Any feedback?
Literature summary for 2.1.1.218 extracted from
- m1A Post-transcriptional modification in tRNAs (2017), Biomolecules, 7, 20 .
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| crystal structure PDB ID 5A7T | Thermococcus kodakarensis |
| crystal structure PDB ID 5A7T | Sulfolobus acidocaldarius |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| S-adenosyl-L-methionine + adenine9 in tRNA | Thermococcus kodakarensis | - |
S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA | - |
? |  |
| S-adenosyl-L-methionine + adenine9 in tRNA | Sulfolobus acidocaldarius | - |
S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA | - |
? | |
| S-adenosyl-L-methionine + adenine9 in tRNA | Homo sapiens | - |
S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA | - |
? | |
| S-adenosyl-L-methionine + adenine9 in tRNA | Thermococcus kodakarensis JCM 12380 | - |
S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA | - |
? | |
| S-adenosyl-L-methionine + adenine9 in tRNA | Sulfolobus acidocaldarius DSM 639 | - |
S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA | - |
? | |
| S-adenosyl-L-methionine + adenine9 in tRNA | Thermococcus kodakarensis ATCC BAA-918 | - |
S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA | - |
? | |
| S-adenosyl-L-methionine + adenine9 in tRNA | Sulfolobus acidocaldarius ATCC 33909 | - |
S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA | - |
? | |
| S-adenosyl-L-methionine + adenine9 in tRNA | Sulfolobus acidocaldarius NBRC 15157 | - |
S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA | - |
? | |
| S-adenosyl-L-methionine + adenine9 in tRNA | Sulfolobus acidocaldarius NCIMB 11770 | - |
S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA | - |
? | |
| S-adenosyl-L-methionine + adenine9 in tRNA | Sulfolobus acidocaldarius JCM 8929 | - |
S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | Q7L0Y3 | - |
- |
| Sulfolobus acidocaldarius | Q4J894 | - |
- |
| Sulfolobus acidocaldarius ATCC 33909 | Q4J894 | - |
- |
| Sulfolobus acidocaldarius DSM 639 | Q4J894 | - |
- |
| Sulfolobus acidocaldarius JCM 8929 | Q4J894 | - |
- |
| Sulfolobus acidocaldarius NBRC 15157 | Q4J894 | - |
- |
| Sulfolobus acidocaldarius NCIMB 11770 | Q4J894 | - |
- |
| Thermococcus kodakarensis | Q5JD38 | - |
- |
| Thermococcus kodakarensis ATCC BAA-918 | Q5JD38 | - |
- |
| Thermococcus kodakarensis JCM 12380 | Q5JD38 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | the archaeal Trm10 enzyme does not exhibit activity on guanine9 residues in tRNA, no activity of EC 2.1.1.221 | Sulfolobus acidocaldarius | ? | - |
- |
|
| additional information | the human Trm10C enzyme is bifunctional and methylates adenine9 (EC 2.1.1.218) and guanine9 (EC 2.1.1.221) residues in tRNA | Homo sapiens | ? | - |
- |
|
| additional information | the Trm10 enzyme from Thermococcus kodakarensis is bifunctional and methylates adenine9 (EC 2.1.1.218) and guanine9 (EC 2.1.1.221) residues in tRNA | Thermococcus kodakarensis | ? | - |
- |
|
| additional information | the Trm10 enzyme from Thermococcus kodakarensis is bifunctional and methylates adenine9 (EC 2.1.1.218) and guanine9 (EC 2.1.1.221) residues in tRNA | Thermococcus kodakarensis JCM 12380 | ? | - |
- |
|
| additional information | the archaeal Trm10 enzyme does not exhibit activity on guanine9 residues in tRNA, no activity of EC 2.1.1.221 | Sulfolobus acidocaldarius DSM 639 | ? | - |
- |
|
| additional information | the Trm10 enzyme from Thermococcus kodakarensis is bifunctional and methylates adenine9 (EC 2.1.1.218) and guanine9 (EC 2.1.1.221) residues in tRNA | Thermococcus kodakarensis ATCC BAA-918 | ? | - |
- |
|
| additional information | the archaeal Trm10 enzyme does not exhibit activity on guanine9 residues in tRNA, no activity of EC 2.1.1.221 | Sulfolobus acidocaldarius ATCC 33909 | ? | - |
- |
|
| additional information | the archaeal Trm10 enzyme does not exhibit activity on guanine9 residues in tRNA, no activity of EC 2.1.1.221 | Sulfolobus acidocaldarius NBRC 15157 | ? | - |
- |
|
| additional information | the archaeal Trm10 enzyme does not exhibit activity on guanine9 residues in tRNA, no activity of EC 2.1.1.221 | Sulfolobus acidocaldarius NCIMB 11770 | ? | - |
- |
|
