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Information on EC 2.1.1.179 - 16S rRNA (guanine1405-N7)-methyltransferase and Organism(s) Micromonospora zionensis and UniProt Accession Q7M0R2

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IUBMB Comments
The enzyme from the antibiotic-producing bacterium Micromonospora zionensis specifically methylates guanine1405 at N7 in 16S rRNA, thereby rendering the ribosome resistant to 4,6-disubstituted deoxystreptamine aminoglycosides, which include gentamicins and kanamycins .
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This record set is specific for:
Micromonospora zionensis
UNIPROT: Q7M0R2
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Word Map
The taxonomic range for the selected organisms is: Micromonospora zionensis
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
Synonyms
16s-rmtase, rmtd2, methyltransferase rmtc, sisomicin-gentamicin resistance methylase, sgm mtase, sgm methyltransferase, methyltransferase sgm, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
16S rRNA (m7G1405) methyltransferase
-
16S rRNA methyltransferase
-
methyltransferase Sgm
-
N7-G1405 16S-RMTase
-
Sgm methyltransferase
-
sisomicin-gentamicin methylase
-
sisomicin-gentamicin methyltransferase
-
sisomicin-gentamicin resistance methylase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + guanine1405 in 16S rRNA = S-adenosyl-L-homocysteine + N7-methylguanine1405 in 16S rRNA
show the reaction diagram
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:16S rRNA (guanine1405-N7)-methyltransferase
The enzyme from the antibiotic-producing bacterium Micromonospora zionensis specifically methylates guanine1405 at N7 in 16S rRNA, thereby rendering the ribosome resistant to 4,6-disubstituted deoxystreptamine aminoglycosides, which include gentamicins and kanamycins [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 + cytosine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine1405 in 16S rRNA
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 7-methylguanine1405 in 16S rRNA
show the reaction diagram
S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine1405 in 16S rRNA
show the reaction diagram
-
-
-
?
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 + cytosine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine1405 in 16S rRNA
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 7-methylguanine1405 in 16S rRNA
show the reaction diagram
S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine1405 in 16S rRNA
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
-
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
Sgm shows intrinsic N7-G1405 16S-RMTase activity
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SGM_MICZI
274
0
30669
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30669
x * 30669, calculated from sequence
32400
x * 32400, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified Sgm is complexed with 5 mM of the cofactors S-adenosylmethionine/S-adenosylhomocysteine. Crystallization trials are carried out at room temperature by hanging-drop vapor-diffusion method, structure of Sgm in complex with cofactors S-adenosylmethionine and S-adenosylhomocysteine is determined at 2.0 A and 2.1 A resolution, respectively
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D156A
D158A
mutant with drastically increased sensitivity to kanamycin
D182A
E205A
E267A
G135A
K199A
K54A
mutant with drastically increased sensitivity to kanamycin
R108A
mutant with drastically increased sensitivity to kanamycin
R187S
mutant with drastically increased sensitivity to kanamycin
R187S/G212S
mutant with strongly reduced activity
R236A
R433A
mutant with drastically increased sensitivity to kanamycin
additional information
analysis of sequence–function relationships of Sgm MTase by limited proteolysis and site-directed and random mutagenesis
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45 - 50
Sgm is fully stable up to 45 to 50°C, after which point the spectra become progressively more like those of an unstructured random coil. No further change is observed beyond 65°C, where all secondary structure appears to be lost
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned in Streptomyces lividans. The sgm gene is expressed in Micromonospora melanosporea, where its own promoter is active, and also in Escherichia coli under the control of the lacZ promoter
cloning of the sgm gene into pET-25b (+) vector with the addition of N-terminal non-cleavable His6 tag, as well as alanine mutagenesis of residues D156, D182 and R108. The constructs are co-transformed along with pGroESL into the strain BL21 (DE3) of Escherichia coli for protein expression
expression in Escherichia coli
gene sgm, phylogenetic analysis, sequence comparisons
introduction of a recombinant version of the Sgm methyltransferase gene from Micromonospora zionensis into an Escherichia coli strain that has a full complement of housekeeping methyltransferases. Analyses of the 16S rRNA shows that the m5C1407-specific housekeeping methyltransferase RsmF (YebU) is outcompeted by Sgm as the resistance methyltransferase gains access to its own m7G1405 target on the 30S ribosomal subunit. A single amino acid change in Sgm, which lowers the level of conferred resistance, reduces the ability of Sgm to interfere with RsmF methylation on the 30S subunit
sgm is cloned into a yeast expression vector to test whether the prokaryotic methylases can modify the 18S rRNA A-site and thus confer resistance to the aminoglycoside antibiotic G-418. Sgm does not provide resistant phenotypes to yeast cells. Despite all similarities in the antibiotic binding site, methylation by Sgm does not occur in yeast, suggesting that the recognition site for these methylases could be different in 30S and 40S subunits
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
development of potent agents against 16S-RMTase producers as targets for treatment of multidrug resistant bacteria
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Maravic Vlahovicek, G.; Cubrilo, S.; Tkaczuk, K.L.; Bujnicki, J.M.
