Literature summary for 2.1.1.80 extracted from

Batra, M.; Sharma, R.; Malik, A.; Dhindwal, S.; Kumar, P.; Tomar, S.
Crystal structure of pentapeptide-independent chemotaxis receptor methyltransferase (CheR) reveals idiosyncratic structural determinants for receptor recognition (2016), J. Struct. Biol., 196, 364-374 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
in complex with S-adenosyl-L-homocysteine	Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
S-adenosyl-L-methionine + protein L-glutamate	Bacillus subtilis	-	S-adenosyl-L-homocysteine + protein L-glutamate methyl ester	-	?

Organism

Organism	UniProt	Comment	Textmining
Bacillus subtilis	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
S-adenosyl-L-methionine + protein L-glutamate	-	Bacillus subtilis	S-adenosyl-L-homocysteine + protein L-glutamate methyl ester	-	?

Synonyms

Synonyms	Comment	Organism
CheR	-	Bacillus subtilis
pentapeptide-independent chemotaxis receptor methyltransferase	-	Bacillus subtilis

General Information

General Information	Comment	Organism
metabolism	the enzyme catalyzes methylation of specific glutamate residues in the cytoplasmic domain of methyl-accepting chemotactic protein receptors which is essential for the chemical sensing and chemotactic bacterial mobility towards favorable chemicals or away from unfavorable ones	Bacillus subtilis

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Release 2023.1 (January 2023)