Glutaminyl-tRNA synthetase (P00962)

Identification
Name:Glutaminyl-tRNA synthetase
Synonyms:
  • Glutamine--tRNA ligase
  • GlnRS
Gene Name:glnS
Enzyme Class:
Biological Properties
General Function:Involved in nucleotide binding
Specific Function:ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-glutaminyl-tRNA(Gln)
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0tRNA(Gln)+1.0tRNA(Gln) ↔ 1.0Thumb+1.0Thumb+1.0Glutaminyl-tRNA+1.0Glutaminyl-tRNA
1.0Adenosine triphosphate + 1.0L-Glutamine + 1.0tRNA(Gln) + 1.0tRNA(Gln) ↔ 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0Glutaminyl-tRNA + 1.0Glutaminyl-tRNA
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb+1.0Thumb+1.0tRNA(Gln) → 1.0Adenosine diphosphate+1.0Pyrophosphate+1.0L-Glutaminyl-tRNA(Gln)+1.0Thumb
1.0L-Glutamine + 1.0Adenosine triphosphate + 1.0Hydrogen ion + 1.0tRNA(Gln) → 1.0Adenosine diphosphate + 1.0Pyrophosphate + 1.0L-Glutaminyl-tRNA(Gln) + 1.0ADP
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0tRNA(Gln) → 1.0Thumb+1.0L-Glutaminyl-tRNA(Gln)+1.0Thumb
1.0Adenosine triphosphate + 1.0L-Glutamine + 1.0tRNA(Gln) → 1.0Adenosine monophosphate + 1.0L-Glutaminyl-tRNA(Gln) + 1.0Pyrophosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00045Adenosine monophosphateMetaboCard
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00641L-GlutamineMetaboCard
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
glutamine-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
glutaminyl-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:b0680
Gene OrientationClockwise
Centisome Percentage:15.20
Left Sequence End705316
Right Sequence End706980
Gene Sequence:
>1665 bp
ATGGCAATACAACACCCTGACATCCAGCCTGCTGTTAACCATAGCGTTCAGGTGGCGATC
GCTGGTGCCGGCCCGGTTGGGCTGATGATGGCGAACTATCTCGGCCAGATGGGCATTGAC
GTGCTGGTGGTGGAGAAACTCGATAAGTTGATCGACTACCCGCGTGCGATTGGTATTGAT
GACGAGGCGCTGCGCACCATGCAGTCGGTCGGCCTGGTCGATGATGTTCTGCCGCACACT
ACGCCGTGGCACGCGATGCGTTTTCTCACCCCGAAAGGCCGCTGTTTTGCTGATATTCAG
CCAATGACCGATGAATTTGGCTGGCCGCGCCGTAACGCCTTTATTCAGCCGCAGGTCGAT
GCGGTGATGCTGGAAGGGGTGTCGCGTTTTCCGAATGTGCGCTGCTTGTTTTCCCGCGAG
CTGGAGGCCTTCAGTCAGCAAGATGACGAAGTGACCTTGCACCTGAAAACGGCAGAAGGG
CAGCGGGAAATAGTCAAAGCCCAGTGGCTGGTAGCCTGTGACGGTGGAGCAAGTTTTGTC
CGTCGCACTCTGAATGTGCCGTTTGAAGGTAAAACTGCGCCAAATCAGTGGATTGTGGTA
GATATCGCCAACGATCCGTTAAGTACGCCGCATATCTATTTGTGTTGCGATCCGGTGCGC
CCGTATGTTTCTGCCGCGCTGCCTCATGCGGTACGTCGCTTTGAATTTATGGTGATGCCG
GGAGAAACCGAAGAGCAGCTGCGTGAGCCGCAAAATATGCGCAAGCTGTTAAGCAAAGTG
CTGCCTAATCCGGACAATGTTGAATTGATTCGCCAGCGTGTCTACACCCACAACGCGCGA
CTGGCGCAACGTTTCCGTATTGATCGCGTACTGCTGGCGGGCGATGCCGCGCACATCATG
CCGGTATGGCAGGGGCAGGGCTATAACAGTGGTATGCGCGACGCCTTTAACCTCGCATGG
AAACTGGCGTTGGTTATCCAGGGGAAAGCCCGCGATGCGCTGCTCGATACCTATCAACAA
GAACGTCGCGATCACGCCAAAGCGATGATTGACCTGTCCGTGACGGCGGGCAACGTGCTG
GCTCCGCCGAAACGCTGGCAGGGTACGTTACGTGACGGCGTTTCCTGGCTGTTGAATTAT
CTGCCGCCAGTAAAACGCTACTTCCTCGAAATGCGCTTCAAGCCGATGCCGCAATATTAC
GGCGGTGCGCTGATGCGTGAGGGCGAAGCGAAGCACTCTCCGGTCGGCAAGATGTTTATT
CAGCCGAAAGTCACGCTGGAAAACGGCGACGTGACGCTGCTCGATAACGCGATCGGCGCG
AACTTCGCGGTAATTGGCTGGGGATGCAATCCACTGTGGGGGATGAGCGACGAGCAAATC
CAGCAGTGGCGCGCGTTGGGCACACGCTTCATTCAGGTGGTGCCGGAAGTGCAAATTCAT
ACCGCACAGGATAACCACGACGGCGTACTACGCGTGGGCGATACGCAAGGTCGCCTGCGT
