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Q6FZP6

- SYE1_BARQU

UniProt

Q6FZP6 - SYE1_BARQU

Protein

Glutamate--tRNA ligase 1

Gene

gltX1

Organism
Bartonella quintana (strain Toulouse) (Rochalimaea quintana)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 71 (01 Oct 2014)
      Sequence version 1 (19 Jul 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 sitei252 – 2521ATPUniRule 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

    BioCyciBQUI283165:GHZA-676-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate--tRNA ligase 1UniRule annotation (EC:6.1.1.17UniRule annotation)
    Alternative name(s):
    Glutamyl-tRNA synthetase 1UniRule annotation
    Short name:
    GluRS 1UniRule annotation
    Gene namesi
    Name:gltX1UniRule annotation
    Ordered Locus Names:BQ06770
    OrganismiBartonella quintana (strain Toulouse) (Rochalimaea quintana)
    Taxonomic identifieri283165 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella
    ProteomesiUP000000597: 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 – 459459Glutamate--tRNA ligase 1PRO_0000119512Add
    BLAST

    Proteomic databases

    PRIDEiQ6FZP6.

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi283165.BQ06770.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6FZP6.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi8 – 1811"HIGH" regionAdd
    BLAST
    Motifi249 – 2535"KMSKS" region

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0008.
    HOGENOMiHOG000252721.
    KOiK01885.
    OMAiRIALFNW.
    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.

    Q6FZP6-1 [UniParc]FASTAAdd to Basket

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    MIKVRFAPSP TGYIHIGNIR IALFNWLYAQ AHNGAFILRY DDTDVERSKQ    50
    EYIDAIAADL EWLDIQPDEI YYQSKRFNRY DEVAEMLKQR GLLYPCYETA 100
    EELDRRRKIQ LSRKLPPVYD RAALKLTPEE KEEFESQGRK PHWRFLLPNF 150
    ENNPLQTKRT EVCWNDVVKG KQTIDLASLS DPVLIREGGS YLYTLPSVVD 200
    DIDMAITHII RGDDHITNTG VQIALFEALN AQLPIFGHIN LLTTVLGKGL 250
    SKRDNDLSIH SLRAEGFESI AIQCFAVLIG TSQNVHPYPH QAALLKHFNL 300
    QDTSRSVTKF DIADLFALNS HLVHDLTYEE VKTRLKNLSI DGEKAECFWN 350
    AIRSNIDKVN DAVLWWKMIH DEQSFDPVAL EDRSFVRQSL NFLPEGPLND 400
    ESWKVWTTTL KEKTGRRGKA LFMPLRQALT GMDHGPEMGK LLQLLGREKV 450
    IDRLTIQGE 459
    Length:459
    Mass (Da):52,789
    Last modified:July 19, 2004 - v1
    Checksum:iB2E0734CD0F05C2E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX897700 Genomic DNA. Translation: CAF26166.1.
    RefSeqiWP_011179421.1. NC_005955.1.
    YP_032314.1. NC_005955.1.

    Genome annotation databases

    EnsemblBacteriaiCAF26166; CAF26166; BQ06770.
    GeneIDi2867044.
    KEGGibqu:BQ06770.
    PATRICi31952651. VBIBarQui58630_0751.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX897700 Genomic DNA. Translation: CAF26166.1 .
    RefSeqi WP_011179421.1. NC_005955.1.
    YP_032314.1. NC_005955.1.

    3D structure databases

    ProteinModelPortali Q6FZP6.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 283165.BQ06770.

    Proteomic databases

    PRIDEi Q6FZP6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAF26166 ; CAF26166 ; BQ06770 .
    GeneIDi 2867044.
    KEGGi bqu:BQ06770.
    PATRICi 31952651. VBIBarQui58630_0751.

    Phylogenomic databases

    eggNOGi COG0008.
    HOGENOMi HOG000252721.
    KOi K01885.
    OMAi RIALFNW.
    OrthoDBi EOG6DRPF7.

    Enzyme and pathway databases

    BioCyci BQUI283165:GHZA-676-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Toulouse.

    Entry informationi

    Entry nameiSYE1_BARQU
    AccessioniPrimary (citable) accession number: Q6FZP6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: July 19, 2004
    Last modified: October 1, 2014
    This is version 71 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