Cysteinyl-tRNA synthetase (P21888)

Identification
Name:Cysteinyl-tRNA synthetase
Synonyms:
  • Cysteine--tRNA ligase
  • CysRS
Gene Name:cysS
Enzyme Class:
Biological Properties
General Function:Involved in cysteine-tRNA ligase activity
Specific Function:ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys)
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0tRNA(Cys)+1.0tRNA(Cys) ↔ 1.0Thumb+1.0L-Cysteinyl-tRNA(Cys)+1.0Thumb+1.0L-Cysteinyl-tRNA(Cys)
1.0Adenosine triphosphate + 1.0L-Cysteine + 1.0tRNA(Cys) + 1.0tRNA(Cys) ↔ 1.0Adenosine monophosphate + 1.0L-Cysteinyl-tRNA(Cys) + 1.0Pyrophosphate + 1.0L-Cysteinyl-tRNA(Cys)
ReactionCard
1.0Thumb+1.0Thumb+1.0tRNA(Cys) ↔ 1.0Thumb+1.0Thumb+1.0L-Cysteinyl-tRNA(Cys)
1.0Adenosine triphosphate + 1.0L-Cysteine + 1.0tRNA(Cys) ↔ 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-Cysteinyl-tRNA(Cys)
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0tRNA(Cys)+1.0Thumb+1.0Thumb → 1.0Pyrophosphate+1.0Thumb+1.0L-cysteinyl-tRNA(Cys)
1.0L-Cysteine + 1.0tRNA(Cys) + 1.0Adenosine triphosphate + 1.0Hydrogen ion → 1.0Pyrophosphate + 1.0Adenosine monophosphate + 1.0L-cysteinyl-tRNA(Cys)
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0tRNA(Cys) → 1.0Thumb+1.0Thumb+1.0L-cysteinyl-tRNA(Cys)
1.0Adenosine triphosphate + 1.0L-Cysteine + 1.0tRNA(Cys) → 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-cysteinyl-tRNA(Cys)
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00045Adenosine monophosphateMetaboCard
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00574L-CysteineMetaboCard
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
cysteine-tRNA ligase activity
ligase activity
ligase activity, forming aminoacyl-tRNA and related compounds
ligase activity, forming carbon-oxygen bonds
nucleoside binding
nucleotide binding
purine nucleoside binding
Process
biosynthetic process
cellular macromolecule biosynthetic process
cellular macromolecule metabolic process
cysteinyl-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:b0526
Gene OrientationClockwise
Centisome Percentage:11.94
Left Sequence End553834
Right Sequence End555219
Gene Sequence:
>1386 bp
ATGCTAAAAATCTTCAATACTCTGACACGCCAAAAAGAGGAATTTAAGCCTATTCACGCC
GGGGAAGTCGGCATGTACGTGTGTGGAATCACCGTTTACGATCTCTGTCATATCGGTCAC
GGGCGTACCTTTGTTGCTTTTGACGTGGTTGCGCGCTATCTGCGTTTCCTCGGCTATAAA
CTGAAGTATGTGCGCAACATTACCGATATCGACGACAAAATCATCAAACGCGCCAATGAA
AATGGCGAAAGCTTTGTGGCGATGGTGGATCGCATGATCGCCGAAATGCACAAAGATTTT
GATGCTTTGAACATTCTGCGCCCGGATATGGAGCCGCGCGCGACGCACCATATCGCAGAA
ATTATTGAACTCACTGAACAACTGATCGCCAAAGGTCACGCTTATGTGGCGGACAACGGC
GACGTGATGTTCGACGTCCCGACCGATCCAACTTATGGCGTGCTGTCGCGTCAGGATCTC
GACCAGCTGCAGGCAGGCGCGCGCGTTGACGTGGTCGACGACAAACGCAACCCAATGGAC
TTCGTTCTGTGGAAGATGTCGAAAGAGGGCGAACCGAGCTGGCCGTCTCCGTGGGGCGCG
GGTCGTCCTGGCTGGCACATTGAATGTTCGGCAATGAACTGCAAGCAGCTGGGTAACCAC
