Modomics - A Database of RNA Modifications

Full name: tRNA (adenosine(37)-N6)-dimethylallyltransferase
Synonym: TrpX
GI: 127087
Orf: b4171
COG: COG0324
UniProt: P16384
Structures: | 3FOZ | 2ZM5 | 2ZXU |
Enzyme type: dimethylallyltransferase
Position of modification - modification: t:37 - i6A


Bacterial MiaA, initially called dimethylallyl diphosphate:tRNA dimethylallyltransferase, belongs to the IPP transferase superfamily including eukaryotic Mod5. It catalyzes the transfer of isopentenyl group on N6 of A37 in most A36A37-containing tRNA. Isopentenyl originates from ispentenyl-pyrophosphate (IPP). MiaA-like proteins are totally absent in Archaea.

Protein sequence:


Enzymatic activities:

Reaction Substrate Type Position
A:i6A tRNA (t)   37


Title Authors Journal Details PubMed Id DOI
Molecular cloning of the Escherichia coli miaA gene involved in the formation of delta 2-isopentenyl adenosine in tRNA. Caillet J, Droogmans L J Bacteriol [details] 3045085 -
Structural bioinformatics analysis of enzymes involved in the biosynthesis pathway of the hypermodified nucleoside ms(2)io(6)A37 in tRNA. Kaminska KH, Baraniak U, Boniecki M, Nowaczyk K, Czerwoniec A, Bujnicki JM Proteins [details] 17910062 -
Snapshots of dynamics in synthesizing N(6)-isopentenyladenosine at the tRNA anticodon. Chimnaronk S, Forouhar F, Sakai J, Yao M, Tron CM, Atta M, Fontecave M, Hunt JF, Tanaka I Biochemistry [details] 19435325 -
RNA-protein mutually induced fit: structure of Escherichia coli isopentenyl-tRNA transferase in complex with tRNA(Phe). Seif E, Hallberg BM J Biol Chem [details] 19158097 -
Escherichia coli dimethylallyl diphosphate:tRNA dimethylallyltransferase: a binding mechanism for recombinant enzyme. Moore JA, Poulter CD Biochemistry [details] 9012675 -



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