ATPase domains. A catalytic cleft is formed by the interface between these two domains, where the sugar substrate and ATP co-substrate bind.

1. The FGGY carbohydrate kinase family: insights into the evolution of functional specificities. PLoS Comput. Biol. 7, e1002318
2. Phosphorylation and processing of the quorum-sensing molecule autoinducer-2 in enteric bacteria. ACS Chem. Biol. 2, 128-36
3. Structure of the regulatory complex of Escherichia coli IIIGlc with glycerol kinase. Science 259, 673-7
4. Crystal structure of a complex of Escherichia coli glycerol kinase and an allosteric effector fructose 1,6-bisphosphate. Biochemistry 37, 16565-72