AC PRU00748; DC Domain; TR PROSITE; PS51415; XYLOSE_ISOMERASE; 1; level=0 XX Names: Xylose isomerase family Function: Xylose isomerase (EC 5.3.1.5) is an enzyme found in microorganisms and plants which catalyzes the interconversion of the aldo sugars D-xylose or D-glucose to the keto sugars D-xylulose and D-fructose. The catalytic activity requires magnesium, cobalt or manganese. XX case DE AltName: Full=Xylose isomerase; DE EC=5.3.1.5; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=alpha-D-xylose = alpha-D-xylulofuranose; Xref=Rhea:RHEA:22816, CC ChEBI:CHEBI:28518, ChEBI:CHEBI:188998; EC=5.3.1.5; end case case not CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Note=Binds 2 magnesium ions per subunit.; else case CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Note=Binds 2 manganese ions per subunit.; end case CC -!- SUBUNIT: Homotetramer. case CC -!- SUBCELLULAR LOCATION: Cytoplasm. end case CC -!- SIMILARITY: Belongs to the xylose isomerase family. XX GO GO:0009045; F:xylose isomerase activity GO GO:0042732; P:D-xylose metabolic process GO GO:0005975; P:carbohydrate metabolic process GO GO:0016853; F:isomerase activity GO GO:0000287; F:magnesium ion binding GO GO:0046872; F:metal ion binding GO GO:0006098; P:pentose-phosphate shunt case GO GO:0030145; F:manganese ion binding end case case GO GO:0005737; C:cytoplasm end case XX KW Carbohydrate metabolism KW Isomerase KW Magnesium KW Metal-binding KW Pentose shunt KW Xylose metabolism case KW Manganese end case case KW Cytoplasm end case XX FT From: PS51415 FT ACT_SITE 66 FT Condition: H case not FT BINDING 197 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT Condition: E FT BINDING 233 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT Condition: E FT BINDING 233 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT Condition: E FT BINDING 236 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT Condition: H FT BINDING 261 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT Condition: D FT BINDING 272 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT Condition: D FT BINDING 274 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT Condition: D FT BINDING 304 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT Condition: D else case FT BINDING 197 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT Condition: E FT BINDING 233 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT Condition: E FT BINDING 233 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT Condition: E FT BINDING 236 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT Condition: H FT BINDING 261 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT Condition: D FT BINDING 272 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT Condition: D FT BINDING 274 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT Condition: D FT BINDING 304 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT Condition: D end case XX Chop: Nter=0; Cter=0; Size: 370-420; Related: None; Repeats: 1; Topology: Undefined; Example: Q93RJ9; Q9FKK7; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.12 2022/11/19 //