The domain within your query sequence starts at position 283 and ends at position 429; the E-value for the FGGY_C domain shown below is 3e-8.
LRHIVKEFKRETGVDLTKDNMALQRVREAAEKAKCELSSSVQTDINLPYLTMDASGPKHL NMKLTRAQFEGIVTDLIKRTIAPCQKAMQDAEVSKSDIGEVILVGGMTRMPKVQQTVQDL FGRAPSKAVNPDEAVAIGAAIQGGVLA
FGGY_C |
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PFAM accession number: | PF02782 |
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Interpro abstract (IPR018485): | 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 C-terminal domain of these proteins. It adopts a ribonuclease H-like fold and is structurally related to the N-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_C