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Q2JKY3

- SYE_SYNJB

UniProt

Q2JKY3 - SYE_SYNJB

Protein

Glutamate--tRNA ligase

Gene

gltX

Organism
Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium Yellowstone B-Prime)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 59 (01 Oct 2014)
      Sequence version 1 (07 Mar 2006)
      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 sitei246 – 2461ATPUniRule 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

    BioCyciSSP321332:GH1B-1680-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:CYB_1680
    OrganismiSynechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium Yellowstone B-Prime)
    Taxonomic identifieri321332 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus
    ProteomesiUP000001938: 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 – 479479Glutamate--tRNA ligasePRO_0000237411Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi321332.CYB_1680.

    Structurei

    3D structure databases

    ProteinModelPortaliQ2JKY3.
    SMRiQ2JKY3. Positions 2-474.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi9 – 1911"HIGH" regionAdd
    BLAST
    Motifi243 – 2475"KMSKS" region

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0008.
    HOGENOMiHOG000252722.
    KOiK01885.
    OMAiDIDMQIS.
    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.

    Q2JKY3-1 [UniParc]FASTAAdd to Basket

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    MSVCVRIAPS PTGNLHIGTA RTAVFNWLYA RRHGGRFILR IEDTDRDRSL    50
    PRYTRNILAG LAWLGLDWDE GPVYQSKRIE RYQAVVQQLL DRGLAYRCYV 100
    SEAELEEMRA AQKAAGKAPR YDNRHRFLTE AQRRAYEAEG RQPVIRFKIE 150
    EPLEVSWVDL IRGPITWNTQ DLGGDMVIAR ADGCPLYNLA VVVDDIDMGI 200
    THVIRGEDHI GNTPKQILLY RALGHEPPQF AHSPLILNPE GKKLSKRDGA 250
    TSVAEFQQLG FLPEALKNYL ALLSWSPPDG EELFSLEKAA ALFDFDRVNR 300
    AAARFDWDKL NWINSQYIKR LSPPELVERL TPFWQAAGFD LSEVPDPTWL 350
    EDVARLIADG IDRLAEAPPL SRFLFQEPLS YTLPALEQLR LPGVAEAMAA 400
    MATTLAAAEL PQVSADSLKP LVDQVAKGQN MKKGLLMKSL RAALTGDLQG 450
    PDLLESFALL QRRGWALGRL EAVQKLVPC 479
    Length:479
    Mass (Da):53,767
    Last modified:March 7, 2006 - v1
    Checksum:i6291942B0C9A6D7B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000240 Genomic DNA. Translation: ABD02639.1.
    RefSeqiWP_011433283.1. NC_007776.1.
    YP_477902.1. NC_007776.1.

    Genome annotation databases

    EnsemblBacteriaiABD02639; ABD02639; CYB_1680.
    GeneIDi3901895.
    KEGGicyb:CYB_1680.
    PATRICi23805688. VBISynSp29577_1686.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000240 Genomic DNA. Translation: ABD02639.1 .
    RefSeqi WP_011433283.1. NC_007776.1.
    YP_477902.1. NC_007776.1.

    3D structure databases

    ProteinModelPortali Q2JKY3.
    SMRi Q2JKY3. Positions 2-474.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 321332.CYB_1680.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABD02639 ; ABD02639 ; CYB_1680 .
    GeneIDi 3901895.
    KEGGi cyb:CYB_1680.
    PATRICi 23805688. VBISynSp29577_1686.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci SSP321332:GH1B-1680-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. "Population level functional diversity in a microbial community revealed by comparative genomic and metagenomic analyses."
      Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N., Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.
      ISME J. 1:703-713(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: JA-2-3B'a(2-13).

    Entry informationi

    Entry nameiSYE_SYNJB
    AccessioniPrimary (citable) accession number: Q2JKY3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2006
    Last sequence update: March 7, 2006
    Last modified: October 1, 2014
    This is version 59 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, 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