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Q8FPU9

- SYE_COREF

UniProt

Q8FPU9 - SYE_COREF

Protein

Glutamate--tRNA ligase

Gene

gltX

Organism
Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 2 (30 Apr 2003)
      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 sitei257 – 2571ATPUniRule 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

    BioCyciCEFF196164:GJW8-1409-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:CE1389
    OrganismiCorynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395)
    Taxonomic identifieri196164 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium
    ProteomesiUP000001409: 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 – 493493Glutamate--tRNA ligasePRO_0000119548Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi196164.CE1389.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8FPU9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi10 – 2011"HIGH" regionAdd
    BLAST
    Motifi254 – 2585"KMSKS" region

    Sequence similaritiesi

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

    Phylogenomic databases

    HOGENOMiHOG000252720.
    KOiK01885.
    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.

    Q8FPU9-1 [UniParc]FASTAAdd to Basket

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    MTDVRVRFCP SPTGTPHVGL VRTALFNWAY ARHTGGKLIF RIEDTDAARD    50
    SEESYAALLD AMNWLGLNWD EGVEVGGPHE PYRQSQRSDI YQDVLKKLID 100
    AGEVYPAYST AEEVEERHRA AGRDPKLGYD NYDRTLTEDE ITAFEAEGRK 150
    PVWRLRMPEQ DWKWNDLVRG EVEFKSFTQP DFVVARSNGQ PLYTLVNPVD 200
    DALMEITHVL RGEDLLPSTP RQIALYEALK RIGVAKQTPV FGHLPFVMGE 250
    GNKKLSKRDP QSDLFQHRTN GIIPEGMLNY LGLLGWSLSA DQDIFTVEEF 300
    VANFDIADVL GNPARFDQKK LEAINADHIR LLPAGEFEER LRAHLSEFTD 350
    FPEDYPAEKF SFAAELVQTR IKTLAEGYDL LKFLVTADED LVLDEKAAKK 400
    NLKEAAIEPL DAGINALEAV AEWTTPNIEA ALTRALIEEL GLKPRVAYGA 450
    LRVAISGAAV SPPLFESMEL LGRESTLTRL RAARAATPYQ AAE 493
    Length:493
    Mass (Da):55,275
    Last modified:April 30, 2003 - v2
    Checksum:i760271536159CB99
    GO

    Sequence cautioni

    The sequence BAC18199.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000035 Genomic DNA. Translation: BAC18199.1. Different initiation.
    RefSeqiNP_737999.1. NC_004369.1.

    Genome annotation databases

    EnsemblBacteriaiBAC18199; BAC18199; BAC18199.
    GeneIDi1033769.
    KEGGicef:CE1389.
    PATRICi21488910. VBICorEff9312_1388.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000035 Genomic DNA. Translation: BAC18199.1 . Different initiation.
    RefSeqi NP_737999.1. NC_004369.1.

    3D structure databases

    ProteinModelPortali Q8FPU9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 196164.CE1389.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAC18199 ; BAC18199 ; BAC18199 .
    GeneIDi 1033769.
    KEGGi cef:CE1389.
    PATRICi 21488910. VBICorEff9312_1388.

    Phylogenomic databases

    HOGENOMi HOG000252720.
    KOi K01885.
    OrthoDBi EOG6DRPF7.

    Enzyme and pathway databases

    BioCyci CEFF196164:GJW8-1409-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. "Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens."
      Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.
      Genome Res. 13:1572-1579(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395.

    Entry informationi

    Entry nameiSYE_COREF
    AccessioniPrimary (citable) accession number: Q8FPU9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 25, 2003
    Last sequence update: April 30, 2003
    Last modified: October 1, 2014
    This is version 77 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference 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