Tyrosine--tRNA ligase

Details

Name
Tyrosine--tRNA ligase
Synonyms
  • 6.1.1.1
  • Tyrosyl-tRNA synthetase
  • TyrRS
Gene Name
tyrS
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0016655|Tyrosine--tRNA ligase
MASSNLIKQLQERGLVAQVTDEEALAERLAQGPIALYCGFDPTADSLHLGHLVPLLCLKR
FQQAGHKPVALVGGATGLIGDPSFKAAERKLNTEETVQEWVDKIRKQVAPFLDFDCGENS
AIAANNYDWFGNMNVLTFLRDIGKHFSVNQMINKEAVKQRLNREDQGISFTEFSYNLLQG
YDFACLNKQYGVVLQIGGSDQWGNITSGIDLTRRLHQNQVFGLTVPLITKADGTKFGKTE
GGAVWLDPKKTSPYKFYQFWINTADADVYRFLKFFTFMSIEEINALEEEDKNSGKAPRAQ
YVLAEQVTRLVHGEEGLQAAKRITECLFSGSLSALSEADFEQLAQDGVPMVEMEKGADLM
QALVDSELQPSRGQARKTIASNAITINGEKQSDPEYFFKEEDRLFGRFTLLRRGKKNYCL
ICWK
Number of residues
424
Molecular Weight
47526.605
Theoretical pI
5.55
GO Classification
Functions
ATP binding / RNA binding / tyrosine-tRNA ligase activity
Processes
tRNA aminoacylation / tyrosyl-tRNA aminoacylation
Components
cytosol / membrane
General Function
Tyrosine-trna ligase activity
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).
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0016656|Tyrosine--tRNA ligase (tyrS)
ATGGCAAGCAGTAACTTGATTAAACAATTGCAAGAGCGGGGGCTGGTAGCCCAGGTGACG
GACGAGGAAGCGTTAGCAGAGCGACTGGCGCAAGGCCCGATCGCGCTCTATTGCGGCTTC
GATCCTACCGCTGACAGCTTGCATTTGGGGCATCTTGTTCCATTGTTATGCCTGAAACGC
TTCCAGCAGGCGGGCCACAAGCCGGTTGCGCTGGTAGGCGGCGCGACGGGTCTGATTGGC
GACCCGAGCTTCAAAGCTGCCGAGCGTAAGCTGAACACCGAAGAAACTGTTCAGGAGTGG
GTGGACAAAATCCGTAAGCAGGTTGCCCCGTTCCTCGATTTCGACTGTGGAGAAAACTCT
GCTATCGCGGCGAACAACTATGACTGGTTCGGCAATATGAATGTGCTGACCTTCCTGCGC
GATATTGGCAAACACTTCTCCGTTAACCAGATGATCAACAAAGAAGCGGTTAAGCAGCGT
CTCAACCGTGAAGATCAGGGGATTTCGTTCACTGAGTTTTCCTACAACCTGTTGCAGGGT
TATGACTTCGCCTGTCTGAACAAACAGTACGGTGTGGTGCTGCAAATTGGTGGTTCTGAC
CAGTGGGGTAACATCACTTCTGGTATCGACCTGACCCGTCGTCTGCATCAGAATCAGGTG
TTTGGCCTGACCGTTCCGCTGATCACTAAAGCAGATGGCACCAAATTTGGTAAAACTGAA
GGCGGCGCAGTCTGGTTGGATCCGAAGAAAACCAGCCCGTACAAATTCTACCAGTTCTGG
ATCAACACTGCGGATGCCGACGTTTACCGCTTCCTGAAGTTCTTCACCTTTATGAGCATT
GAAGAGATCAACGCCCTGGAAGAAGAAGATAAAAACAGCGGTAAAGCACCGCGCGCCCAG
TATGTACTGGCGGAGCAGGTGACTCGTCTGGTTCACGGTGAAGAAGGTTTACAGGCGGCA
AAACGTATTACCGAATGCCTGTTCAGCGGTTCTTTGAGTGCGCTGAGTGAAGCGGACTTC
GAACAGCTGGCGCAGGACGGCGTACCGATGGTTGAGATGGAAAAGGGCGCAGACCTGATG
CAGGCACTGGTCGATTCTGAACTGCAACCTTCCCGTGGTCAGGCACGTAAAACTATCGCC
TCCAATGCCATCACCATTAACGGTGAAAAACAGTCCGATCCTGAATACTTCTTTAAAGAA
GAAGATCGTCTGTTTGGTCGTTTTACCTTACTGCGTCGCGGTAAAAAGAATTACTGTCTG
ATTTGCTGGAAATAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP0AGJ9
UniProtKB Entry NameSYY_ECOLI
GenBank Protein ID148094
GenBank Gene IDJ01719
General References
  1. Barker DG, Bruton CJ, Winter G: The tyrosyl-tRNA synthetase from Escherichia coli. Complete nucleotide sequence of the structural gene. FEBS Lett. 1982 Dec 27;150(2):419-23. [Article]
  2. 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 al.: 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. 1996 Dec 31;3(6):363-77. [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. Lam HM, Winkler ME: Characterization of the complex pdxH-tyrS operon of Escherichia coli K-12 and pleiotropic phenotypes caused by pdxH insertion mutations. J Bacteriol. 1992 Oct;174(19):6033-45. [Article]
  6. VanBogelen RA, Abshire KZ, Moldover B, Olson ER, Neidhardt FC: Escherichia coli proteome analysis using the gene-protein database. Electrophoresis. 1997 Aug;18(8):1243-51. [Article]
  7. Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y: Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli. Mol Cell Proteomics. 2009 Feb;8(2):215-25. doi: 10.1074/mcp.M800187-MCP200. Epub 2008 Aug 23. [Article]
  8. Kobayashi T, Takimura T, Sekine R, Kelly VP, Kamata K, Sakamoto K, Nishimura S, Yokoyama S: Structural snapshots of the KMSKS loop rearrangement for amino acid activation by bacterial tyrosyl-tRNA synthetase. J Mol Biol. 2005 Feb 11;346(1):105-17. Epub 2004 Dec 15. [Article]
  9. Kobayashi T, Sakamoto K, Takimura T, Sekine R, Kelly VP, Kamata K, Nishimura S, Yokoyama S: Structural basis of nonnatural amino acid recognition by an engineered aminoacyl-tRNA synthetase for genetic code expansion. Proc Natl Acad Sci U S A. 2005 Feb 1;102(5):1366-71. Epub 2005 Jan 25. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB017583-Iodo-TyrosineexperimentalunknownDetails
DB03325TyrosyladenylateexperimentalunknownDetails