Canmetcon
Identification
Name:Glutamine synthetase
Synonyms:
  • Glutamate--ammonia ligase
Gene Name:glnA
Enzyme Class:
Biological Properties
General Function:Involved in glutamate-ammonia ligase activity
Specific Function:ATP + L-glutamate + NH(3) = ADP + phosphate + L-glutamine
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
  • Alanine, aspartate and glutamate metabolism ec00250
  • Arginine and proline metabolism ec00330
  • D-Glutamine and D-glutamate metabolism ec00471
  • Glyoxylate and dicarboxylate metabolism ec00630
  • Metabolic pathways eco01100
  • Microbial metabolism in diverse environments ec01120
  • Nitrogen metabolism ec00910
KEGG Reactions:
Thumb+Thumb+ThumbThumb+Thumb+Thumb
SMPDB Reactions:
Thumb+L-Glutamic acid+Thumb+Thumb+ThumbThumb+Thumb+Adenosine diphosphate+Thumb
Ammonia + L-Glutamic acid + Adenosine triphosphate + Oxoglutaric acid + L-GlutamatePhosphate + L-Glutamine + Adenosine diphosphate + ADP
ReactionCard
L-Glutamic acid+Thumb+Thumb+ThumbThumb+Thumb+Adenosine diphosphate+Thumb+Thumb
L-Glutamic acid + Adenosine triphosphate + Ammonium + L-GlutamateL-Glutamine + Hydrogen ion + Adenosine diphosphate + Phosphate + ADP
ReactionCard
EcoCyc Reactions:
Thumb+Thumb+ThumbThumb+Thumb+Thumb
Complex Reactions:
Thumb+Thumb+ThumbThumb+Thumb+Thumb+Thumb
Thumb+Thumb+ThumbThumb+Thumb+Thumb
Metabolites:
ECMDB IDNameView
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB00051AmmoniaMetaboCard
ECMDB21186AmmoniumMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB00148L-GlutamateMetaboCard
ECMDB00641L-GlutamineMetaboCard
ECMDB04123Oxoglutaric acidMetaboCard
ECMDB01429PhosphateMetaboCard
GO Classification:
Component
cell part
cytoplasm
intracellular part
Function
acid-ammonia (or amide) ligase activity
ammonia ligase activity
catalytic activity
glutamate-ammonia ligase activity
ligase activity
ligase activity, forming carbon-nitrogen bonds
Process
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
cellular metabolic process
glutamine biosynthetic process
glutamine family amino acid metabolic process
glutamine metabolic process
metabolic process
nitrogen compound metabolic process
nitrogen cycle metabolic process
nitrogen fixation
Gene Properties
Blattner:b3870
Gene OrientationCounterclockwise
Centisome Percentage:87.39
Left Sequence End4054648
Right Sequence End4056057
Gene Sequence:
>1410 bp
ATGTTCAATGGTCGTCCTTTCCCTGTAGATGCATTTCCTAAAATTATCAGGAATGCAATT
TATGAAGTGGAACAGCATACGCAGGCCCCTCAAGGTTTGATTGCTGCTTCTGCTCTTGGG
GTAATTTCTCTTGCCTGTCAGAACCGGATTGATGTTTGCCGATTGAATAATCTACGTGGC
CCGGTATCACTTTTCTTAATGACTCTGGCTGAATCAGGTGAACGTAAGAGTACGGTTGAT
AAACTGCTGATGAAGCCATTATATCAACTGGAAGAGGATTTATTTGAAAAATACACCCAC
GATCTTACCGCATGGAGAAATGATGAAGCAATTTTTAATATTGAAAAAAAAGCACTGATG
TCAAAACTTAAATCAGATATTCGACGTAACAAAGATCACTTGGCAACAAATGAAAGACTT
AAAGAACTACTTACGACAAACCCGAAAGCTCCAGTGAGATTCAAATTTTTATTTAACGAT
GCCACACCTGCAGCTATTAAAGCTCATCTCTGTGGGCACTGGCGATCAGTCGGCATCATG
TCTGATGAAGCTGGGATCATTTTTAATGGTTACACACTTAACGAGCTGCCGTTTATCAAT
AAGATGTGGGATGGTTCAATATTTACGGTGGAAAGGAAAAACGAGCCCGAGAAATTAATT
AGAGATGCAAGAATAACACTGTCGCTGATGGTCCAGCCTAATGTTTTTAAGGGTTATATC
GACAGGAAAGGAGATATGGCAAAGGGGATTGGATTTTTTGCACGGTGCCTCATGTGCCAG
CCTGCTTCAACACAAGGTAACAGAAAAATTTCCAACCCAATTTTTTCAAATGAACATTTG
CCGGTATTTCACCAACGTCTTATGGAAATTGTTAATGAGAGCATCATTAAAATTAATGAA
AATAATCGCATCTGCCTCCGATTCTCTGCAGAAGCAGAAAGACATTGGATCGAATTCTAC
