EC Number   |
General Information |
Reference |
|---|
   2.1.1.224 | evolution |
analysis of RNA methylation by phylogenetically diverse Cfr radical SAM enzymes reveals an ironbinding accessory domain in a clostridial enzyme. Sequence comparisons and phylogenetic analysis and tree, overview. Cfr homologues from Bacillus amyloliquefaciens, Enterococcus faecalis, Paenibacillus lautus, and Clostridioides difficile act as C8 adenine RNA methylases in biochemical assays |
-, 758141 |
| 2.1.1.224 | evolution |
analysis of RNA methylation by phylogenetically diverse Cfr radical SAM enzymes reveals an ironbinding accessory domain in a clostridial enzyme. Sequence comparisons and phylogenetic analysis and tree, overview. Cfr homologues from Bacillus amyloliquefaciens, Enterococcus faecalis, Paenibacillus lautus, and Clostridioides difficile act as C8 adenine RNA methylases in biochemical assays. Clostridioides difficile Cfr contains an additional Cys-rich C-terminal domain that binds a mononuclear Fe2+ ion in a rubredoxin-type Cys4 motif, which has an important purpose for the observed C-terminal iron in the native fusion protein. Bioinformatic analysis of the Clostridioides difficile Cfr Cys-rich domain shows that it is widespread (about 1400 homologues) as a stand-alone gene in pathogenic or commensal Bacilli and Clostridia, with >10% encoded adjacent to a predicted radical SAM RNA methylase |
-, 758141 |
| 2.1.1.224 | evolution |
bioinformatics analysis of the Cfr/RlmN family establishes their significant evolutionary link with radical-S-adenosyl-L-methionine enzymes. The RlmN subfamily is likely the ancestral form, whereas the Cfr subfamily arose via duplication and horizontal gene transfer |
705983 |
| 2.1.1.224 | evolution |
cfr(C) is part of a putative 24 kb-transposon, which generated a detectable circular intermediate. An element differing by a single nucleotide is found in Clostridium difficile DA00203 from GenBank data, consistent with a recent horizontal transfer |
-, 756922 |
| 2.1.1.224 | evolution |
ClbA acts via the same mechanism as the Cfr methyltransferase |
-, 718601 |
| 2.1.1.224 | evolution |
ClbB acts via the same mechanism as the Cfr methyltransferase |
-, 718601 |
| 2.1.1.224 | evolution |
ClbC acts via the same mechanism as the Cfr methyltransferase |
718601 |
| 2.1.1.224 | evolution |
enzyme Cfr belongs to the radical SAM (RS) superfamily of enzymes, catalysts that use S-adenosyl-L-methionine (SAM) as an oxidant to perform difficult and often complex transformations by radical mechanisms. RS superfamily enzymes employ a [4Fe-4S] cluster to supply the requisite electron for reductive cleavage of SAM, usually to L-methionine and a 5'-deoxyadenosyl 5'-radical. Similar enzyme RlmN (EC 2.1.1.192) is proposed to be an evolutionary precursor to Cfr. Residues conserved among both enzymes in a pairwise alignment of Escherichia coli RlmN and Staphylococcus aureus Cfr are mapped onto the RlmN structure. The catalytic residues in the active site are strictly conserved as are most of the surrounding residues within the core of the barrel, supporting the proposal that the enzymes use a common mechanism for C-methylation. The high degree of sequence conservation near the active site suggests that methylation site specificity during the reaction may be controlled in part by more distant structural elements. In Cfr, two large conformationally flexible regions in the RlmN structure are absent |
758461 |
| 2.1.1.224 | evolution |
evolutionary relationship between the Cfr and RlmN (EC 2.1.1.192) enzymes, phylogenetic analysis, overview |
758128 |
| 2.1.1.224 | evolution |
RlmN and Cfr belong to the radical SAM (RS) superfamily of enzymes. RlmN is proposed to be an evolutionary precursor to Cfr. The catalytic residues in theactive site are strictly conserved as are most of the surrounding residues within the core of the barrel |
758461 |
