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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)DescriptionActionsGraphical viewLength
    Binding sitei15ATP1
    Binding sitei41Glutamate1
    Binding sitei205Glutamate1
    Binding sitei208ATP1
    Binding sitei236ATP; via amide nitrogen and carbonyl oxygen1
    Sitei358Essential for discrimination between tRNA(Glu) and tRNA(Gln)1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi243 – 247ATP5

    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

    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
    Proteomesi
    • UP000000532 Componenti: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi358R → Q: Reduces affinity for tRNA and abolishes the ability to discriminate between tRNA(Glu) and tRNA(Gln). 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001196831 – 468Glutamate--tRNA ligaseAdd BLAST468

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sitei354Interaction with tRNA; via carbonyl oxygen1

    Protein-protein interaction databases

    DIPiDIP-29168N.
    STRINGi300852.TTHA0438.

    Structurei

    Secondary structure

    1468
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi3 – 6Combined sources4
    Beta strandi11 – 13Combined sources3
    Helixi16 – 31Combined sources16
    Beta strandi35 – 38Combined sources4
    Turni45 – 47Combined sources3
    Helixi52 – 62Combined sources11
    Beta strandi68 – 70Combined sources3
    Turni71 – 73Combined sources3
    Beta strandi76 – 78Combined sources3
    Helixi82 – 84Combined sources3
    Helixi86 – 98Combined sources13
    Beta strandi101 – 105Combined sources5
    Helixi109 – 119Combined sources11
    Helixi125 – 128Combined sources4
    Helixi131 – 139Combined sources9
    Beta strandi145 – 148Combined sources4
    Beta strandi155 – 160Combined sources6
    Turni161 – 163Combined sources3
    Beta strandi164 – 169Combined sources6
    Helixi170 – 172Combined sources3
    Beta strandi177 – 179Combined sources3
    Helixi187 – 197Combined sources11
    Beta strandi202 – 206Combined sources5
    Helixi207 – 212Combined sources6
    Helixi213 – 223Combined sources11
    Beta strandi229 – 233Combined sources5
    Beta strandi241 – 243Combined sources3
    Turni246 – 248Combined sources3
    Helixi253 – 258Combined sources6
    Helixi263 – 273Combined sources11
    Helixi286 – 292Combined sources7
    Helixi295 – 297Combined sources3
    Helixi307 – 320Combined sources14
    Helixi324 – 337Combined sources14
    Helixi345 – 355Combined sources11
    Helixi356 – 358Combined sources3
    Helixi364 – 368Combined sources5
    Helixi370 – 372Combined sources3
    Helixi381 – 403Combined sources23
    Helixi409 – 423Combined sources15
    Helixi427 – 439Combined sources13
    Helixi447 – 453Combined sources7
    Helixi456 – 467Combined sources12

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP27000.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni5 – 7Glutamate binding3
    Regioni187 – 191Glutamate binding5
    Regioni432 – 447Interaction with tRNAAdd BLAST16

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Motifi8 – 18"HIGH" regionAdd BLAST11
    Motifi243 – 247"KMSKS" region5

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105C20. Bacteria.
    COG0008. LUCA.
    HOGENOMiHOG000252720.
    KOiK01885.
    OMAiQLCYMPL.
    PhylomeDBiP27000.

    Family and domain databases

    CDDicd00808. GluRS_core. 1 hit.
    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. 1 hit.
    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.
    IPR033910. GluRS_core.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view]
    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)DescriptionActionsGraphical viewLength
    Sequence conflicti74 – 77GGPH → AAPT in CAA45854 (PubMed:1541262).Curated4

    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
    PDB 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.
    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

    eggNOGiENOG4105C20. Bacteria.
    COG0008. LUCA.
    HOGENOMiHOG000252720.
    KOiK01885.
    OMAiQLCYMPL.
    PhylomeDBiP27000.

    Enzyme and pathway databases

    BRENDAi6.1.1.17. 2305.

    Miscellaneous databases

    EvolutionaryTraceiP27000.

    Family and domain databases

    CDDicd00808. GluRS_core. 1 hit.
    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. 1 hit.
    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.
    IPR033910. GluRS_core.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view]
    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...

    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: November 30, 2016
    This is version 124 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

    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 one 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.