Information on EC 2.1.1.309 - 18S rRNA (guanine1575-N7)-methyltransferase

Word Map on EC 2.1.1.309
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.1.1.309
-
RECOMMENDED NAME
GeneOntology No.
18S rRNA (guanine1575-N7)-methyltransferase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + guanine1575 in 18S rRNA = S-adenosyl-L-homocysteine + N7-methylguanine1575 in 18S rRNA
show the reaction diagram
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:18S rRNA (guanine1575-N7)-methyltransferase
The enzyme, found in eukaryotes, is involved in pre-rRNA processing. The numbering corresponds to the enzyme from the yeast Saccharomyces cerevisiae [1].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
WBS22; gene WBSCR22
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
-
Bud23 and Trm112 interact through formation of a beta-zipper involving main-chain atoms, burying an important hydrophobic surface and stabilizing the complex. The structures reveal that the coactivator Trm112 undergoes an induced fit to accommodate its methyltransferase (MTase) partner, identification of Bud23 residues important for Bud23-Trm112 complex formation and recruitment to pre-ribosomes
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 + guanine10 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine10 in tRNA
show the reaction diagram
S-adenosyl-L-methionine + guanine1575 in 18S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine1575 in 18S rRNA
show the reaction diagram
additional information
?
-
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 + guanine10 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine10 in tRNA
show the reaction diagram
S-adenosyl-L-methionine + guanine1575 in 18S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine1575 in 18S rRNA
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
additional information
a multifunctional methyltransferase subunit TRM112-like protein with methyltransferase activity participates both in methylation of protein and tRNA species. TRMT112 is required for WBSCR22 metabolic stability
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
TRM112
-
Trm112 is a small zinc finger protein of 15 kDa which acts as a coactivator of several class I S-adenosyl-L-methionine (SAM)-dependent MTases. Trm112 interacts directly with Bud23 in vitro and that it is absolutely required for Bud23 stability in vivo. Trm112 increases the solubility of Bud23
-
TRMT112
a multifunctional methyltransferase subunit TRM112-like protein with methyltransferase activity, it participates both in methylation of protein and tRNA species. TRMT112 is required for WBSCR22 metabolic stability
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
analysis of crystal structures of Bud23-Trm112 MTase complexes, overview
-
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Trm112 interacts directly with Bud23 in vitro and that it is required for Bud23 stability in vivo
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
tandem purification of recombinant His6-tagged Bud23 with untagged Trm112 by nickel affinity chromatography from Escherichia coli, Trm112 increases the solubility of Bud23
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant co-expression of His6-tagged Bud23 with untagged Trm112 in Escherichia coli
-
recombinant expression of wild-type and mutant enzymes
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D112A
-
site-directed mutagenesis
D112R
-
site-directed mutagenesis, methylation inactive mutant
D77A
-
site-directed mutagenesis, methylation inactive mutant, 25% remaining S-adenosyl-L-methionine binding activity
D94A
-
site-directed mutagenesis
D94R
-
site-directed mutagenesis
E18A
-
site-directed mutagenesis
I31W
-
site-directed mutagenesis, methylation inactive mutant, 25% remaining S-adenosyl-L-methionine binding activity
K21E/R27E
-
site-directed mutagenesis, methylation inactive mutant
M96A
-
site-directed mutagenesis
S118E
-
site-directed mutagenesis, methylation and S-adenosyl-L-methionine binding inactive mutant
S118R
-
site-directed mutagenesis, methylation and S-adenosyl-L-methionine binding inactive mutant
W122A
-
site-directed mutagenesis, methylation inactive mutant
Y159A
-
site-directed mutagenesis, methylation inactive mutant, 50% remaining S-adenosyl-L-methionine binding activity
Y22A
-
site-directed mutagenesis, methylation inactive mutant
additional information