ExplorEnz: EC 2.1.1.257

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2.1.1.257

Accepted name:

tRNA (pseudouridine⁵⁴-N¹)-methyltransferase

Reaction:

S-adenosyl-L-methionine + pseudouridine⁵⁴ in tRNA = S-adenosyl-L-homocysteine + N¹-methylpseudouridine⁵⁴ in tRNA

Other name(s):

TrmY; m¹Ψ methyltransferase

Systematic name:

S-adenosyl-L-methionine:tRNA (pseudouridine⁵⁴-N¹)-methyltransferase

Comments:

While this archaeal enzyme is specific for the 54 position and does not methylate pseudouridine at position 55, the presence of pseudouridine at position 55 is necessary for the efficient methylation of pseudouridine at position 54 [2,3].

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Chen, H.Y. and Yuan, Y.A. Crystal structure of Mj1640/DUF358 protein reveals a putative SPOUT-class RNA methyltransferase. J. Mol. Cell. Biol. 2 (2010) 366–374. [DOI] [PMID: 21098051]
2.	Wurm, J.P., Griese, M., Bahr, U., Held, M., Heckel, A., Karas, M., Soppa, J. and Wohnert, J. Identification of the enzyme responsible for N¹-methylation of pseudouridine 54 in archaeal tRNAs. RNA 18 (2012) 412–420. [DOI] [PMID: 22274954]
3.	Chatterjee, K., Blaby, I.K., Thiaville, P.C., Majumder, M., Grosjean, H., Yuan, Y.A., Gupta, R. and de Crecy-Lagard, V. The archaeal COG1901/DUF358 SPOUT-methyltransferase members, together with pseudouridine synthase Pus10, catalyze the formation of 1-methylpseudouridine at position 54 of tRNA. RNA 18 (2012) 421–433. [DOI] [PMID: 22274953]

[EC 2.1.1.257 created 2012]