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Information on EC 2.1.1.264 - 23S rRNA (guanine2069-N7)-methyltransferase
for references in articles please use BRENDA:EC2.1.1.264
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EC Tree 2 Transferases
2.1 Transferring one-carbon groups
2.1.1 Methyltransferases
2.1.1.264 23S rRNA (guanine2069-N7)-methyltransferase
IUBMB Comments
The enzyme specifically methylates guanine2069 at position N7 in 23S rRNA. In γ-proteobacteria the enzyme also catalyses EC 2.1.1.173, 23S rRNA (guanine2445-N2)-methyltransferase, while in β-proteobacteria the activities are carried out by separate proteins . The enzyme from the γ-proteobacterium Escherichia coli has RNA unwinding activity as well .
The enzyme appears in viruses and cellular organisms
Reaction Schemes
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guanine2069 in 23S rRNA
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N7-methylguanine2069 in 23S rRNA
Synonyms
sav1081, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3S rRNA m7G2069 methyltransferase
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bifunctional methyltransferase
ribosomal large subunit methyltransferase
rlmK
RlmKL
ycbY
rlmK
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + guanine2069 in 23S rRNA = S-adenosyl-L-homocysteine + N7-methylguanine2069 in 23S rRNA
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:23S rRNA (guanine2069-N7)-methyltransferase
The enzyme specifically methylates guanine2069 at position N7 in 23S rRNA. In gamma-proteobacteria the enzyme also catalyses EC 2.1.1.173, 23S rRNA (guanine2445-N2)-methyltransferase, while in beta-proteobacteria the activities are carried out by separate proteins [1]. The enzyme from the gamma-proteobacterium Escherichia coli has RNA unwinding activity as well [1].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + guanine2069 in 23S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine2069 in 23S rRNA
S-adenosyl-L-methionine + guanine2069 in 23S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine2069 in 23S rRNA
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Substrates: RlmK activity in helix 74 of Escherichia coli 23S rRNA
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine2069 in 23S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine2069 in 23S rRNA
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Substrates: RlmK activity in helix 74 of Escherichia coli 23S rRNA, methylation sites in the peptidyl transferase region of Escherichia coli 23S rRNA. structure, overview
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine2069 in 23S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine2069 in 23S rRNA
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Substrates: RlmK activity in helix 74 of Escherichia coli 23S rRNA
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine2069 in 23S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine2069 in 23S rRNA
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Substrates: RlmK activity in helix 74 of Escherichia coli 23S rRNA, methylation sites in the peptidyl transferase region of Escherichia coli 23S rRNA. structure, overview
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine2069 in 23S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine2069 in 23S rRNA
Substrates: RlmK activity in helix 74 of Escherichia coli 23S rRNA
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine2069 in 23S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine2069 in 23S rRNA
Substrates: RlmK activity in helix 74 of Escherichia coli 23S rRNA
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine2069 in 23S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine2069 in 23S rRNA
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Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine2069 in 23S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine2069 in 23S rRNA
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Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine2069 in 23S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine2069 in 23S rRNA
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Substrates: methylation sites in the peptidyl transferase region of Escherichia coli 23S rRNA. structure, overview
Products: -
Products: -
?
additional information
?
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Substrates: the enzyme also catalyzes the N2-methylation of guanine2445 in 23S rRNA, RlmL activity, reaction of EC 2.1.1.173
Products: -
Products: -
?
additional information
?
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Substrates: the bifunctional methyltransferase YcbY, i.e. RlmKL, adds the m7G2069 and m2G2445 modifications in Escherichia coli 23S rRNA, recognition of dual rRNA targets by YcbY
Products: -
Products: -
?
additional information
?
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Substrates: the enzyme also catalyzes the N2-methylation of guanine2445 in 23S rRNA, RlmL activity, reaction of EC 2.1.1.173. Product identification by mass spectrometry
Products: -
Products: -
?
additional information
?
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Substrates: the bifunctional methyltransferase YcbY, i.e. RlmKL, adds the m7G2069 and m2G2445 modifications in Escherichia coli 23S rRNA, recognition of dual rRNA targets by YcbY
Products: -
Products: -
?
additional information
?
