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Literature summary for 2.1.1.192 extracted from

  • Gumkowski, J.D.; Martinie, R.J.; Corrigan, P.S.; Pan, J.; Bauerle, M.R.; Almarei, M.; Booker, S.J.; Silakov, A.; Krebs, C.; Boal, A.K.
    Analysis of RNA methylation by phylogenetically diverse Cfr radical S-adenosylmethionine enzymes reveals an iron-binding accessory domain in a clostridial enzyme (2019), Biochemistry, 58, 3169-3184 .
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
C363A mutation in putative metyl-binding residue, substitution alters iron-sulfur cluster stability. Mutant exhibits negligible activity Clostridioides difficile
additional information Cfr contains an additional Cys-rich C-terminal domain that binds a mononuclear Fe2+ ion in a rubredoxin-type Cys4 motif. The C-terminal domain can be truncated with minimal impact on Cfr activity, but the rate of turnover is decreased upon disruption of the Fe2+-binding site by Zn2+ substitution or ligand mutation Clostridioides difficile

Metals/Ions

Metals/Ions Comment Organism Structure
Iron 4.4 mol iron per mol of protein Clostridioides difficile

Organism

Organism UniProt Comment Textmining
Clostridioides difficile
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 S-adenosyl-L-methionine + adenine in 155mer RNA
-
 Clostridioides difficile S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine in 155mer RNA
-
 ?

Synonyms

Synonyms Comment Organism
Cfr
-
 Clostridioides difficile