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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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei6 – 61Glutamate1 Publication
    Binding sitei192 – 1921Glutamate1 Publication
    Binding sitei251 – 2511ATPBy similarity

    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 lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesThermosynechococcus
    ProteomesiUP000000440 Componenti: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 485485Glutamate--tRNA ligasePRO_0000119674Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    STRINGi197221.tll0506.

    Structurei

    Secondary structure

    1
    485
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 74Combined sources
    Helixi17 – 3216Combined sources
    Beta strandi36 – 416Combined sources
    Beta strandi45 – 484Combined sources
    Helixi51 – 6313Combined sources
    Beta strandi69 – 746Combined sources
    Helixi75 – 773Combined sources
    Helixi79 – 9113Combined sources
    Beta strandi94 – 985Combined sources
    Helixi102 – 11514Combined sources
    Turni124 – 1274Combined sources
    Helixi130 – 1389Combined sources
    Beta strandi144 – 1474Combined sources
    Beta strandi154 – 1596Combined sources
    Turni160 – 1623Combined sources
    Beta strandi163 – 1686Combined sources
    Helixi169 – 1724Combined sources
    Beta strandi174 – 1796Combined sources
    Helixi192 – 20211Combined sources
    Beta strandi206 – 2116Combined sources
    Helixi212 – 2165Combined sources
    Helixi217 – 22711Combined sources
    Beta strandi234 – 2385Combined sources
    Beta strandi244 – 2485Combined sources
    Helixi258 – 2636Combined sources
    Helixi268 – 27710Combined sources
    Turni284 – 2863Combined sources
    Helixi292 – 2987Combined sources
    Helixi313 – 32412Combined sources
    Helixi329 – 34214Combined sources
    Turni349 – 3524Combined sources
    Helixi353 – 36311Combined sources
    Helixi364 – 3663Combined sources
    Helixi370 – 3723Combined sources
    Helixi373 – 3819Combined sources
    Beta strandi382 – 3843Combined sources
    Helixi389 – 3957Combined sources
    Helixi400 – 41011Combined sources
    Beta strandi413 – 4153Combined sources
    Helixi419 – 43315Combined sources
    Helixi437 – 44913Combined sources
    Beta strandi450 – 4534Combined sources
    Helixi457 – 46610Combined sources
    Helixi470 – 48415Combined sources

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiQ8DLI5.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni210 – 2145Glutamate binding

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi9 – 1911"HIGH" regionAdd
    BLAST
    Motifi248 – 2525"KMSKS" region

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0008.
    HOGENOMiHOG000252722.
    KOiK01885.
    OMAiMSKRHGS.
    OrthoDBiEOG6DRPF7.

    Family and domain databases

    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.
    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.
    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.

    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
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CFOX-ray2.45A/B2-485[»]
    ProteinModelPortaliQ8DLI5.
    SMRiQ8DLI5. Positions 2-485.
    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

    eggNOGiCOG0008.
    HOGENOMiHOG000252722.
    KOiK01885.
    OMAiMSKRHGS.
    OrthoDBiEOG6DRPF7.

    Miscellaneous databases

    EvolutionaryTraceiQ8DLI5.

    Family and domain databases

    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.
    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.
    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: BP-1.
    2. "Crystal structure of a non-discriminating glutamyl-tRNA synthetase."
      Schulze J.O., Masoumi A., Nickel D., Jahn M., Jahn D., Schubert W.-D., Heinz D.W.
      J. Mol. Biol. 361:888-897(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) IN COMPLEX WITH GLUTAMATE, FUNCTION, ABSENCE OF COFACTOR REQUIREMENT, BIOPHYSICOCHEMICAL PROPERTIES.

    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: April 29, 2015
    This is version 80 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

    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.