Valyl-tRNA synthetase (P07118)

Identification
Name:Valyl-tRNA synthetase
Synonyms:
  • Valine--tRNA ligase
  • ValRS
Gene Name:valS
Enzyme Class:
Biological Properties
General Function:Involved in nucleotide binding
Specific Function:Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a "posttransfer" editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
  • Aminoacyl-tRNA biosynthesis ec00970
  • Valine, leucine and isoleucine biosynthesis ec00290
KEGG Reactions:
1.0Thumb+1.0tRNA(Val)+1.0Thumb+1.0tRNA(Val) ↔ 1.0Thumb+1.0Thumb+1.0L-Valyl-tRNA(Val)+1.0Thumb
1.0Adenosine triphosphate + 1.0tRNA(Val) + 1.0L-Valine + 1.0tRNA(Val) ↔ 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-Valyl-tRNA(Val) + 1.0L-Valyl-tRNA(Val)
ReactionCard
1.0Thumb+1.0Thumb+1.0tRNA(Val) ↔ 1.0Thumb+1.0Thumb+1.0L-Valyl-tRNA(Val)
1.0Adenosine triphosphate + 1.0L-Valine + 1.0tRNA(Val) ↔ 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-Valyl-tRNA(Val)
ReactionCard
SMPDB Reactions:
1.0L-Valine+1.0Thumb+1.0Thumb+1.0tRNA(Val)+1.0Thumb → 1.0Thumb+1.0Pyrophosphate+1.0L-Valyl-tRNA(Val)
1.0L-Valine + 1.0Adenosine triphosphate + 1.0Hydrogen ion + 1.0tRNA(Val) + 1.0L-Valine → 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-Valyl-tRNA(Val)
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0tRNA(Val) → 1.0Thumb+1.0Thumb+1.0L-valyl-tRNA(Val)
1.0Adenosine triphosphate + 1.0L-Valine + 1.0tRNA(Val) → 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-valyl-tRNA(Val)
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00045Adenosine monophosphateMetaboCard
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00883L-ValineMetaboCard
ECMDB23797L-Valyl-tRNA(Val)MetaboCard
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
valine-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
valyl-tRNA aminoacylation
Gene Properties
Blattner:b4258
Gene OrientationCounterclockwise
Centisome Percentage:96.54
Left Sequence End4479005
Right Sequence End4481860
Gene Sequence:
>2856 bp
ATGGAAAAGACATATAACCCACAAGATATCGAACAGCCGCTTTACGAGCACTGGGAAAAG
CAGGGCTACTTTAAGCCTAATGGCGATGAAAGCCAGGAAAGTTTCTGCATCATGATCCCG
CCGCCGAACGTCACCGGCAGTTTGCATATGGGTCACGCCTTCCAGCAAACCATCATGGAT
ACCATGATCCGCTATCAGCGCATGCAGGGCAAAAACACCCTGTGGCAGGTCGGTACTGAC
CACGCCGGGATCGCTACCCAGATGGTCGTTGAGCGCAAGATTGCCGCAGAAGAAGGTAAA
ACCCGTCACGACTACGGCCGCGAAGCTTTCATCGACAAAATCTGGGAATGGAAAGCGGAA
TCTGGCGGCACCATTACCCGTCAGATGCGCCGTCTCGGCAACTCCGTCGACTGGGAGCGT
GAACGCTTCACCATGGACGAAGGCCTGTCCAATGCGGTGAAAGAAGTTTTCGTTCGTCTG
TATAAAGAAGACCTGATTTACCGTGGCAAACGCCTGGTAAACTGGGATCCGAAACTGCGC
