Xylose isomerase (IPR001998)

Short name: Xylose_isomerase

Overlapping homologous superfamilies

Family relationships


Xylose isomerase (EC: [PMID: 2651156] 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 alpha-beta barrel; the C-terminal domain is a loop structure consisting of 5 helices and is involved in intermolecular contacts between adjacent subunits [PMID: 2769749]. 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 [PMID: 2769749].

Xylose isomerase also exists in plants [PMID: 8620879] where it is homodimeric and is manganese-dependent.

GO terms

Biological Process

GO:0005975 carbohydrate metabolic process

Molecular Function

GO:0009045 xylose isomerase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE profiles