Identification
Name: Glutamyl-tRNA synthetase, cytoplasmic
Synonyms
  • Glutamate--tRNA ligase
  • GluRS
  • P85
Gene Name: GUS1 Link_out
Enzyme Class:
Biological Properties
General Function: Involved in nucleotide binding
Specific Function: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction:glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu)
Cellular Location: Cytoplasm
Pathways:
  • Porphyrin and chlorophyll metabolism 00860 Link_out
  • Reactions:
    • ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu).
    Metabolites:
    YMDB ID Name View
    YMDB00097Adenosine monophosphate
    YMDB00109Adenosine triphosphate
    YMDB00219Pyrophosphate
    YMDB00271L-Glutamic acid
    GO Classification:
    Component
    intracellular part
    cytoplasm
    cell part
    Function
    ligase activity
    nucleotide binding
    binding
    nucleoside binding
    purine nucleoside binding
    adenyl nucleotide binding
    adenyl ribonucleotide binding
    catalytic activity
    ATP binding
    ligase activity, forming carbon-oxygen bonds
    glutamate-tRNA ligase activity
    ligase activity, forming aminoacyl-tRNA and related compounds
    aminoacyl-tRNA ligase activity
    Process
    biosynthetic process
    cellular macromolecule metabolic process
    RNA metabolic process
    ncRNA metabolic process
    tRNA metabolic process
    tRNA aminoacylation
    tRNA aminoacylation for protein translation
    macromolecule biosynthetic process
    cellular macromolecule biosynthetic process
    translation
    metabolic process
    macromolecule metabolic process
    glutamyl-tRNA aminoacylation
    Gene Properties
    Chromosome Location: chromosome 7
    Locus: YGL245W Link_out
    Gene Sequence:
    >YGL245W GUS1 SGDID:S000003214, Chr VII from 39023-41149, Verified ORF, "Glutamyl-tRNA synthetase (GluRS), forms a complex with methionyl-tRNA synthetase (Mes1p) and Arc1p; complex formation increases the catalytic efficiency of both tRNA synthetases and e
    ATGCCATCTACCTTGACTATTAATGGAAAAGCCCCAATTGTGGCTTATGCTGAACTAATT
    GCTGCTCGTATTGTGAATGCGTTAGCTCCTAACTCCATAGCTATTAAGTTGGTGGACGAT
    AAGAAAGCACCTGCTGCCAAGCTCGATGATGCTACTGAAGATGTCTTCAACAAGATAACT
    AGCAAATTCGCCGCCATCTTCGATAATGGTGATAAAGAGCAAGTTGCTAAATGGGTTAAT
    CTGGCCCAAAAGGAATTAGTTATCAAGAACTTTGCTAAATTATCACAATCATTGGAAACA
    CTAGATTCTCAATTGAACCTAAGAACCTTTATTCTTGGCGGCTTGAAGTATTCTGCCGCT
    GATGTAGCATGTTGGGGTGCTTTAAGATCCAATGGTATGTGCGGTTCCATCATCAAGAAC
    AAGGTTGATGTTAACGTTTCTCGTTGGTACACTTTGTTAGAAATGGATCCCATCTTCGGC
    GAAGCTCACGATTTCTTGAGCAAATCTTTACTAGAATTAAAGAAAAGTGCTAATGTGGGT
