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Literature summary extracted from

  • Zhao, X.; Wang, Y.; Wang, Y.; Liu, Y.; Gao, S.
    Histone methyltransferase TXR1 is required for both H3 and H3.3 lysine 27 methylation in the well-known ciliated protist Tetrahymena thermophila (2017), Sci. China Life Sci., 60, 264-270 .
    View publication on PubMed

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.356 S-adenosyl-L-methionine + [histone H3.3]-L-lysine27 Tetrahymena thermophila
-
 S-adenosyl-L-homocysteine + [histone H3.3]-N6-methyl-L-lysine27
-
 ?
2.1.1.356 S-adenosyl-L-methionine + [histone H3.3]-L-lysine27 Tetrahymena thermophila SB210
-
 S-adenosyl-L-homocysteine + [histone H3.3]-N6-methyl-L-lysine27
-
 ?
2.1.1.356 S-adenosyl-L-methionine + [histone H3]-L-lysine27 Tetrahymena thermophila
-
 S-adenosyl-L-homocysteine + [histone H3]-N6-methyl-L-lysine27
-
 ?
2.1.1.356 S-adenosyl-L-methionine + [histone H3]-L-lysine27 Tetrahymena thermophila SB210
-
 S-adenosyl-L-homocysteine + [histone H3]-N6-methyl-L-lysine27
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.356 Tetrahymena thermophila Q23QI3
-
-
2.1.1.356 Tetrahymena thermophila SB210 Q23QI3
-
-
2.1.1.369 Tetrahymena thermophila
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.356 S-adenosyl-L-methionine + [histone H3.3]-L-lysine27
-
 Tetrahymena thermophila S-adenosyl-L-homocysteine + [histone H3.3]-N6-methyl-L-lysine27
-
 ?
2.1.1.356 S-adenosyl-L-methionine + [histone H3.3]-L-lysine27
-
 Tetrahymena thermophila SB210 S-adenosyl-L-homocysteine + [histone H3.3]-N6-methyl-L-lysine27
-
 ?
2.1.1.356 S-adenosyl-L-methionine + [histone H3]-L-lysine27
-
 Tetrahymena thermophila S-adenosyl-L-homocysteine + [histone H3]-N6-methyl-L-lysine27
-
 ?
2.1.1.356 S-adenosyl-L-methionine + [histone H3]-L-lysine27
-
 Tetrahymena thermophila SB210 S-adenosyl-L-homocysteine + [histone H3]-N6-methyl-L-lysine27
-
 ?
2.1.1.369 additional information K27Q mutation in variant H3.3 further aggravates the replication stress phenotype of K27Q mutation in canonical H3. H3.3 is a physiologically relevant substrate of TXR1 Tetrahymena thermophila ?
-
-
2.1.1.369 S-adenosyl-L-methionine + [histone H3.3]-L-lysine27
-
 Tetrahymena thermophila S-adenosyl-L-homocysteine + [histone H3.3]-N6-methyl-L-lysine27
-
 ?
2.1.1.369 S-adenosyl-L-methionine + [histone H3]-L-lysine27
-
 Tetrahymena thermophila S-adenosyl-L-homocysteine + [histone H3]-N6-methyl-L-lysine27
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.1.1.356 TXR1
-
 Tetrahymena thermophila
2.1.1.369 Tetrahymena Trithorax related protein 1
-
 Tetrahymena thermophila
2.1.1.369 TXR1
-
 Tetrahymena thermophila

General Information

EC Number General Information Comment Organism
2.1.1.356 physiological function the enzyme affects DNA replication elongation in Tetrahymena thermophila Tetrahymena thermophila