ProRule PRU00748
General rule information
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Accession | PRU00748 |
Dates | 3-MAR-2009 (Created)
19-NOV-2022 (Last updated, Version 12) |
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 (XYLA_STROI); Q9FKK7 (XYLA_ARATH); |
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