_EC 2.1.1.220 tRNA (adenine(58)-N(1))-methyltransferase. 3 PDB entries  
EC 2.-.-.- Transferases. [17,943 PDB entries]
EC 2.1.-.- Transferring one-carbon groups. [1,710 PDB entries]
EC 2.1.1.- Methyltransferases. [1,380 PDB entries]
EC 2.1.1.220 tRNA (adenine(58)-N(1))-methyltransferase. [3 PDB entries]    
1i9g

Reaction: S-adenosyl-L-methionine + adenine(58) in tRNA = S-adenosyl-L-homocysteine + N(1)-methyladenine(58) in tRNA.
 


S-adenosyl-L-methionine
+ adenine(58) in tRNA
=
S-adenosyl-L-homocysteine
+ N(1)-methyladenine(58) in tRNA
Molecule diagrams generated from .mol files obtained from the KEGG ftp site.

Other name(s): tRNA (m(1)A(58)) methyltransferase. tRNA m(1)A(58) methyltransferase.
Comments: The enzyme specifically methylates adenine(58) in tRNA. The methylation of A(58) is critical for maintaining the stability of initiator tRNA(Met) in yeast. Formerly Ec 2.1.1.36.
Links:   [IntEnz]   [ExPASy]   [KEGG]  

There are 3 PDB entries in enzyme class E.C.2.1.1.220

  PDB code Protein
1i9g
Crystal structure of an adomet dependent methyltransferase
Source: Mycobacterium tuberculosis. Organism_taxid: 1773. Gene: rv2118c. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chain: A (264 residues) CATH domains: 3.10.330.20 3.40.50.150
Bound ligand:   Het Group SAM corresponds to enzyme reactant S-adenosyl-L-methionine
2b25
Human putative tRNA(1-methyladenosine)methyltransferase
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B (254 residues) CATH domains: 3.10.330.20 3.40.50.150
Bound ligand:   Het Group SAM is 96.30% similar to enzyme reactant S-adenosyl-L-methionine
2pwy
Crystal structure of a m1a58 tRNA methyltransferase
Source: Thermus thermophilus. Organism_taxid: 262724. Strain: hb27. Gene: trmi. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (251 residues) CATH domains: 3.10.330.20 3.40.50.150
Bound ligand:   Het Group SAH corresponds to enzyme product S-adenosylhomocysteine