Asparaginyl-tRNA synthetase (P0A8M0)

Identification
Name:Asparaginyl-tRNA synthetase
Synonyms:
  • Asparagine--tRNA ligase
  • AsnRS
Gene Name:asnS
Enzyme Class:
Biological Properties
General Function:Involved in nucleotide binding
Specific Function:ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + L-asparaginyl-tRNA(Asn)
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0tRNA(Asn)+1.0tRNA(Asn) ↔ 1.0Thumb+1.0L-Asparaginyl-tRNA(Asn)+1.0Thumb+1.0L-Asparaginyl-tRNA(Asn)
1.0L-Asparagine + 1.0Adenosine triphosphate + 1.0tRNA(Asn) + 1.0tRNA(Asn) ↔ 1.0Adenosine monophosphate + 1.0L-Asparaginyl-tRNA(Asn) + 1.0Pyrophosphate + 1.0L-Asparaginyl-tRNA(Asn)
ReactionCard
1.0Thumb+1.0Thumb+1.0tRNA(Asn) ↔ 1.0Thumb+1.0Thumb+1.0L-Asparaginyl-tRNA(Asn)
1.0Adenosine triphosphate + 1.0L-Asparagine + 1.0tRNA(Asn) ↔ 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-Asparaginyl-tRNA(Asn)
ReactionCard
SMPDB Reactions:
1.0L-Asparagine+1.0Thumb+1.0Thumb+1.0tRNA(Asn)+1.0Thumb → 1.0Pyrophosphate+1.0Thumb+1.0L-asparaginyl-tRNA(Asn)
1.0L-Asparagine + 1.0Adenosine triphosphate + 1.0Hydrogen ion + 1.0tRNA(Asn) + 1.0L-Asparagine → 1.0Pyrophosphate + 1.0Adenosine monophosphate + 1.0L-asparaginyl-tRNA(Asn)
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0tRNA(Asn) → 1.0Thumb+1.0Thumb+1.0L-asparaginyl-tRNA(Asn)
1.0Adenosine triphosphate + 1.0L-Asparagine + 1.0tRNA(Asn) → 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-asparaginyl-tRNA(Asn)
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00045Adenosine monophosphateMetaboCard
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00168L-AsparagineMetaboCard
ECMDB04142PyrophosphateMetaboCard
GO Classification:
Component
cell part
cytoplasm
intracellular part
Function
adenyl nucleotide binding
adenyl ribonucleotide binding
aminoacyl-tRNA ligase activity
asparagine-tRNA ligase activity
aspartate-tRNA ligase activity
ATP binding
binding
catalytic activity
ligase activity
ligase activity, forming aminoacyl-tRNA and related compounds
ligase activity, forming carbon-oxygen bonds
nucleic acid binding
nucleoside binding
nucleotide binding
purine nucleoside binding
Process
asparaginyl-tRNA aminoacylation
aspartyl-tRNA aminoacylation
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
Gene Properties
Blattner:b0930
Gene OrientationCounterclockwise
Centisome Percentage:21.27
Left Sequence End986808
Right Sequence End988208
Gene Sequence:
>1401 bp
ATGAGCGTTGTGCCTGTAGCCGACGTACTCCAGGGCCGTGTAGCCGTTGACAGCGAAGTC
ACCGTGCGCGGATGGGTACGTACCCGCCGAGATTCAAAAGCTGGCATCTCCTTCCTCGCC
GTTTATGACGGTTCCTGCTTTGATCCTGTACAGGCTGTCATCAATAATTCTCTGCCCAAT
TACAATGAAGACGTCCTGCGTCTGACCACCGGCTGCTCGGTCATTGTGACGGGTAAAGTC
GTGGCGTCGCCGGGCCAGGGGCAACAATTTGAAATTCAGGCCAGCAAGGTTGAAGTTGCT
GGTTGGGTTGAAGATCCAGACACTTACCCGATGGCGGCAAAACGCCACAGCATTGAGTAT
CTGCGTGAAGTCGCTCACCTGCGTCCGCGCACAAACCTGATTGGTGCCGTCGCGCGCGTT
CGCCATACGCTGGCGCAGGCGCTGCATCGCTTCTTTAACGAGCAGGGATTCTTCTGGGTT
TCAACGCCACTGATTACCGCATCTGATACCGAAGGTGCAGGCGAAATGTTCCGCGTTTCT
ACGCTGGATCTGGAAAACCTGCCGCGTAACGATCAGGGCAAAGTGGATTTCGACAAAGAC
TTCTTTGGTAAAGAGTCTTTCCTGACCGTATCTGGCCAGTTGAACGGCGAAACCTACGCT
TGCGCATTGTCCAAAATTTATACCTTCGGCCCGACTTTCCGTGCTGAAAACTCCAACACC
