Threonyl-tRNA synthetase (P0A8M3)

Identification
Name:Threonyl-tRNA synthetase
Synonyms:
  • Threonine--tRNA ligase
  • ThrRS
Gene Name:thrS
Enzyme Class:
Biological Properties
General Function:Involved in nucleotide binding
Specific Function:ThrS is also a translational repressor protein, it controls the translation of its own gene by binding to its mRNA
Cellular Location:Cytoplasm
SMPDB Pathways:Not Available
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0tRNA(Thr)+1.0tRNA(Thr) ↔ 1.0Thumb+1.0Thumb+1.0L-Threonyl-tRNA(Thr)+1.0L-Threonyl-tRNA(Thr)
1.0Adenosine triphosphate + 1.0L-Threonine + 1.0tRNA(Thr) + 1.0tRNA(Thr) ↔ 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-Threonyl-tRNA(Thr) + 1.0L-Threonyl-tRNA(Thr)
ReactionCard
1.0Thumb+1.0Thumb+1.0tRNA(Thr) ↔ 1.0Thumb+1.0Thumb+1.0L-Threonyl-tRNA(Thr)
1.0Adenosine triphosphate + 1.0L-Threonine + 1.0tRNA(Thr) ↔ 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-Threonyl-tRNA(Thr)
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0tRNA(Thr) → 1.0Thumb+1.0Thumb+1.0L-threonyl-tRNA(Thr)
1.0Adenosine triphosphate + 1.0L-Threonine + 1.0tRNA(Thr) → 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-threonyl-tRNA(Thr)
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00045Adenosine monophosphateMetaboCard
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB00167L-ThreonineMetaboCard
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
ligase activity
ligase activity, forming aminoacyl-tRNA and related compounds
ligase activity, forming carbon-oxygen bonds
nucleoside binding
nucleotide binding
purine nucleoside binding
threonine-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
threonyl-tRNA aminoacylation
translation
tRNA aminoacylation
tRNA aminoacylation for protein translation
tRNA metabolic process
Gene Properties
Blattner:b1719
Gene OrientationCounterclockwise
Centisome Percentage:38.77
Left Sequence End1798666
Right Sequence End1800594
Gene Sequence:
>1929 bp
ATGCCTGTTATAACTCTTCCTGATGGCAGCCAACGCCATTACGATCACGCTGTAAGCCCC
ATGGATGTTGCGCTGGACATTGGTCCAGGTCTGGCGAAAGCCTGTATCGCAGGGCGCGTT
AATGGCGAACTGGTTGATGCTTGCGATCTGATTGAAAACGACGCACAACTGTCGATCATT
ACCGCCAAAGACGAAGAAGGTCTGGAGATCATTCGTCACTCCTGTGCGCACCTGTTAGGG
CACGCGATTAAACAACTTTGGCCGCATACCAAAATGGCAATCGGCCCGGTTATTGACAAC
GGTTTTTATTACGACGTTGATCTTGACCGCACGTTAACCCAGGAAGATGTCGAAGCACTC
GAGAAGCGGATGCATGAGCTTGCTGAGAAAAACTACGACGTCATTAAGAAGAAAGTCAGC
TGGCACGAAGCGCGTGAAACTTTCGCCAACCGTGGGGAGAGCTACAAAGTCTCCATTCTT
GACGAAAACATCGCCCATGATGACAAGCCAGGTCTGTACTTCCATGAAGAATATGTCGAT
ATGTGCCGCGGTCCGCACGTACCGAACATGCGTTTCTGCCATCATTTCAAACTAATGAAA
ACGGCAGGGGCTTACTGGCGTGGCGACAGCAACAACAAAATGTTGCAACGTATTTACGGT
ACGGCGTGGGCAGACAAAAAAGCACTTAACGCTTACCTGCAGCGCCTGGAAGAAGCCGCG
AAACGCGACCACCGTAAAATCGGTAAACAGCTCGACCTGTACCATATGCAGGAAGAAGCG
CCGGGTATGGTATTCTGGCACAACGACGGCTGGACCATCTTCCGTGAACTGGAAGTGTTT
GTTCGTTCTAAACTGAAAGAGTACCAGTATCAGGAAGTTAAAGGTCCGTTCATGATGGAC
CGTGTCCTGTGGGAAAAAACCGGTCACTGGGACAACTACAAAGATGCAATGTTCACCACA
TCTTCTGAGAACCGTGAATACTGCATTAAGCCGATGAACTGCCCGGGTCACGTACAAATT
TTCAACCAGGGGCTGAAGTCTTATCGCGATCTGCCGCTGCGTATGGCCGAGTTTGGTAGC
TGCCACCGTAACGAGCCGTCAGGTTCGCTGCATGGCCTGATGCGCGTGCGTGGATTTACC
