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 2.3e-82.

LVGAVVQGTNSTRFLVFNSKTAELVCSHQVELTQEYPKEGWVEQDPKEILKSVYECIAKA
CEKLAEVNIDISNIKAIGVSNQRETTVVWDKFTGDPLYNAVVWLDLRTQSTVETLTKKIP
GNSNFVKSKTGLPLSTYFSAVKLRWMLDNLRPIQKAVEEGRAMFGTIDSWLIWCMTGGVN
GGIHCTDVTNACRTMLFNIHSLEWDKDLCDFFEIPMSILPNVCSSSEIYGLMTSGALEGV
PISGCLGDQSAALVG

FGGY_N

FGGY_N
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 2.7.1.16) (gene araB); Erythriol kinase (EC 2.7.1.27) (gene eryA); L-fucolokinase (EC 2.7.1.51) (gene fucK); gluconokinase (EC 2.7.1.12) (gene gntK); glycerol kinase (EC 2.7.1.30) (gene glpK); xylulokinase (EC 2.7.1.17) (gene xylB); L-xylulose kinase (EC 2.7.1.53) (gene lyxK), D-ribulokinase (EC 2.7.1.47) (gene rbtK); and rhamnulokinase (EC 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) [(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