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Q5WVE0

- SYE_LEGPL

UniProt

Q5WVE0 - SYE_LEGPL

Protein

Glutamate--tRNA ligase

Gene

gltX

Organism
Legionella pneumophila (strain Lens)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 68 (01 Oct 2014)
      Sequence version 1 (23 Nov 2004)
      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).UniRule annotation

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei239 – 2391ATPUniRule annotation

    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

    BioCyciLPNE297245:GJD4-2021-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate--tRNA ligaseUniRule annotation (EC:6.1.1.17UniRule annotation)
    Alternative name(s):
    Glutamyl-tRNA synthetaseUniRule annotation
    Short name:
    GluRSUniRule annotation
    Gene namesi
    Name:gltXUniRule annotation
    Ordered Locus Names:lpl1875
    OrganismiLegionella pneumophila (strain Lens)
    Taxonomic identifieri297245 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella
    ProteomesiUP000002517: Chromosome

    Organism-specific databases

    LegioListilpl1875.

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 470470Glutamate--tRNA ligasePRO_0000119588Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi297245.lpl1875.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5WVE0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi9 – 1911"HIGH" regionAdd
    BLAST
    Motifi236 – 2405"KMSKS" region

    Sequence similaritiesi

    Belongs to the class-I aminoacyl-tRNA synthetase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0008.
    HOGENOMiHOG000252722.
    KOiK01885.
    OMAiWINGYYL.
    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.

    Q5WVE0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTVRTRFAPS PTGFLHVGGV RTALFSWLYA KHHNGQFILR IEDTDRERST    50
    QESVQAILDG MAWLGLNFDE GPYYQTERYA RYQQVAQQLL EEGKAYRCQC 100
    SKERLEALRE AQLAAKEKPR YDGHCRNQSL PDSGIPYVIR FRNPDGGIVS 150
    FHDEVYGDIH VDNSELDDLI LVRSDGHPTY NFAVVIDDWD MKITHVIRGD 200
    DHINNTPRQI NLFKALDAPV PVFAHLPMIL GEDGKRLSKR HGAVSVLQFK 250
    ELGVLPHALL NYLVRLGWSH GDQEIFSVQE MITSFDLKNV SRGVSSFNYD 300
    KLYWLNQHYQ KSDSPESVAN ALQWHFEQAG IDLNQGPDLK DLVAVQAERC 350
    KSLAEMCQIS QYFYTDTIEY NEDAVKKHLR PVVLEPLMVL HERLKALDEW 400
    KNDKIQECIN DVSLQFDLNL GKIAQPLRVA VTGSGTSPSI DMTLALLGKN 450
    KSIKRLEDAL EKIRARASVV 470
    Length:470
    Mass (Da):53,548
    Last modified:November 23, 2004 - v1
    Checksum:iEACE7D81A3A3DBBC
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR628337 Genomic DNA. Translation: CAH16114.1.
    RefSeqiWP_011215873.1. NC_006369.1.
    YP_127213.1. NC_006369.1.

    Genome annotation databases

    EnsemblBacteriaiCAH16114; CAH16114; lpl1875.
    GeneIDi3113956.
    KEGGilpf:lpl1875.
    PATRICi22317493. VBILegPne33733_2064.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR628337 Genomic DNA. Translation: CAH16114.1 .
    RefSeqi WP_011215873.1. NC_006369.1.
    YP_127213.1. NC_006369.1.

    3D structure databases

    ProteinModelPortali Q5WVE0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 297245.lpl1875.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAH16114 ; CAH16114 ; lpl1875 .
    GeneIDi 3113956.
    KEGGi lpf:lpl1875.
    PATRICi 22317493. VBILegPne33733_2064.

    Organism-specific databases

    LegioListi lpl1875.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci LPNE297245:GJD4-2021-MONOMER.

    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. "Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity."
      Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L., Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J., Glaser P., Buchrieser C.
      Nat. Genet. 36:1165-1173(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Lens.

    Entry informationi

    Entry nameiSYE_LEGPL
    AccessioniPrimary (citable) accession number: Q5WVE0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: November 23, 2004
    Last modified: October 1, 2014
    This is version 68 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome

    Documents

    1. Aminoacyl-tRNA synthetases
      List of aminoacyl-tRNA synthetase entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3