Protein Summary

CmoA from Escherichia coli

Full name: tRNA (uridine-5-oxyacetic acid methyl ester)(34) synthase
Synonym: YecO
GI: 3025151
Orf: b1870
COG: COG2226
UniProt: P76290
Structures: | 4GEK | 4IWN |
Complex:
Enzyme type: methyltransferase
Position of modification - modification: t:34 - cmo5U
t:34 - mcmo5U

Comments:

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:

MSHRDTLFSAPIARLGDWTFDERVAEVFPDMIQRSVPGYSNIISMIGMLA
ERFVQPGTQVYDLGCSLGAATLSVRRNIHHDNCKIIAIDNSPAMIERCRR
HIDAYKAPTPVDVIEGDIRDIAIENASMVVLNFTLQFLEPSERQALLDKI
YQGLNPGGALVLSEKFSFEDAKVGELLFNMHHDFKRANGYSELEISQKRS
MLENVMLTDSVETHKARLHNAGFEHSELWFQCFNFGSLVALKAEDAA

Publications

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 -
A novel link between the biosynthesis of aromatic amino acids and transfer RNA modification in Escherichia coli. Bjork GR J Mol Biol [details] 6160251 -
Structure-guided discovery of the metabolite carboxy-SAM that modulates tRNA function. Kim J, Xiao H, Bonanno JB, Kalyanaraman C, Brown S, Tang X, Al-Obaidi NF, Patskovsky Y, Babbitt PC, Jacobson MP, Lee YS, Almo SC... Nature [details] 23676670 -
S-Adenosyl-S-carboxymethyl-L-homocysteine: a novel cofactor found in the putative tRNA-modifying enzyme CmoA. Byrne RT, Whelan F, Aller P, Bird LE, Dowle A, Lobley CM, Reddivari Y, Nettleship JE, Owens RJ, Antson AA, Waterman DG... Acta Crystallogr D Biol Crystallogr [details] 23695253 -

Links

_EcoCyc_
_PubMed_

Last modification of this entry: 2013-06-21 13:27:00.863976
Edited by a user: magda
Edited content: Changed comments.