ProRule PRU00748
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PURL: https://purl.expasy.org/prosite/rule/PRU00748
General rule information
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| Accession | PRU00748 |
| Dates | 03-MAR-2009 (Created)
19-NOV-2022 (Last updated, Version 13) |
| Data class | Domain; |
| Predictors |
PROSITE; PS51415; XYLOSE_ISOMERASE |
Name | 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. |
| Scope(s) |
Eukaryota Bacteria |
| Example(s) | Q93RJ9; Q9FKK7; |
Propagated annotation
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Identifier, protein and gene names
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| case <FT:1> | |
| Protein name | AltName: Full=Xylose isomerase; EC=5.3.1.5; |
Comments
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| CATALYTIC ACTIVITY | Reaction=alpha-D-xylose = alpha-D-xylulofuranose; Xref=Rhea:RHEA:22816, ChEBI:CHEBI:28518, ChEBI:CHEBI:188998; EC=5.3.1.5; |
| end case | |
| case not <OC:Viridiplantae> | |
| COFACTOR | Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 2 magnesium ions per subunit.; |
| else case <OC:Viridiplantae> | |
| COFACTOR | Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Note=Binds 2 manganese ions per subunit.; |
| end case | |
| SUBUNIT | Homotetramer. |
| case <OC:Bacteria> | |
| SUBCELLULAR LOCATION | Cytoplasm. |
| end case | |
| SIMILARITY | Belongs to the xylose isomerase family. |
Keywords
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| Carbohydrate metabolism | |
| Isomerase | |
| Magnesium | |
| Metal-binding | |
| Pentose shunt | |
| Xylose metabolism | |
| case <OC:Viridiplantae> | |
| Manganese | |
| end case | |
| case <OC:Bacteria> | |
| Cytoplasm | |
| end case | |
Gene Ontology
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| GO:0009045; Molecular function:xylose isomerase activity | |
| GO:0042732; Biological process:D-xylose metabolic process | |
| GO:0005975; Biological process:carbohydrate metabolic process | |
| GO:0016853; Molecular function:isomerase activity | |
| GO:0000287; Molecular function:magnesium ion binding | |
| GO:0046872; Molecular function:metal ion binding | |
| GO:0006098; Biological process:pentose-phosphate shunt | |
| case <OCellular component:Viridiplantae> | |
| GO:0030145; Molecular function:manganese ion binding | |
| end case | |
| case <OCellular component:Bacteria> | |
| GO:0005737; Cellular component:cytoplasm | |
| end case | |
Features
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| From: PS51415 | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| ACT_SITE | 66 | 66 | H | |||||||||
| case not <OC:Viridiplantae> | ||||||||||||
| BINDING | 197 | 197 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="1" |
E | ||||||||
| BINDING | 233 | 233 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="1" |
E | ||||||||
| BINDING | 233 | 233 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="2" |
E | ||||||||
| BINDING | 236 | 236 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="2" |
H | ||||||||
| BINDING | 261 | 261 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="1" |
D | ||||||||
| BINDING | 272 | 272 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="2" |
D | ||||||||
| BINDING | 274 | 274 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="2" |
D | ||||||||
| BINDING | 304 | 304 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="1" |
D | ||||||||
| else case <OC:Viridiplantae> | ||||||||||||
| BINDING | 197 | 197 | /ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035" /ligand_label="1" |
E | ||||||||
| BINDING | 233 | 233 | /ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035" /ligand_label="1" |
E | ||||||||
| BINDING | 233 | 233 | /ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035" /ligand_label="2" |
E | ||||||||
| BINDING | 236 | 236 | /ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035" /ligand_label="2" |
H | ||||||||
| BINDING | 261 | 261 | /ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035" /ligand_label="1" |
D | ||||||||
| BINDING | 272 | 272 | /ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035" /ligand_label="2" |
D | ||||||||
| BINDING | 274 | 274 | /ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035" /ligand_label="2" |
D | ||||||||
| BINDING | 304 | 304 | /ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035" /ligand_label="1" |
D | ||||||||
| end case | ||||||||||||
Additional information
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| Size range | 370-420 amino acids |
| Related rules |
None |
| Fusion | None |
| Repeats | 1 |
| Topology | Undefined |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.
UniProtKB rule member sequences
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- UniProtKB/Swiss-Prot sets
Bacteria [195] Eukaryota [2] All [ 197 ]
- Retrieve set of proteins with 3D structure for this domain