EC Number   |
General Information |
Reference |
|---|
   2.1.1.228 | evolution |
archaeal Trm5a, a member of the archaeal Trm5a/b/c family of enzymes involved in the biosynthesis of the wyosine derivatives, division of the family aTrm5 into three subfamilies aTrm5a (further divided into Taw21 and Taw22 which are monofunctional and bifunctional aTrm5a), aTrm5b, and aTrm5c. While the enzymes belonging to these subfamilies do not significantly differ in their AdoMet-binding site, small differences have been observed within the NPPY motif, which, in certain amino-methyltransferases, is involved in the positioning of the target nitrogen atom. In contrast, the N-terminal sequences of the aforementioned enzymes differ substantially, e.g. a small conservative domain called D1 is present in aTrm5b and aTrm5c but absent in most of the aTrm5a proteins. Evolution of tRNAPhe:imG2 methyltransferases involved in the biosynthesis of wyosine derivatives in Archaea. Amino acid sequence alignment of Trm5a/b/c family of proteins. Monofunctional and bifunctional aTrm5a enzymes, overview |
758324 |
| 2.1.1.228 | evolution |
archaeal Trm5a, a member of the archaeal Trm5a/b/c family of enzymes involved in the biosynthesis of the wyosine derivatives, division of the family aTrm5 into three subfamilies aTrm5a (further divided into Taw21 and Taw22 which are monofunctional and bifunctional aTrm5a), aTrm5b, and aTrm5c. While the enzymes belonging to these subfamilies do not significantly differ in their AdoMet-binding site, small differences have been observed within the NPPY motif, which, in certain amino-methyltransferases, is involved in the positioning of the target nitrogen atom. In contrast, the N-terminal sequences of the aforementioned enzymes differ substantially, e.g. a small conservative domain called D1 is present in aTrm5b and aTrm5c but absent in most of the aTrm5a proteins. Evolution of tRNAPhe:imG2 methyltransferases involved in the biosynthesis of wyosine derivatives in Archaea. Amino acid sequence alignment of Trm5a/b/c/ family of proteins. Monofunctional and bifunctional aTrm5a enzymes, overview |
-, 758324 |
| 2.1.1.228 | evolution |
at least 5 classes (class I-V) of structurally distinct AdoMet-dependent methyltransferases have been identified. Trm5 belongs to the class I tRNA methyl transferases. Trm5 is an active monomer that uses the class I-fold. Methanococcus jannaschii MjTrm5 is homologous to human Trm5 |
757582 |
| 2.1.1.228 | evolution |
at least 5 classes (class I-V) of structurally distinct AdoMet-dependent methyltransferases have been identified. Trm5 belongs to the class I tRNA methyl transferases. Trm5 is an active monomer that uses the class I-fold. MjTrm5 is homologous to human Trm5 |
-, 757582 |
| 2.1.1.228 | evolution |
at least 5 classes (class I-V) of structurally distinct AdoMet-dependent methyltransferases have been identified. TrmD belongs to the class IV tRNA methyl transferases. TrmD is an obligated dimer that uses the class IV-fold for AdoMet binding. EcTrmD is homologous to Haemophilus influenza TrmD |
757582 |
| 2.1.1.228 | evolution |
at least 5 classes (class I-V) of structurally distinct AdoMet-dependent methyltransferases have been identified. TrmD belongs to the class IV tRNA methyl transferases. TrmD is an obligated dimer that uses the class IV-fold for AdoMet binding. Escherichia coli EcTrmD is homologous to Haemophilus influenza TrmD |
-, 757582 |
| 2.1.1.228 | evolution |
during the evolutionary process, some euryarchaeota like Thermococcus and Pyrococcus preserved both the trm5 genes from the crenarchaeal origin as well as the native copy, but others apparently lost the latter. Phylogenetic distribution analyses of trm5 homologues in archaeal genomes allow the identification of three archaeal Trm5 (aTrm5) subfamilies: Trm5a, Trm5b, and Trm5c. Trm5b refers to the native form, while Trm5a refers to the crenarchaeal origin, and Trm5c to other members with divergent Trm5 sequences11. The three Trm5s differ substantially in primary sequences |
758376 |
| 2.1.1.228 | evolution |
in the bacterial domain, the biosynthesis of m1G37 is catalyzed by the tRNA methyltransferase TrmD, whereas in the eukaryotic and archaeal domains, it is catalyzed by Trm5. While both TrmD and Trm5 perform the same methyl transfer reaction, using S-adenosyl methionine (AdoMet) as the methyl donor, they are fundamentally different in structure, where TrmD is a member of the SpoU-TrmD family and Trm5 is a member of the Rossmann-fold family. TrmD and Trm5 also differ in virtually all aspects of the reaction mechanism |
-, 756774 |
| 2.1.1.228 | evolution |
phylogenetic analyses revealed that the archaeal Trm5s can be grouped into three categories: Trm5a, Trm5b, and Trm5c, which all perform the N1-methylation of tRNAPhe G37. Trm5a exists in all crenarchaea. On the other hand, Trm5b is ubiquitously found in euryarchaeota, and is regarded as the original Trm5. Trm5c can be originated from euryarchaeota by horizontal gene transfer and exists in two crenarchaeal orders. In addition, both aTrm5b and aTrm5c contain an N-terminal domain named D1, which is responsible for the G19:C56 base pair recognition but may be absent from most aTrm5as. Despite the differences at the N-termini, all Trm5s have the Rossmann fold at the C-termini for catalysis, with the consensus NPPY motif located in the fourth beta-strand. The motif is known to position the nitrogen atom of G37 from the substrate, but specific sequences may vary from this consensus. Structure comparison of Methanococcus jannaschii MjTrm5b and PaTrm5b, overview |
755960 |
| 2.1.1.228 | evolution |
the dedication of Mg2+ to rate enhancement separates TrmD from O- and N6-methyl transferases. TrmD shows the topologically knotted protein fold |
735927 |
