Lysyl-tRNA synthetase (P0A8N3)

Identification
Name:Lysyl-tRNA synthetase
Synonyms:
  • Lysine--tRNA ligase
  • LysRS
Gene Name:lysS
Enzyme Class:
Biological Properties
General Function:Involved in nucleotide binding
Specific Function:ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys)
Cellular Location:Cytoplasm
SMPDB Pathways:Not Available
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0tRNA(Lys)+1.0tRNA(Lys) ↔ 1.0Thumb+1.0Thumb+1.0L-Lysyl-tRNA+1.0Thumb
1.0Adenosine triphosphate + 1.0L-Lysine + 1.0tRNA(Lys) + 1.0tRNA(Lys) ↔ 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-Lysyl-tRNA + 1.0L-Lysyl-tRNA
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0tRNA(Lys) → 1.0Thumb+1.0L-Lysine-tRNA (Lys)+1.0Thumb
1.0Adenosine triphosphate + 1.0L-Lysine + 1.0tRNA(Lys) → 1.0Adenosine monophosphate + 1.0L-Lysine-tRNA (Lys) + 1.0Pyrophosphate
ReactionCard
1.0Thumb+1.0Thumb+1.0tRNA(Lys) → 1.0Thumb+1.0Thumb+1.0L-lysyl-tRNA(Lys)
1.0Adenosine triphosphate + 1.0L-Lysine + 1.0tRNA(Lys) → 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-lysyl-tRNA(Lys)
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00045Adenosine monophosphateMetaboCard
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB00182L-LysineMetaboCard
ECMDB23777L-Lysyl-tRNAMetaboCard
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
lysine-tRNA ligase activity
nucleic acid binding
nucleoside binding
nucleotide binding
purine nucleoside binding
Process
biosynthetic process
cellular macromolecule biosynthetic process
cellular macromolecule metabolic process
lysyl-tRNA aminoacylation
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
Gene Properties
Blattner:b2890
Gene OrientationCounterclockwise
Centisome Percentage:65.34
Left Sequence End3031679
Right Sequence End3033196
Gene Sequence:
>1518 bp
ATGGCACAGATTGATTTCCGAAAAAAAATAAACTGGCATCGTCGTTACCGTTCACCGCAG
GGCGTTAAAACCGAACATGAGATCCTGCGGATCTTCGAGAGCGATCGCGGGCGTATCATC
AACTCTCCGGCAATTCGTCGTCTGCAACAAAAGACCCAGGTTTTTCCACTGGAGCGCAAT
GCCGCCGTGCGCACGCGTCTTACCCACTCGATGGAAGTCCAGCAGGTGGGGCGCTACATC
GCCAAAGAAATTTTAAGCCGTCTGAAAGAGCTTAAATTACTGGAAGCATACGGCCTGGAT
GAACTGACCGGTCCCTTTGAAAGCATTGTTGAGATGTCATGCCTGATGCACGATATCGGC
AATCCGCCGTTTGGTCATTTTGGCGAAGCGGCGATAAATGACTGGTTTCGCCAACGTTTG
CACCCGGAAGATGCCGAAAGCCAGCCTCTGACTGACGATCGCTGCAGCGTGGCGGCACTA
CGTTTACGGGACGGGGAAGAACCGCTTAACGAGCTGCGGCGCAAGATTCGTCAGGACTTA
TGTCATTTTGAGGGGAATGCACAAGGCATTCGCCTGGTGCATACATTGATGCGGATGAAT
CTCACCTGGGCACAGGTTGGCGGTATTTTAAAATATACCCGTCCGGCGTGGTGGCGTGGC
GAAACGCCTGAGACACATCACTATTTAATGAAAAAGCCGGGTTATTATCTTTCTGAAGAA
GCCTATATTGCCCGGTTGCGTAAAGAACTTAATTTGGCGCTTTACAGTCGTTTTCCATTA
