You are using an unsupported browser. Please upgrade your browser to a newer version to get the best experience on Yeast Metabolome Database.
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
Pathways
  • Alanine, aspartate and glutamate metabolism00250
  • Arginine and proline metabolism00330
  • Nitrogen metabolism00910
Reactions
  • ATP + L-glutamate + NH(3) = ADP + phosphate + L-glutamine.
Metabolites
YMDB IDNameView
YMDB00002L-GlutamineShow
YMDB00091AmmoniaShow
YMDB00109Adenosine triphosphateShow
YMDB00271L-Glutamic acidShow
YMDB00423AmmoniumShow
YMDB00862hydronShow
YMDB00907phosphateShow
YMDB00914ADPShow
GO Classification
Component
Not Available
Function
ligase activity, forming carbon-nitrogen bonds
catalytic activity
acid-ammonia (or amide) ligase activity
ammonia ligase activity
ligase activity
glutamate-ammonia ligase activity
Process
glutamine biosynthetic 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
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