Protein Domain : Xylose isomerase IPR001998

Type	Family
Description	Xylose isomerase ( ) [ ] is an enzyme found in microorganisms which catalyzes the interconversion of D-xylose to D-xylulose. It can also isomerize D-ribose to D-ribulose and D-glucose to D-fructose. The enzyme is a homotetramer, which is stabilised by cobalt, and requires magnesium for its catalytic activity. Each subunit contains 2 domains: the core domain is a parallel α-β barrel; the C-terminal domain is a loop structure consisting of 5 helices and is involved in intermolecular contacts between adjacent subunits []. The active site lies in a deep pocket near the C-terminal ends of the strands of the barrel domain and includes residues from a second subunit. The tetramer is effectively a dimer of "active"dimers, the active sites being composed of residues from both subunits [ ].Xylose isomerase also exists in plants [ ] where it is homodimeric and is manganese-dependent.
Short Name	Xylose_isomerase