2.1.1.224: 23S rRNA (adenine2503-C8)-methyltransferase
This is an abbreviated version!
For detailed information about 23S rRNA (adenine2503-C8)-methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.224
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2.1.1.224
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linezolid
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oxazolidinone
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5\'-deoxyadenosyl
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thiopeptide
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optra
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linezolid-resistant
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phenicols
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cobalamin-dependent
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phlopsa
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pleuromutilins
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nosiheptide
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5'-deoxyadenosine
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poxta
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ribosome-targeting
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cobiialamin
- 2.1.1.224
- linezolid
-
oxazolidinone
-
5\'-deoxyadenosyl
-
thiopeptide
-
optra
-
linezolid-resistant
-
phenicols
-
cobalamin-dependent
-
phlopsa
-
pleuromutilins
-
nosiheptide
- 5'-deoxyadenosine
-
poxta
-
ribosome-targeting
-
cobiialamin
Reaction
2 S-adenosyl-L-methionine + + 2 reduced [2Fe-2S] ferredoxin = + + + + 2 oxidized [2Fe-2S] ferredoxin
Synonyms
antibiotic resistance protein, Ba Cfr, C8 adenine RNA methylase, Cd Cfr, Cfr, Cfr methyltransferase, Cfr rRNA methyltransferase, cfr(C), Cfr(E), cfr-like, Cfr-like protein, ClbA, ClbB, ClbC, EC 2.1.1.194, Ef Cfr, Pl Cfr, radical AdoMet rRNA methyltransferase, radical S-adenosylmethionine enzyme, radical S-adenosylmethionine methylase, radical-S-adenosyl-L-methionine enzyme, radical-SAM enzyme, radical-SAM rRNA methyltransferase, RS methylase
ECTree
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Metals Ions
Metals Ions on EC 2.1.1.224 - 23S rRNA (adenine2503-C8)-methyltransferase
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Fe-S-clusters
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contains a 4Fe-4S cluster. Radical-SAM enzymes contain a [4Fe-4S]+ cluster that is coordinated by the three conserved cysteine thiolate side chains in the CX3CX2C motif and one molecule of S-adenosyl-L-methionine
Fe2+
Mg2+
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4Fe-4S cluster. Fe-S clusters are of structural, as well as functional, importance to Cfr. Radical-SAM enzymes use an Fe-S cluster to generate the 5'-deoxyadenosyl radical from SAM, enabling them to modify intrinsically unreactive centres such as adenosine C8. Anaerobic purification from Azotobacter vinelandii Cfr
Fe2+
Clostridioides difficile Cfr contains an additional Cys-rich C-terminal domain that binds a mononuclear Fe2+ ion in a rubredoxin-type Cys4 motif. The rate of turnover is decreased upon disruption of the Fe2+-binding site by Zn2+ substitution or ligand mutation