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P27000

- SYE_THET8

UniProt

P27000 - SYE_THET8

Protein

Glutamate--tRNA ligase

Gene

gltX

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 2 (29 Mar 2005)
      Previous versions | rss
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    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

    1. ATP binding Source: UniProtKB-HAMAP
    2. glutamate-tRNA ligase activity Source: UniProtKB-HAMAP
    3. tRNA binding Source: InterPro

    GO - Biological processi

    1. glutamyl-tRNA aminoacylation Source: UniProtKB-HAMAP

    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.

    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: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    OMAiVTGQTHG.
    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

    MVVTRIAPSP TGDPHVGTAY IALFNYAWAR RNGGRFIVRI EDTDRARYVP    50
    GAEERILAAL KWLGLSYDEG PDVGGPHGPY RQSERLPLYQ KYAEELLKRG 100
    WAYRAFETPE ELEQIRKEKG GYDGRARNIP PEEAEERARR GEPHVIRLKV 150
    PRPGTTEVKD ELRGVVVYDN QEIPDVVLLK SDGYPTYHLA NVVDDHLMGV 200
    TDVIRAEEWL VSTPIHVLLY RAFGWEAPRF YHMPLLRNPD KTKISKRKSH 250
    TSLDWYKAEG FLPEALRNYL CLMGFSMPDG REIFTLEEFI QAFTWERVSL 300
    GGPVFDLEKL RWMNGKYIRE VLSLEEVAER VKPFLREAGL SWESEAYLRR 350
    AVELMRPRFD TLKEFPEKAR YLFTEDYPVS EKAQRKLEEG LPLLKELYPR 400
    LRAQEEWTEA ALEALLRGFA AEKGVKLGQV AQPLRAALTG SLETPGLFEI 450
    LALLGKERAL RRLERALA 468
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X64557 Genomic DNA. Translation: CAA45854.1 .
    AP008226 Genomic DNA. Translation: BAD70261.1 .
    RefSeqi WP_011227935.1. NC_006461.1.
    YP_143704.1. NC_006461.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1G59 X-ray 2.40 A/C 1-468 [» ]
    1GLN X-ray 2.50 A 1-468 [» ]
    1J09 X-ray 1.80 A 1-468 [» ]
    1N75 X-ray 1.90 A 1-468 [» ]
    1N77 X-ray 2.40 A/B 1-468 [» ]
    1N78 X-ray 2.10 A/B 1-468 [» ]
    2CUZ X-ray 1.98 A 1-468 [» ]
    2CV0 X-ray 2.40 A/B 1-468 [» ]
    2CV1 X-ray 2.41 A/B 1-468 [» ]
    2CV2 X-ray 2.69 A/B 1-468 [» ]
    2DXI X-ray 2.20 A/B 1-468 [» ]
    ProteinModelPortali P27000.
    SMRi P27000. Positions 1-468.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-29168N.
    STRINGi 300852.TTHA0438.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAD70261 ; BAD70261 ; BAD70261 .
    GeneIDi 3168748.
    KEGGi ttj:TTHA0438.
    PATRICi 23955847. VBITheThe93045_0438.

    Phylogenomic databases

    eggNOGi COG0008.
    HOGENOMi HOG000252720.
    KOi K01885.
    OMAi VTGQTHG.
    OrthoDBi EOG6DRPF7.
    PhylomeDBi P27000.

    Enzyme and pathway databases

    BioCyci TTHE300852:GH8R-459-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P27000.

    Family and domain databases

    Gene3Di 1.10.10.350. 1 hit.
    1.10.1160.10. 1 hit.
    1.10.8.70. 1 hit.
    3.40.50.620. 2 hits.
    HAMAPi MF_00022_B. Glu_tRNA_synth_B.
    InterProi IPR008925. 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 ]
    PANTHERi PTHR10119. PTHR10119. 1 hit.
    Pfami PF00749. tRNA-synt_1c. 1 hit.
    [Graphical view ]
    PRINTSi PR00987. TRNASYNTHGLU.
    SUPFAMi SSF48163. SSF48163. 1 hit.
    TIGRFAMsi TIGR00464. gltX_bact. 1 hit.
    PROSITEi PS00178. AA_TRNA_LIGASE_I. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 111 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