Isoleucyl-tRNA synthetase (P00956)

Identification
Name:Isoleucyl-tRNA synthetase
Synonyms:
  • Isoleucine--tRNA ligase
  • IleRS
Gene Name:ileS
Enzyme Class:
Biological Properties
General Function:Involved in nucleotide binding
Specific Function:Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile)
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
  • Aminoacyl-tRNA biosynthesis ec00970
  • Valine, leucine and isoleucine biosynthesis ec00290
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0tRNA(Ile)+1.0tRNA(Ile) ↔ 1.0Thumb+1.0L-Isoleucyl-tRNA(Ile)+1.0Thumb+1.0L-Isoleucyl-tRNA(Ile)
1.0Adenosine triphosphate + 1.0L-Isoleucine + 1.0tRNA(Ile) + 1.0tRNA(Ile) ↔ 1.0Adenosine monophosphate + 1.0L-Isoleucyl-tRNA(Ile) + 1.0Pyrophosphate + 1.0L-Isoleucyl-tRNA(Ile)
ReactionCard
1.0Thumb+1.0Thumb+1.0tRNA(Ile) ↔ 1.0Thumb+1.0Thumb+1.0L-Isoleucyl-tRNA(Ile)
1.0Adenosine triphosphate + 1.0L-Isoleucine + 1.0tRNA(Ile) ↔ 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-Isoleucyl-tRNA(Ile)
ReactionCard
SMPDB Reactions:
1.0L-Isoleucine+1.0Thumb+1.0Thumb+1.0tRNA(Ile)+1.0Thumb → 1.0L-Isoleucyl-tRNA(Ile)+1.0Thumb+1.0Pyrophosphate
1.0L-Isoleucine + 1.0Adenosine triphosphate + 1.0Hydrogen ion + 1.0tRNA(Ile) + 1.0L-Isoleucine → 1.0L-Isoleucyl-tRNA(Ile) + 1.0Adenosine monophosphate + 1.0Pyrophosphate
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0tRNA(Ile) → 1.0Thumb+1.0Thumb+1.0L-isoleucyl-tRNA(Ile)
1.0Adenosine triphosphate + 1.0L-Isoleucine + 1.0tRNA(Ile) → 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-isoleucyl-tRNA(Ile)
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00045Adenosine monophosphateMetaboCard
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00172L-IsoleucineMetaboCard
ECMDB04142PyrophosphateMetaboCard
GO Classification:
Component
cell part
cytoplasm
intracellular part
Function
adenyl nucleotide binding
adenyl ribonucleotide binding
aminoacyl-tRNA ligase activity
ATP binding
binding
catalytic activity
isoleucine-tRNA ligase activity
ligase activity
ligase activity, forming aminoacyl-tRNA and related compounds
ligase activity, forming carbon-oxygen bonds
nucleoside binding
nucleotide binding
purine nucleoside binding
Process
biosynthetic process
cellular macromolecule biosynthetic process
cellular macromolecule metabolic process
isoleucyl-tRNA aminoacylation
macromolecule biosynthetic process
macromolecule metabolic process
metabolic process
ncRNA metabolic process
RNA metabolic process
translation
tRNA aminoacylation
tRNA aminoacylation for protein translation
tRNA metabolic process
Gene Properties
Blattner:b0026