AACCAGGTCGAGTCAGAAATGAGAATGATTGGCCTTCTTTATGATTTTAAGGATTATGCT
TCTAAAATGGCGGAGAACATGGCGAGGCTTGCTGCCTTACTTCATTACTTCAGCGGTGAT
GGAGGCGATATATCTGTTACCGCAGTAAAAGCAGCAGTGGAGATAGTGGCTTGGTATATT
GAAGAATACATCCGCTTGTTCTCTAAAAAAGAAGAGTTTTCTTTAGATGTTTCAGAAGCA
GATGAGCTTTATTGTTGGATAAAAGATTACTGCACGCAAAAATTTTCTTCCTGCATCAAG
AAAAATATTATCTTACAATTTGGGCCAAATAAATTTAGAAATCGTGACAAGGCAAATGAA
TTAATTAGAATCTTAATTTCACAAAACAAAATATTTATATCTTCATGGGGTAAAACAAAA
ATAATAAACATAACTCATTGTGTTTTTTGA
Protein Properties
Pfam Domain Function:
Protein Residues:469
Protein Molecular Weight:51903
Protein Theoretical pI:5
PDB File:2GLS
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Glutamine synthetase
MSAEHVLTMLNEHEVKFVDLRFTDTKGKEQHVTIPAHQVNAEFFEEGKMFDGSSIGGWKG
INESDMVLMPDASTAVIDPFFADSTLIIRCDILEPGTLQGYDRDPRSIAKRAEDYLRSTG
IADTVLFGPEPEFFLFDDIRFGSSISGSHVAIDDIEGAWNSSTQYEGGNKGHRPAVKGGY
FPVPPVDSAQDIRSEMCLVMEQMGLVVEAHHHEVATAGQNEVATRFNTMTKKADEIQIYK
YVVHNVAHRFGKTATFMPKPMFGDNGSGMHCHMSLSKNGVNLFAGDKYAGLSEQALYYIG
GVIKHAKAINALANPTTNSYKRLVPGYEAPVMLAYSARNRSASIRIPVVSSPKARRIEVR
FPDPAANPYLCFAALLMAGLDGIKNKIHPGEAMDKNLYDLPPEEAKEIPQVAGSLEEALN
ELDLDREFLKAGGVFTDEAIDAYIALRREEDDRVRMTPHPVEFELYYSV
References
External Links:
ResourceLink
Uniprot ID:P0A9C5
Uniprot Name:GLNA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85675488
PDB ID:2GLS
Ecogene ID:EG10383
Ecocyc:EG10383
ColiBase:b3870
Kegg Gene:b3870
EchoBASE ID:EB0378
CCDB:GLNA_ECOLI
BacMap:16131710
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
  • Colombo, G., Villafranca, J. J. (1986). "Amino acid sequence of Escherichia coli glutamine synthetase deduced from the DNA nucleotide sequence." J Biol Chem 261:10587-10591. Pubmed: 2874141
  • Covarrubias, A. A., Bastarrachea, F. (1983). "Nucleotide sequence of the glnA control region of Escherichia coli." Mol Gen Genet 190:171-175. Pubmed: 6134228
  • 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
  • Heinrikson, R. L., Kingdon, H. S. (1970). "The amino acid sequence in the vicinity of the covalently bound adenylic acid in glutamine synthetase from Escherichia coli." J Biol Chem 245:138-142. Pubmed: 4904088
  • Heinrikson, R. L., Kingdon, H. S. (1971). "Primary structure of Escherichia coli glutamine synthetase. II. The complete amino acid sequence of a tryptic heneicosapeptide containing covalently bound adenylic acid." J Biol Chem 246:1099-1106. Pubmed: 5543675
  • 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
  • Miranda-Rios, J., Sanchez-Pescador, R., Urdea, M., Covarrubias, A. A. (1987). "The complete nucleotide sequence of the glnALG operon of Escherichia coli K12." Nucleic Acids Res 15:2757-2770. Pubmed: 2882477
  • Plunkett, G. 3rd, Burland, V., Daniels, D. L., Blattner, F. R. (1993). "Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes." Nucleic Acids Res 21:3391-3398. Pubmed: 8346018
  • Reitzer, L. J., Magasanik, B. (1985). "Expression of glnA in Escherichia coli is regulated at tandem promoters." Proc Natl Acad Sci U S A 82:1979-1983. Pubmed: 2858855
  • Rocha, M., Vazquez, M., Garciarrubio, A., Covarrubias, A. A. (1985). "Nucleotide sequence of the glnA-glnL intercistronic region of Escherichia coli." Gene 37:91-99. Pubmed: 2865194
  • Ueno-Nishio, S., Mango, S., Reitzer, L. J., Magasanik, B. (1984). "Identification and regulation of the glnL operator-promoter of the complex glnALG operon of Escherichia coli." J Bacteriol 160:379-384. Pubmed: 6148334