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Protein

Glutamate--tRNA ligase

Gene

gltX

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).2 Publications

Catalytic activityi

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu).

Enzyme regulationi

In the absence of bound tRNA, ATP is bound in a non-productive mode, and the enzyme cannot activate amino acids.1 Publication

Kineticsi

  1. KM=4.7 µM for tRNA-Glu1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei15 – 151ATP
    Binding sitei41 – 411Glutamate
    Binding sitei205 – 2051Glutamate
    Binding sitei208 – 2081ATP
    Binding sitei236 – 2361ATP; via amide nitrogen and carbonyl oxygen
    Sitei354 – 3541Interaction with tRNA; via carbonyl oxygen
    Sitei358 – 3581Essential for discrimination between tRNA(Glu) and tRNA(Gln)

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi243 – 2475ATP

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Aminoacyl-tRNA synthetase, Ligase

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciTTHE300852:GH8R-459-MONOMER.
    BRENDAi6.1.1.17. 2305.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate--tRNA ligase (EC:6.1.1.17)
    Alternative name(s):
    Glutamyl-tRNA synthetase
    Short name:
    GluRS
    Gene namesi
    Name:gltX
    Ordered Locus Names:TTHA0438
    OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
    Taxonomic identifieri300852 [NCBI]
    Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
    ProteomesiUP000000532 Componenti: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi358 – 3581R → Q: Reduces affinity for tRNA and abolishes the ability to discriminate between tRNA(Glu) and tRNA(Gln). 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 468468Glutamate--tRNA ligasePRO_0000119683Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    DIPiDIP-29168N.
    STRINGi300852.TTHA0438.

    Structurei

    Secondary structure

    1
    468
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 64Combined sources
    Beta strandi11 – 133Combined sources
    Helixi16 – 3116Combined sources
    Beta strandi35 – 384Combined sources
    Turni45 – 473Combined sources
    Helixi52 – 6211Combined sources
    Beta strandi68 – 703Combined sources
    Turni71 – 733Combined sources
    Beta strandi76 – 783Combined sources
    Helixi82 – 843Combined sources
    Helixi86 – 9813Combined sources
    Beta strandi101 – 1055Combined sources
    Helixi109 – 11911Combined sources
    Helixi125 – 1284Combined sources
    Helixi131 – 1399Combined sources
    Beta strandi145 – 1484Combined sources
    Beta strandi155 – 1606Combined sources
    Turni161 – 1633Combined sources
    Beta strandi164 – 1696Combined sources
    Helixi170 – 1723Combined sources
    Beta strandi177 – 1793Combined sources
    Helixi187 – 19711Combined sources
    Beta strandi202 – 2065Combined sources
    Helixi207 – 2126Combined sources
    Helixi213 – 22311Combined sources
    Beta strandi229 – 2335Combined sources
    Beta strandi241 – 2433Combined sources
    Turni246 – 2483Combined sources
    Helixi253 – 2586Combined sources
    Helixi263 – 27311Combined sources
    Helixi286 – 2927Combined sources
    Helixi295 – 2973Combined sources
    Helixi307 – 32014Combined sources
    Helixi324 – 33714Combined sources
    Helixi345 – 35511Combined sources
    Helixi356 – 3583Combined sources
    Helixi364 – 3685Combined sources
    Helixi370 – 3723Combined sources
    Helixi381 – 40323Combined sources
    Helixi409 – 42315Combined sources
    Helixi427 – 43913Combined sources
    Helixi447 – 4537Combined sources
    Helixi456 – 46712Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1G59X-ray2.40A/C1-468[»]
    1GLNX-ray2.50A1-468[»]
    1J09X-ray1.80A1-468[»]
    1N75X-ray1.90A1-468[»]
    1N77X-ray2.40A/B1-468[»]
    1N78X-ray2.10A/B1-468[»]
    2CUZX-ray1.98A1-468[»]
    2CV0X-ray2.40A/B1-468[»]
    2CV1X-ray2.41A/B1-468[»]
    2CV2X-ray2.69A/B1-468[»]
    2DXIX-ray2.20A/B1-468[»]
    ProteinModelPortaliP27000.
    SMRiP27000. Positions 1-468.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP27000.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni5 – 73Glutamate binding
    Regioni187 – 1915Glutamate binding
    Regioni432 – 44716Interaction with tRNAAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi8 – 1811"HIGH" regionAdd
    BLAST
    Motifi243 – 2475"KMSKS" region

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0008.
    HOGENOMiHOG000252720.
    KOiK01885.
    OMAiPQLCYMP.
    OrthoDBiEOG6DRPF7.
    PhylomeDBiP27000.

