Full name: Threonylcarbamoyladenosine tRNA methylthiotransferase MtaB
Synonym: YqeV
GI: 1730990
Orf: BSU25430
COG: COG0621
UniProt: P54462
Structures: | |
Complex:
Enzyme type: methyltiotransferase
Position of modification - modification: t:37 - ms2t6A

Comments:

ms2 on t6A has been identified so far only in bacterial U36A37-containing tRNALys (anticodon U*UU, U* stands for a modified U-residue). The B. subtilis TmtB (Yqev) is a radical-SAM methyltransferase that displays two [4Fe-4S] clusters and one TRAM-domain. However, this characteristic tRNA binding motif is not involved in the discrimination of t6A37 or i6A37. A distinct methylthiotransferase (MiaB) is acting on i6A-containing tRNA, and another one (RimO) is acting exclusively on ribosomal protein S12.

Protein sequence:

MATVAFHTLGCKVNHYETEAIWQLFKEAGYERRDFEQTADVYVINTCTVTNTGDKKSRQVIRRAIRQNPDGVICVTGCYAQTSPAEIMAIPGVDIVVGTQ
DREKMLGYIDQYREERQPINGVSNIMKARVYEELDVPAFTDRTRASLKIQEGCNNFCTFCIIPWARGLLRSRDPEEVIKQAQQLVDAGYKEIVLTGIHTG
GYGEDMKDYNFAKLLSELDTRVEGVKRIRISSIEASQITDEVIEVLDRSDKIVNHLHIPIQSGSNTVLKRMRRKYTMEFFADRLNKLKKALPGLAVTSDV
IVGFPGETEEEFMETYNFIKEHKFSELHVFPYSKRTGTPAARMEDQVDENVKNERVHRLIALSDQLAKEYASQYENEVLEIIPEEAFKETEEENMFVGYT
DNYMKVVFKGTEDMIGKIVKVKILKAGYPYNEGQFVRVVEDEITEHMRLSS

Enzymatic activities:

Reaction Substrate Type Position
t6A:ms2t6A tRNA (t) many/many/prokaryotic cytosol 37

Publications:

Title Authors Journal Details PubMed Id DOI
Functional characterization of the YmcB and YqeV tRNA methylthiotransferases of Bacillus subtilis. Anton BP, Russell SP, Vertrees J, Kasif S, Raleigh EA, Limbach PA, Roberts RJ Nucleic Acids Res [details] 20472640 -
Identification of eukaryotic and prokaryotic methylthiotransferase for biosynthesis of 2-methylthio-N6-threonylcarbamoyladenosine in tRNA. Arragain S, Handelman SK, Forouhar F, Wei FY, Tomizawa K, Hunt JF, Douki T, Fontecave M, Mulliez E, Atta M J Biol Chem [details] 20584901 -
The methylthiolation reaction mediated by the Radical-SAM enzymes. Atta M, Arragain S, Fontecave M, Mulliez E, Hunt JF, Luff JD, Forouhar F Biochim Biophys Acta [details] 22178611 -

Links:

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