Gene OrientationClockwise
Centisome Percentage:0.48
Left Sequence End22391
Right Sequence End25207
Gene Sequence:
>2817 bp
ATGAGTGACTATAAATCAACCCTGAATTTGCCGGAAACAGGGTTCCCGATGCGTGGCGAT
CTCGCCAAGCGCGAACCCGGAATGCTGGCGCGTTGGACTGATGATGATCTGTACGGCATC
ATCCGTGCGGCTAAAAAAGGCAAAAAAACCTTCATTCTGCATGATGGCCCTCCTTATGCG
AATGGCAGCATTCATATTGGTCACTCGGTTAACAAGATTCTGAAAGACATTATCGTGAAG
TCCAAAGGGCTTTCCGGTTATGACTCGCCGTATGTGCCTGGCTGGGACTGCCACGGTCTG
CCGATCGAGCTGAAAGTCGAGCAAGAATACGGTAAGCCGGGTGAGAAATTCACCGCCGCC
GAGTTCCGCGCCAAGTGCCGCGAATACGCGGCGACCCAGGTTGACGGTCAACGCAAAGAC
TTTATCCGTCTGGGCGTGCTGGGCGACTGGTCGCACCCGTACCTGACCATGGACTTCAAA
ACTGAAGCCAACATCATCCGCGCGCTGGGCAAAATCATCGGCAACGGTCACCTGCACAAA
GGCGCGAAGCCAGTTCACTGGTGCGTTGACTGCCGTTCTGCGCTGGCGGAAGCGGAAGTT
GAGTATTACGACAAAACTTCTCCGTCCATCGACGTTGCTTTCCAGGCAGTCGATCAGGAT
GCACTGAAAGCAAAATTTGCCGTAAGCAACGTTAACGGCCCAATCTCGCTGGTAATCTGG
ACCACCACGCCGTGGACTCTGCCTGCCAACCGCGCAATCTCTATTGCACCAGATTTCGAC
TATGCGCTGGTGCAGATCGACGGTCAGGCCGTGATTCTGGCGAAAGATCTGGTTGAAAGC
GTAATGCAGCGTATCGGCGTGACCGATTACACCATTCTCGGCACGGTAAAAGGTGCGGAG
CTTGAGCTGCTGCGCTTTACCCATCCGTTTATGGGCTTCGACGTTCCGGCAATCCTCGGC
GATCACGTTACCCTGGATGCCGGTACCGGTGCCGTTCACACCGCGCCTGGCCACGGCCCG
GACGACTATGTGATCGGTCAGAAATACGGCCTGGAAACCGCTAACCCGGTTGGCCCGGAC
GGCACTTATCTGCCGGGCACTTATCCGACGCTGGATGGCGTGAACGTCTTCAAAGCGAAC
GACATCGTCGTTGCGCTGCTGCAGGAAAAAGGCGCGCTGCTGCACGTTGAGAAAATGCAG
CACAGCTATCCGTGCTGCTGGCGTCACAAAACGCCGATCATCTTCCGCGCGACGCCGCAG
TGGTTCGTCAGCATGGATCAGAAAGGTCTGCGTGCGCAGTCACTGAAAGAGATCAAAGGC
GTGCAGTGGATCCCGGACTGGGGCCAGGCGCGTATCGAGTCGATGGTTGCTAACCGTCCT
GACTGGTGTATCTCCCGTCAGCGCACCTGGGGTGTACCGATGTCACTGTTCGTGCACAAA
GACACGGAAGAGCTGCATCCGCGTACCCTTGAACTGATGGAAGAAGTGGCAAAACGCGTT
GAAGTCGATGGCATCCAGGCGTGGTGGGATCTCGATGCGAAAGAGATCCTCGGCGACGAA
GCTGATCAGTACGTGAAAGTGCCGGACACATTGGATGTATGGTTTGACTCCGGATCTACC
CACTCTTCTGTTGTTGACGTGCGTCCGGAATTTGCCGGTCACGCAGCGGACATGTATCTG
GAAGGTTCTGACCAACACCGCGGCTGGTTCATGTCTTCCCTAATGATCTCCACCGCGATG
AAGGGTAAAGCGCCGTATCGTCAGGTACTGACCCACGGCTTTACCGTGGATGGTCAGGGC
CGCAAGATGTCTAAATCCATCGGCAATACCGTTTCGCCGCAGGATGTGATGAACAAACTG
GGCGCGGATATTCTGCGTCTGTGGGTGGCATCAACCGACTACACCGGTGAAATGGCCGTT
TCTGACGAGATCCTGAAACGTGCTGCCGATAGCTATCGTCGTATCCGTAACACCGCGCGC
TTCCTGCTGGCAAACCTGAACGGTTTTGATCCAGCAAAAGATATGGTGAAACCGGAAGAG
ATGGTGGTACTGGATCGCTGGGCCGTAGGTTGTGCGAAAGCGGCACAGGAAGACATCCTC
AAGGCGTACGAAGCATACGATTTCCACGAAGTGGTACAGCGTCTGATGCGCTTCTGCTCC
GTTGAGATGGGTTCCTTCTACCTCGACATCATCAAAGACCGTCAGTACACCGCCAAAGCG
GACAGTGTGGCGCGTCGTAGCTGCCAGACTGCGCTATATCACATCGCAGAAGCGCTGGTG
CGCTGGATGGCACCAATCCTCTCCTTCACCGCTGATGAAGTGTGGGGCTACCTGCCGGGC
GAACGTGAAAAATACGTCTTCACCGGTGAGTGGTACGAAGGCCTGTTTGGCCTGGCAGAC
