Carbohydrate kinase FGGY, N-terminal

Definition

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 [[cite:PMID:8430315], [cite:PMID:9843423]]. 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: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) 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.

7 human proteins with this domain

Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.

Download CSV (7 proteins: gene, accession, name)

• FGGY
• GK
• GK2
• GK3
• GK5
• SHPK
• XYLB