ACGTGGATTATGGAAGCTGCCGACGACATCTCCTATTGTGTGGCAGACCTTGAAGATGCG
GTAGAGAAAAGAATATTTACCGTTGAGCAGCTTTATCATCATTTGCACGAAGCGTGGGGC
CAGCATGAGAAAGGTTCGCTCTTTTCGCTGGTGGTTGAAAATGCCTGGGAAAAATCACGC
TCAAATAGTTTAAGCCGCAGTACGGAAGATCAGTTTTTTATGTATTTACGGGTAAACACC
CTAAATAAACTGGTACCCTACGCGGCACAACGATTTATTGATAATCTGCCTGCGATTTTC
GCCGGAACGTTTAATCATGCATTATTGGAAGATGCCAGCGAATGCAGCGATCTTCTTAAG
CTATATAAAAATGTCGCTGTAAAACATGTGTTTAGCCATCCAGATGTCGAGCGGCTTGAA
TTGCAGGGCTATCGGGTCATTAGCGGATTATTAGAGATTTATCGTCCTTTATTAAGCCTG
TCGTTATCAGACTTTACTGAACTGGTAGAAAAAGAACGGGTGAAACGTTTCCCTATTGAA
TCGCGCTTATTCCACAAACTCTCGACGCGCCATCGGCTGGCCTATGTCGAGGCTGTCAGT
AAATTACCGTCAGATTCTCCTGAGTTTCCGCTATGGGAATATTATTACCGTTGCCGCCTG
CTGCAGGATTATATCAGCGGTATGACCGACCTCTATGCGTGGGATGAATACCGACGTCTG
ATGGCCGTAGAACAATAA
Protein Properties
Pfam Domain Function:
Protein Residues:505
Protein Molecular Weight:57603
Protein Theoretical pI:5
PDB File:1BBW
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Lysyl-tRNA synthetase
MSEQHAQGADAVVDLNNELKTRREKLANLREQGIAFPNDFRRDHTSDQLHAEFDGKENEE
LEALNIEVAVAGRMMTRRIMGKASFVTLQDVGGRIQLYVARDDLPEGVYNEQFKKWDLGD
ILGAKGKLFKTKTGELSIHCTELRLLTKALRPLPDKFHGLQDQEARYRQRYLDLISNDES
RNTFKVRSQILSGIRQFMVNRGFMEVETPMMQVIPGGAAARPFITHHNALDLDMYLRIAP
ELYLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYKDLIELTESLFRT
LAQDILGKTEVTYGDVTLDFGKPFEKLTMREAIKKYRPETDMADLDNFDSAKAIAESIGI
HVEKSWGLGRIVTEIFEEVAEAHLIQPTFITEYPAEVSPLARRNDVNPEITDRFEFFIGG
REIGNGFSELNDAEDQAQRFLDQVAAKDAGDDEAMFYDEDYVTALEHGLPPTAGLGIGID
RMVMLFTNSHTIRDVILFPAMRPVK
References
External Links:
ResourceLink
Uniprot ID:P0A8N3
Uniprot Name:SYK1_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:21239016
PDB ID:1BBW
Ecogene ID:EG10552
Ecocyc:EG10552
ColiBase:b2890
Kegg Gene:b2890
EchoBASE ID:EB0547
CCDB:SYK1_ECOLI
BacMap:16130792
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
  • Commans, S., Plateau, P., Blanquet, S., Dardel, F. (1995). "Solution structure of the anticodon-binding domain of Escherichia coli lysyl-tRNA synthetase and studies of its interaction with tRNA(Lys)." J Mol Biol 253:100-113. Pubmed: 7473706
  • 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
  • Kawakami, K., Jonsson, Y. H., Bjork, G. R., Ikeda, H., Nakamura, Y. (1988). "Chromosomal location and structure of the operon encoding peptide-chain-release factor 2 of Escherichia coli." Proc Natl Acad Sci U S A 85:5620-5624. Pubmed: 2456575
  • Leveque, F., Plateau, P., Dessen, P., Blanquet, S. (1990). "Homology of lysS and lysU, the two Escherichia coli genes encoding distinct lysyl-tRNA synthetase species." Nucleic Acids Res 18:305-312. Pubmed: 2183178