Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.1.1.266 - 23S rRNA (adenine2030-N6)-methyltransferase and Organism(s) Escherichia coli and UniProt Accession P37634

for references in articles please use BRENDA:EC2.1.1.266
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
The recombinant RlmJ protein is most active in methylating deproteinized 23S ribosomal subunit, and does not methylate the completely assembled 50S subunits .
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Escherichia coli
UNIPROT: P37634
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
hide
S-adenosyl-L-methionine
+
adenine2030 in 23S rRNA
=
S-adenosyl-L-homocysteine
+
N6-methyladenine2030 in 23S rRNA
+
adenine2030 in 23S rRNA
=
+
N6-methyladenine2030 in 23S rRNA
Synonyms
ribosomal rna large subunit methyltransferase j, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23S rRNA methyltransferase
-
adenine-N6 methyltransferase
-
ribosomal RNA large subunit methyltransferase J
UniProt
rRNA m6A methyltransferase
-
m6A2030 methyltransferase
-
-
YhiR protein
-
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:23S rRNA (adenine2030-N6)-methyltransferase
The recombinant RlmJ protein is most active in methylating deproteinized 23S ribosomal subunit, and does not methylate the completely assembled 50S subunits [1].
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 + adenine2030 in 23S rRNA
S-adenosyl-L-homocysteine + N6-methyladenine2030 in 23S rRNA
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL 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 + adenine2030 in 23S rRNA
S-adenosyl-L-homocysteine + N6-methyladenine2030 in 23S rRNA
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the active site of RlmJ with motif IV sequence 164DPPY167 is more similar to DNA m6A MTases than to RNA m6 2A MTases, and structural comparison suggests that RlmJ binds its substrate base similarly to DNA MTases T4Dam and M.TaqI
malfunction
physiological function
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant C-terminally His6-tagged enzyme, sitting drop vapour diffusion method, mixing of 0.0015 ml of protein solution with an equal amount of reservoir solution containing 0.2 M sodium sulfate decahydrate, 0.1 M Tris-HCl pH 8.5, 30% w/v PEG 4000, and equilibration against 0.08 ml of reservoir solution, 8 days, 20°C, X-ray diffraction strucure determination and analysis at 1.8 A resolution
purified recombinant enzyme in apoform, in complex with the cofactor S-adenosyl-L-methionine, or with product S-adenosyl-L-homocysteine plus substrate analogue AMP, X-ray diffraction structure determination and analysis at 1.85-2.0 A resolution, enzyme apostructure analysis using PDB ID 2OO3, rigid-body refinement of the RlmJAPO structure against the RlmJSAM data
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D164A
site-directed mutagenesis
H6D
site-directed mutagenesis
K18A
site-directed mutagenesis
K18R
site-directed mutagenesis
Y4A
site-directed mutagenesis
Y4F
site-directed mutagenesis
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, ultrafiltration, and gel filtration
recombinant wild-type and mutant enzymes
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene rlmJ, sequence comparisons, recombinant expression of wild-type and mutant enzymes
gene yhiR, expression as C-terminally His6-tagged protein in escherichia coli strain AG1
gene yhiR, recombinant expresssion of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Golovina, A.Y.; Dzama, M.M.; Osterman, I.A.; Sergiev, P.V.; Serebryakova, M.V.; Bogdanov, A.A.; Dontsova, O.A.
The last rRNA methyltransferase of E. coli revealed: The yhiR gene encodes adenine-N6 methyltransferase specific for modification of A2030 of 23S ribosomal RNA
RNA
18
1725-1734
2012
Escherichia coli, Escherichia coli (P37634)
Manually annotated by BRENDA team
Punekar, A.S.; Selmer, M.
Purification, crystallization and preliminary X-ray diffraction analysis of the 23S rRNA methyltransferase RlmJ from Escherichia coli
Acta Crystallogr. Sect. F
69
1001-1003
2013
Escherichia coli (P37634)
Manually annotated by BRENDA team
Punekar, A.; Liljeruhm, J.; Shepherd, T.; Forster, A.; Selmer, M.
Structural and functional insights into the molecular mechanism of rRNA m6A methyltransferase RlmJ
Nucleic Acids Res.
41
9537-9548
2013
Escherichia coli (P37634), Escherichia coli
Manually annotated by BRENDA team