tRNA dimethylallyltransferase
Details
- Name
- tRNA dimethylallyltransferase
- Kind
- protein
- 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
- UniProtKB Entry
- P16384Swiss-Prot
- Organism
- Escherichia coli (strain K12)
- NCBI Taxonomy ID
- 83333
- 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
- FunctionsATP binding / tRNA dimethylallyltransferase activityProcessescellular response to heat / tRNA modification
- General 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).
- Specific Function
- ATP binding
- Pfam Domain Function
- IPPT (PF01715)
- Signal Regions
- Not Available
- 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
Resource Link UniProtKB ID P16384 UniProtKB Entry Name MIAA_ECOLI PDB ID(s) 2ZM5, 2ZXU, 3FOZ KEGG ID ecj:JW4129 NCBI Gene ID 948690 - General References
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details Dimethylallyl S-Thiolodiphosphate experimental unknown target Details