Aspartyl-tRNA synthetase (P21889)

Identification
Name:Aspartyl-tRNA synthetase
Synonyms:
  • Aspartate--tRNA ligase
  • AspRS
Gene Name:aspS
Enzyme Class:
Biological Properties
General Function:Involved in nucleotide binding
Specific Function:ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp)
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0tRNA(Asp)+1.0tRNA(Asp) ↔ 1.0Thumb+1.0L-Aspartyl-tRNA(Asp)+1.0Thumb+1.0L-Aspartyl-tRNA(Asp)
1.0L-Aspartic acid + 1.0Adenosine triphosphate + 1.0tRNA(Asp) + 1.0tRNA(Asp) ↔ 1.0Adenosine monophosphate + 1.0L-Aspartyl-tRNA(Asp) + 1.0Pyrophosphate + 1.0L-Aspartyl-tRNA(Asp)
ReactionCard
1.0tRNA(Asp)+1.0Thumb+1.0Thumb ↔ 1.0L-Aspartyl-tRNA(Asp)+1.0Thumb+1.0Thumb
1.0tRNA(Asp) + 1.0L-Aspartic acid + 1.0Adenosine triphosphate ↔ 1.0L-Aspartyl-tRNA(Asp) + 1.0Pyrophosphate + 1.0Adenosine monophosphate
ReactionCard
SMPDB Reactions:
1.0L-Aspartic acid+1.0Thumb+1.0Thumb+1.0tRNA(Asp)+1.0Thumb → 1.0Pyrophosphate+1.0Thumb+1.0L-aspartyl-tRNA(Asp)
1.0L-Aspartic acid + 1.0Adenosine triphosphate + 1.0Hydrogen ion + 1.0tRNA(Asp) + 1.0L-Aspartic acid → 1.0Pyrophosphate + 1.0Adenosine monophosphate + 1.0L-aspartyl-tRNA(Asp)
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0tRNA(Asp) → 1.0Thumb+1.0Thumb+1.0L-aspartyl-tRNA(Asp)
1.0Adenosine triphosphate + 1.0L-Aspartic acid + 1.0tRNA(Asp) → 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-aspartyl-tRNA(Asp)
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00045Adenosine monophosphateMetaboCard
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00191L-Aspartic acidMetaboCard
ECMDB04142PyrophosphateMetaboCard
GO Classification:
Component
cell part
cytoplasm
intracellular part
Function
adenyl nucleotide binding
adenyl ribonucleotide binding
aminoacyl-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
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:b1866
Gene OrientationCounterclockwise
Centisome Percentage:41.96
Left Sequence End1946774
Right Sequence End1948546
Gene Sequence:
>1773 bp
GTGCGATTATTTGCTCAATTAAGCTGGTATTTCCGTCGGGAATGGCGTCGCTATCTCGGG
GCTGTCGCCTTGCTTGTCATTATCGCGATGCTGCAACTGGTTCCGCCAAAAGTGGTTGGT
ATTGTTGTCGATGGCGTGACAGAACAACACTTTACTACCGGGCAGATCCTGATGTGGATC
GCCACCATGGTGCTGATTGCCGTTGTGGTTTATCTCCTGCGTTACGTCTGGCGGGTATTG
CTGTTTGGTGCGTCTTATCAACTGGCTGTTGAACTGCGTGAAGATTATTACCGTCAGCTA
AGCCGGCAGCATCCTGAGTTTTACCTGCGTCATCGCACCGGTGACCTCATGGCTCGTGCG
ACCAATGACGTCGATCGCGTCGTGTTTGCCGCCGGAGAAGGGGTGCTGACGCTGGTGGAT
TCACTGGTGATGGGCTGCGCTGTGTTGATTATGATGTCTACGCAAATTAGCTGGCAGTTG
ACCTTATTTTCCCTGTTGCCGATGCCAGTGATGGCGATCATGATTAAGCGCAACGGCGAT
GCTTTGCATGAACGCTTTAAGCTGGCACAGGCGGCGTTTTCCAGTCTTAATGACCGCACC
CAGGAAAGCCTCACCAGTATCCGCATGATCAAAGCCTTTGGTCTGGAAGATCGCCAGTCG
GCGTTATTTGCCGCGGATGCCGAAGATACCGGCAAAAAAAACATGCGGGTGGCGCGTATT
GATGCTCGTTTCGACCCGACCATCTATATCGCGATTGGTATGGCGAACTTGCTGGCGATT
GGCGGCGGTAGTTGGATGGTGGTGCAGGGCAGTTTAACGCTGGGCCAGCTCACCAGTTTT
ATGATGTATTTAGGTCTGATGATTTGGCCAATGCTGGCGCTGGCATGGATGTTTAACATT
GTGGAACGTGGTAGTGCTGCGTACAGCCGTATTCGCGCGATGCTGGCGGAAGCGCCGGTG
GTGAACGATGGTAGCGAACCCGTGCCGGAAGGGCGTGGCGAACTGGATGTAAATATTCAC
CAGTTCACGTATCCGCAGACTGACCATCCTGCGCTGGAAAACGTCAATTTCGCCCTGAAA
CCCGGTCAGATGCTGGGTATCTGCGGGCCGACTGGTTCCGGCAAAAGTACCCTGTTGTCG
CTCATTCAGCGTCATTTCGACGTCAGCGAGGGGGATATTCGCTTTCATGATATTCCTCTG
