D-xylulose kinases, subgroup 1; members of the FGGY family of carbohydrate kinases
This subgroup is composed of D-xylulose kinases (XK, also known as xylulokinase; EC 2.7.1.17) from bacteria and eukaryota. They share high sequence similarity with Escherichia coli xylulokinase (EcXK), which catalyzes the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P) and ADP. Some uncharacterized sequences are also included in this subfamily. EcXK exists as a dimer. Each monomer consists of two large domains separated by an open cleft that forms an active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The presence of Mg2+ or Mn2+ might be required for catalytic activity. Members of this subgroup belong to the FGGY family of carbohydrate kinases.
Jiyao W et al.(2023). "The conserved domain database in 2023.",