AGCTGGTTCGCGCAACACAATGCTTCGCTGGTGGTGATGCGCCCGGATCGCTTTGTTGCC
GCCACCGCCATTCCGCAAACCCTGGGCAAGACCCTGAATAAACTGGCGTCGGTGATGACG
CTGACCCGCCCTGATGCCGACGTTTCTGTCGAAAAGGTAGCCTGA
Protein Properties
Pfam Domain Function:
Protein Residues:554
Protein Molecular Weight:63477
Protein Theoretical pI:6
PDB File:1O0C
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Glutaminyl-tRNA synthetase
MSEAEARPTNFIRQIIDEDLASGKHTTVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYKG
QCNLRFDDTNPVKEDIEYVESIKNDVEWLGFHWSGNVRYSSDYFDQLHAYAIELINKGLA
YVDELTPEQIREYRGTLTQPGKNSPYRDRSVEENLALFEKMRAGGFEEGKACLRAKIDMA
SPFIVMRDPVLYRIKFAEHHQTGNKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRL
YDWVLDNITIPVHPRQYEFSRLNLEYTVMSKRKLNLLVTDKHVEGWDDPRMPTISGLRRR
GYTAASIREFCKRIGVTKQDNTIEMASLESCIREDLNENAPRAMAVIDPVKLVIENYQGE
GEMVTMPNHPNKPEMGSRQVPFSGEIWIDRADFREEANKQYKRLVLGKEVRLRNAYVIKA
ERVEKDAEGNITTIFCTYDADTLSKDPADGRKVKGVIHWVSAAHALPVEIRLYDRLFSVP
NPGAADDFLSVINPESLVIKQGFAEPSLKDAVAGKAFQFEREGYFCLDSRHSTAEKPVFN
RTVGLRDTWAKVGE
References
External Links:
ResourceLink
Uniprot ID:P00962
Uniprot Name:SYQ_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674489
PDB ID:1O0C
Ecogene ID:EG10390
Ecocyc:EG10390
ColiBase:b0680
Kegg Gene:b0680
EchoBASE ID:EB0385
CCDB:SYQ_ECOLI
BacMap:16128656
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
  • 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
  • Hoben, P., Royal, N., Cheung, A., Yamao, F., Biemann, K., Soll, D. (1982). "Escherichia coli glutaminyl-tRNA synthetase. II. Characterization of the glnS gene product." J Biol Chem 257:11644-11650. Pubmed: 6749844
  • Hoben, P., Uemura, H., Yamao, F., Cheung, A., Swanson, R., Sumner-Smith, M., Soll, D. (1984). "Misaminoacylation by glutaminyl-tRNA synthetase: relaxed specificity in wild-type and mutant enzymes." Fed Proc 43:2972-2976. Pubmed: 6389180
  • 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
  • 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
  • Rath, V. L., Silvian, L. F., Beijer, B., Sproat, B. S., Steitz, T. A. (1998). "How glutaminyl-tRNA synthetase selects glutamine." Structure 6:439-449. Pubmed: 9562563
  • Rould, M. A., Perona, J. J., Soll, D., Steitz, T. A. (1989). "Structure of E. coli glutaminyl-tRNA synthetase complexed with tRNA(Gln) and ATP at 2.8 A resolution." Science 246:1135-1142. Pubmed: 2479982
  • Rould, M. A., Perona, J. J., Steitz, T. A. (1991). "Structural basis of anticodon loop recognition by glutaminyl-tRNA synthetase." Nature 352:213-218. Pubmed: 1857417
  • Sherlin, L. D., Bullock, T. L., Newberry, K. J., Lipman, R. S., Hou, Y. M., Beijer, B., Sproat, B. S., Perona, J. J. (2000). "Influence of transfer RNA tertiary structure on aminoacylation efficiency by glutaminyl and cysteinyl-tRNA synthetases." J Mol Biol 299:431-446. Pubmed: 10860750
  • Uemura, H., Conley, J., Yamao, F., Rogers, J., Soll, D. (1988). "Escherichia coli glutaminyl-tRNA synthetase: a single amino acid replacement relaxes rRNA specificity." Protein Seq Data Anal 1:479-485. Pubmed: 2464170
  • Yamao, F., Inokuchi, H., Cheung, A., Ozeki, H., Soll, D. (1982). "Escherichia coli glutaminyl-tRNA synthetase. I. Isolation and DNA sequence of the glnS gene." J Biol Chem 257:11639-11643. Pubmed: 6288695