AGTGAAGCGATGAACGATGCGTTCTGGGACGAGCTGTTGAAAGTGCGTGGCGAAGTGAAC
AAAGTCATTGAGCAAGCGCGTGCCGACAAGAAAGTGGGTGGCTCGCTGGAAGCGGCAGTA
ACCTTGTATGCAGAACCGGAACTGTCGGCGAAACTGACCGCGCTGGGCGATGAATTACGA
TTTGTCCTGTTGACCTCCGGCGCTACCGTTGCAGACTATAACGACGCACCTGCTGATGCT
CAGCAGAGCGAAGTACTCAAAGGGCTGAAAGTCGCGTTGAGTAAAGCCGAAGGTGAGAAG
TGCCCACGCTGCTGGCACTACACCCAGGATGTCGGCAAGGTGGCGGAACACGCAGAAATC
TGCGGCCGCTGTGTCAGCAACGTCGCCGGTGACGGTGAAAAACGTAAGTTTGCCTGA
Protein Properties
Pfam Domain Function:
Protein Residues:938
Protein Molecular Weight:104296
Protein Theoretical pI:6
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Isoleucyl-tRNA synthetase
MSDYKSTLNLPETGFPMRGDLAKREPGMLARWTDDDLYGIIRAAKKGKKTFILHDGPPYA
NGSIHIGHSVNKILKDIIVKSKGLSGYDSPYVPGWDCHGLPIELKVEQEYGKPGEKFTAA
EFRAKCREYAATQVDGQRKDFIRLGVLGDWSHPYLTMDFKTEANIIRALGKIIGNGHLHK
GAKPVHWCVDCRSALAEAEVEYYDKTSPSIDVAFQAVDQDALKAKFAVSNVNGPISLVIW
TTTPWTLPANRAISIAPDFDYALVQIDGQAVILAKDLVESVMQRIGVTDYTILGTVKGAE
LELLRFTHPFMGFDVPAILGDHVTLDAGTGAVHTAPGHGPDDYVIGQKYGLETANPVGPD
GTYLPGTYPTLDGVNVFKANDIVVALLQEKGALLHVEKMQHSYPCCWRHKTPIIFRATPQ
WFVSMDQKGLRAQSLKEIKGVQWIPDWGQARIESMVANRPDWCISRQRTWGVPMSLFVHK
DTEELHPRTLELMEEVAKRVEVDGIQAWWDLDAKEILGDEADQYVKVPDTLDVWFDSGST
HSSVVDVRPEFAGHAADMYLEGSDQHRGWFMSSLMISTAMKGKAPYRQVLTHGFTVDGQG
RKMSKSIGNTVSPQDVMNKLGADILRLWVASTDYTGEMAVSDEILKRAADSYRRIRNTAR
FLLANLNGFDPAKDMVKPEEMVVLDRWAVGCAKAAQEDILKAYEAYDFHEVVQRLMRFCS
VEMGSFYLDIIKDRQYTAKADSVARRSCQTALYHIAEALVRWMAPILSFTADEVWGYLPG
EREKYVFTGEWYEGLFGLADSEAMNDAFWDELLKVRGEVNKVIEQARADKKVGGSLEAAV
TLYAEPELSAKLTALGDELRFVLLTSGATVADYNDAPADAQQSEVLKGLKVALSKAEGEK
CPRCWHYTQDVGKVAEHAEICGRCVSNVAGDGEKRKFA
References
External Links:
ResourceLink
Uniprot ID:P00956
Uniprot Name:SYI_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674290
Ecogene ID:EG10492
Ecocyc:EG10492
ColiBase:b0026
Kegg Gene:b0026
EchoBASE ID:EB0487
CCDB:SYI_ECOLI
BacMap:16128020
General Reference:
  • Bishop, A. C., Beebe, K., Schimmel, P. R. (2003). "Interstice mutations that block site-to-site translocation of a misactivated amino acid bound to a class I tRNA synthetase." Proc Natl Acad Sci U S A 100:490-494. Pubmed: 12515858
  • Bishop, A. C., Nomanbhoy, T. K., Schimmel, P. (2002). "Blocking site-to-site translocation of a misactivated amino acid by mutation of a class I tRNA synthetase." Proc Natl Acad Sci U S A 99:585-590. Pubmed: 11782529
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Clarke, N. D., Lien, D. C., Schimmel, P. (1988). "Evidence from cassette mutagenesis for a structure-function motif in a protein of unknown structure." Science 240:521-523. Pubmed: 3282306