CAGGATGACGCGCATATCTTCTGTACTGAAGAACAAATTCGCGATGAAGTTAACGGATGT
ATCCGTTTAGTCTATGATATGTACAGCACTTTTGGCTTCGAGAAGATCGTCGTCAAACTC
TCCACTCGTCCTGAAAAACGTATTGGCAGCGACGAAATGTGGGATCGTGCTGAGGCGGAC
CTGGCGGTTGCGCTGGAAGAAAACAACATCCCGTTTGAATATCAACTGGGTGAAGGCGCT
TTCTACGGTCCGAAAATTGAATTTACCCTGTATGACTGCCTCGATCGTGCATGGCAGTGC
GGTACAGTACAGCTGGACTTCTCTTTGCCGTCTCGTCTGAGCGCTTCTTATGTAGGCGAA
GACAATGAACGTAAAGTACCGGTAATGATTCACCGCGCAATTCTGGGGTCGATGGAACGT
TTCATCGGTATCCTGACCGAAGAGTTCGCTGGTTTCTTCCCGACCTGGCTTGCGCCGGTT
CAGGTTGTTATCATGAATATTACCGATTCACAGTCTGAATACGTTAACGAATTGACGCAA
AAACTATCAAATGCGGGCATTCGTGTTAAAGCAGACTTGAGAAATGAGAAGATTGGCTTT
AAAATCCGCGAGCACACTTTGCGTCGCGTCCCATATATGCTGGTCTGTGGTGATAAAGAG
GTGGAATCAGGCAAAGTTGCCGTTCGCACCCGCCGTGGTAAAGACCTGGGAAGCATGGAC
GTAAATGAAGTGATCGAGAAGCTGCAACAAGAGATTCGCAGCCGCAGTCTTAAACAATTG
GAGGAATAA
Protein Properties
Pfam Domain Function:
Protein Residues:642
Protein Molecular Weight:74014
Protein Theoretical pI:6
PDB File:1QF6
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Threonyl-tRNA synthetase
MPVITLPDGSQRHYDHAVSPMDVALDIGPGLAKACIAGRVNGELVDACDLIENDAQLSII
TAKDEEGLEIIRHSCAHLLGHAIKQLWPHTKMAIGPVIDNGFYYDVDLDRTLTQEDVEAL
EKRMHELAEKNYDVIKKKVSWHEARETFANRGESYKVSILDENIAHDDKPGLYFHEEYVD
MCRGPHVPNMRFCHHFKLMKTAGAYWRGDSNNKMLQRIYGTAWADKKALNAYLQRLEEAA
KRDHRKIGKQLDLYHMQEEAPGMVFWHNDGWTIFRELEVFVRSKLKEYQYQEVKGPFMMD
RVLWEKTGHWDNYKDAMFTTSSENREYCIKPMNCPGHVQIFNQGLKSYRDLPLRMAEFGS
CHRNEPSGSLHGLMRVRGFTQDDAHIFCTEEQIRDEVNGCIRLVYDMYSTFGFEKIVVKL
STRPEKRIGSDEMWDRAEADLAVALEENNIPFEYQLGEGAFYGPKIEFTLYDCLDRAWQC
GTVQLDFSLPSRLSASYVGEDNERKVPVMIHRAILGSMERFIGILTEEFAGFFPTWLAPV
QVVIMNITDSQSEYVNELTQKLSNAGIRVKADLRNEKIGFKIREHTLRRVPYMLVCGDKE
VESGKVAVRTRRGKDLGSMDVNEVIEKLQQEIRSRSLKQLEE
References
External Links:
ResourceLink
Uniprot ID:P0A8M3
Uniprot Name:SYT_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1742811
PDB ID:1QF6
Ecogene ID:EG11001
Ecocyc:EG11001
ColiBase:b1719
Kegg Gene:b1719
EchoBASE ID:EB0994
CCDB:SYT_ECOLI
BacMap:16129675
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
  • 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
  • Mayaux, J. F., Fayat, G., Fromant, M., Springer, M., Grunberg-Manago, M., Blanquet, S. (1983). "Structural and transcriptional evidence for related thrS and infC expression." Proc Natl Acad Sci U S A 80:6152-6156. Pubmed: 6353409
  • Sankaranarayanan, R., Dock-Bregeon, A. C., Rees, B., Bovee, M., Caillet, J., Romby, P., Francklyn, C. S., Moras, D. (2000). "Zinc ion mediated amino acid discrimination by threonyl-tRNA synthetase." Nat Struct Biol 7:461-465. Pubmed: 10881191
  • Sankaranarayanan, R., Dock-Bregeon, A. C., Romby, P., Caillet, J., Springer, M., Rees, B., Ehresmann, C., Ehresmann, B., Moras, D. (1999). "The structure of threonyl-tRNA synthetase-tRNA(Thr) complex enlightens its repressor activity and reveals an essential zinc ion in the active site." Cell 97:371-381. Pubmed: 10319817
  • Springer, M., Graffe, M., Butler, J. S., Grunberg-Manago, M. (1986). "Genetic definition of the translational operator of the threonine-tRNA ligase gene in Escherichia coli." Proc Natl Acad Sci U S A 83:4384-4388. Pubmed: 3086882
  • 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