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Information on EC 2.1.1.230 - 23S rRNA (adenosine1067-2'-O)-methyltransferase and Organism(s) Streptomyces actuosus and UniProt Accession P52391

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IUBMB Comments
The methylase that is responsible for autoimmunity in the thiostrepton producer Streptomyces azureus, renders ribosomes completely resistant to thiostrepton .
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This record set is specific for:
Streptomyces actuosus
UNIPROT: P52391
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Word Map
The taxonomic range for the selected organisms is: Streptomyces actuosus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
nosiheptide-resistance methyltransferase, thiostrepton-resistance methyltransferase, nhr protein, nosiheptide resistance methyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nosiheptide resistance methyltransferase
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nosiheptide-resistance methyltransferase
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:23S rRNA (adenosine1067-2'-O)-methyltransferase
The methylase that is responsible for autoimmunity in the thiostrepton producer Streptomyces azureus, renders ribosomes completely resistant to thiostrepton [2].
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 + adenosine1067 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyladenosine1067 in 23S rRNA
show the reaction diagram
S-adenosyl-L-methionine + adenosine1067 in Escherichia coli 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyladenosine1067 in Escherichia coli 23S rRNA
show the reaction diagram
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-
-
?
additional information
?
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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 + adenosine1067 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyladenosine1067 in 23S rRNA
show the reaction diagram
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-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NSHR_STRAS
274
0
29184
Swiss-Prot
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
SDS-PAGE and gel filtration
homodimer
dimerization is required for methyltransferase activity
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of the enzyme and the enzyme in complex with S-adenosyl-L-methionine at 2.0 and 2.1 A resolution, respectively
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D36A
mutation significantly decreases activity
E220Q
mutant has 10% of activity compared to wild-type enzyme
E35A
mutation significantly decreases activity
E91A
mutation significantly decreases activity
F88A
mutation significantly decreases activity
H258A/E259A
double mutaion decreases methyltransferase activity to 40% compared to wild-type activity
R135A
R165A
mutation significantly decreases activity
R92A
mutation significantly decreases activity
S219A
mutation slightly decreases activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminally His6-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant expression of N-terminally His6-tagged wild-type and mutant enzymes, with additional FLAG and HA tags, in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yang, H.; Wang, Z.; Shen, Y.; Wang, P.; Jia, X.; Zhao, L.; Zhou, P.; Gong, R.; Li, Z.; Yang, Y.; Chen, D.; Murchie, A.I.; Xu, Y.
Crystal structure of the nosiheptide-resistance methyltransferase of Streptomyces actuosus
Biochemistry
49
6440-6450
2010
Streptomyces actuosus (P52391), Streptomyces actuosus
Manually annotated by BRENDA team
Yin, S.; Jiang, H.; Chen, D.; Murchie, A.I.
Substrate recognition and modification by the nosiheptide resistance methyltransferase
PLoS ONE
10
e0122972
2015
Streptomyces actuosus (P52391), Streptomyces actuosus
Manually annotated by BRENDA team