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Hendrickson, T. L., Nomanbhoy, T. K., de Crecy-Lagard, V., Fukai, S., Nureki, O., Yokoyama, S., Schimmel, P. (2002). "Mutational separation of two pathways for editing by a class I tRNA synthetase." Mol Cell 9:353-362. Pubmed: 11864608
  • Hendrickson, T. L., Nomanbhoy, T. K., Schimmel, P. (2000). "Errors from selective disruption of the editing center in a tRNA synthetase." Biochemistry 39:8180-8186. Pubmed: 10889024
  • Innis, M. A., Tokunaga, M., Williams, M. E., Loranger, J. M., Chang, S. Y., Chang, S., Wu, H. C. (1984). "Nucleotide sequence of the Escherichia coli prolipoprotein signal peptidase (lsp) gene." Proc Natl Acad Sci U S A 81:3708-3712. Pubmed: 6374664
  • Kamio, Y., Lin, C. K., Regue, M., Wu, H. C. (1985). "Characterization of the ileS-lsp operon in Escherichia coli. Identification of an open reading frame upstream of the ileS gene and potential promoter(s) for the ileS-lsp operon." J Biol Chem 260:5616-5620. Pubmed: 2985604
  • Nomanbhoy, T. K., Hendrickson, T. L., Schimmel, P. (1999). "Transfer RNA-dependent translocation of misactivated amino acids to prevent errors in protein synthesis." Mol Cell 4:519-528. Pubmed: 10549284
  • Nureki, O., Vassylyev, D. G., Tateno, M., Shimada, A., Nakama, T., Fukai, S., Konno, M., Hendrickson, T. L., Schimmel, P., Yokoyama, S. (1998). "Enzyme structure with two catalytic sites for double-sieve selection of substrate." Science 280:578-582. Pubmed: 9554847
  • Webster, T., Tsai, H., Kula, M., Mackie, G. A., Schimmel, P. (1984). "Specific sequence homology and three-dimensional structure of an aminoacyl transfer RNA synthetase." Science 226:1315-1317. Pubmed: 6390679
  • Yanagisawa, T., Lee, J. T., Wu, H. C., Kawakami, M. (1994). "Relationship of protein structure of isoleucyl-tRNA synthetase with pseudomonic acid resistance of Escherichia coli. A proposed mode of action of pseudomonic acid as an inhibitor of isoleucyl-tRNA synthetase." J Biol Chem 269:24304-24309. Pubmed: 7929087
  • Yu, F., Yamada, H., Daishima, K., Mizushima, S. (1984). "Nucleotide sequence of the lspA gene, the structural gene for lipoprotein signal peptidase of Escherichia coli." FEBS Lett 173:264-268. Pubmed: 6378662
  • Yura, T., Mori, H., Nagai, H., Nagata, T., Ishihama, A., Fujita, N., Isono, K., Mizobuchi, K., Nakata, A. (1992). "Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region." Nucleic Acids Res 20:3305-3308. Pubmed: 1630901
  • Zhang, J., Sprung, R., Pei, J., Tan, X., Kim, S., Zhu, H., Liu, C. F., Grishin, N. V., Zhao, Y. (2009). "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Mol Cell Proteomics 8:215-225. Pubmed: 18723842