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B5RLR1

- SYE_BORDL

UniProt

B5RLR1 - SYE_BORDL

Protein

Glutamate--tRNA ligase

Gene

gltX

Organism
Borrelia duttonii (strain Ly)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 43 (01 Oct 2014)
      Sequence version 1 (04 Nov 2008)
      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

    Cofactori

    Binds 1 zinc ion per subunit.UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi121 – 1211ZincUniRule annotation
    Metal bindingi123 – 1231ZincUniRule annotation
    Metal bindingi148 – 1481ZincUniRule annotation
    Metal bindingi150 – 1501ZincUniRule annotation
    Binding sitei269 – 2691ATPUniRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-HAMAP
    2. glutamate-tRNA ligase activity Source: UniProtKB-HAMAP
    3. metal ion binding Source: UniProtKB-KW
    4. 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, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    BioCyciBDUT412419:GJ78-367-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:BDU_367
    OrganismiBorrelia duttonii (strain Ly)
    Taxonomic identifieri412419 [NCBI]
    Taxonomic lineageiBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeBorrelia
    ProteomesiUP000000611: Chromosome

    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 – 506506Glutamate--tRNA ligasePRO_0000367619Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi412419.BDU_367.

    Structurei

    3D structure databases

    ProteinModelPortaliB5RLR1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi24 – 3411"HIGH" regionAdd
    BLAST
    Motifi266 – 2705"KMSKS" region

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0008.
    HOGENOMiHOG000252720.
    KOiK01885.
    OMAiWLPEEMG.
    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.
    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.

    Sequencei

    Sequence statusi: Complete.

    B5RLR1-1 [UniParc]FASTAAdd to Basket

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    MIFQKRTFFI KRGCVLNIRV RYAPSPTGLQ HIGGIRTALF NYFFAKSFNG    50
    KFLLRIEDTD QTRYYKEAEE DLYQSLAWLG IDFDEGPTCG GSYSPYIQSQ 100
    RTEIYRKYAK ELIESGNAYY CYCSPDRLER IRKIQTINKM APGYDRHCRH 150
    LNKDEIKDAL SLGISPVIRF KIPFDGETSF NDILLGKITW ANKDISPDPV 200
    ILKSDGFPTY HLANVVDDHL MEISHVLRAQ EWISSGPLHV LLYNAFRWNP 250
    PIYCHLPMVM GSDGQKLSKR HGATALKQFI DDGYLPEAII NYVTLLGWSY 300
    DGKSEFFTKN ELQKLFSIDK ISKSPAVFDY NKLDFFNSHY IRTKEDHELA 350
    ELLLPFLQKA GYIKKDSNSC DKEKLLLLVP LIKPRIRKLG DAVGMLRFFY 400
    TNISTWNLNE FLGKKKTVRD IYLLLEKIKP VLEGFETRIL SENEQIFYNF 450
    AKENDLKIGE VLLPIRIAVL GSKVSPPLFD SLQLLGKVTV FDRINKAQDF 500
    LKKYEL 506
    Length:506
    Mass (Da):58,556
    Last modified:November 4, 2008 - v1
    Checksum:i4BAB79F89CB51DA7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000976 Genomic DNA. Translation: ACH93319.1.
    RefSeqiYP_002222025.1. NC_011229.1.

    Genome annotation databases

    EnsemblBacteriaiACH93319; ACH93319; BDU_367.
    GeneIDi6918451.
    KEGGibdu:BDU_367.
    PATRICi20562842. VBIBorDut9941_0394.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000976 Genomic DNA. Translation: ACH93319.1 .
    RefSeqi YP_002222025.1. NC_011229.1.

    3D structure databases

    ProteinModelPortali B5RLR1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 412419.BDU_367.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACH93319 ; ACH93319 ; BDU_367 .
    GeneIDi 6918451.
    KEGGi bdu:BDU_367.
    PATRICi 20562842. VBIBorDut9941_0394.

    Phylogenomic databases

    eggNOGi COG0008.
    HOGENOMi HOG000252720.
    KOi K01885.
    OMAi WLPEEMG.
    OrthoDBi EOG6DRPF7.

    Enzyme and pathway databases

    BioCyci BDUT412419:GJ78-367-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.
    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.
    ProtoNeti Search...

    Publicationsi

    1. "The genome of Borrelia recurrentis, the agent of deadly louse-borne relapsing fever, is a degraded subset of tick-borne Borrelia duttonii."
      Lescot M., Audic S., Robert C., Nguyen T.T., Blanc G., Cutler S.J., Wincker P., Couloux A., Claverie J.-M., Raoult D., Drancourt M.
      PLoS Genet. 4:E1000185-E1000185(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Ly.

    Entry informationi

    Entry nameiSYE_BORDL
    AccessioniPrimary (citable) accession number: B5RLR1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 24, 2009
    Last sequence update: November 4, 2008
    Last modified: October 1, 2014
    This is version 43 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