| additional information | the archaeal Trm10 enzyme does not exhibit activity on guanine9 residues in tRNA, no activity of EC 2.1.1.221 | Sulfolobus acidocaldarius JCM 8929 | ? | - |
- |
|
| S-adenosyl-L-methionine + adenine9 in tRNA | - |
Thermococcus kodakarensis | S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA | - |
? | |
| S-adenosyl-L-methionine + adenine9 in tRNA | - |
Sulfolobus acidocaldarius | S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA | - |
? | |
| S-adenosyl-L-methionine + adenine9 in tRNA | - |
Homo sapiens | S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA | - |
? | |
| S-adenosyl-L-methionine + adenine9 in tRNA | - |
Thermococcus kodakarensis JCM 12380 | S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA | - |
? | |
| S-adenosyl-L-methionine + adenine9 in tRNA | - |
Sulfolobus acidocaldarius DSM 639 | S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA | - |
? | |
| S-adenosyl-L-methionine + adenine9 in tRNA | - |
Thermococcus kodakarensis ATCC BAA-918 | S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA | - |
? | |
| S-adenosyl-L-methionine + adenine9 in tRNA | - |
Sulfolobus acidocaldarius ATCC 33909 | S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA | - |
? | |
| S-adenosyl-L-methionine + adenine9 in tRNA | - |
Sulfolobus acidocaldarius NBRC 15157 | S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA | - |
? | |
| S-adenosyl-L-methionine + adenine9 in tRNA | - |
Sulfolobus acidocaldarius NCIMB 11770 | S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA | - |
? | |
| S-adenosyl-L-methionine + adenine9 in tRNA | - |
Sulfolobus acidocaldarius JCM 8929 | S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| m1A9 MTase | - |
Sulfolobus acidocaldarius |
| More | see also EC 2.1.1.221 | Thermococcus kodakarensis |
| More | see also EC 2.1.1.221 | Homo sapiens |
| SPOUT MTase | - |
Thermococcus kodakarensis |
| SPOUT MTase | - |
Sulfolobus acidocaldarius |
| SPOUT MTase | - |
Homo sapiens |
| Trm10 | - |
Thermococcus kodakarensis |
| Trm10 | - |
Sulfolobus acidocaldarius |
| Trmt10C | - |
Homo sapiens |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| S-adenosyl-L-methionine | - |
Thermococcus kodakarensis | |
| S-adenosyl-L-methionine | - |
Sulfolobus acidocaldarius | |
| S-adenosyl-L-methionine | - |
Homo sapiens | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | aside from an active site aspartate residue, alignment of the available Trm10 protein structures and their primary sequences show no other obvious amino acid candidates in the active site that could account for the differences between m1G9-specific (Saccharomyces cerevisiae and Schizosaccharomyces pombe), m1A9-specific (Sulfolobus acidocaldarius) and m1A9/m1G9 dual-specific (human Trmt10C and Trm10 from Thermococcus kodakarensis) Trm10 MTases. It is possible that the purine specificity might simply be due to differences in surface charge around the active site and size and/or layout of the purine-binding pocket, which could allow different Trm10 family members to accommodate different purine substrates, rather than to specific residues for catalysis. The active site pocket is more open for the m1G9-specific Trmt10A and m1A9-specific Trm10, compared to the other Trm10 proteins. No obvious similarities are observed within the m1G9-specific group of proteins that are also clearly different from the m1A9-specific Trm10, and altered in the m1G9/m1A9 dual-specific protein | Thermococcus kodakarensis |
| evolution | aside from an active site aspartate residue, alignment of the available Trm10 protein structures and their primary sequences show no other obvious amino acid candidates in the active site that could account for the differences between m1G9-specific (Saccharomyces cerevisiae and Schizosaccharomyces pombe), m1A9-specific (Sulfolobus acidocaldarius) and m1A9/m1G9 dual-specific (human Trmt10C and Trm10 from Thermococcus kodakarensis) Trm10 MTases. It is possible that the purine specificity might simply be due to differences in surface charge around the active site and size and/or layout of the purine-binding pocket, which could allow different Trm10 family members to accommodate different purine substrates, rather than to specific residues for catalysis. The active site pocket is more open for the m1G9-specific Trmt10A and m1A9-specific Trm10, compared to the other Trm10 proteins. No obvious similarities are observed within the m1G9-specific group of proteins that are also clearly different from the m1A9-specific Trm10, and altered in the m1G9/m1A9 dual-specific protein | Sulfolobus acidocaldarius |
