Literature summary extracted from

Guelorget, A.; Barraud, P.; Tisne, C.; Golinelli-Pimpaneau, B.
Structural comparison of tRNA m(1)A58 methyltransferases revealed different molecular strategies to maintain their oligomeric architecture under extreme conditions (2011), BMC Struct. Biol., 11, 48.

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
2.1.1.220	ligand-free TrmI, X-ray diffraction structure determination and analysis at 1.65 A resolution	Thermotoga maritima
2.1.1.220	TrmI complexed with S-adenosyl-L-methionine, X-ray diffraction structure determination and analysis at 1.98 A resolution	Mycobacterium tuberculosis
2.1.1.220	TrmI complexed with S-adenosyl-L-methionine, X-ray diffraction structure determination and analysis at 2.2 A resolution	Aquifex aeolicus
2.1.1.220	TrmI protein complexed as tetramer with S-adenosyl-L-homocysteine or as monomer with S-adenosyl-L-methionine, X-ray diffraction structure determination and analysis at 2.05-2.6 A or 1.6 A resolution, respectively	Pyrococcus abyssi
2.1.1.220	TrmI protein complexed with S-adenosyl-L-homocysteine, X-ray diffraction structure determination and analysis at 1.7 A resolution	Thermus thermophilus
2.1.1.220	TrmI-61 protein complexed with S-adenosyl-L-methionine, X-ray diffraction structure determination and analysis at 2.5 A resolution	Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number	Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.
2.1.1.220	S-adenosyl-L-methionine + adenine58 in tRNA	Thermus thermophilus	tRNA m1A58 methyltransferase, TrmI, catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to N1 of adenine 58 in the T-loop of tRNAs	S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA	-	?
2.1.1.220	S-adenosyl-L-methionine + adenine58 in tRNA	Homo sapiens	tRNA m1A58 methyltransferase, TrmI, catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to N1 of adenine 58 in the T-loop of tRNAs	S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA	-	?
2.1.1.220	S-adenosyl-L-methionine + adenine58 in tRNA	Saccharomyces cerevisiae	tRNA m1A58 methyltransferase, TrmI, catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to N1 of adenine 58 in the T-loop of tRNAs	S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA	-	?
2.1.1.220	S-adenosyl-L-methionine + adenine58 in tRNA	Mycobacterium tuberculosis	tRNA m1A58 methyltransferase, TrmI, catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to N1 of adenine 58 in the T-loop of tRNAs	S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA	-	?
2.1.1.220	S-adenosyl-L-methionine + adenine58 in tRNA	Thermotoga maritima	tRNA m1A58 methyltransferase, TrmI, catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to N1 of adenine 58 in the T-loop of tRNAs	S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA	-	?
2.1.1.220	S-adenosyl-L-methionine + adenine58 in tRNA	Aquifex aeolicus	tRNA m1A58 methyltransferase, TrmI, catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to N1 of adenine 58 in the T-loop of tRNAs	S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA	-	?
2.1.1.220	S-adenosyl-L-methionine + adenine58 in tRNA	Pyrococcus abyssi	tRNA m1A58 methyltransferase, TrmI, catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to N1 of adenine 58 in the T-loop of tRNAs	S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA	-	?

