Protein Summary

CmoA from Haemophilus influenzae

Full name: tRNA (cmo5U34)-methyltransferase
Synonym: YecO
GI: 16272273
COG: COG2226
UniProt: P43985
Structures: | 1IM8 |
Enzyme type: methyltransferase
Position of modification - modification: t:34 - cmo5U


In E. coli CmoA is involved in conversion of ho5U to cmo5U (addition of carboxymethyl group) in tRNA. It transforms S-AdoMet and prephenate into carboxy-S-adenosyl-L-methionine (Cx-SAM) and phenyl pyruvate. Cx-SAM is the carboxymethyl group donor in the next reaction catalyzed by CmoB. Null mutation of CmoA results in the accumulation of tRNA containing mo5U34 and ho5U34. CmoA (YecO) is paralogous to AdoMet-dependent methyltransferases YgdE and FtsJ. A metabolic link exists between the biosynthesis of cmo5U and the biosynthesis of aromatic amino acids Tyr and Phe via the chorismic acid. Of note, no homolog of CmoA exists in B. subtilis, attesting that the enzymatic formation of mo5U34 in tRNA of this organism probably follows another mechanism than in E. coli.

Protein sequence:



Title Authors Journal Details PubMed Id DOI
The modified wobble nucleoside uridine-5-oxyacetic acid in tRNAPro(cmo5UGG) promotes reading of all four proline codons in vivo. Nasvall SJ, Chen P, Bjork GR RNA [details] 15383682 -
The wobble hypothesis revisited: uridine-5-oxyacetic acid is critical for reading of G-ending codons. Nasvall SJ, Chen P, Bjork GR RNA [details] 17942742 -
Crystal structure of YecO from Haemophilus influenzae (HI0319) reveals a methyltransferase fold and a bound S-adenosylhomocysteine. Lim K, Zhang H, Tempczyk A, Bonander N, Toedt J, Howard A, Eisenstein E, Herzberg O Proteins [details] 11746687 -
A novel link between the biosynthesis of aromatic amino acids and transfer RNA modification in Escherichia coli. Bjork GR J Mol Biol [details] 6160251 -

Last modification of this entry: 2013-06-21 13:27:19.970681
Edited by a user: magda
Edited content: Changed comments.