    AAGAAGAAGGAAACTCACAAGGCTAACTTTGAAATTGATTTGCCAGATGCCAAAATGGGT
    GAAGTCGTCACTCGTTTCCCACCTGAACCTTCTGGATACTTACATATTGGACATGCCAAA
    GCTGCCTTGTTGAACCAATATTTTGCTCAAGCTTACAAGGGTAAGTTGATTATTAGATTC
    GATGACACCAACCCATCGAAGGAAAAGGAAGAATTCCAAGACTCTATTTTGGAAGATTTG
    GATTTATTAGGAATCAAGGGTGATAGAATAACCTACTCATCTGACTACTTCCAAGAAATG
    TACGACTACTGTGTTCAAATGATCAAGGATGGTAAAGCTTACTGTGACGACACTCCAACT
    GAAAAGATGAGAGAAGAACGTATGGATGGTGTTGCTTCTGCCAGAAGAGATCGTTCTGTT
    GAAGAGAACTTAAGAATTTTTACCGAAGAAATGAAAAACGGTACTGAAGAAGGTTTGAAG
    AACTGTGTTCGTGCCAAGATCGATTACAAGGCTTTGAACAAGACTCTAAGAGATCCTGTC
    ATTTACAGATGTAATCTAACCCCTCACCACAGAACCGGATCAACTTGGAAGATCTACCCA
    ACTTATGATTTCTGTGTCCCAATTGTTGATGCTATTGAAGGTGTTACCCACGCTTTACGT
    ACCATTGAATATAGAGACCGTAACGCTCAATATGATTGGATGTTACAAGCTTTGCGTTTG
    AGAAAAGTCCATATTTGGGATTTCGCTCGTATCAATTTCGTTAGAACCTTGTTGTCTAAG
    AGAAAGTTACAATGGATGGTTGACAAGGACTTGGTCGGAAATTGGGACGATCCAAGGTTC
    CCAACTGTCAGGGGTGTGAGAAGAAGAGGTATGACTGTCGAAGGTTTGAGGAACTTCGTC
    TTATCCCAAGGTCCATCCAGAAATGTCATTAACTTGGAATGGAACTTGATCTGGGCTTTC
    AACAAGAAGGTCATTGATCCAATTGCTCCAAGACACACTGCTATCGTCAACCCAGTTAAA
    ATCCACTTGGAAGGCTCCGAAGCTCCACAAGAACCAAAGATTGAAATGAAACCAAAACAC
    AAGAAAAACCCAGCTGTGGGCGAAAAGAAAGTCATTTACTACAAAGACATTGTTGTCGAC
    AAAGATGATGCTGACGTCATCAATGTTGATGAAGAAGTCACTTTAATGGACTGGGGTAAT
    GTCATTATTACTAAAAAGAATGACGATGGTTCTATGGTTGCCAAATTGAATTTGGAAGGT
    GATTTCAAAAAGACCAAGCACAAGTTGACTTGGTTAGCTGATACTAAAGATGTCGTCCCT
    GTTGATTTAGTTGACTTCGACCATTTGATTACCAAGGACAGATTGGAAGAAGACGAAAGT
    TTCGAAGATTTCTTGACTCCTCAAACAGAATTCCACACGGATGCCATTGCTGACTTGAAT
    GTTAAGGATATGAAGATTGGTGATATCATCCAATTCGAAAGAAAGGGCTACTACAGATTG
    GATGCTTTACCCAAGGATGGTAAGCCATATGTCTTTTTTACCATCCCAGATGGTAAATCT
    GTCAACAAGTATGGTGCAAAGAAATAA
    Protein Properties
    Pfam Domain Function:
    Protein Residues: 708
    Protein Molecular Weight: 80842.0
    Protein Theoretical pI: 7.61
    Signalling Regions:
    • None
    Transmembrane Regions:
    • None
    Protein Sequence:
    >Glutamyl-tRNA synthetase, cytoplasmic
    MPSTLTINGKAPIVAYAELIAARIVNALAPNSIAIKLVDDKKAPAAKLDDATEDVFNKIT
    SKFAAIFDNGDKEQVAKWVNLAQKELVIKNFAKLSQSLETLDSQLNLRTFILGGLKYSAA
    DVACWGALRSNGMCGSIIKNKVDVNVSRWYTLLEMDPIFGEAHDFLSKSLLELKKSANVG
    KKKETHKANFEIDLPDAKMGEVVTRFPPEPSGYLHIGHAKAALLNQYFAQAYKGKLIIRF
    DDTNPSKEKEEFQDSILEDLDLLGIKGDRITYSSDYFQEMYDYCVQMIKDGKAYCDDTPT
    EKMREERMDGVASARRDRSVEENLRIFTEEMKNGTEEGLKNCVRAKIDYKALNKTLRDPV
    IYRCNLTPHHRTGSTWKIYPTYDFCVPIVDAIEGVTHALRTIEYRDRNAQYDWMLQALRL
    RKVHIWDFARINFVRTLLSKRKLQWMVDKDLVGNWDDPRFPTVRGVRRRGMTVEGLRNFV
    LSQGPSRNVINLEWNLIWAFNKKVIDPIAPRHTAIVNPVKIHLEGSEAPQEPKIEMKPKH