| evolution | aside from an active site aspartate residue, alignment of the available Trm10 protein structures and their primary sequences show no other obvious amino acid candidates in the active site that could account for the differences between m1G9-specific (Saccharomyces cerevisiae and Schizosaccharomyces pombe), m1A9-specific (Sulfolobus acidocaldarius) and m1A9/m1G9 dual-specific (human Trmt10C and Trm10 from Thermococcus kodakarensis) Trm10 MTases. It is possible that the purine specificity might simply be due to differences in surface charge around the active site and size and/or layout of the purine-binding pocket, which could allow different Trm10 family members to accommodate different purine substrates, rather than to specific residues for catalysis. The active site pocket is more open for the m1G9-specific Trmt10A and m1A9-specific Trm10, compared to the other Trm10 proteins. No obvious similarities are observed within the m1G9-specific group of proteins that are also clearly different from the m1A9-specific Trm10, and altered in the m1G9/m1A9 dual-specific protein | Homo sapiens |
| malfunction | mutation of catalytic residue Asp184 abolishes m1A9 activity in the archaeal Trm10 protein | Sulfolobus acidocaldarius |
| malfunction | mutation of catalytic residue Asp206 abolishes m1A9 activity in the archaeal Trm10 protein | Thermococcus kodakarensis |
| metabolism | the methylation on the N1 atom of adenosine to form 1-methyladenosine (m1A) has been identified at nucleotide position 9, 14, 22, 57, and 58 in different tRNAs. In some cases, these modifications have been shown to increase tRNA structural stability and induce correct tRNA folding. The m1A9 MTases belong to the Trm10 subfamily of the SPOUT superfamily. In addition to the m1A9 modification, the Trm10 subfamily of MTases methylates guanosine in some organisms | Thermococcus kodakarensis |
| metabolism | the methylation on the N1 atom of adenosine to form 1-methyladenosine (m1A) has been identified at nucleotide position 9, 14, 22, 57, and 58 in different tRNAs. In some cases, these modifications have been shown to increase tRNA structural stability and induce correct tRNA folding. The m1A9 MTases belong to the Trm10 subfamily of the SPOUT superfamily. In addition to the m1A9 modification, the Trm10 subfamily of MTases methylates guanosine in some organisms | Sulfolobus acidocaldarius |
| metabolism | the methylation on the N1 atom of adenosine to form 1-methyladenosine (m1A) has been identified at nucleotide position 9, 14, 22, 57, and 58 in different tRNAs. In some cases, these modifications have been shown to increase tRNA structural stability and induce correct tRNA folding. The m1A9 MTases belong to the Trm10 subfamily of the SPOUT superfamily. In addition to the m1A9 modification, the Trm10 subfamily of MTases methylates guanosine in some organisms | Homo sapiens |
| additional information | in human Trmt10C, the catalytic aspartate residue, found in archaeal m1A9 MTases, is replaced by leucine that, due to its uncharged nature, is likely to act differently in catalysis than a charged aspartate residue. Another aspartate residue is located deep in the active site pocket of human Trmt10C (Asp293) and might be involved in catalysis, but seems unlikely to be the determinant for m1A9 activity, as this position is occupied by aspartate in the m1G9-specific Trm10 proteins from yeast, and is not conserved in m1A9 active Trm10 proteins from Sulfolobus acidocaldarius and Thermococcus kodakarensis. tRNA recognition by Trm10 enzymes, overview | Homo sapiens |
| additional information | tRNA recognition by Trm10 enzymes, overview | Thermococcus kodakarensis |
| additional information | tRNA recognition by Trm10 enzymes, overview | Sulfolobus acidocaldarius |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
