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Enzyme Nomenclature
Information on EC 2.1.1.177 - 23S rRNA (pseudouridine1915-N3)-methyltransferase
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The expected taxonomic range for this enzyme is: Escherichia coli
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EC NUMBER 
COMMENTARY 
2.1.1.177
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RECOMMENDED NAME
GeneOntology No.
23S rRNA (pseudouridine1915-N3)-methyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:23S rRNA (pseudouridine1915-N3)-methyltransferase
YbeA does not methylate uridine at position 1915 [1].
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
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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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
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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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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LINKS TO OTHER DATABASES (specific for EC-Number 2.1.1.177)
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