Carbohydrate kinase, FGGY, C-terminal (IPR018485)

Short name: Carb_kinase_FGGY_C

Overlapping homologous superfamilies


Domain relationships



FGGY carbohydrate kinases carry out ATP-dependent phosphorylation on one out of at least nine distinct sugar substrates [PMID: 22215998]. These enzymes include L-ribulokinase (EC: (gene araB); Erythriol kinase (EC: (gene eryA); L-fucolokinase (EC: (gene fucK); gluconokinase (EC: (gene gntK); glycerol kinase (EC: (gene glpK); xylulokinase (EC: (gene xylB); L-xylulose kinase (EC: (gene lyxK), D-ribulokinase (EC: (gene rbtK); and rhamnulokinase (EC: (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) [PMID: 17274596].

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.

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 [PMID: 8430315, PMID: 9843423].

GO terms

Biological Process

GO:0005975 carbohydrate metabolic process

Molecular Function

GO:0016773 phosphotransferase activity, alcohol group as acceptor

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.