ACGAAGTTACAACTCGATAGCTGGCGTAGCCGCCTGGCGGTAGTTAGCCAGACGCCATTC
CTTTTTTCTGACACTGTGGCGAATAACATCGCGCTGGGTTGCCCGAATGCCACCCAGCAA
GAGATTGAGCATGTCGCGCGGTTAGCCAGCGTACATGACGATATTTTGCGTCTACCGCAA
GGTTACGATACAGAGGTGGGCGAGCGCGGTGTGATGCTTTCCGGCGGGCAAAAACAGCGT
ATCTCCATTGCTCGTGCGTTATTAGTCAACGCGGAAATCCTCATCCTTGATGATGCGCTT
TCGGCGGTGGACGGACGCACTGAGCACCAGATCCTGCATAACCTGCGTCAGTGGGGGCAG
GGAAGAACGGTAATCATCAGTGCCCATCGCCTTTCTGCACTGACGGAAGCCAGTGAAATT
ATTGTGATGCAGCACGGACATATCGCCCAGCGTGGCAATCATGATGTGCTGGCACAACAA
AGCGGCTGGTATCGCGATATGTATCGCTATCAACAACTGGAGGCGGCGCTCGACGACGCT
CCGGAAAATCGCGAGGAGGCCGTCGATGCGTAG
Protein Properties
Pfam Domain Function:
Protein Residues:590
Protein Molecular Weight:65913
Protein Theoretical pI:5
PDB File:1IL2
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Aspartyl-tRNA synthetase
MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLA
SELRNEFCIQVTGTVRARDEKNINRDMATGEIEVLASSLTIINRADVLPLDSNHVNTEEA
RLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPS
RVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMT
APQVREVMEALVRHLWLEVKGVDLGDFPVMTFAEAERRYGSDKPDLRNPMELTDVADLLK
SVEFAVFAGPANDPKGRVAALRVPGGASLTRKQIDEYGNFVKIYGAKGLAYIKVNERAKG
LEGINSPVAKFLNAEIIEDILDRTAAQDGDMIFFGADNKKIVADAMGALRLKVGKDLGLT
DESKWAPLWVIDFPMFEDDGEGGLTAMHHPFTSPKDMTAAELKAAPENAVANAYDMVING
YEVGGGSVRIHNGDMQQTVFGILGINEEEQREKFGFLLDALKYGTPPHAGLAFGLDRLTM
LLTGTDNIRDVIAFPKTTAAACLMTEAPSFANPTALAELSIQVVKKAENN
References
External Links:
ResourceLink
Uniprot ID:P21889
Uniprot Name:SYD_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674588
PDB ID:1IL2
Ecogene ID:EG10097
Ecocyc:EG10097
ColiBase:b1866
Kegg Gene:b1866
EchoBASE ID:EB0095
CCDB:SYD_ECOLI
BacMap:16129819
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
  • Eiler, S., Dock-Bregeon, A., Moulinier, L., Thierry, J. C., Moras, D. (1999). "Synthesis of aspartyl-tRNA(Asp) in Escherichia coli--a snapshot of the second step." EMBO J 18:6532-6541. Pubmed: 10562565
  • Eriani, G., Dirheimer, G., Gangloff, J. (1990). "Aspartyl-tRNA synthetase from Escherichia coli: cloning and characterisation of the gene, homologies of its translated amino acid sequence with asparaginyl- and lysyl-tRNA synthetases." Nucleic Acids Res 18:7109-7118. Pubmed: 2129559
  • 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
  • Itoh, T., Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Kasai, H., Kimura, S., Kitakawa, M., Kitagawa, M., Makino, K., Miki, T., Mizobuchi, K., Mori, H., Mori, T., Motomura, K., Nakade, S., Nakamura, Y., Nashimoto, H., Nishio, Y., Oshima, T., Saito, N., Sampei, G., Seki, Y., Horiuchi, T., et, a. l. .. (1996). "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map." DNA Res 3:379-392. Pubmed: 9097040
  • Rees, B., Webster, G., Delarue, M., Boeglin, M., Moras, D. (2000). "Aspartyl tRNA-synthetase from Escherichia coli: flexibility and adaptability to the substrates." J Mol Biol 299:1157-1164. Pubmed: 10873442
  • Sharples, G. J., Lloyd, R. G. (1991). "Location of a mutation in the aspartyl-tRNA synthetase gene of Escherichia coli K12." Mutat Res 264:93-96. Pubmed: 1944398
  • Takahagi, M., Iwasaki, H., Nakata, A., Shinagawa, H. (1991). "Molecular analysis of the Escherichia coli ruvC gene, which encodes a Holliday junction-specific endonuclease." J Bacteriol 173:5747-5753. Pubmed: 1885548