TTTGATATCCACGGCGGCGGTTCAGACCTGATGTTCCCGCACCACGAAAACGAAATCGCG
CAGTCCACCTGTGCCCATGATGGTCAGTATGTGAACTACTGGATGCACTCGGGGATGGTG
ATGGTTGACCGCGAGAAGATGTCCAAATCGCTGGGTAACTTCTTTACCGTGCGCGATGTG
CTGAAATACTACGACGCGGAAACCGTGCGTTACTTCCTGATGTCGGGCCACTATCGCAGC
CAGTTGAACTACAGCGAAGAGAACCTGAAGCAGGCGCGTGCGGCGCTGGAGCGTCTCTAC
ACTGCGCTGCGCGGCACAGATAAAACCGTTGCGCCTGCCGGTGGCGAAGCGTTTGAAGCG
CGCTTTATTGAAGCGATGGACGACGATTTCAACACCCCGGAAGCCTATTCCGTACTGTTT
GATATGGCGCGTGAAGTAAACCGTCTGAAAGCAGAAGATATGGCAGCGGCGAATGCAATG
GCATCTCACCTGCGTAAACTTTCCGCTGTATTGGGCCTGCTGGAGCAAGAACCGGAAGCG
TTCCTGCAAAGCGGCGCGCAGGCAGACGACAGCGAAGTGGCTGAGATTGAAGCGTTAATT
CAACAGCGTCTGGATGCCCGTAAAGCGAAAGACTGGGCGGCGGCGGATGCGGCGCGTGAT
CGTCTTAACGAGATGGGGATCGTGCTGGAAGATGGCCCGCAAGGGACCACCTGGCGTCGT
AAGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:461
Protein Molecular Weight:52202
Protein Theoretical pI:5
PDB File:1LI7
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Cysteinyl-tRNA synthetase
MLKIFNTLTRQKEEFKPIHAGEVGMYVCGITVYDLCHIGHGRTFVAFDVVARYLRFLGYK
LKYVRNITDIDDKIIKRANENGESFVAMVDRMIAEMHKDFDALNILRPDMEPRATHHIAE
IIELTEQLIAKGHAYVADNGDVMFDVPTDPTYGVLSRQDLDQLQAGARVDVVDDKRNPMD
FVLWKMSKEGEPSWPSPWGAGRPGWHIECSAMNCKQLGNHFDIHGGGSDLMFPHHENEIA
QSTCAHDGQYVNYWMHSGMVMVDREKMSKSLGNFFTVRDVLKYYDAETVRYFLMSGHYRS
QLNYSEENLKQARAALERLYTALRGTDKTVAPAGGEAFEARFIEAMDDDFNTPEAYSVLF
DMAREVNRLKAEDMAAANAMASHLRKLSAVLGLLEQEPEAFLQSGAQADDSEVAEIEALI
QQRLDARKAKDWAAADAARDRLNEMGIVLEDGPQGTTWRRK
References
External Links:
ResourceLink
Uniprot ID:P21888
Uniprot Name:SYC_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674663
PDB ID:1LI7
Ecogene ID:EG10196
Ecocyc:EG10196
ColiBase:b0526
Kegg Gene:b0526
EchoBASE ID:EB0193
CCDB:SYC_ECOLI
BacMap:16128510
General Reference:
  • Avalos, J., Corrochano, L. M., Brenner, S. (1991). "Cysteinyl-tRNA synthetase is a direct descendant of the first aminoacyl-tRNA synthetase." FEBS Lett 286:176-180. Pubmed: 1864365
  • 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
  • Eriani, G., Dirheimer, G., Gangloff, J. (1991). "Cysteinyl-tRNA synthetase: determination of the last E. coli aminoacyl-tRNA synthetase primary structure." Nucleic Acids Res 19:265-269. Pubmed: 2014166
  • 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
  • Hou, Y. M., Shiba, K., Mottes, C., Schimmel, P. (1991). "Sequence determination and modeling of structural motifs for the smallest monomeric aminoacyl-tRNA synthetase." Proc Natl Acad Sci U S A 88:976-980. Pubmed: 1992490
  • Newberry, K. J., Hou, Y. M., Perona, J. J. (2002). "Structural origins of amino acid selection without editing by cysteinyl-tRNA synthetase." EMBO J 21:2778-2787. Pubmed: 12032090
  • Newberry, K. J., Kohn, J., Hou, Y. M., Perona, J. J. (1999). "Crystallization and preliminary diffraction analysis of Escherichia coli cysteinyl-tRNA synthetase." Acta Crystallogr D Biol Crystallogr 55:1046-1047. Pubmed: 10216301