Organism

EC Number	Organism	UniProt	Comment	Textmining
2.1.1.220	Aquifex aeolicus	-	-	-
2.1.1.220	Homo sapiens	-	gene TRM61 encoding subunit TrmI-61	-
2.1.1.220	Mycobacterium tuberculosis	-	-	-
2.1.1.220	Pyrococcus abyssi	-	-	-
2.1.1.220	Saccharomyces cerevisiae	-	-	-
2.1.1.220	Thermotoga maritima	-	-	-
2.1.1.220	Thermus thermophilus	-	-	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
2.1.1.220	S-adenosyl-L-methionine + adenine58 in tRNA	-	Thermus thermophilus	S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA	-	?
2.1.1.220	S-adenosyl-L-methionine + adenine58 in tRNA	-	Homo sapiens	S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA	-	?
2.1.1.220	S-adenosyl-L-methionine + adenine58 in tRNA	-	Saccharomyces cerevisiae	S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA	-	?
2.1.1.220	S-adenosyl-L-methionine + adenine58 in tRNA	-	Mycobacterium tuberculosis	S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA	-	?
2.1.1.220	S-adenosyl-L-methionine + adenine58 in tRNA	-	Thermotoga maritima	S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA	-	?
2.1.1.220	S-adenosyl-L-methionine + adenine58 in tRNA	-	Aquifex aeolicus	S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA	-	?
2.1.1.220	S-adenosyl-L-methionine + adenine58 in tRNA	-	Pyrococcus abyssi	S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA	-	?
2.1.1.220	S-adenosyl-L-methionine + adenine58 in tRNA	tRNA m1A58 methyltransferase, TrmI, catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to N1 of adenine 58 in the T-loop of tRNAs	Thermus thermophilus	S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA	-	?
2.1.1.220	S-adenosyl-L-methionine + adenine58 in tRNA	tRNA m1A58 methyltransferase, TrmI, catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to N1 of adenine 58 in the T-loop of tRNAs	Homo sapiens	S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA	-	?
2.1.1.220	S-adenosyl-L-methionine + adenine58 in tRNA	tRNA m1A58 methyltransferase, TrmI, catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to N1 of adenine 58 in the T-loop of tRNAs	Saccharomyces cerevisiae	S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA	-	?
2.1.1.220	S-adenosyl-L-methionine + adenine58 in tRNA	tRNA m1A58 methyltransferase, TrmI, catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to N1 of adenine 58 in the T-loop of tRNAs	Mycobacterium tuberculosis	S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA	-	?
2.1.1.220	S-adenosyl-L-methionine + adenine58 in tRNA	tRNA m1A58 methyltransferase, TrmI, catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to N1 of adenine 58 in the T-loop of tRNAs	Thermotoga maritima	S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA	-	?
2.1.1.220	S-adenosyl-L-methionine + adenine58 in tRNA	tRNA m1A58 methyltransferase, TrmI, catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to N1 of adenine 58 in the T-loop of tRNAs	Aquifex aeolicus	S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA	-	?
2.1.1.220	S-adenosyl-L-methionine + adenine58 in tRNA	tRNA m1A58 methyltransferase, TrmI, catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to N1 of adenine 58 in the T-loop of tRNAs	Pyrococcus abyssi	S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA	-	?

Subunits

EC Number	Subunits	Comment	Organism
2.1.1.220	heterotetramer	dimers of tightly assembled heterodimers, formed by TrmI-6 and TrmI-61 subunits, interactions and structure analysis, overview	Homo sapiens
2.1.1.220	More	comparative structural analysis of TrmIs, overview	Thermus thermophilus
2.1.1.220	More	comparative structural analysis of TrmIs, overview	Homo sapiens
2.1.1.220	More	comparative structural analysis of TrmIs, overview	Saccharomyces cerevisiae
2.1.1.220	More	comparative structural analysis of TrmIs, overview	Mycobacterium tuberculosis
2.1.1.220	More	comparative structural analysis of TrmIs, overview	Thermotoga maritima
2.1.1.220	More	comparative structural analysis of TrmIs, overview	Aquifex aeolicus
2.1.1.220	More	comparative structural analysis of TrmIs, overview	Pyrococcus abyssi
2.1.1.220	tetramer	dimers of tightly assembled dimers, bacterial enzymes from thermophilic organisms display additional intermolecular ionic interactions across the dimer interfaces, interactions and structure analysis, overview	Thermus thermophilus
2.1.1.220	tetramer	dimers of tightly assembled dimers, bacterial enzymes from thermophilic organisms display additional intermolecular ionic interactions across the dimer interfaces, interactions and structure analysis, overview	Thermotoga maritima
2.1.1.220	tetramer	dimers of tightly assembled dimers, hyperthermophilic enzymes present additional hydrophobic contacts at the dimer interfaces, and the tetramer is strengthened by four intersubunit disulfide bridges, interactions and structure analysis, overview	Pyrococcus abyssi
2.1.1.220	tetramer	dimers of tightly assembled dimers, hyperthermophilic enzymes present additional hydrophobic contacts at the dimer interfaces, interactions and structure analysis, overview	Aquifex aeolicus
2.1.1.220	tetramer	dimers of tightly assembled dimers, interactions and structure analysis, overview	Saccharomyces cerevisiae
2.1.1.220	tetramer	dimers of tightly assembled dimers, interactions and structure analysis, overview	Mycobacterium tuberculosis

