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B2SE01

- SYE_FRATM

UniProt

B2SE01 - SYE_FRATM

Protein

Glutamate--tRNA ligase

Gene

gltX

Organism
Francisella tularensis subsp. mediasiatica (strain FSC147)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 45 (01 Oct 2014)
      Sequence version 1 (01 Jul 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 bindingi97 – 971ZincUniRule annotation
    Metal bindingi99 – 991ZincUniRule annotation
    Metal bindingi124 – 1241ZincUniRule annotation
    Metal bindingi126 – 1261ZincUniRule annotation
    Binding sitei239 – 2391ATPUniRule 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

    BioCyciFTUL441952:GIY0-1539-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:FTM_1545
    OrganismiFrancisella tularensis subsp. mediasiatica (strain FSC147)
    Taxonomic identifieri441952 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella
    ProteomesiUP000001196: 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 – 468468Glutamate--tRNA ligasePRO_1000090076Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi441952.FTM_1545.

    Structurei

    3D structure databases

    ProteinModelPortaliB2SE01.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi8 – 1811"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.

    B2SE01-1 [UniParc]FASTAAdd to Basket

    « Hide

    MITTRFAPSP TGFLHVGGVR TALFSWLYAK NNNGKFILRI EDTDLERSTQ    50
    EAVDAILDGM SWLGLKNDGE IYYQTKRFDR YKEVIQELIA DGKAYYCSCS 100
    KERLEELREY QQANNLKTGY DGKCRDANYI PQQGESYVVR FKNPQDGVVS 150
    WDDAVKGRIS ISNHELDDMI IQRADGSPTY NFCVVVDDID MAITHIIRGD 200
    DHVNNTPKQI NIYKALNANV PVFAHVPMIL GPDGAKLSKR HGAVNVMQYR 250
    EDGYLPQAIL NYLVRLGWSH GDQEIFSIEE MIKAFNLEHI NASPSRFDFE 300
    KLKWLNKHYI KESKFDDIQT EVEYHFAKTG LDISNGPDLK ELVAVMAEKV 350
    DTLVELAEKS SYFYSDDISY DENAVKKHIK ASTGEIFVKL LENFEALDAQ 400
    QWQDPDVLHN IVSTTAEQCQ VGMGKVGMPL RVAITGSGQS PDIGITLKLL 450
    GKNKVVARLT KALEELCK 468
    Length:468
    Mass (Da):52,939
    Last modified:July 1, 2008 - v1
    Checksum:iF5D3A1C70C11C12E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000915 Genomic DNA. Translation: ACD31365.1.
    RefSeqiYP_001892144.1. NC_010677.1.

    Genome annotation databases

    EnsemblBacteriaiACD31365; ACD31365; FTM_1545.
    GeneIDi6291039.
    KEGGiftm:FTM_1545.
    PATRICi17958079. VBIFraTul67519_1915.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000915 Genomic DNA. Translation: ACD31365.1 .
    RefSeqi YP_001892144.1. NC_010677.1.

    3D structure databases

    ProteinModelPortali B2SE01.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 441952.FTM_1545.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACD31365 ; ACD31365 ; FTM_1545 .
    GeneIDi 6291039.
    KEGGi ftm:FTM_1545.
    PATRICi 17958079. VBIFraTul67519_1915.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci FTUL441952:GIY0-1539-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. "Molecular evolutionary consequences of niche restriction in Francisella tularensis, a facultative intracellular pathogen."
      Larsson P., Elfsmark D., Svensson K., Wikstroem P., Forsman M., Brettin T., Keim P., Johansson A.
      PLoS Pathog. 5:E1000472-E1000472(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: FSC147.

    Entry informationi

    Entry nameiSYE_FRATM
    AccessioniPrimary (citable) accession number: B2SE01
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 24, 2009
    Last sequence update: July 1, 2008
    Last modified: October 1, 2014
    This is version 45 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