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Q8DLI5

- SYE_THEEB

UniProt

Q8DLI5 - SYE_THEEB

Protein

Glutamate--tRNA ligase

Gene

gltX

Organism
Thermosynechococcus elongatus (strain BP-1)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 74 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    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

    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

    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

    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: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

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

    3D structure databases

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

    MTVRVRLAPS PTGNLHIGTA RTAVFNWLYA RHRGGKFILR IEDTDRERSR    50
    PEYTENILEG LQWLGLTWDE GPYFQSDRLD LYRQAIQTLL DKGLAYYCYC 100
    TPEELEALRA EQKAKGQAPR YDNRHRHLTP EEQAAFEAAG RTPVIRFKIE 150
    DDRQIEWQDL VRGRVSWQGA DLGGDMVIAR AAPRGEIGYP LYNLVVVVDD 200
    IAMGITDVIR GEDHIGNTPK QILLYEALGA TPPNFAHTPL ILNSTGQKLS 250
    KRDGVTSISD FRAMGYLAPA LANYMTLLGW SPPEGVGELF TLDLAAKHFS 300
    FERINKAGAR FDWDKLNWLN RQYIQQLEPE EFLAELIPLW QGAGYAFDEE 350
    RDRPWLFDLA QLLQPGLNTL REAIDQGAVF FIPSVTFDSE AMAQLGQPQS 400
    ATILAYLLEH LPAEPALTVA MGQQLIQQAA KAAGVKKGAT MRTLRAALTG 450
    AVHGPDLMAA WQILHQRGWD EPRLAAALKQ AQTTS 485
    Length:485
    Mass (Da):54,362
    Last modified:March 1, 2003 - v1
    Checksum:iC3547C6415FDDCBA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000039 Genomic DNA. Translation: BAC08058.1.
    RefSeqiNP_681296.1. NC_004113.1.

    Genome annotation databases

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

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000039 Genomic DNA. Translation: BAC08058.1 .
    RefSeqi NP_681296.1. NC_004113.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CFO X-ray 2.45 A/B 2-485 [» ]
    ProteinModelPortali Q8DLI5.
    SMRi Q8DLI5. Positions 2-485.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 197221.tll0506.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAC08058 ; BAC08058 ; BAC08058 .
    GeneIDi 1012165.
    KEGGi tel:tll0506.
    PATRICi 23926260. VBITheElo119873_0533.

    Phylogenomic databases

    eggNOGi COG0008.
    HOGENOMi HOG000252722.
    KOi K01885.
    OMAi DSHEHHA.
    OrthoDBi EOG6DRPF7.

    Miscellaneous databases

    EvolutionaryTracei Q8DLI5.

    Family and domain databases

    Gene3Di 1.10.10.350. 1 hit.
    1.10.1160.10. 1 hit.
    3.40.50.620. 2 hits.
    HAMAPi MF_00022_B. Glu_tRNA_synth_B.
    InterProi IPR008925. 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 ]
    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. 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: October 1, 2014
    This is version 74 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