Information on EC 2.1.1.176 - 16S rRNA (cytosine967-C5)-methyltransferase

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The expected taxonomic range for this enzyme is: Bacteria, Archaea

EC NUMBER
COMMENTARY hide
2.1.1.176
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RECOMMENDED NAME
GeneOntology No.
16S rRNA (cytosine967-C5)-methyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + cytosine967 in 16S rRNA = S-adenosyl-L-homocysteine + 5-methylcytosine967 in 16S rRNA
show the reaction diagram
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:16S rRNA (cytosine967-C5)-methyltransferase
The enzyme specifically methylates cytosine967 at C5 in 16S rRNA.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene TTHA0851 or rsmB
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
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two methyltransferases, RsmB and RsmF, are responsible for all four 5-methylcytidine modifications in 16S rRNA of Thermus thermophilus, overview. RsmB produces m5C967, while RsmF methylates C1400, C1404, and C1407 in a 30S subunit substrate, but only C1400 and C1404 when naked 16S rRNA is the substrate
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + cytosine967 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine967 in 16S rRNA
show the reaction diagram
additional information
?
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substrate recognition mechanism, overview
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + cytosine967 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine967 in 16S rRNA
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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no requirement for added Mg2+, suggesting that extensive secondary or tertiary structure in the RNA substrate may not be a requirement for recognition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00067
cytosine967 in 16S rRNA
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pH 7.5, 37C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.012
cytosine967 in 16S rRNA
Escherichia coli
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pH 7.5, 37C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0558
cytosine967 in 16S rRNA
Escherichia coli
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pH 7.5, 37C
27224
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 47000, SDS-PAGE; x * 47140, calculated from sequence
monomer
two domains and one linker: an N-terminal domain formed by residues 1-145, a C-terminal domain formed by residues 185-448, and an alpha-helical linker formed by residues 146-184
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor diffusion method, crystal structure of Escherichia coli Fmu, determined at 1.65 A resolution for the apoenzyme and 2.1 A resolution in complex with S-adenosyl-L-methionine
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purified wild-type and SeMet-labeled PH0851 complexed with S-adenosyl-L-methionine-analogue sinefungin, hanging drop vapour diffusion method, mixing of protein solution, containing 1.7 mg/ml protein in 20 mM Tris-HCl buffer, pH 8.0, 400 mM NaCl, and 1 mM sinefungin, with reservoir solution, containing 80 mM HEPES-Na buffer, pH 7.0, 1.15 M sodium citrate, and 7-15% w/v 1,6-hexanediol, in a 4:1 ratio, 20C, 1 week, X-ray diffraction structure determination and analysis at 2.55-3.0 A resolution, molecular replacement
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene TTHA0851
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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construction of a null mutant strain in which TTHA0851 is inactivated by homologous recombination and insertion of a heat stable kanamycin-resistance gene
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