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Protein

Glutamate--tRNA ligase

Gene

gltX

Organism
Thermosynechococcus elongatus (strain BP-1)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Non-discriminating glutamyl-tRNA synthetase. 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). Acylates both tRNA(Glu) and tRNA(Gln) with glutamate, but has 13-fold higher efficiency with tRNA(Glu).1 Publication

Catalytic activityi

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

Cofactori

Note: Does not require zinc.

Kineticsi

  1. KM=0.79 µM for tRNA-Glu1 Publication
  2. KM=3.7 µM for tRNA-Gln1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei6Glutamate1 Publication1
    Binding sitei192Glutamate1 Publication1
    Binding sitei251ATPBy similarity1

    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

    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:tll0506
    OrganismiThermosynechococcus elongatus (strain BP-1)
    Taxonomic identifieri197221 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaSynechococcalesSynechococcaceaeThermosynechococcus
    Proteomesi
    • UP000000440 Componenti: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001196741 – 485Glutamate--tRNA ligaseAdd BLAST485

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    STRINGi197221.tll0506.

    Structurei

    Secondary structure

    1485
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi4 – 7Combined sources4
    Helixi17 – 32Combined sources16
    Beta strandi36 – 41Combined sources6
    Beta strandi45 – 48Combined sources4
    Helixi51 – 63Combined sources13
    Beta strandi69 – 74Combined sources6
    Helixi75 – 77Combined sources3
    Helixi79 – 91Combined sources13
    Beta strandi94 – 98Combined sources5
    Helixi102 – 115Combined sources14
    Turni124 – 127Combined sources4
    Helixi130 – 138Combined sources9
    Beta strandi144 – 147Combined sources4
    Beta strandi154 – 159Combined sources6
    Turni160 – 162Combined sources3
    Beta strandi163 – 168Combined sources6
    Helixi169 – 172Combined sources4
    Beta strandi174 – 179Combined sources6
    Helixi192 – 202Combined sources11
    Beta strandi206 – 211Combined sources6
    Helixi212 – 216Combined sources5
    Helixi217 – 227Combined sources11
    Beta strandi234 – 238Combined sources5
    Beta strandi244 – 248Combined sources5
    Helixi258 – 263Combined sources6
    Helixi268 – 277Combined sources10
    Turni284 – 286Combined sources3
    Helixi292 – 298Combined sources7
    Helixi313 – 324Combined sources12
    Helixi329 – 342Combined sources14
    Turni349 – 352Combined sources4
    Helixi353 – 363Combined sources11
    Helixi364 – 366Combined sources3
    Helixi370 – 372Combined sources3
    Helixi373 – 381Combined sources9
    Beta strandi382 – 384Combined sources3
    Helixi389 – 395Combined sources7
    Helixi400 – 410Combined sources11
    Beta strandi413 – 415Combined sources3
    Helixi419 – 433Combined sources15
    Helixi437 – 449Combined sources13
    Beta strandi450 – 453Combined sources4
    Helixi457 – 466Combined sources10
    Helixi470 – 484Combined sources15

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2CFOX-ray2.45A/B2-485[»]
    ProteinModelPortaliQ8DLI5.
    SMRiQ8DLI5.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8DLI5.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni210 – 214Glutamate binding5

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Motifi9 – 19"HIGH" regionAdd BLAST11
    Motifi248 – 252"KMSKS" region5

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105C20. Bacteria.
    COG0008. LUCA.
    HOGENOMiHOG000252722.
    KOiK01885.
    OMAiHGATNVM.
    OrthoDBiPOG091H021W.

    Family and domain databases

    CDDicd00808. GluRS_core. 1 hit.
    Gene3Di1.10.10.350. 1 hit.
    1.10.1160.10. 1 hit.
    3.40.50.620. 2 hits.
    HAMAPiMF_00022_B. Glu_tRNA_synth_B. 1 hit.
    InterProiIPR008925. aa-tRNA-synth_I_codon-bd.
    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.

    Q8DLI5-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTVRVRLAPS PTGNLHIGTA RTAVFNWLYA RHRGGKFILR IEDTDRERSR
    60 70 80 90 100
    PEYTENILEG LQWLGLTWDE GPYFQSDRLD LYRQAIQTLL DKGLAYYCYC
    110 120 130 140 150
    TPEELEALRA EQKAKGQAPR YDNRHRHLTP EEQAAFEAAG RTPVIRFKIE
    160 170 180 190 200
    DDRQIEWQDL VRGRVSWQGA DLGGDMVIAR AAPRGEIGYP LYNLVVVVDD
    210 220 230 240 250
    IAMGITDVIR GEDHIGNTPK QILLYEALGA TPPNFAHTPL ILNSTGQKLS
    260 270 280 290 300
    KRDGVTSISD FRAMGYLAPA LANYMTLLGW SPPEGVGELF TLDLAAKHFS
    310 320 330 340 350
    FERINKAGAR FDWDKLNWLN RQYIQQLEPE EFLAELIPLW QGAGYAFDEE
    360 370 380 390 400
    RDRPWLFDLA QLLQPGLNTL REAIDQGAVF FIPSVTFDSE AMAQLGQPQS
    410 420 430 440 450
    ATILAYLLEH LPAEPALTVA MGQQLIQQAA KAAGVKKGAT MRTLRAALTG
    460 470 480
    AVHGPDLMAA WQILHQRGWD EPRLAAALKQ AQTTS
    Length:485
    Mass (Da):54,362
    Last modified:March 1, 2003 - v1
    Checksum:iC3547C6415FDDCBA
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    BA000039 Genomic DNA. Translation: BAC08058.1.
    RefSeqiNP_681296.1. NC_004113.1.
    WP_011056357.1. NC_004113.1.

    Genome annotation databases

    EnsemblBacteriaiBAC08058; BAC08058; BAC08058.
    GeneIDi1012165.
    KEGGitel:tll0506.
    PATRICi23926260. VBITheElo119873_0533.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    BA000039 Genomic DNA. Translation: BAC08058.1.
    RefSeqiNP_681296.1. NC_004113.1.
    WP_011056357.1. NC_004113.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2CFOX-ray2.45A/B2-485[»]
    ProteinModelPortaliQ8DLI5.
    SMRiQ8DLI5.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi197221.tll0506.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiBAC08058; BAC08058; BAC08058.
    GeneIDi1012165.
    KEGGitel:tll0506.
    PATRICi23926260. VBITheElo119873_0533.

    Phylogenomic databases

    eggNOGiENOG4105C20. Bacteria.
    COG0008. LUCA.
    HOGENOMiHOG000252722.
    KOiK01885.
    OMAiHGATNVM.
    OrthoDBiPOG091H021W.

    Miscellaneous databases

    EvolutionaryTraceiQ8DLI5.

    Family and domain databases

    CDDicd00808. GluRS_core. 1 hit.
    Gene3Di1.10.10.350. 1 hit.
    1.10.1160.10. 1 hit.
    3.40.50.620. 2 hits.
    HAMAPiMF_00022_B. Glu_tRNA_synth_B. 1 hit.
    InterProiIPR008925. aa-tRNA-synth_I_codon-bd.
    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_THEEB
    AccessioniPrimary (citable) accession number: Q8DLI5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 23, 2003
    Last sequence update: March 1, 2003
    Last modified: November 30, 2016
    This is version 88 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    This organism lacks a tRNA synthetase for tRNA(Gln). Instead, tRNA(Gln) is first charged with Glu, and then the bound glutamate is converted to glutamine by GatCAB.

    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.