cd07776: FGGY_D-XK_euk (this model, PSSM-Id:212660 is obsolete and has been replaced by 466795)
eukaryotic D-xylulose kinases; a subfamily of the FGGY family of carbohydrate kinases
This subfamily is composed of eukaryotic D-xylulose kinases (XK, also known as xylulokinase; EC 2.7.1.17), which catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P) and ADP. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. Members of this subfamily are similar to bacterial D-XKs, which exist as dimers with active sites that lie at the interface between two large domains. The presence of Mg2+ or Mn2+ is required for catalytic activity.
Comment:based on similarity with other members of the FGGY family
Comment:FGGY proteins contain two domains, separated by a deep cleft that forms the active site. The N-terminal domain is primarily involved in substrate binding, while the C-terminal domain is mainly responsible for ATP binding.
Jiyao W et al.(2023). "The conserved domain database in 2023.",