Information on EC 2.1.1.178 - 16S rRNA (cytosine1407-C5)-methyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.1.1.178
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RECOMMENDED NAME
GeneOntology No.
16S rRNA (cytosine1407-C5)-methyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + cytosine1407 in 16S rRNA = S-adenosyl-L-homocysteine + 5-methylcytosine1407 in 16S rRNA
show the reaction diagram
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:16S rRNA (cytosine1407-C5)-methyltransferase
The enzyme specifically methylates cytosine1407 at C5 in 16S rRNA.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
i.e. strain BB1074, gene rsmF
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Manually annotated by BRENDA team
gene TTHA1387 or rsmF
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
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. C1400 and C1404 are sufficiently buried in the mature ribosome structure so require extensive unfolding of the rRNA to be accessible to RsmF
physiological function
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 + cytosine1400 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine1400 in 16S rRNA
show the reaction diagram
S-adenosyl-L-methionine + cytosine1404 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine1404 in 16S rRNA
show the reaction diagram
S-adenosyl-L-methionine + cytosine1407 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine1407 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 + cytosine1400 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine1400 in 16S rRNA
show the reaction diagram
Q5SJI2
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?
S-adenosyl-L-methionine + cytosine1404 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine1404 in 16S rRNA
show the reaction diagram
Q5SJI2
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?
S-adenosyl-L-methionine + cytosine1407 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine1407 in 16S rRNA
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
16S rRNA methyltransferase NpmA
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additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.6
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
54000
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x * 54000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 54000, SDS-PAGE
additional information
comparison of Thermus thermophilus RsmB and RsmF protein sequences, secondary and tertiary structure, differences in substrate binding, overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
YebU crystals are grown at room temperature by the hanging-drop, vapour-diffusion method, Crystal structure solved at 2.9 A resolution. The enzyme has an N-terminal catalytic domain that binds S-adenosylmethionine. The C-terminal domain has structural similarity to PUA domains of pseudouridine synthases and archaeosine-specific transglycosylases. The YebU structure is used to propose the most likely mechanism for its substrate specificity and recognition
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RsmF in a complex with cofactor S-adenosyl-methionine, three crystal structures, X-ray diffrcation structure determination and analysis at 1.3 A resolution
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60 - 70
no difference in the relative growth proportions of the wild-type and rsmF mutant at 70C. However, at 60C, the rsmF null mutant constitutes only around 5% of the population, and at 80C the rsmF null mutant is unable to grow at all
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene rsmF, expression of wild-type enzyme in Escherichi coli Top10 cells
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the Escherichia coli YebU gene is cloned into the PT73.3HisGW vector.25 The resulting construct encodes a polypeptide with the YebU gene and both N- and C-terminal hexa-histidine tails
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the yebU gene is cloned as a partial and as a fulllength sequence with the respective purposes of creating a knockout strain and expressing recombinant YebU protein. Full-length YebU protein with a C-terminal histidine-tag is expressed in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Show AA Sequence (1442 entries)
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