The domain within your query sequence starts at position 12 and ends at position 266; the E-value for the FGGY_N domain shown below is 6.8e-90.



PFAM accession number:PF00370
Interpro abstract (IPR018484):

FGGY carbohydrate kinases carry out ATP-dependent phosphorylation on one out of at least nine distinct sugar substrates [ (PUBMED: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) [ (PUBMED:17274596) ].

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 [ (PUBMED:8430315) (PUBMED:9843423) ].

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.

GO process:carbohydrate metabolic process (GO:0005975)
GO function:phosphotransferase activity, alcohol group as acceptor (GO:0016773)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry FGGY_N