Tyrosyl-tRNA synthetase (P0AGJ9)

Identification
Name:Tyrosyl-tRNA synthetase
Synonyms:
  • Tyrosine--tRNA ligase
  • TyrRS
Gene Name:tyrS
Enzyme Class:
Biological Properties
General Function:Involved in nucleotide binding
Specific Function:Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction:tyrosine is first activated by ATP to form Tyr- AMP and then transferred to the acceptor end of tRNA(Tyr)
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0tRNA(Tyr)+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0L-Tyrosyl-tRNA(Tyr)+1.0Thumb
1.0Adenosine triphosphate + 1.0tRNA(Tyr) + 1.0L-Tyrosine + 1.0tRNA(Tyr) ↔ 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-Tyrosyl-tRNA(Tyr) + 1.0L-Tyrosyl-tRNA(Tyr)
ReactionCard
1.0Thumb+1.0Thumb+1.0tRNA(Tyr) ↔ 1.0Thumb+1.0Thumb+1.0L-Tyrosyl-tRNA(Tyr)
1.0Adenosine triphosphate + 1.0L-Tyrosine + 1.0tRNA(Tyr) ↔ 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-Tyrosyl-tRNA(Tyr)
ReactionCard
SMPDB Reactions:
1.0L-Tyrosine+1.0Thumb+1.0Thumb+1.0tRNA(Tyr)+1.0Thumb → 1.0Thumb+1.0Pyrophosphate+1.0L-tyrosyl-tRNA(Tyr)
1.0L-Tyrosine + 1.0Adenosine triphosphate + 1.0Hydrogen ion + 1.0tRNA(Tyr) + 1.0L-Tyrosine → 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-tyrosyl-tRNA(Tyr)
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0tRNA(Tyr) → 1.0Thumb+1.0Thumb+1.0L-tyrosyl-tRNA(Tyr)
1.0Adenosine triphosphate + 1.0L-Tyrosine + 1.0tRNA(Tyr) → 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-tyrosyl-tRNA(Tyr)
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00045Adenosine monophosphateMetaboCard
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00158L-TyrosineMetaboCard
ECMDB23804L-Tyrosyl-tRNA(Tyr)MetaboCard
ECMDB04142PyrophosphateMetaboCard
ECMDB23864tRNA(Tyr)MetaboCard
GO Classification:
Component
cell part
cytoplasm
intracellular part
Function
adenyl nucleotide binding
adenyl ribonucleotide binding
aminoacyl-tRNA ligase activity
ATP binding
binding
catalytic activity
ligase activity
ligase activity, forming aminoacyl-tRNA and related compounds
ligase activity, forming carbon-oxygen bonds
nucleic acid binding
nucleoside binding
nucleotide binding
purine nucleoside binding
RNA binding
tyrosine-tRNA ligase activity
Process
biosynthetic process
cellular macromolecule biosynthetic process
cellular macromolecule metabolic process
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
tyrosyl-tRNA aminoacylation
Gene Properties
Blattner:b1637
Gene OrientationCounterclockwise
Centisome Percentage:36.94
Left Sequence End1713972
Right Sequence End1715246
Gene Sequence:
>1275 bp
ATGACAGATAAACGCAAAGATGGCTCAGGCAAATTGCTGTATTGCTCTTTTTGCGGCAAA
AGCCAGCATGAAGTGCGCAAGCTGATTGCCGGTCCATCCGTGTATATCTGCGACGAATGT
GTTGATTTATGTAACGACATCATTCGCGAAGAGATTAAAGAAGTTGCACCGCATCGTGAA
CGCAGTGCGCTACCGACGCCGCATGAAATTCGCAACCACCTGGACGATTACGTTATCGGC
CAGGAACAGGCGAAAAAAGTGCTGGCGGTCGCGGTATACAACCATTACAAACGTCTGCGC
AACGGCGATACCAGCAATGGCGTCGAGTTGGGCAAAAGTAACATTCTGCTGATCGGTCCG
ACCGGTTCCGGTAAAACGCTGCTGGCTGAAACGCTGGCGCGCCTGCTGGATGTTCCGTTC
ACCATGGCCGACGCGACTACACTGACCGAAGCCGGTTATGTGGGTGAAGACGTTGAAAAC
ATCATTCAGAAGCTGTTGCAGAAATGCGACTACGATGTCCAGAAAGCACAGCGTGGTATT
GTCTACATCGATGAAATCGACAAGATTTCTCGTAAGTCAGACAACCCGTCCATTACCCGA