    Family and domain databases

    Gene3Di1.10.10.350. 1 hit.
    1.10.1160.10. 1 hit.
    1.10.8.70. 1 hit.
    3.40.50.620. 2 hits.
    HAMAPiMF_00022_B. Glu_tRNA_synth_B.
    InterProiIPR008925. aa-tRNA-synth_I_codon-bd.
    IPR020752. aa-tRNA-synth_I_codon-bd_sub1.
    IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
    IPR001412. aa-tRNA-synth_I_CS.
    IPR004527. Glu-tRNA-ligase_bac/mito.
    IPR000924. Glu/Gln-tRNA-synth.
    IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
    IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view]
    PANTHERiPTHR10119. PTHR10119. 1 hit.
    PfamiPF00749. tRNA-synt_1c. 1 hit.
    [Graphical view]
    PRINTSiPR00987. TRNASYNTHGLU.
    SUPFAMiSSF48163. SSF48163. 1 hit.
    TIGRFAMsiTIGR00464. gltX_bact. 1 hit.
    PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P27000-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MVVTRIAPSP TGDPHVGTAY IALFNYAWAR RNGGRFIVRI EDTDRARYVP
    60 70 80 90 100
    GAEERILAAL KWLGLSYDEG PDVGGPHGPY RQSERLPLYQ KYAEELLKRG
    110 120 130 140 150
    WAYRAFETPE ELEQIRKEKG GYDGRARNIP PEEAEERARR GEPHVIRLKV
    160 170 180 190 200
    PRPGTTEVKD ELRGVVVYDN QEIPDVVLLK SDGYPTYHLA NVVDDHLMGV
    210 220 230 240 250
    TDVIRAEEWL VSTPIHVLLY RAFGWEAPRF YHMPLLRNPD KTKISKRKSH
    260 270 280 290 300
    TSLDWYKAEG FLPEALRNYL CLMGFSMPDG REIFTLEEFI QAFTWERVSL
    310 320 330 340 350
    GGPVFDLEKL RWMNGKYIRE VLSLEEVAER VKPFLREAGL SWESEAYLRR
    360 370 380 390 400
    AVELMRPRFD TLKEFPEKAR YLFTEDYPVS EKAQRKLEEG LPLLKELYPR
    410 420 430 440 450
    LRAQEEWTEA ALEALLRGFA AEKGVKLGQV AQPLRAALTG SLETPGLFEI
    460
    LALLGKERAL RRLERALA
    Length:468
    Mass (Da):53,910
    Last modified:March 29, 2005 - v2
    Checksum:i920E7F3363AF19E9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti74 – 774GGPH → AAPT in CAA45854 (PubMed:1541262).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X64557 Genomic DNA. Translation: CAA45854.1.
    AP008226 Genomic DNA. Translation: BAD70261.1.
    RefSeqiWP_011227935.1. NC_006461.1.
    YP_143704.1. NC_006461.1.

    Genome annotation databases

    EnsemblBacteriaiBAD70261; BAD70261; BAD70261.
    GeneIDi3168748.
    KEGGittj:TTHA0438.
    PATRICi23955847. VBITheThe93045_0438.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X64557 Genomic DNA. Translation: CAA45854.1.
    AP008226 Genomic DNA. Translation: BAD70261.1.
    RefSeqiWP_011227935.1. NC_006461.1.
    YP_143704.1. NC_006461.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1G59X-ray2.40A/C1-468[»]
    1GLNX-ray2.50A1-468[»]
    1J09X-ray1.80A1-468[»]
    1N75X-ray1.90A1-468[»]
    1N77X-ray2.40A/B1-468[»]
    1N78X-ray2.10A/B1-468[»]
    2CUZX-ray1.98A1-468[»]
    2CV0X-ray2.40A/B1-468[»]
    2CV1X-ray2.41A/B1-468[»]
    2CV2X-ray2.69A/B1-468[»]
    2DXIX-ray2.20A/B1-468[»]
    ProteinModelPortaliP27000.
    SMRiP27000. Positions 1-468.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-29168N.
    STRINGi300852.TTHA0438.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiBAD70261; BAD70261; BAD70261.
    GeneIDi3168748.
    KEGGittj:TTHA0438.
    PATRICi23955847. VBITheThe93045_0438.

