Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
S-adenosyl-L-methionine + guanine37 in tRNA | Aquifex aeolicus | - |
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA | - |
? | |
S-adenosyl-L-methionine + guanine37 in tRNA | Escherichia coli | - |
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA | - |
? | |
S-adenosyl-L-methionine + guanine37 in tRNA | Haemophilus influenzae | - |
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aquifex aeolicus | O67463 | - |
- |
Escherichia coli | P0A873 | - |
- |
Haemophilus influenzae | A0A0D0GZF5 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | TrmD can methylate a truncated tRNA, in which T- and D-arms have been deleted, the anticodon-arm region is mainly protected | Escherichia coli | ? | - |
- |
|
additional information | TrmD can methylate a truncated tRNA, in which T- and D-arms have been deleted, the anticodon-arm region is mainly protected | Haemophilus influenzae | ? | - |
- |
|
additional information | TrmD can methylate a truncated tRNA, in which T- and D-arms have been deleted, the anticodon-arm region is mainly protected. The tRNA recognition mechanism of Aquifex aeolicus TrmD shows that a micro-helix RNA corresponding to the anticodon-arm is the minimal substrate for this enzyme | Aquifex aeolicus | ? | - |
- |
|
S-adenosyl-L-methionine + guanine37 in tRNA | - |
Aquifex aeolicus | S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA | - |
? | |
S-adenosyl-L-methionine + guanine37 in tRNA | - |
Escherichia coli | S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA | - |
? | |
S-adenosyl-L-methionine + guanine37 in tRNA | - |
Haemophilus influenzae | S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | knot structures, domain arrangements, subunit structures and reaction mechanisms of tRNA methyltransferases with a SPOUT fold, overview | Aquifex aeolicus |
More | knot structures, domain arrangements, subunit structures and reaction mechanisms of tRNA methyltransferases with a SPOUT fold, overview | Escherichia coli |
More | knot structures, domain arrangements, subunit structures and reaction mechanisms of tRNA methyltransferases with a SPOUT fold, overview | Haemophilus influenzae |
Synonyms | Comment | Organism |
---|---|---|
TrmD | - |
Aquifex aeolicus |
TrmD | - |
Escherichia coli |
TrmD | - |
Haemophilus influenzae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
S-adenosyl-L-methionine | - |
Aquifex aeolicus | |
S-adenosyl-L-methionine | - |
Escherichia coli | |
S-adenosyl-L-methionine | - |
Haemophilus influenzae |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme TrmD belongs to the 2'-O-methyltransferase family, previously SpoU family of enzymes, conserved motifs in the TrmH (SpoU) and TrmD families, overview. Comparisons of topological knot structures in TrmH (SpoU) and TrmD. AdoMet-dependent enzymes can be divided into more than five classes according to the structure of their catalytic domain. Most methyltransferases have a Rossman fold catalytic domain and are classified as class I enzymes. In contrast, members of SPOUT RNA methyltransferase superfamily are classified as class IV enzymes, whose catalytic domain forms a deep trefoil (topological) knot. TrmD from Aquifex aeolicus belongs to the m1G37 methyltransferases | Aquifex aeolicus |
evolution | the enzyme TrmD belongs to the 2'-O-methyltransferase family, previously SpoU family of enzymes, conserved motifs in the TrmH (SpoU) and TrmD families, overview. Comparisons of topological knot structures in TrmH (SpoU) and TrmD. AdoMet-dependent enzymes can be divided into more than five classes according to the structure of their catalytic domain. Most methyltransferases have a Rossman fold catalytic domain and are classified as class I enzymes. In contrast, members of SPOUT RNA methyltransferase superfamily are classified as class IV enzymes, whose catalytic domain forms a deep trefoil (topological) knot. TrmD from Escherichia coli belongs to the m1G37 methyltransferases | Escherichia coli |
evolution | the enzyme TrmD belongs to the 2'-O-methyltransferase family, previously SpoU family of enzymes, conserved motifs in the TrmH (SpoU) and TrmD families, overview. Comparisons of topological knot structures in TrmH (SpoU) and TrmD. AdoMet-dependent enzymes can be divided into more than five classes according to the structure of their catalytic domain. Most methyltransferases have a Rossman fold catalytic domain and are classified as class I enzymes. In contrast, members of SPOUT RNA methyltransferase superfamily are classified as class IV enzymes, whose catalytic domain forms a deep trefoil (topological) knot. TrmD from Haemophilus influenzae belongs to the m1G37 methyltransferases | Haemophilus influenzae |
additional information | Aquifex aeolicus TrmD can methylate G37 in the A36G37 sequence, showing that purine36 is a positive determinant for the TrmD. Formation of a disulfide bond between the two subunits stabilizes the dimer structure of Aquifex aeolicus TrmD and is required for enzymatic activity at high temperatures | Aquifex aeolicus |
physiological function | enzyme TrmD catalyzes the transfer of methyl group from AdoMet to N1-atom of G37 in tRNA to form m1G37 | Aquifex aeolicus |
physiological function | enzyme TrmD catalyzes the transfer of methyl group from AdoMet to N1-atom of G37 in tRNA to form m1G37 | Escherichia coli |
physiological function | enzyme TrmD catalyzes the transfer of methyl group from AdoMet to N1-atom of G37 in tRNA to form m1G37 | Haemophilus influenzae |