GACGTTTCCGGTGAAGGCGTACAGCAGGCACTGTTGAAACTGATCGAAGGTACGGTAGCT
GCTGTTCCACCGCAAGGTGGGCGTAAACATCCGCAGCAGGAATTCTTGCAGGTTGATACC
TCTAAGATCCTGTTTATTTGTGGCGGTGCGTTTGCCGGTCTGGATAAAGTGATTTCCCAC
CGTGTAGAAACCGGCTCCGGCATTGGTTTTGGCGCGACGGTAAAAGCGAAGTCCGACAAA
GCAAGCGAAGGCGAGCTGCTGGCGCAGGTTGAACCGGAAGATCTGATCAAGTTTGGTCTT
ATCCCTGAGTTTATTGGTCGTCTGCCGGTTGTCGCAACGTTGAATGAACTGAGCGAAGAA
GCTCTGATTCAGATCCTCAAAGAGCCGAAAAACGCCCTGACCAAGCAGTATCAGGCGCTG
TTTAATCTGGAAGGCGTGGATCTGGAATTCCGTGACGAGGCGCTGGATGCTATCGCTAAG
AAAGCGATGGCGCGTAAAACCGGTGCCCGTGGCCTGCGTTCCATCGTAGAAGCCGCACTG
CTCGATACCATGTACGATCTGCCGTCCATGGAAGACGTCGAAAAAGTGGTTATCGACGAG
TCGGTAATTGATGGTCAAAGCAAACCGTTGCTGATTTATGGCAAGCCGGAAGCGCAACAG
GCATCTGGTGAATAA
Protein Properties
Pfam Domain Function:
Protein Residues:424
Protein Molecular Weight:47527
Protein Theoretical pI:6
PDB File:1X8X
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Tyrosyl-tRNA synthetase
MASSNLIKQLQERGLVAQVTDEEALAERLAQGPIALYCGFDPTADSLHLGHLVPLLCLKR
FQQAGHKPVALVGGATGLIGDPSFKAAERKLNTEETVQEWVDKIRKQVAPFLDFDCGENS
AIAANNYDWFGNMNVLTFLRDIGKHFSVNQMINKEAVKQRLNREDQGISFTEFSYNLLQG
YDFACLNKQYGVVLQIGGSDQWGNITSGIDLTRRLHQNQVFGLTVPLITKADGTKFGKTE
GGAVWLDPKKTSPYKFYQFWINTADADVYRFLKFFTFMSIEEINALEEEDKNSGKAPRAQ
YVLAEQVTRLVHGEEGLQAAKRITECLFSGSLSALSEADFEQLAQDGVPMVEMEKGADLM
QALVDSELQPSRGQARKTIASNAITINGEKQSDPEYFFKEEDRLFGRFTLLRRGKKNYCL
ICWK
References
External Links:
ResourceLink
Uniprot ID:P0AGJ9
Uniprot Name:SYY_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674578
PDB ID:1X8X
Ecogene ID:EG11043
Ecocyc:EG11043
ColiBase:b1637
Kegg Gene:b1637
EchoBASE ID:EB1036
CCDB:SYY_ECOLI
BacMap:16129595
General Reference:
  • Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kasai, H., Kashimoto, K., Kimura, S., Kitakawa, M., Kitagawa, M., Makino, K., Miki, T., Mizobuchi, K., Mori, H., Mori, T., Motomura, K., Nakade, S., Nakamura, Y., Nashimoto, H., Nishio, Y., Oshima, T., Saito, N., Sampei, G., Horiuchi, T., et, a. l. .. (1996). "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." DNA Res 3:363-377. Pubmed: 9097039
  • Barker, D. G., Bruton, C. J., Winter, G. (1982). "The tyrosyl-tRNA synthetase from Escherichia coli. Complete nucleotide sequence of the structural gene." FEBS Lett 150:419-423. Pubmed: 6761148
  • 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
  • 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
  • Kobayashi, T., Sakamoto, K., Takimura, T., Sekine, R., Kelly, V. P., Kamata, K., Nishimura, S., Yokoyama, S. (2005). "Structural basis of nonnatural amino acid recognition by an engineered aminoacyl-tRNA synthetase for genetic code expansion." Proc Natl Acad Sci U S A 102:1366-1371. Pubmed: 15671170
  • Kobayashi, T., Takimura, T., Sekine, R., Kelly, V. P., Kamata, K., Sakamoto, K., Nishimura, S., Yokoyama, S. (2005). "Structural snapshots of the KMSKS loop rearrangement for amino acid activation by bacterial tyrosyl-tRNA synthetase." J Mol Biol 346:105-117. Pubmed: 15663931
  • Lam, H. M., Winkler, M. E. (1992). "Characterization of the complex pdxH-tyrS operon of Escherichia coli K-12 and pleiotropic phenotypes caused by pdxH insertion mutations." J Bacteriol 174:6033-6045. Pubmed: 1356963
  • 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