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annotation rule: PRU00805

General rule information [?]

Accession PRU00805
Dates 8-DEC-2009 (Created)
19-DEC-2016 (Last updated, Version 7)
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.
GO:0055114; Biological process: oxidation-reduction process.
end case

case <FTGroup:2>
GO:0016706; Molecular function: oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors.
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 #        
METAL     20     20       Iron     H   1,2
METAL     22     22       Iron     D   1,2
METAL     70     70       Iron     H   1,2
BINDING     80     80       2-oxoglutarate     [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

Copyright

PROSITE is copyright. It is produced by the SIB Swiss Institute Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified. Usage by and for commercial entities requires a license agreement. For information about the licensing scheme send an email to license@isb-sib.ch or see: prosite_license.html.



UniProtKB rule member sequences [?]