| Primary Identifier | IPR018484 | Type | Domain |
| Short Name | Carb_kinase_FGGY_N |
| 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. |
