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B2G868

- SYE_LACRJ

UniProt

B2G868 - SYE_LACRJ

Protein

Glutamate--tRNA ligase

Gene

gltX

Organism
Lactobacillus reuteri (strain JCM 1112)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 47 (01 Oct 2014)
      Sequence version 1 (10 Jun 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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei260 – 2601ATPUniRule 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

    BioCyciLREU557433:GHNR-1195-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:LAR_1134
    OrganismiLactobacillus reuteri (strain JCM 1112)
    Taxonomic identifieri557433 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus
    ProteomesiUP000009150: 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 – 501501Glutamate--tRNA ligasePRO_1000090084Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi557433.LAR_1134.

    Structurei

    3D structure databases

    ProteinModelPortaliB2G868.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi11 – 2111"HIGH" regionAdd
    BLAST
    Motifi257 – 2615"KMSKS" region

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0008.
    HOGENOMiHOG000252720.
    KOiK09698.
    OMAiTISPIFH.
    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.

    B2G868-1 [UniParc]FASTAAdd to Basket

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    MDQKVRVRYA PSPTGFLHIG NAQSALFNYL FARHFDGTMV LRIEDTDTKR    50
    NVEDGEASQR ENLHWLGIDW DEGPNKPNPK YAPYRQSERN KEGIYHKYIQ 100
    ELLDKGIAYK DYSTEEELAE MRERQKANNE PPHYDGRWYG KSEEEQKAAE 150
    AKGLKPTIRF HFPKDHDYEW DDIARGHVSF NSDNLGGDFI IEKSDGMPTY 200
    NFAVVVDDHT MDITHVLRGA DHISNTPKQI AIYEALGWEH PTFCHIPLIF 250
    NPKTRKKLSK RDKDTLQFIS EYKKHGYLHE AIFNFIAFLG WSPVGEREIY 300
    SKEELIKVYD PKRMSKAPAY FDQKKLDWMN AQYIKSMSID ELTDRTMELI 350
    KEGETEEAKR LQSIPEEQLT ELLKKTIKVH QRDVNKLLEV IQYAWSYYTV 400
    LDQSFNYDLL KDNEDFANED VLAVLKGLKA KLENGDDDLD YSQAIKEVGK 450
    DTGIKGRGLY FPLNLAFTGS TSAPQIYEIM DIYSRDTDIE LLDRMIKAFE 500
    N 501
    Length:501
    Mass (Da):58,350
    Last modified:June 10, 2008 - v1
    Checksum:i299495BBD03FBE6A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP007281 Genomic DNA. Translation: BAG25650.1.
    RefSeqiYP_001842130.1. NC_010609.1.

    Genome annotation databases

    EnsemblBacteriaiBAG25650; BAG25650; LAR_1134.
    GeneIDi6231269.
    KEGGilrf:LAR_1134.
    PATRICi22259788. VBILacReu111271_1250.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP007281 Genomic DNA. Translation: BAG25650.1 .
    RefSeqi YP_001842130.1. NC_010609.1.

    3D structure databases

    ProteinModelPortali B2G868.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 557433.LAR_1134.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAG25650 ; BAG25650 ; LAR_1134 .
    GeneIDi 6231269.
    KEGGi lrf:LAR_1134.
    PATRICi 22259788. VBILacReu111271_1250.

    Phylogenomic databases

    eggNOGi COG0008.
    HOGENOMi HOG000252720.
    KOi K09698.
    OMAi TISPIFH.
    OrthoDBi EOG6DRPF7.

    Enzyme and pathway databases

    BioCyci LREU557433:GHNR-1195-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. "Comparative genome analysis of Lactobacillus reuteri and Lactobacillus fermentum reveal a genomic island for reuterin and cobalamin production."
      Morita H., Toh H., Fukuda S., Horikawa H., Oshima K., Suzuki T., Murakami M., Hisamatsu S., Kato Y., Takizawa T., Fukuoka H., Yoshimura T., Itoh K., O'Sullivan D.J., McKay L.L., Ohno H., Kikuchi J., Masaoka T., Hattori M.
      DNA Res. 15:151-161(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: JCM 1112.

    Entry informationi

    Entry nameiSYE_LACRJ
    AccessioniPrimary (citable) accession number: B2G868
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 24, 2009
    Last sequence update: June 10, 2008
    Last modified: October 1, 2014
    This is version 47 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