Gene Ontology annotation through association of InterPro records with GO terms
An integrative computational model for large-scale identification of metalloproteins in microbial genomes: a focus on iron-sulfur cluster proteins.
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YhcC was predicted and then experimentally validated as a genuine iron-sulfur protein.
"Two newly-identified proteins, YhcC and YdiJ, were functionally validated as genuine iron-sulfur proteins"
The Escherichia coli Radical SAM Enzyme YhcC Substitutes for the FAD-Dependent Oxidase Activity of MnmC in 5-Methylaminomethyl-2-Thiouridine tRNA Modification Under Anaerobic Conditions.
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YhcC is required in vivo for conversion of cmnm5s2U to nm5s2U, and hence for mnm5s2U synthesis, under anaerobic growth, with complementation and a cluster-ligand variant showing the requirement is catalytic.
"we find YhcC is necessary for cmnm5s2U demodification in vivo under anaerobic growth"
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Purified, reconstituted YhcC binds tRNA and catalyses the cmnm5s2U to nm5s2U conversion in a SAM-dependent manner in vitro.
"providing direct in vitro evidence that YhcC catalyzes the cmnm5s2U to nm5s2U reaction on tRNA"
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The authors propose renaming yhcC to mnmL in E. coli and related facultative anaerobes.
"yhcC should be renamed to mnmL in E. coli and in related facultative anaerobes"
Alternate routes to mnm(5)s(2)U synthesis in Gram-positive bacteria.
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MnmL, a YtqA-subgroup radical SAM enzyme, is required for mnm5s2U synthesis in Bacillus subtilis and Streptococcus mutans, acting with the MnmM methylase.
"a member of the YtqA subgroup of the radical Sam superfamily was found to be involved in the synthesis of mnm5s2U in both Bacillus subtilis and Streptococcus mutans"
Compendium of RNA modifications for bacterial stress adaptation.
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A review records that under anaerobiosis the cmnm5U to nm5U conversion in E. coli is catalysed by YhcC, a radical SAM enzyme orthologous to MnmL.
"under anaerobiosis, this reaction is catalyzed by YhcC, a radical SAM-dependent enzyme that is orthologous to MnmL"
UniProtKB entry P0ADW6 (YHCC_ECOLI)