PROSITE logo

ProRule PRU01266


General rule information [?]

Accession PRU01266
Dates 20-MAR-2020 (Created)
19-NOV-2022 (Last updated, Version 4)
Data class Domain;
Predictors PROSITE; PS51918; RADICAL_SAM
Name 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.
Scope(s) Bacteria
Eukaryota
Archaea
Viruses
Example(s) Q5YT08 (MIAB_NOCFA);

Propagated annotation [?]

Comments [?]

case <FTGroup:1>
COFACTOR Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;

Keywords [?]


Gene Ontology [?]

GO:0051539; Molecular function:4 iron, 4 sulfur cluster binding
GO:0046872; Molecular function:metal ion binding

Features [?]

From: PS51918
Key From To Description Tag Condition FTGroup
DOMAIN from to /note="Radical SAM core #"
BINDING 15 15 /ligand="[4Fe-4S] cluster"
/ligand_id="ChEBI:CHEBI:49883"
/ligand_note="4Fe-4S-S-AdoMet"
C 1
BINDING 19 19 /ligand="[4Fe-4S] cluster"
/ligand_id="ChEBI:CHEBI:49883"
/ligand_note="4Fe-4S-S-AdoMet"
C 1
BINDING 22 22 /ligand="[4Fe-4S] cluster"
/ligand_id="ChEBI:CHEBI:49883"
/ligand_note="4Fe-4S-S-AdoMet"
C 1

Additional information [?]

Size range 200-300 amino acids
Related rules None
Fusion None
Repeats 1
Topology Undefined

Copyright

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.



View rule in raw text format (no links)

UniProtKB rule member sequences [?]