PRU00805
General rule information
[?]
Accession | PRU00805 |
Dates | 8-DEC-2009 (Created) 19-NOV-2022 (Last updated, Version 12) |
Data class | Domain |
Predictors | PROSITE; PS51471; FE2OG_OXY |
Names | Fe(2+) 2-oxoglutarate dioxygenase domain; Fe(II) 2-oxoglutarate dioxygenase domain; PKHD (prolyl/lysyl hydroxylase) domain; P4Hc domain; 2-oxoglutarate and Fe(II)-dependent oxygenases; 2OG-Fe(II) oxygenase superfamily; 2OG oxygenase families |
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. |
Propagated annotation
[?]
Description
[?]
case <FTGroup:2>
+ RecName: EC 1.14.11.-; |
else case <FTGroup:1>
+ RecName: EC 1.14.-.-; |
end case
Comments
[?]
case <FTGroup:1>
Cofactor | Fe(2+) Note: Binds 1 Fe(2+) ion per subunit. |
end case
Gene Ontology
[?]
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
Keywords
[?]
case <FTGroup:1>
end case
Features
[?]
From: PS51471 | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
DOMAIN | from | to | Fe2OG dioxygenase # | |||||||||
BINDING | 20 | 20 | /ligand="Fe cation" /ligand_id="ChEBI:CHEBI:24875 | H | 1,2 | |||||||
BINDING | 22 | 22 | /ligand="Fe cation" /ligand_id="ChEBI:CHEBI:24875 | D | 1,2 | |||||||
BINDING | 70 | 70 | /ligand="Fe cation" /ligand_id="ChEBI:CHEBI:24875 | H | 1,2 | |||||||
BINDING | 80 | 80 | /ligand="2-oxoglutarate" /ligand_id="ChEBI:CHEBI:16810 | [RK] | 2 |
Additional information
[?]
Size range | 80-160 amino acids |
Related rules | None |
Repeats | 1 |
Topology | Undefined |
Example | A1K320 (Y608_AZOSB) |
Scope | Bacteria
Eukaryota
Viruses |
Comments | None |
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
[?]
-
UniProtKB/Swiss-Prot sets
Bacteria [204] Eukaryota [334] Viruses [17] All [ 555 ]
- Retrieve set of proteins with 3D structure for this domain