Modeling and experimental analyses reveal a two-domain structure and amino acids important for the activity of aminoglycoside resistance methyltransferase Sgm
Biochim. Biophys. Acta
1784
582-590
2008
Micromonospora zionensis (Q7M0R2)
Manually annotated by BRENDA team
Kojic, M.; Topisirovic, L.; Vasiljevic, B.
Cloning and characterization of an aminoglycoside resistance determinant from Micromonospora zionensis
J. Bacteriol.
174
7868-7872
1992
Micromonospora zionensis (Q7M0R2), Micromonospora zionensis
Manually annotated by BRENDA team
Kojic, M.; Topisirovic, L.; Vasiljevic, B.
Translational autoregulation of the sgm gene from Micromonospora zionensis
J. Bacteriol.
178
5493-5498
1996
Micromonospora zionensis (Q7M0R2), Micromonospora zionensis
Manually annotated by BRENDA team
Savic, M.; Ilic-Tomic, T.; Macmaster, R.; Vasiljevic, B.; Conn, G.L.
Critical residues for cofactor binding and catalytic activity in the aminoglycoside resistance methyltransferase Sgm
J. Bacteriol.
190
5855-5861
2008
Micromonospora zionensis (Q7M0R2)
Manually annotated by BRENDA team
Savic, M.; Lovric, J.; Tomic, T.I.; Vasiljevic, B.; Conn, G.L.
Determination of the target nucleosides for members of two families of 16S rRNA methyltransferases that confer resistance to partially overlapping groups of aminoglycoside antibiotics
Nucleic Acids Res.
37
5420-5431
2009
Frankia sp. (Q2J7L5), Frankia sp. CcI3 (Q2J7L5), Micromonospora echinospora (Q70KC8), Micromonospora zionensis (Q7M0R2)
Manually annotated by BRENDA team
Husain, N.; Tkaczuk, K.L.; Tulsidas, S.R.; Kaminska, K.H.; Cubrilo, S.; Maravic-Vlahovicek, G.; Bujnicki, J.M.; Sivaraman, J.
Structural basis for the methylation of G1405 in 16S rRNA by aminoglycoside resistance methyltransferase Sgm from an antibiotic producer: a diversity of active sites in m7G methyltransferases
Nucleic Acids Res.
38
4120-4132
2010
Micromonospora zionensis (Q7M0R2), Micromonospora zionensis
Manually annotated by BRENDA team
Tomic, T.I.; Moric, I.; Conn, G.L.; Vasiljevic, B.
Aminoglycoside resistance genes sgm and kgmB protect bacterial but not yeast small ribosomal subunits in vitro despite high conservation of the rRNA A-site
Res. Microbiol.
159
658-662
2008
Micromonospora zionensis (Q7M0R2)
Manually annotated by BRENDA team
Cubrilo, S.; Babic, F.; Douthwaite, S.; Maravic Vlahovicek, G.
The aminoglycoside resistance methyltransferase Sgm impedes RsmF methylation at an adjacent rRNA nucleotide in the ribosomal A site
RNA
15
1492-1497
2009
Micromonospora zionensis (Q7M0R2)
Manually annotated by BRENDA team
Wachino, J.; Arakawa, Y.
Exogenously acquired 16S rRNA methyltransferases found in aminoglycoside-resistant pathogenic Gram-negative bacteria: an update
Drug Resist. Updat.
15
133-148
2012
Citrobacter freundii (E9N3S1), Micromonospora echinospora (Q70KC8), Micromonospora inyonensis (Q5Y813), Micromonospora olivasterospora (Q08325), Micromonospora rosea (P24619), Micromonospora zionensis (Q7M0R2), Proteus mirabilis (Q33DX5), Proteus mirabilis ARS68 (Q33DX5), Pseudomonas aeruginosa (A0MK31), Pseudomonas aeruginosa (Q8GRA1), Serratia marcescens (Q76G15), Streptoalloteichus hindustanus (O52472), Streptomyces kanamyceticus (Q75PS4)
Manually annotated by BRENDA team
Correa, L.L.; Witek, M.A.; Zelinskaya, N.; Picao, R.C.; Conn, G.L.
Heterologous expression and functional characterization of the exogenously acquired aminoglycoside resistance methyltransferases RmtD, RmtD2, and RmtG
Antimicrob. Agents Chemother.
60
699-702
2015
Escherichia coli, Micromonospora zionensis (Q7M0R2)
Manually annotated by BRENDA team