Information on EC 2.1.1.199 - 16S rRNA (cytosine1402-N4)-methyltransferase

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The expected taxonomic range for this enzyme is: Escherichia coli

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EC NUMBER
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2.1.1.199
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RECOMMENDED NAME
GeneOntology No.
16S rRNA (cytosine1402-N4)-methyltransferase
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REACTION
REACTION DIAGRAM
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ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + cytosine1402 in 16S rRNA = S-adenosyl-L-homocysteine + N4-methylcytosine1402 in 16S rRNA
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:16S rRNA (cytosine1402-N4)-methyltransferase
RsmH catalyses the N4-methylation of cytosine1402 and RsmI (EC 2.1.1.198) catalyses the 2'-O-methylation of cytosine1402 in 16S rRNA. Both methylations are necessary for efficient translation initiation at the UUG and GUG codons.
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
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both the 2'-O-methylation (catalyzed by RsmI) and N4-methylation of C1402 (catalyzed by RsmH) are needed for efficient initiation at the UUG and GUG codon. m4Cm1402 in the 16S rRNA modulates the accuracy of P-site function. The modification is needed for efficient translation initiation at the UUG and GUG codons
additional information
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RsmH in complex with S-adenosyl-L-methionine and cytidine consists of two distinct but structurally related domains: the typical MTase domain and the putative substrate recognition and binding domain. A deep pocket occurs in the conserved AdoMet binding domain, cytidine binds far from S-adenosyl-L-methionine with the distance of 25.9 A, The complex is not in a catalytically active state, and structural rearrangement of RsmH or the nucleotides neighboring C1402 may be necessary to trigger catalysis
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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 + cytidine1402 in 16S rRNA
S-adenosyl-L-homocysteine + N4-methylcytidine1402 in 16S rRNA
show the reaction diagram
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S-adenosyl-L-methionine + cytosine1402 in 16S rRNA
S-adenosyl-L-homocysteine + N4-methylcytosine1402 in 16S rRNA
show the reaction diagram
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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 + cytidine1402 in 16S rRNA
S-adenosyl-L-homocysteine + N4-methylcytidine1402 in 16S rRNA
show the reaction diagram
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S-adenosyl-L-methionine + cytosine1402 in 16S rRNA
S-adenosyl-L-homocysteine + N4-methylcytosine1402 in 16S rRNA
show the reaction diagram
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COFACTOR
ORGANISM
UNIPROT
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LITERATURE
IMAGE
S-adenosyl-L-methionine
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the cofactor binds in the active site, structure, overview
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PDB
SCOP
CATH
UNIPROT
ORGANISM
P60390
Escherichia coli (strain K12);
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099);
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SUBUNITS
ORGANISM
UNIPROT
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LITERATURE
homodimer
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active enzyme in solution, structure analysis, overview
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant His6-tagged RsmH in complex with S-adenosyl-L-methionine and cytidine in a 1:5:5 ratio, sitting drop vapour diffusion method, from 20 mM Tris, 100 mM NaCl, 5% v/v glycerol, 2 mM DTT, pH 8.0, room temperature, the best crystal is obtained in the mixture solution 1.0 M ammonium sulfate, 0.1 M HEPES, pH 6.5, and 0.5% w/v PEG 8, 000 in 3-4 days, X-ray diffraction structure determination and analysis at 2.25 A resolution
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged RsmH from Escherichia coli strain BL21 DE3 star by nickel affinity chromatigraphy and gel filtration
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recombinant protein with N-terminal 6His-tags
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene rsmH, expression of His6-tagged RsmH in Escherichia coli strain BL21 DE3 star
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LINKS TO OTHER DATABASES (specific for EC-Number 2.1.1.199)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)