v5.1.0.3
Glycine data from LIS
Type | Domain |
Description | FGGY carbohydrate kinases carry out ATP-dependent phosphorylation on one out of at least nine distinct sugar substrates [ ]. These enzymes include L-ribulokinase () (gene araB); Erythriol kinase ( ) (gene eryA); L-fucolokinase ( ) (gene fucK); gluconokinase ( ) (gene gntK); glycerol kinase ( ) (gene glpK); xylulokinase ( ) (gene xylB); L-xylulose kinase ( ) (gene lyxK), D-ribulokinase ( ) (gene rbtK); and rhamnulokinase ( ) (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) [ ].This entry represents the N-terminal domain of these proteins. It adopts a ribonuclease H-like fold and is structurally related to the C-terminal domain [ , ].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. |
Short Name | Carb_kinase_FGGY_N |