Synonyms

EC Number	Synonyms	Comment	Organism
2.1.1.220	m1A58 MTase	-	Thermus thermophilus
2.1.1.220	m1A58 MTase	-	Homo sapiens
2.1.1.220	m1A58 MTase	-	Saccharomyces cerevisiae
2.1.1.220	m1A58 MTase	-	Mycobacterium tuberculosis
2.1.1.220	m1A58 MTase	-	Thermotoga maritima
2.1.1.220	m1A58 MTase	-	Aquifex aeolicus
2.1.1.220	m1A58 MTase	-	Pyrococcus abyssi
2.1.1.220	Rv2118c	-	Mycobacterium tuberculosis
2.1.1.220	TrmI	-	Thermus thermophilus
2.1.1.220	TrmI	-	Homo sapiens
2.1.1.220	TrmI	-	Saccharomyces cerevisiae
2.1.1.220	TrmI	-	Mycobacterium tuberculosis
2.1.1.220	TrmI	-	Thermotoga maritima
2.1.1.220	TrmI	-	Aquifex aeolicus
2.1.1.220	TrmI	-	Pyrococcus abyssi
2.1.1.220	tRNA m1A58 methyltransferase	-	Thermus thermophilus
2.1.1.220	tRNA m1A58 methyltransferase	-	Homo sapiens
2.1.1.220	tRNA m1A58 methyltransferase	-	Saccharomyces cerevisiae
2.1.1.220	tRNA m1A58 methyltransferase	-	Mycobacterium tuberculosis
2.1.1.220	tRNA m1A58 methyltransferase	-	Thermotoga maritima
2.1.1.220	tRNA m1A58 methyltransferase	-	Aquifex aeolicus
2.1.1.220	tRNA m1A58 methyltransferase	-	Pyrococcus abyssi

Cofactor

EC Number	Cofactor	Comment	Organism
2.1.1.220	S-adenosyl-L-methionine	-	Thermus thermophilus
2.1.1.220	S-adenosyl-L-methionine	-	Homo sapiens
2.1.1.220	S-adenosyl-L-methionine	-	Saccharomyces cerevisiae
2.1.1.220	S-adenosyl-L-methionine	-	Mycobacterium tuberculosis
2.1.1.220	S-adenosyl-L-methionine	-	Thermotoga maritima
2.1.1.220	S-adenosyl-L-methionine	-	Aquifex aeolicus
2.1.1.220	S-adenosyl-L-methionine	-	Pyrococcus abyssi

General Information

EC Number	General Information	Comment	Organism
2.1.1.220	evolution	comparative structural analysis of TrmIs from archea, prokaryota, and eukaryota, overview	Thermus thermophilus
2.1.1.220	evolution	comparative structural analysis of TrmIs from archea, prokaryota, and eukaryota, overview	Homo sapiens
2.1.1.220	evolution	comparative structural analysis of TrmIs from archea, prokaryota, and eukaryota, overview	Saccharomyces cerevisiae
2.1.1.220	evolution	comparative structural analysis of TrmIs from archea, prokaryota, and eukaryota, overview	Mycobacterium tuberculosis
2.1.1.220	evolution	comparative structural analysis of TrmIs from archea, prokaryota, and eukaryota, overview	Thermotoga maritima
2.1.1.220	evolution	comparative structural analysis of TrmIs from archea, prokaryota, and eukaryota, overview	Aquifex aeolicus
2.1.1.220	evolution	comparative structural analysis of TrmIs from archea, prokaryota, and eukaryota, overview	Pyrococcus abyssi
2.1.1.220	physiological function	tRNA m1A58 methyltransferase catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to N1 of adenine 58 in the T-loop of tRNAs	Mycobacterium tuberculosis
2.1.1.220	physiological function	tRNA m1A58 methyltransferase catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to N1 of adenine 58 in the T-loop of tRNAs, a modification, that is essential for cell growth at high temperatures	Thermus thermophilus
2.1.1.220	physiological function	tRNA m1A58 methyltransferase catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to N1 of adenine 58 in the T-loop of tRNAs, a modification, that is essential for cell growth at high temperatures	Thermotoga maritima
2.1.1.220	physiological function	tRNA m1A58 methyltransferase catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to N1 of adenine 58 in the T-loop of tRNAs, a modification, that is essential for cell growth at high temperatures	Aquifex aeolicus
2.1.1.220	physiological function	tRNA m1A58 methyltransferase catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to N1 of adenine 58 in the T-loop of tRNAs, a modification, that is essential for cell growth at high temperatures	Pyrococcus abyssi
2.1.1.220	physiological function	tRNA m1A58 methyltransferase catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to N1 of adenine 58 in the T-loop of tRNAs, a modification, that is essential for cell growth in yeast	Homo sapiens
2.1.1.220	physiological function	tRNA m1A58 methyltransferase catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to N1 of adenine 58 in the T-loop of tRNAs, a modification, that is essential for cell growth in yeast	Saccharomyces cerevisiae