    Phylogenomic databases

    eggNOGiCOG0008.
    HOGENOMiHOG000252720.
    KOiK01885.
    OMAiPQLCYMP.
    OrthoDBiEOG6DRPF7.
    PhylomeDBiP27000.

    Enzyme and pathway databases

    BioCyciTTHE300852:GH8R-459-MONOMER.
    BRENDAi6.1.1.17. 2305.

    Miscellaneous databases

    EvolutionaryTraceiP27000.

    Family and domain databases

    Gene3Di1.10.10.350. 1 hit.
    1.10.1160.10. 1 hit.
    1.10.8.70. 1 hit.
    3.40.50.620. 2 hits.
    HAMAPiMF_00022_B. Glu_tRNA_synth_B.
    InterProiIPR008925. aa-tRNA-synth_I_codon-bd.
    IPR020752. aa-tRNA-synth_I_codon-bd_sub1.
    IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
    IPR001412. aa-tRNA-synth_I_CS.
    IPR004527. Glu-tRNA-ligase_bac/mito.
    IPR000924. Glu/Gln-tRNA-synth.
    IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
    IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view]
    PANTHERiPTHR10119. PTHR10119. 1 hit.
    PfamiPF00749. tRNA-synt_1c. 1 hit.
    [Graphical view]
    PRINTSiPR00987. TRNASYNTHGLU.
    SUPFAMiSSF48163. SSF48163. 1 hit.
    TIGRFAMsiTIGR00464. gltX_bact. 1 hit.
    PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Glutamyl-tRNA synthetase from Thermus thermophilus HB8. Molecular cloning of the gltX gene and crystallization of the overproduced protein."
      Nureki O., Suzuki K., Hara-Yokoyama M., Kohno T., Matsuzawa H., Ohta T., Shimizu T., Morikawa K., Miyazawa T., Yokoyama S.
      Eur. J. Biochem. 204:465-472(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Complete genome sequence of Thermus thermophilus HB8."
      Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
      Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: HB8 / ATCC 27634 / DSM 579.
    3. "Architectures of class-defining and specific domains of glutamyl-tRNA synthetase."
      Nureki O., Vassylyev D.G., Katayanagi K., Shimizu T., Sekine S., Kigawa T., Miyazawa T., Yokoyama S., Morikawa K.
      Science 267:1958-1965(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    4. "Structural basis for anticodon recognition by discriminating glutamyl-tRNA synthetase."
      Sekine S., Nureki O., Shimada A., Vassylyev D.G., Yokoyama S.
      Nat. Struct. Biol. 8:203-206(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH TRNA-GLU, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-358.
    5. "ATP binding by glutamyl-tRNA synthetase is switched to the productive mode by tRNA binding."
      Sekine S., Nureki O., Dubois D.Y., Bernier S., Chenevert R., Lapointe J., Vassylyev D.G., Yokoyama S.
      EMBO J. 22:676-688(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEXES WITH ATP; GLUTAMATE AND TRNA.
    6. "Structural bases of transfer RNA-dependent amino acid recognition and activation by glutamyl-tRNA synthetase."
      Sekine S., Shichiri M., Bernier S., Chenevert R., Lapointe J., Yokoyama S.
      Structure 14:1791-1799(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEXES WITH ATP; GLUTAMATE AND TRNA, FUNCTION, ENZYME REGULATION.

    Entry informationi

    Entry nameiSYE_THET8
    AccessioniPrimary (citable) accession number: P27000
    Secondary accession number(s): Q5SL55
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: March 29, 2005
    Last modified: July 22, 2015
    This is version 117 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Aminoacyl-tRNA synthetases
      List of aminoacyl-tRNA synthetase entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.