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Substrates: the enzyme also catalyzes the N2-methylation of guanine2445 in 23S rRNA, RlmL activity, reaction of EC 2.1.1.173. Product identification by mass spectrometry
Products: -
Products: -
?
additional information
?
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Substrates: the enzyme also catalyzes the N2-methylation of guanine2445 in 23S rRNA, reaction of EC 2.1.1.173
Products: -
Products: -
?
additional information
?
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Substrates: Smu472 does not target G2445, and this nucleotide remains unmodified in Gram-positive rRNAs. Product identification by mass spectrometry
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + guanine2069 in 23S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine2069 in 23S rRNA
S-adenosyl-L-methionine + guanine2069 in 23S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine2069 in 23S rRNA
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Substrates: RlmK activity in helix 74 of Escherichia coli 23S rRNA
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine2069 in 23S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine2069 in 23S rRNA
-
Substrates: RlmK activity in helix 74 of Escherichia coli 23S rRNA
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine2069 in 23S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine2069 in 23S rRNA
Substrates: RlmK activity in helix 74 of Escherichia coli 23S rRNA
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine2069 in 23S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine2069 in 23S rRNA
Substrates: RlmK activity in helix 74 of Escherichia coli 23S rRNA
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine2069 in 23S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine2069 in 23S rRNA
-
Substrates: -
Products: -
Products: -
?
additional information
?
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Substrates: the enzyme also catalyzes the N2-methylation of guanine2445 in 23S rRNA, RlmL activity, reaction of EC 2.1.1.173
Products: -
Products: -
?
additional information
?
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Substrates: the bifunctional methyltransferase YcbY, i.e. RlmKL, adds the m7G2069 and m2G2445 modifications in Escherichia coli 23S rRNA, recognition of dual rRNA targets by YcbY
Products: -
Products: -
?
additional information
?
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Substrates: the bifunctional methyltransferase YcbY, i.e. RlmKL, adds the m7G2069 and m2G2445 modifications in Escherichia coli 23S rRNA, recognition of dual rRNA targets by YcbY
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
physiological function
evolution
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SAV1081 belongs to te cluster of orthologous groups (COG) 1092, functional classification, overview
evolution
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the enzyme is a member of the COG1092 family, evolutionary implications of the apparent emergence of Escherichia coli YcbY from the fusion of Streptococcus mutans Smu472 and Smu776 orthologues are considered, Streptococcus mutans proteins Smu472 and Smu776 are respectively Gram-positive orthologs of the N- and C-halves of YcbY
evolution
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the enzyme is a member of the COG1092 family, evolutionary implications of the apparent emergence of Escherichia coli YcbY from the fusion of Streptococcus mutans Smu472 and Smu776 orthologues are considered, Streptococcus mutans proteins Smu472 and Smu776 are respectively Gram-positive orthologs of the N- and C-halves of YcbY
evolution
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the enzyme is a member of the COG1092 family, evolutionary implications of the apparent emergence of Escherichia coli YcbY from the fusion of Streptococcus mutans Smu472 and Smu776 orthologues are considered, Streptococcus mutans proteins Smu472 and Smu776 are respectively Gram-positive orthologs of the N- and C-halves of YcbY
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malfunction
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Neisseria meningitidis rlmL and rlmK homologues rescue m2G2445 and m7G2069 formation, respectively, in the Escherichia coli DELTArlmKL strain
malfunction
Neisseria meningitidis rlmL and rlmK homologues rescue m2G2445 and m7G2069 formation, respectively, in the Escherichia coli DELTArlmKL strain, overview
malfunction
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Neisseria meningitidis rlmL and rlmK homologues rescue m2G2445 and m7G2069 formation, respectively, in the Escherichia coli DELTArlmKL strain, overview
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physiological function
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rlmKL encodes a fused methyltransferase responsible for forming both m7G2069 and m2G2445, the N-terminal RlmL activity for m2G2445 formation is significantly enhanced by the C-terminal RlmK. RlmKL has an unwinding activity of Helix 74, facilitating cooperative methylations of m7G2069 and m2G2445 during biogenesis of 50S subunit. For unwinding single-stranded RNA is a good substrate for RlmKL, substrate speccificity, overview. RlmKL is involved in the efficient assembly of 50S subunit in a mutant strain lacking an RNA helicase deaD
physiological function
