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Identification
NameGlutamine synthetase
Synonyms
  • GS
  • Glutamate--ammonia ligase
Gene NameGLN1
Enzyme Class
Biological Properties
General FunctionInvolved in glutamate-ammonia ligase activity
Specific FunctionATP + L-glutamate + NH(3) = ADP + phosphate + L-glutamine
Cellular LocationCytoplasm
SMPDB Pathways
Nitrogen metabolismPW002504 Pw002504Pw002504 greyscalePw002504 simple
KEGG Pathways
Alanine, aspartate and glutamate metabolismec00250 Map00250
Arginine and proline metabolismec00330 Map00330
Nitrogen metabolismec00910 Map00910
SMPDB Reactions
Ammonia + L-Glutamic acid + Adenosine triphosphateL-Glutamine + ADP + phosphate
KEGG Reactions
Adenosine triphosphate + L-Glutamic acid + Ammoniumphosphate + L-Glutamine + hydron + ADP
Metabolites
YMDB IDNameView
YMDB00002L-GlutamineShow
YMDB00091AmmoniaShow
YMDB00109Adenosine triphosphateShow
YMDB00271L-Glutamic acidShow
YMDB00423AmmoniumShow
YMDB00862hydronShow
YMDB00907phosphateShow
YMDB00914ADPShow
GO Classification
Component
Not Available
Function
catalytic activity
acid-ammonia (or amide) ligase activity
ammonia ligase activity
ligase activity
glutamate-ammonia ligase activity
ligase activity, forming carbon-nitrogen bonds
Process
nitrogen compound metabolic process
cellular metabolic process
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
glutamine family amino acid metabolic process
glutamine metabolic process
metabolic process
glutamine biosynthetic process
Gene Properties
Chromosome Locationchromosome 16
LocusYPR035W
Gene Sequence>1113 bp ATGGCTGAAGCAAGCATCGAAAAGACTCAAATTTTACAAAAATATCTAGAACTGGACCAA AGAGGTAGAATAATTGCCGAATACGTTTGGATCGATGGTACTGGTAACTTACGTTCCAAA GGTAGAACTTTGAAGAAGAGAATCACATCCATTGACCAATTGCCAGAATGGAACTTCGAC GGTTCTTCTACCAACCAAGCGCCAGGCCACGACTCTGACATCTATTTGAAACCCGTTGCT TACTACCCAGATCCCTTCAGGAGAGGTGACAACATTGTTGTCTTGGCCGCATGTTACAAC AATGACGGTACTCCAAACAAGTTCAACCACAGACACGAAGCTGCCAAGCTATTTGCTGCT CATAAGGATGAAGAAATCTGGTTTGGTCTAGAACAAGAATACACTCTATTTGACATGTAT GACGATGTTTACGGATGGCCAAAGGGTGGGTACCCAGCTCCACAAGGTCCTTACTACTGT GGTGTTGGTGCCGGTAAGGTTTATGCCAGAGACATGATCGAAGCTCACTACAGAGCTTGT TTGTATGCCGGATTAGAAATTTCTGGTATTAACGCTGAAGTCATGCCATCTCAATGGGAA TTCCAAGTCGGTCCATGTACCGGTATTGACATGGGTGACCAATTATGGATGGCCAGATAC TTTTTGCACAGAGTGGCAGAAGAGTTTGGTATCAAGATCTCATTCCATCCAAAGCCATTG AAGGGTGACTGGAACGGTGCCGGTTGTCACGCTAACGTTTCCACCAAGGAAATGAGACAA CCAGGTGGTACGAAATACATCGAACAAGCCATCGAGAAGTTATCCAAGAGACACGCTGAA CACATTAAGTTGTACGGTAGCGATAACGACATGAGATTAACTGGTAGACATGAAACCGCT TCCATGACTGCCTTTTCTTCTGGTGTCGCCAACAGAGGTAGCTCAATTAGAATCCCAAGA TCCGTCGCCAAGGAAGGTTACGGTTACTTTGAAGACCGTAGACCAGCTTCCAACATCGAC CCATACTTGGTTACAGGTATCATGTGTGAAACTGTTTGCGGTGCTATTGACAATGCTGAC ATGACGAAGGAATTTGAAAGAGAATCTTCATAA
Protein Properties
Pfam Domain Function
Protein Residues370
Protein Molecular Weight41705.60156
Protein Theoretical pI6.29
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Glutamine synthetase MAEASIEKTQILQKYLELDQRGRIIAEYVWIDGTGNLRSKGRTLKKRITSIDQLPEWNFD GSSTNQAPGHDSDIYLKPVAYYPDPFRRGDNIVVLAACYNNDGTPNKFNHRHEAAKLFAA HKDEEIWFGLEQEYTLFDMYDDVYGWPKGGYPAPQGPYYCGVGAGKVYARDMIEAHYRAC LYAGLEISGINAEVMPSQWEFQVGPCTGIDMGDQLWMARYFLHRVAEEFGIKISFHPKPL KGDWNGAGCHANVSTKEMRQPGGTKYIEQAIEKLSKRHAEHIKLYGSDNDMRLTGRHETA SMTAFSSGVANRGSSIRIPRSVAKEGYGYFEDRRPASNIDPYLVTGIMCETVCGAIDNAD MTKEFERESS
References
External Links
ResourceLink
Saccharomyces Genome Database GLN1
Uniprot IDP32288
Uniprot NameGLNA_YEAST
GenBank Gene IDZ68111
Genebank Protein ID1072403
General Reference
  • Minehart, P. L., Magasanik, B. (1992). "Sequence of the GLN1 gene of Saccharomyces cerevisiae: role of the upstream region in regulation of glutamine synthetase expression." J Bacteriol 174:1828-1836.1347768
  • Bussey, H., Storms, R. K., Ahmed, A., Albermann, K., Allen, E., Ansorge, W., Araujo, R., Aparicio, A., Barrell, B., Badcock, K., Benes, V., Botstein, D., Bowman, S., Bruckner, M., Carpenter, J., Cherry, J. M., Chung, E., Churcher, C., Coster, F., Davis, K., Davis, R. W., Dietrich, F. S., Delius, H., DiPaolo, T., Hani, J., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI." Nature 387:103-105.9169875
  • Kim, K. H., Rhee, S. G. (1988). "Sequence of peptides from Saccharomyces cerevisiae glutamine synthetase. N-terminal peptide and ATP-binding domain." J Biol Chem 263:833-838.2891705
  • Garrels, J. I., McLaughlin, C. S., Warner, J. R., Futcher, B., Latter, G. I., Kobayashi, R., Schwender, B., Volpe, T., Anderson, D. S., Mesquita-Fuentes, R., Payne, W. E. (1997). "Proteome studies of Saccharomyces cerevisiae: identification and characterization of abundant proteins." Electrophoresis 18:1347-1360.9298649
  • Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106
  • Peng, J., Schwartz, D., Elias, J. E., Thoreen, C. C., Cheng, D., Marsischky, G., Roelofs, J., Finley, D., Gygi, S. P. (2003). "A proteomics approach to understanding protein ubiquitination." Nat Biotechnol 21:921-926.12872131
  • Hitchcock, A. L., Auld, K., Gygi, S. P., Silver, P. A. (2003). "A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery." Proc Natl Acad Sci U S A 100:12735-12740.14557538