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 PRU00796
View rule in raw text format (no links)
PURL: https://purl.expasy.org/prosite/rule/PRU00796
General rule information
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| Accession | PRU00796 |
| Dates | 10-SEP-2009 (Created)
11-NOV-2021 (Last updated, Version 7) |
| Data class | Protein; |
| Predictors |
PROSITE; PS51463; P_GLUCOSE_ISOMERASE_3 |
Name | Glucose-6-phosphate isomerase family |
| Function | Glucose-6-phosphate isomerase (GPI) (EC 5.3.1.9) or phosphoglucose isomerase (PGI) is a glycolytic enzyme that catalyzes the reversible isomerization of glucose-6-phosphate and fructose-6-phosphate. |
| Scope(s) |
Bacteria Eukaryota Archaea |
| Example(s) | Q39SU1; |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | G6PI |
| Protein name | + RecName: Full=Glucose-6-phosphate isomerase; Short=GPI; EC=5.3.1.9; AltName: Full=Phosphoglucose isomerase; Short=PGI; AltName: Full=Phosphohexose isomerase; Short=PHI; |
| Gene name | Name=pgi; |
Comments
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| CATALYTIC ACTIVITY | Reaction=alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate; Xref=Rhea:RHEA:11816, ChEBI:CHEBI:57634, ChEBI:CHEBI:58225; EC=5.3.1.9; |
| PATHWAY | Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- phosphate and glycerone phosphate from D-glucose: step 2/4. |
| SUBCELLULAR LOCATION | Cytoplasm. |
| SIMILARITY | Belongs to the GPI family. |
Keywords
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Gene Ontology
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| GO:0004347; Molecular function:glucose-6-phosphate isomerase activity |
| GO:0006096; Biological process:glycolytic process |
| GO:0006094; Biological process:gluconeogenesis |
| GO:0005737; Cellular component:cytoplasm |
Cross-references
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Features
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| From: PS51463 | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| ACT_SITE | 328 | 328 | /note="Proton donor" | E | ||||||||
| ACT_SITE | 360 | 360 | H | |||||||||
| ACT_SITE | 472 | 472 | K | |||||||||
Additional information
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| Size range | 150-600 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
Archaea [6] Bacteria [569] Eukaryota [48] All [ 623 ]
- Retrieve set of proteins with 3D structure for this domain