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 PRU00805
View rule in raw text format (no links)
PURL: https://purl.expasy.org/prosite/rule/PRU00805
General rule information
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| Accession | PRU00805 |
| Dates | 08-DEC-2009 (Created)
19-NOV-2022 (Last updated, Version 13) |
| Data class | Domain; |
| Predictors |
PROSITE; PS51471; FE2OG_OXY |
Name | Fe(2+) 2-oxoglutarate dioxygenase domain |
| Function | Enzymes with the Fe(2+) and 2-oxoglutarate (2OG)-dependent dioxygenase domain typically catalyse the oxidation of an organic substrate using a dioxygen molecule, mostly by using ferrous iron as the active site cofactor and 2OG as a cosubstrate which is decarboxylated to succinate and CO2. |
| Scope(s) |
Bacteria Eukaryota Viruses |
| Example(s) | A1K320; |
Propagated annotation
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Identifier, protein and gene names
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| case <FTGroup:2> | |
| Protein name | + RecName: EC=1.14.11.-; |
| else case <FTGroup:1> | |
| Protein name | + RecName: EC=1.14.-.-; |
| end case | |
Comments
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| case <FTGroup:1> | |
| COFACTOR | Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Note=Binds 1 Fe(2+) ion per subunit.; |
| end case | |
Keywords
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| case <FTGroup:1> | |
| Dioxygenase | |
| Iron | |
| Metal-binding | |
| Oxidoreductase | |
| end case | |
Gene Ontology
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| case <FTGroup:1> | |
| GO:0005506; Molecular function:iron ion binding | |
| end case | |
| case <FTGroup:2> | |
| GO:0016706; Molecular function:2-oxoglutarate-dependent dioxygenase activity | |
| else case <FTGroup:1> | |
| GO:0016705; Molecular function:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen | |
| end case | |
Features
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| From: PS51471 | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| DOMAIN | from | to | /note="Fe2OG dioxygenase #" | |||||||||
| BINDING | 20 | 20 | /ligand="Fe cation" /ligand_id="ChEBI:CHEBI:24875" |
H | 1 | |||||||
| BINDING | 20 | 20 | /ligand="Fe cation" /ligand_id="ChEBI:CHEBI:24875" |
H | 2 | |||||||
| BINDING | 22 | 22 | /ligand="Fe cation" /ligand_id="ChEBI:CHEBI:24875" |
D | 1 | |||||||
| BINDING | 22 | 22 | /ligand="Fe cation" /ligand_id="ChEBI:CHEBI:24875" |
D | 2 | |||||||
Additional information
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| Size range | 80-160 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 [204] Eukaryota [346] Viruses [17] All [ 567 ]
- Retrieve set of proteins with 3D structure for this domain