Information on EC 2.1.1.209 - 23S rRNA (guanine2535-N1)-methyltransferase

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The expected taxonomic range for this enzyme is: Streptomyces viridochromogenes

EC NUMBER
COMMENTARY hide
2.1.1.209
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RECOMMENDED NAME
GeneOntology No.
23S rRNA (guanine2535-N1)-methyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + guanine2535 in 23S rRNA = S-adenosyl-L-homocysteine + N1-methylguanine2535 in 23S rRNA
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:23S rRNA (guanine2535-N1)-methyltransferase
Streptomyces viridochromogenes produces the antibiotic avilamycin A which binds to the 50S ribosomal subunit to inhibit protein synthesis. To protect itself from the antibiotic, Streptomyces viridochromogenes utilizes two methyltransferases, 23S rRNA (guanine2535-N1)-methyltransferase and EC 2.1.1.208 [23S rRNA (uridine2479-2-O)-methyltransferase], whose actions confer avilamycin resistance to the RNA.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain Tü57
UniProt
Manually annotated by BRENDA team
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 + guanine2535 in 23S rRNA
S-adenosyl-L-homocysteine + N1-methylguanine2535 in 23S rRNA
show the reaction diagram
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 + guanine2535 in 23S rRNA
S-adenosyl-L-homocysteine + N1-methylguanine2535 in 23S rRNA
show the reaction diagram
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour-diffusion method at 20°C. 1.5 A crystal structure
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified as fusion protein
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Streptomyces lividans TK66 or Escherichia coli
expression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
I11SeMet/L239SeMet
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as active as wild-type enzyme
I11SeMet/L246SeMet
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as active as wild-type enzyme
L173SeMet/L239SeMet
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as active as wild-type enzyme
L239SeMet/L246SeMet
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as active as wild-type enzyme