Tryptophanyl-tRNA synthetase (P00954)

Identification
Name:Tryptophanyl-tRNA synthetase
Synonyms:
  • Tryptophan--tRNA ligase
  • TrpRS
Gene Name:trpS
Enzyme Class:
Biological Properties
General Function:Involved in nucleotide binding
Specific Function:ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + L-tryptophyl-tRNA(Trp)
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0tRNA(Trp)+1.0Thumb+1.0tRNA(Trp) ↔ 1.0Thumb+1.0Thumb+1.0L-Tryptophanyl-tRNA(Trp)
1.0Adenosine triphosphate + 1.0tRNA(Trp) + 1.0L-Tryptophan + 1.0tRNA(Trp) ↔ 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-Tryptophanyl-tRNA(Trp)
ReactionCard
1.0Thumb+1.0Thumb+1.0tRNA(Trp) ↔ 1.0Thumb+1.0Thumb+1.0L-Tryptophanyl-tRNA(Trp)
1.0Adenosine triphosphate + 1.0L-Tryptophan + 1.0tRNA(Trp) ↔ 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-Tryptophanyl-tRNA(Trp)
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb+1.0Thumb+1.0tRNA(Trp) → 1.0Thumb+1.0Pyrophosphate+1.0L-tryptophyl-tRNA(Trp)
1.0L-Tryptophan + 1.0Adenosine triphosphate + 1.0Hydrogen ion + 1.0tRNA(Trp) → 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-tryptophyl-tRNA(Trp)
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0tRNA(Trp) → 1.0Thumb+1.0Thumb+1.0L-tryptophyl-tRNA(Trp)
1.0Adenosine triphosphate + 1.0L-Tryptophan + 1.0tRNA(Trp) → 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-tryptophyl-tRNA(Trp)
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00045Adenosine monophosphateMetaboCard
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00929L-TryptophanMetaboCard
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
tryptophan-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
tryptophanyl-tRNA aminoacylation
Gene Properties
Blattner:b3384
Gene OrientationCounterclockwise
Centisome Percentage:75.67
Left Sequence End3510656
Right Sequence End3511660
Gene Sequence:
>1005 bp
GTGAAACTGGATGAAATCGCTCGGCTGGCGGGAGTGTCGCGGACCACTGCAAGCTATGTT
ATTAACGGCAAAGCGAAGCAATACCGTGTGAGCGACAAAACCGTTGAAAAAGTCATGGCT
GTGGTGCGTGAGCACAATTACCACCCGAACGCCGTGGCAGCTGGGCTTCGTGCTGGACGC
ACACGTTCTATTGGTCTTGTGATCCCCGATCTGGAGAACACCAGCTATACCCGCATCGCT
AACTATCTTGAACGCCAGGCGCGGCAACGGGGTTATCAACTGCTGATTGCCTGCTCAGAA
GATCAGCCAGACAACGAAATGCGGTGCATTGAGCACCTTTTACAGCGTCAGGTTGATGCC
ATTATTGTTTCGACGTCGTTGCCTCCTGAGCATCCTTTTTATCAACGCTGGGCTAACGAC
CCGTTCCCGATTGTCGCGCTGGACCGCGCCCTCGATCGTGAACACTTCACCAGCGTGGTT
GGTGCCGATCAGGATGATGCCGAAATGCTGGCGGAAGAGTTACGTAAGTTTCCCGCCGAG
ACGGTGCTTTATCTTGGTGCGCTACCGGAGCTTTCTGTCAGCTTCCTGCGTGAACAAGGT
TTCCGTACTGCCTGGAAAGATGATCCGCGCGAAGTGCATTTCCTGTATGCCAACAGCTAT
GAGCGGGAGGCGGCTGCCCAGTTATTCGAAAAATGGCTGGAAACGCATCCGATGCCGCAG
GCGCTGTTCACAACGTCGTTTGCGTTGTTGCAAGGAGTGATGGATGTCACGCTGCGTCGC
GACGGCAAACTGCCTTCTGACCTGGCAATTGCCACCTTTGGCGATAACGAACTGCTCGAC
TTCTTACAGTGTCCGGTGCTGGCAGTGGCTCAACGTCACCGCGATGTCGCAGAGCGTGTG
CTGGAGATTGTCCTGGCAAGCCTGGACGAACCGCGTAAGCCAAAACCTGGTTTAACGCGC
ATTAAACGTAATCTCTATCGCCGCGGCGTGCTCAGCCGTAGCTAA
Protein Properties
Pfam Domain Function:
Protein Residues:334
Protein Molecular Weight:37438
Protein Theoretical pI:7
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Tryptophanyl-tRNA synthetase
MTKPIVFSGAQPSGELTIGNYMGALRQWVNMQDDYHCIYCIVDQHAITVRQDAQKLRKAT
LDTLALYLACGIDPEKSTIFVQSHVPEHAQLGWALNCYTYFGELSRMTQFKDKSARYAEN
INAGLFDYPVLMAADILLYQTNLVPVGEDQKQHLELSRDIAQRFNALYGEIFKVPEPFIP
KSGARVMSLLEPTKKMSKSDDNRNNVIGLLEDPKSVVKKIKRAVTDSDEPPVVRYDVQNK
AGVSNLLDILSAVTGQSIPELEKQFEGKMYGHLKGEVADAVSGMLTELQERYHRFRNDEA
FLQQVMKDGAEKASAHASRTLKAVYEAIGFVAKP
References
External Links:
ResourceLink
Uniprot ID:P00954
Uniprot Name:SYW_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:21321961
Ecogene ID:EG11030
Ecocyc:EG11030
ColiBase:b3384
Kegg Gene:b3384
EchoBASE ID:EB1023
CCDB:SYW_ECOLI
BacMap:16131262
General Reference:
  • 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
  • Hall, C. V., vanCleemput, M., Muench, K. H., Yanofsky, C. (1982). "The nucleotide sequence of the structural gene for Escherichia coli tryptophanyl-tRNA synthetase." J Biol Chem 257:6132-6136. Pubmed: 7042706
  • Hall, C. V., Yanofsky, C. (1981). "Cloning and characterization of the gene for Escherichia coli tryptophanyl-transfer ribonucleic acid synthetase." J Bacteriol 148:941-949. Pubmed: 6171561
  • 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
  • Lyngstadaas, A., Lobner-Olesen, A., Boye, E. (1995). "Characterization of three genes in the dam-containing operon of Escherichia coli." Mol Gen Genet 247:546-554. Pubmed: 7603433
  • Sever, S., Rogers, K., Rogers, M. J., Carter, C. Jr, Soll, D. (1996). "Escherichia coli tryptophanyl-tRNA synthetase mutants selected for tryptophan auxotrophy implicate the dimer interface in optimizing amino acid binding." Biochemistry 35:32-40. Pubmed: 8555191
  • Winter, G. P., Hartley, B. S., McLachlan, A. D., Lee, M., Muench, K. H. (1977). "Sequence homologies between the tryptophanyl tRNA synthetases of Bacillus stearothermophilus and Escherichia coli." FEBS Lett 82:348-350. Pubmed: 334569