Literature summary for 2.1.1.176 extracted from

Foster, P.G.; Nunes, C.R.; Greene, P.; Moustakas, D.; Stroud, R.M.
The first structure of an RNA m5C methyltransferase, Fmu, provides insight into catalytic mechanism and specific binding of RNA substrate (2003), Structure, 11, 1609-1620.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging-drop vapor diffusion method, crystal structure of Escherichia coli Fmu, determined at 1.65 A resolution for the apoenzyme and 2.1 A resolution in complex with S-adenosyl-L-methionine	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P36929	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
S-adenosyl-L-methionine + cytosine967 in 16S rRNA = S-adenosyl-L-homocysteine + 5-methylcytosine967 in 16S rRNA	a model for the reaction mechanism is proposed	Escherichia coli	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
S-adenosyl-L-methionine + cytosine967 in 16S rRNA	-	Escherichia coli	S-adenosyl-L-homocysteine + 5-methylcytosine967 in 16S rRNA	-	?

Synonyms

Synonyms	Comment	Organism
fma	-	Escherichia coli
m5C methyltransferase Fmu	-	Escherichia coli

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Release 2023.1 (January 2023)