tRNA dimethylallyltransferase

Details

Name
tRNA dimethylallyltransferase
Synonyms
  • 2.5.1.75
  • Dimethylallyl diphosphate:tRNA dimethylallyltransferase
  • DMAPP:tRNA dimethylallyltransferase
  • DMATase
  • IPP transferase
  • IPPT
  • IPTase
  • Isopentenyl-diphosphate:tRNA isopentenyltransferase
  • trpX
Gene Name
miaA
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0020735|tRNA dimethylallyltransferase
MSDISKASLPKAIFLMGPTASGKTALAIELRKILPVELISVDSALIYKGMDIGTAKPNAE
ELLAAPHRLLDIRDPSQAYSAADFRRDALAEMADITAAGRIPLLVGGTMLYFKALLEGLS
PLPSADPEVRARIEQQAAEQGWESLHRQLQEVDPVAAARIHPNDPQRLSRALEVFFISGK
TLTELTQTSGDALPYQVHQFAIAPASRELLHQRIEQRFHQMLASGFEAEVRALFARGDLH
TDLPSIRCVGYRQMWSYLEGEISYDEMVYRGVCATRQLAKRQITWLRGWEGVHWLDSEKP
EQARDEVLQVVGAIAG
Number of residues
316
Molecular Weight
35064.745
Theoretical pI
Not Available
GO Classification
Functions
ATP binding / tRNA dimethylallyltransferase activity
Processes
cellular response to heat / tRNA modification
General Function
Trna dimethylallyltransferase activity
Specific Function
Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0020736|tRNA dimethylallyltransferase (miaA)
ATGAGTGATATCAGTAAGGCGAGCCTGCCTAAGGCGATTTTTTTGATGGGGCCGACGGCC
TCCGGTAAAACGGCGTTAGCCATTGAGCTGCGTAAAATTTTACCAGTAGAGTTGATAAGC
GTTGATTCTGCCCTTATTTACAAAGGGATGGATATCGGGACGGCGAAGCCGAACGCTGAA
GAGTTACTCGCCGCGCCGCACCGATTGCTGGATATTCGCGATCCGTCGCAGGCTTACTCG
GCTGCTGATTTTCGCCGCGATGCGCTGGCGGAAATGGCCGATATCACCGCGGCGGGGCGG
ATCCCACTGTTAGTGGGCGGTACGATGTTGTATTTCAAGGCATTGCTGGAAGGGTTGTCG
CCGCTACCGTCGGCAGACCCGGAAGTACGGGCCAGAATTGAGCAACAGGCGGCAGAGCAA
GGTTGGGAGTCATTGCATCGTCAACTTCAGGAGGTAGATCCGGTTGCGGCAGCAAGGATT
CATCCAAATGATCCACAAAGGCTTTCCCGGGCACTGGAAGTTTTTTTCATTTCGGGTAAA
ACTTTAACGGAACTGACGCAAACGTCAGGAGACGCTCTACCGTATCAGGTGCATCAGTTC
GCCATCGCCCCGGCGAGCCGTGAACTGCTCCATCAACGCATTGAGCAGCGTTTTCATCAG
ATGTTGGCTTCAGGTTTTGAAGCAGAAGTCCGGGCGCTTTTTGCCCGAGGAGATTTGCAT
ACGGACTTGCCTTCCATTCGTTGCGTGGGTTATCGCCAGATGTGGTCTTACCTTGAAGGC
GAAATCTCATACGATGAAATGGTTTATCGAGGTGTTTGCGCCACGAGACAGTTGGCGAAG
CGGCAGATAACCTGGCTGCGTGGTTGGGAAGGGGTTCACTGGCTTGACAGTGAAAAACCA
GAACAGGCGCGTGACGAAGTATTACAGGTTGTTGGTGCTATCGCAGGCTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP16384
UniProtKB Entry NameMIAA_ECOLI
General References
  1. Connolly DM, Winkler ME: Structure of Escherichia coli K-12 miaA and characterization of the mutator phenotype caused by miaA insertion mutations. J Bacteriol. 1991 Mar;173(5):1711-21. [Article]
  2. Burland V, Plunkett G 3rd, Sofia HJ, Daniels DL, Blattner FR: Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes. Nucleic Acids Res. 1995 Jun 25;23(12):2105-19. [Article]
  3. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  4. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  5. Connolly DM, Winkler ME: Genetic and physiological relationships among the miaA gene, 2-methylthio-N6-(delta 2-isopentenyl)-adenosine tRNA modification, and spontaneous mutagenesis in Escherichia coli K-12. J Bacteriol. 1989 Jun;171(6):3233-46. [Article]
  6. Kajitani M, Ishihama A: Identification and sequence determination of the host factor gene for bacteriophage Q beta. Nucleic Acids Res. 1991 Mar 11;19(5):1063-6. [Article]
  7. Tsui HT, Mandavilli BS, Winkler ME: Nonconserved segment of the MutL protein from Escherichia coli K-12 and Salmonella typhimurium. Nucleic Acids Res. 1992 May 11;20(9):2379. [Article]
  8. Moore JA, Poulter CD: Escherichia coli dimethylallyl diphosphate:tRNA dimethylallyltransferase: a binding mechanism for recombinant enzyme. Biochemistry. 1997 Jan 21;36(3):604-14. [Article]
  9. Leung HC, Chen Y, Winkler ME: Regulation of substrate recognition by the MiaA tRNA prenyltransferase modification enzyme of Escherichia coli K-12. J Biol Chem. 1997 May 16;272(20):13073-83. [Article]
  10. Seif E, Hallberg BM: RNA-protein mutually induced fit: structure of Escherichia coli isopentenyl-tRNA transferase in complex with tRNA(Phe). J Biol Chem. 2009 Mar 13;284(11):6600-4. doi: 10.1074/jbc.C800235200. Epub 2009 Jan 21. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB02270Dimethylallyl S-ThiolodiphosphateexperimentalunknownDetails