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Information on EC 2.1.1.177 - 23S rRNA (pseudouridine1915-N3)-methyltransferase for references in articles please use BRENDA:EC2.1.1.177Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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The expected taxonomic range for this enzyme is: Escherichia coli
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23S rRNA (pseudouridine1915-N3)-methyltransferase
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S-adenosyl-L-methionine + pseudouridine1915 in 23S rRNA = S-adenosyl-L-homocysteine + N3-methylpseudouridine1915 in 23S rRNA
S-adenosyl-L-methionine + pseudouridine1915 in 23S rRNA = S-adenosyl-L-homocysteine + N3-methylpseudouridine1915 in 23S rRNA
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S-adenosyl-L-methionine + pseudouridine1915 in 23S rRNA = S-adenosyl-L-homocysteine + N3-methylpseudouridine1915 in 23S rRNA
mechanism: the enzyme docks into the ribosomal A site without encroaching into the P site. YbeA makes extensive interface contacts with both the 30S and 50S subunits to align its active site cofactor adjacent to nucleotide C1915
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S-adenosyl-L-methionine:23S rRNA (pseudouridine1915-N3)-methyltransferase
YbeA does not methylate uridine at position 1915 [1].
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m3Psi methyltransferase
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pseudouridine methyltransferase
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Psi1915-specific methyltransferase
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rRNA large subunit methyltransferase H
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SwissProt
brenda
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physiological function
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methylation by YbeA possibly functions as a stamp of approval signifying that the 50S subunit has engaged in translational initiation
malfunction
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the Escherichia coli ybeA gene deletion strain lacks the N3-methylation at position 1915 of 23S rRNA
malfunction
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inactivation of the ybeA gene leads to loss of methylation at nucleotide C1915, loss of ybeA function in Escherichia coli causes a slight slowing of the growth rate
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S-adenosyl-L-methionine + pseudouridine1915 in 23S rRNA
S-adenosyl-L-homocysteine + N3-methylpseudouridine1915 in 23S rRNA
S-adenosyl-L-methionine + pseudouridine1915 in 23S rRNA
S-adenosyl-L-homocysteine + N3-methylpseudouridine1915 in 23S rRNA
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S-adenosyl-L-methionine + pseudouridine1915 in 23S rRNA
S-adenosyl-L-homocysteine + N3-methylpseudouridine1915 in 23S rRNA
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YbeA is acting at the final stage during ribosome assembly, probably during translation initiation
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S-adenosyl-L-methionine + pseudouridine1915 in 23S rRNA
S-adenosyl-L-homocysteine + N3-methylpseudouridine1915 in 23S rRNA
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pseudouridine is the preferred substrate, inability of YbeA to methylate uridine at position 1915. The enzyme requires the intact ribosome and the presence of pseudouridine at position 1915 in 23S rRNA for activity
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S-adenosyl-L-methionine + pseudouridine1915 in 23S rRNA
S-adenosyl-L-homocysteine + N3-methylpseudouridine1915 in 23S rRNA
S-adenosyl-L-methionine + pseudouridine1915 in 23S rRNA
S-adenosyl-L-homocysteine + N3-methylpseudouridine1915 in 23S rRNA
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S-adenosyl-L-methionine + pseudouridine1915 in 23S rRNA
S-adenosyl-L-homocysteine + N3-methylpseudouridine1915 in 23S rRNA
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YbeA is acting at the final stage during ribosome assembly, probably during translation initiation
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Escherichia coli (strain K12);
P0A8I8
Escherichia coli (strain K12);
P0A8I8
Escherichia coli (strain K12);
P0A8I8
Escherichia coli (strain K12);
P0C1V0
Staphylococcus aureus;
P0C1V0
Staphylococcus aureus;
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homodimer
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belongs to the alpha/beta-knot superfamily of proteins that are dimeric in solution. The enzyme folds via an intermediate state populated under equilibrium conditions that is monomeric and considerably structured. The unfolding/refolding kinetics of YbeA involves two phases attributed to the formation of a monomeric intermediate state and a dimerisation step
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recombinant N-terminal His6-tagged YbeA
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Mallam, A.L.; Jackson, S.E.
A comparison of the folding of two knotted proteins: YbeA and YibK
J. Mol. Biol.
366
650-665
2007
Escherichia coli (P0A8I8)
brenda
Ero, R.; Peil, L.; Liiv, A.; Remme, J.
Identification of pseudouridine methyltransferase in Escherichia coli
RNA
14
2223-2233
2008
Escherichia coli, Escherichia coli (P0A8I8)
brenda
Purta, E.; Kaminska, K.H.; Kasprzak, J.M.; Bujnicki, J.M.; Douthwaite, S.
YbeA is the m3Psi methyltransferase RlmH that targets nucleotide 1915 in 23S rRNA
RNA
14
2234-2244
2008
Escherichia coli, Escherichia coli (P0A8I8)
brenda
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