ACCGCTATCTCTGACCTGGAAGTCGAAAACCGCGAATCGAAAGGTTCGATGTGGCACATC
CGCTATCCGCTGGCTGACGGTGCGAAAACCGCAGACGGTAAAGATTATCTGGTGGTCGCG
ACTACCCGTCCAGAAACCCTGCTGGGCGATACTGGCGTAGCCGTTAACCCGGAAGATCCG
CGTTACAAAGATCTGATTGGCAAATATGTCATTCTGCCGCTGGTTAACCGTCGTATTCCG
ATCGTTGGCGACGAACACGCCGACATGGAAAAAGGCACCGGCTGCGTGAAAATCACTCCG
GCGCACGACTTTAACGACTATGAAGTGGGTAAACGTCACGCCCTGCCGATGATCAACATC
CTGACCTTTGACGGCGATATCCGTGAAAGCGCCCAGGTGTTCGATACCAAAGGTAACGAA
TCTGACGTTTATTCCAGCGAAATCCCTGCAGAGTTCCAGAAACTGGAGCGTTTTGCTGCA
CGTAAAGCAGTCGTTGCCGCAGTTGACGCGCTTGGCCTGCTGGAAGAAATTAAACCGCAC
GACCTGACCGTTCCTTACGGCGACCGTGGCGGCGTAGTTATCGAACCAATGCTGACCGAC
CAGTGGTACGTGCGTGCCGATGTCCTGGCGAAACCGGCGGTTGAAGCGGTTGAGAACGGC
GACATTCAGTTCGTACCGAAGCAGTACGAAAACATGTACTTCTCCTGGATGCGCGATATT
CAGGACTGGTGTATCTCTCGTCAGTTGTGGTGGGGTCACCGTATCCCGGCATGGTATGAC
GAAGCGGGTAACGTTTATGTTGGCCGCAACGAAGACGAAGTGCGTAAAGAAAATAACCTC
GGTGCTGATGTTGTCCTGCGTCAGGACGAAGACGTTCTCGATACCTGGTTCTCTTCTGCG
CTGTGGACCTTCTCTACCCTTGGCTGGCCGGAAAATACCGACGCCCTGCGTCAGTTCCAC
CCAACCAGCGTGATGGTATCTGGTTTCGACATCATTTTCTTCTGGATTGCCCGCATGATC
ATGATGACCATGCACTTCATCAAAGATGAAAATGGCAAACCGCAGGTGCCGTTCCACACC
GTTTACATGACCGGCCTGATTCGTGATGACGAAGGCCAGAAGATGTCCAAATCCAAGGGT
AACGTTATCGACCCACTGGATATGGTTGACGGTATTTCGCTGCCAGAACTGCTGGAAAAA
CGTACCGGCAATATGATGCAGCCGCAGCTGGCGGACAAAATCCGTAAGCGCACCGAGAAG
CAGTTCCCGAACGGTATTGAGCCGCACGGTACTGACGCGCTGCGCTTCACCCTGGCGGCG
CTGGCGTCTACCGGTCGTGACATCAACTGGGATATGAAGCGTCTGGAAGGTTACCGTAAC
TTCTGTAACAAGCTGTGGAACGCCAGCCGCTTTGTGCTGATGAACACAGAAGGTCAGGAT
TGCGGCTTCAACGGCGGCGAAATGACGCTGTCGCTGGCGGACCGCTGGATTCTGGCGGAG
TTCAACCAGACCATCAAAGCGTACCGCGAAGCGCTGGACAGCTTCCGCTTCGATATCGCC
GCAGGCATTCTGTATGAGTTCACCTGGAACCAGTTCTGTGACTGGTATCTCGAGCTGACC
AAGCCGGTAATGAACGGTGGCACCGAAGCAGAACTGCGCGGTACTCGCCATACGCTGGTG
ACTGTACTGGAAGGTCTGCTGCGCCTCGCGCATCCGATCATTCCGTTCATCACCGAAACC
ATCTGGCAGCGTGTGAAAGTACTTTGCGGTATCACTGCCGACACCATCATGCTGCAGCCG
TTCCCGCAGTACGATGCATCTCAGGTTGATGAAGCCGCACTGGCCGACACCGAATGGCTG
AAACAGGCGATCGTTGCGGTACGTAACATCCGTGCAGAAATGAACATCGCGCCGGGCAAA
CCGCTGGAGCTGCTGCTGCGTGGTTGCAGCGCGGATGCAGAACGTCGCGTAAATGAAAAC
CGTGGCTTCCTGCAAACCCTGGCGCGTCTGGAAAGTATCACCGTGCTGCCTGCCGATGAC
AAAGGTCCGGTTTCCGTTACGAAGATCATCGACGGTGCAGAGCTGCTGATCCCGATGGCT
GGCCTCATCAACAAAGAAGATGAGCTGGCGCGTCTGGCGAAAGAAGTGGCGAAGATTGAA
GGTGAAATCAGCCGTATCGAGAACAAACTGGCGAACGAAGGCTTTGTCGCCCGCGCACCG
GAAGCGGTCATCGCGAAAGAGCGTGAGAAGCTGGAAGGCTATGCGGAAGCGAAAGCGAAA
CTGATTGAACAGCAGGCTGTTATCGCCGCGCTGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:951
Protein Molecular Weight:108192
Protein Theoretical pI:5
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Valyl-tRNA synthetase