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the YcbY enzyme is a methyltransferase catalyzing two mechanistically different types of RNA modification. The N-terminal region of YcbY adds the m2G2445 modification, while the C-terminal region of YcbY is responsible for the m7G2069 methylation on the opposite side of the same helix, H74. YcbY enzyme is an example of a methyltransferase catalyzing two mechanistically different types of RNA modification
physiological function
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the YcbY enzyme is a methyltransferase catalyzing two mechanistically different types of RNA modification. The N-terminal region of YcbY adds the m2G2445 modification, while the C-terminal region of YcbY is responsible for the m7G2069 methylation on the opposite side of the same helix, H74. YcbY enzyme is an example of a methyltransferase catalyzing two mechanistically different types of RNA modification
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Show AA Sequence and Transmembrane Helices (4026 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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structure comparisons with Streptococcus mutans proteins Smu472 and Smu776, the active site and their folding patterns respectively resemble each other, overview
additional information
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structure comparisons with Streptococcus mutans proteins Smu472 and Smu776, the active site and their folding patterns respectively resemble each other, overview
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additional information
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structure comparisosns of Streptococcus mutans proteins Smu472 and Smu776 with Escherichia coli RlmKL protein, the active site and their folding patterns respectively resemble each other, overview
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant YcbY, in presence of S-adenosyl-L-methionine and S-adenosyl-L-homocysteine, hanging drop or sitting drop vapor diffusion method, 16°C, X-ray diffraction structure determination and analysis
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purified recombinant Smu472, in presence of S-adenosyl-L-methionine and S-adenosyl-L-homocysteine, hanging drop or sitting drop vapor diffusion method, 16°C, X-ray diffraction structure determination and analysis
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D195A
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site-directed mutagenesis, the mutation does not affect the methylation activity
D568A
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site-directed mutagenesis, the D568A mutation in the C-terminal domain does not rescue m7G2069 formation, but m2G2445 is efficiently formed in this mutant
D597A
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site-directed mutagenesis, the mutation does not affect the methylation activity
N309A
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site-directed mutagenesis, the N309A mutation in the NTD impairs m2G2445 formation, but rescues m7G2069 formation
N397A
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site-directed mutaagenesis, the N397A mutant exhibits no m2G2445 formation but rescues m7G2069 formation
R530A
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site-directed mutagenesis, the mutation does not affect the methylation activity
additional information
additional information
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generation of a ycbY knock-out strain, completely inactive in methylation, from Escherichia coli strain BW25113 and complementation with active ycbY
additional information
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generation of a ycbY knock-out strain, completely inactive in methylation, from Escherichia coli strain BW25113 and complementation with active ycbY
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged Smu472 from Escherichiac coli strain BL21(DE3) by nickel affinity chromatography
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recombinant His-tagged YcbY from Escherichiac coli strain BL21(DE3) by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene rlmL, renamed rlmKL, encodes a fused methyltransferase responsible for forming both m7G2069 and m2G2445
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gene ycbY, DNA and amino acid sequence determination and analysis, expression of His-tagged YcbY in Escherichiac coli strain BL21(DE3)
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kimura, S.; Ikeuchi, Y.; Kitahara, K.; Sakaguchi, Y.; Suzuki, T.; Suzuki, T.
Base methylations in the double-stranded RNA by a fused methyltransferase bearing unwinding activity
Nucleic Acids Res.
40
4071-4085
2012
Escherichia coli, Neisseria meningitidis (Q9JYY8), Neisseria meningitidis MC58 (Q9JYY8)
brenda
Wang, K.T.; Desmolaize, B.; Nan, J.; Zhang, X.W.; Li, L.F.; Douthwaite, S.; Su, X.D.
Structure of the bifunctional methyltransferase YcbY (RlmKL) that adds the m7G2069 and m2G2445 modifications in Escherichia coli 23S rRNA
Nucleic Acids Res.
40
5138-5148
2012
Escherichia coli, Escherichia coli BW25113, Streptococcus mutans
brenda
Kita, S.; Tanaka, Y.; Hirano, N.; Kimura, S.; Suzuki, T.; Suzuki, T.; Yao, M.; Tanaka, I.
Crystal structure of a putative methyltransferase SAV1081 from Staphylococcus aureus
Protein Pept. Lett.
20
530-537
2013
Staphylococcus aureus
brenda
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