We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
ProRule PRU00748
View rule in raw text format (no links)
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