MEKTYNPQDIEQPLYEHWEKQGYFKPNGDESQESFCIMIPPPNVTGSLHMGHAFQQTIMD
TMIRYQRMQGKNTLWQVGTDHAGIATQMVVERKIAAEEGKTRHDYGREAFIDKIWEWKAE
SGGTITRQMRRLGNSVDWERERFTMDEGLSNAVKEVFVRLYKEDLIYRGKRLVNWDPKLR
TAISDLEVENRESKGSMWHIRYPLADGAKTADGKDYLVVATTRPETLLGDTGVAVNPEDP
RYKDLIGKYVILPLVNRRIPIVGDEHADMEKGTGCVKITPAHDFNDYEVGKRHALPMINI
LTFDGDIRESAQVFDTKGNESDVYSSEIPAEFQKLERFAARKAVVAAVDALGLLEEIKPH
DLTVPYGDRGGVVIEPMLTDQWYVRADVLAKPAVEAVENGDIQFVPKQYENMYFSWMRDI
QDWCISRQLWWGHRIPAWYDEAGNVYVGRNEDEVRKENNLGADVVLRQDEDVLDTWFSSA
LWTFSTLGWPENTDALRQFHPTSVMVSGFDIIFFWIARMIMMTMHFIKDENGKPQVPFHT
VYMTGLIRDDEGQKMSKSKGNVIDPLDMVDGISLPELLEKRTGNMMQPQLADKIRKRTEK
QFPNGIEPHGTDALRFTLAALASTGRDINWDMKRLEGYRNFCNKLWNASRFVLMNTEGQD
CGFNGGEMTLSLADRWILAEFNQTIKAYREALDSFRFDIAAGILYEFTWNQFCDWYLELT
KPVMNGGTEAELRGTRHTLVTVLEGLLRLAHPIIPFITETIWQRVKVLCGITADTIMLQP
FPQYDASQVDEAALADTEWLKQAIVAVRNIRAEMNIAPGKPLELLLRGCSADAERRVNEN
RGFLQTLARLESITVLPADDKGPVSVTKIIDGAELLIPMAGLINKEDELARLAKEVAKIE
GEISRIENKLANEGFVARAPEAVIAKEREKLEGYAEAKAKLIEQQAVIAAL
References
External Links:
ResourceLink
Uniprot ID:P07118
Uniprot Name:SYV_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85677005
Ecogene ID:EG11067
Ecocyc:EG11067
ColiBase:b4258
Kegg Gene:b4258
EchoBASE ID:EB1060
CCDB:SYV_ECOLI
BacMap:16132080
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
  • Burland, V., Plunkett, G. 3rd, Sofia, H. J., Daniels, D. L., Blattner, F. R. (1995). "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes." Nucleic Acids Res 23:2105-2119. Pubmed: 7610040
  • Doring, V., Mootz, H. D., Nangle, L. A., Hendrickson, T. L., de Crecy-Lagard, V., Schimmel, P., Marliere, P. (2001). "Enlarging the amino acid set of Escherichia coli by infiltration of the valine coding pathway." Science 292:501-504. Pubmed: 11313495
  • Hartlein, M., Frank, R., Madern, D. (1987). "Nucleotide sequence of Escherichia coli valyl-tRNA synthetase gene valS." Nucleic Acids Res 15:9081-9082. Pubmed: 3317277
  • 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
  • Heck, J. D., Hatfield, G. W. (1988). "Valyl-tRNA synthetase gene of Escherichia coli K12. Primary structure and homology within a family of aminoacyl-TRNA synthetases." J Biol Chem 263:868-877. Pubmed: 3275660
  • Hountondji, C., Lazennec, C., Beauvallet, C., Dessen, P., Pernollet, J. C., Plateau, P., Blanquet, S. (2002). "Crucial role of conserved lysine 277 in the fidelity of tRNA aminoacylation by Escherichia coli valyl-tRNA synthetase." Biochemistry 41:14856-14865. Pubmed: 12475234
  • Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646