    KKNPAVGEKKVIYYKDIVVDKDDADVINVDEEVTLMDWGNVIITKKNDDGSMVAKLNLEG
    DFKKTKHKLTWLADTKDVVPVDLVDFDHLITKDRLEEDESFEDFLTPQTEFHTDAIADLN
    VKDMKIGDIIQFERKGYYRLDALPKDGKPYVFFTIPDGKSVNKYGAKK
    References
    External Links:
    Resource Link
    Saccharomyces Genome Database: GUS1 Link_out
    Uniprot ID: P46655 Link_out
    Uniprot Name: SYEC_YEAST Link_out
    General Reference:
    • Vandenbol, M., Durand, P., Portetelle, D., Hilger, F. (1995). "The sequence of an 11.1 kb DNA fragment between ADH4 and ADE5 on the left arm of chromosome VII reveals the presence of eight open reading frames." Yeast 11:1519-1523. Pubmed: 8750240 Link_out
    • Tettelin, H., Agostoni Carbone, M. L., Albermann, K., Albers, M., Arroyo, J., Backes, U., Barreiros, T., Bertani, I., Bjourson, A. J., Bruckner, M., Bruschi, C. V., Carignani, G., Castagnoli, L., Cerdan, E., Clemente, M. L., Coblenz, A., Coglievina, M., Coissac, E., Defoor, E., Del Bino, S., Delius, H., Delneri, D., de Wergifosse, P., Dujon, B., Kleine, K., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Nature 387:81-84. Pubmed: 9169869 Link_out
    • Coissac, E., Maillier, E., Robineau, S., Netter, P. (1996). "Sequence of a 39,411 bp DNA fragment covering the left end of chromosome VII of Saccharomyces cerevisiae." Yeast 12:1555-1562. Pubmed: 8972578 Link_out
    • Kellis, M., Patterson, N., Endrizzi, M., Birren, B., Lander, E. S. (2003). "Sequencing and comparison of yeast species to identify genes and regulatory elements." Nature 423:241-254. Pubmed: 12748633 Link_out
    • Huh, W. K., Falvo, J. V., Gerke, L. C., Carroll, A. S., Howson, R. W., Weissman, J. S., O'Shea, E. K. (2003). "Global analysis of protein localization in budding yeast." Nature 425:686-691. Pubmed: 14562095 Link_out
    • 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. Pubmed: 14562106 Link_out
    • Albuquerque, C. P., Smolka, M. B., Payne, S. H., Bafna, V., Eng, J., Zhou, H. (2008). "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Mol Cell Proteomics 7:1389-1396. Pubmed: 18407956 Link_out
    • Simader, H., Hothorn, M., Suck, D. (2006). "Structures of the interacting domains from yeast glutamyl-tRNA synthetase and tRNA-aminoacylation and nuclear-export cofactor Arc1p reveal a novel function for an old fold." Acta Crystallogr D Biol Crystallogr 62:1510-1519. Pubmed: 17139087 Link_out
    • Simader, H., Hothorn, M., Kohler, C., Basquin, J., Simos, G., Suck, D. (2006). "Structural basis of yeast aminoacyl-tRNA synthetase complex formation revealed by crystal structures of two binary sub-complexes." Nucleic Acids Res 34:3968-3979. Pubmed: 16914447 Link_out