AC   PRU01266;
DC   Domain;
TR   PROSITE; PS51918; RADICAL_SAM; 1; level=0
XX
Names: Radical SAM core domain
Function: The radical SAM enzymes biochemically characterized to date have in
 common the cleavage of the [4Fe-4S]1+-SAM complex to [4Fe-4S]2+-Met and the
 5'-deoxyadenosyl radical, which abstracts a hydrogen atom from the substrate
 to initiate a radical mechanism.
XX
case <FTGroup:1>
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
XX
GO   GO:0051539; F:4 iron, 4 sulfur cluster binding
GO   GO:0046872; F:metal ion binding
XX
KW   Metal-binding
KW   Iron
KW   Iron-sulfur
KW   S-adenosyl-L-methionine
KW   4Fe-4S
end case
XX
FT   From: PS51918
FT   DOMAIN          from..to
FT                   /note="Radical SAM core #"
FT   BINDING         15
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT   Group: 1; Condition: C
FT   BINDING         19
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT   Group: 1; Condition: C
FT   BINDING         22
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT   Group: 1; Condition: C
XX
Chop: Nter=0; Cter=0;
Size: 200-300;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q5YT08;
Scope:
 Bacteria
 Eukaryota
 Archaea
 Viruses
Comments: None;
XX
# Revision 1.4 2022/11/19
//