AGCCGTCACCTGGCGGAATTCTGGATGCTGGAGCCGGAAGTGGCGTTTGCTAACCTGAAC
GATATTGCGGGTCTGGCTGAAGCCATGCTGAAATATGTCTTCAAAGCGGTTCTCGAAGAA
CGCGCTGACGACATGAAATTCTTCGCTGAACGCGTAGATAAAGATGCCGTTTCACGTCTG
GAACGCTTCATTGAAGCCGATTTTGCGCAGGTGGATTATACCGACGCAGTGACCATTCTC
GAAAACTGCGGCAGGAAGTTTGAAAACCCGGTTTACTGGGGAGTCGATCTCTCTTCTGAG
CATGAGCGTTATCTGGCGGAAGAACACTTTAAAGCACCGGTAGTGGTTAAAAACTATCCG
AAAGATATTAAAGCGTTCTATATGCGCCTTAACGAAGACGGTAAAACCGTTGCGGCTATG
GACGTTCTGGCTCCGGGCATCGGTGAGATCATTGGTGGCTCCCAGCGTGAAGAACGTCTG
GACGTGCTGGACGAGCGTATGCTGGAAATGGGCCTGAATAAAGAAGATTACTGGTGGTAT
CGCGATCTGCGTCGCTACGGTACTGTTCCGCATTCAGGTTTCGGTCTTGGTTTTGAACGT
CTGATTGCTTACGTAACTGGCGTGCAAAACGTACGTGATGTGATTCCGTTCCCACGTACT
CCGCGTAACGCCAGCTTCTAA
Protein Properties
Pfam Domain Function:
Protein Residues:466
Protein Molecular Weight:52570
Protein Theoretical pI:5
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Asparaginyl-tRNA synthetase
MSVVPVADVLQGRVAVDSEVTVRGWVRTRRDSKAGISFLAVYDGSCFDPVQAVINNSLPN
YNEDVLRLTTGCSVIVTGKVVASPGQGQQFEIQASKVEVAGWVEDPDTYPMAAKRHSIEY
LREVAHLRPRTNLIGAVARVRHTLAQALHRFFNEQGFFWVSTPLITASDTEGAGEMFRVS
TLDLENLPRNDQGKVDFDKDFFGKESFLTVSGQLNGETYACALSKIYTFGPTFRAENSNT
SRHLAEFWMLEPEVAFANLNDIAGLAEAMLKYVFKAVLEERADDMKFFAERVDKDAVSRL
ERFIEADFAQVDYTDAVTILENCGRKFENPVYWGVDLSSEHERYLAEEHFKAPVVVKNYP
KDIKAFYMRLNEDGKTVAAMDVLAPGIGEIIGGSQREERLDVLDERMLEMGLNKEDYWWY
RDLRRYGTVPHSGFGLGFERLIAYVTGVQNVRDVIPFPRTPRNASF
References
External Links:
ResourceLink
Uniprot ID:P0A8M0
Uniprot Name:SYN_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1651455
Ecogene ID:EG10094
Ecocyc:EG10094
ColiBase:b0930
Kegg Gene:b0930
EchoBASE ID:EB0092
CCDB:SYN_ECOLI
BacMap:16128897
General Reference:
  • Anselme, J., Hartlein, M. (1989). "Asparaginyl-tRNA synthetase from Escherichia coli has significant sequence homologies with yeast aspartyl-tRNA synthetase." Gene 84:481-485. Pubmed: 2693216
  • Anselme, J., Hartlein, M. (1991). "Tyr-426 of the Escherichia coli asparaginyl-tRNA synthetase, an amino acid in a C-terminal conserved motif, is involved in ATP binding." FEBS Lett 280:163-166. Pubmed: 2009959
  • Aoki, H., Yaworsky, P. J., Patel, S. D., Margolin-Brzezinski, D., Park, K. S., Ganoza, M. C. (1992). "The asparaginyl-tRNA synthetase gene encodes one of the complementing factors for thermosensitive translation in the Escherichia coli mutant strain, N4316." Eur J Biochem 209:511-521. Pubmed: 1425658
  • 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
  • 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
  • Madern, D., Anselme, J., Hartlein, M. (1992). "Asparaginyl-tRNA synthetase from the Escherichia coli temperature-sensitive strain HO202. A proline replacement in motif 2 is responsible for a large increase in Km for asparagine and ATP." FEBS Lett 299:85-89. Pubmed: 1544480
  • Oshima, T., Aiba, H., Baba, T., Fujita, K., Hayashi, K., Honjo, A., Ikemoto, K., Inada, T., Itoh, T., Kajihara, M., Kanai, K., Kashimoto, K., Kimura, S., Kitagawa, M., Makino, K., Masuda, S., Miki, T., Mizobuchi, K., Mori, H., Motomura, K., Nakamura, Y., Nashimoto, H., Nishio, Y., Saito, N., Horiuchi, T., et, a. l. .. (1996). "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." DNA Res 3:137-155. Pubmed: 8905232