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Q2SX36

- SYE_BURTA

UniProt

Q2SX36 - SYE_BURTA

Protein

Glutamate--tRNA ligase

Gene

gltX

Organism
Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 59 (01 Oct 2014)
      Sequence version 1 (24 Jan 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

    BioCyciBTHA271848:GJMY-1985-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:BTH_I1984
    OrganismiBurkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301)
    Taxonomic identifieri271848 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group
    ProteomesiUP000001930: Chromosome I

    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 – 469469Glutamate--tRNA ligasePRO_0000237349Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi271848.BTH_I1984.

    Structurei

    Secondary structure

    1
    469
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 94
    Helixi19 – 3416
    Beta strandi38 – 436
    Helixi48 – 503
    Helixi53 – 6513
    Beta strandi71 – 766
    Helixi77 – 793
    Helixi81 – 9313
    Beta strandi96 – 1005
    Beta strandi145 – 1484
    Beta strandi153 – 1608
    Turni161 – 1633
    Beta strandi164 – 1696
    Helixi170 – 1723
    Beta strandi177 – 1793
    Helixi187 – 19711
    Beta strandi202 – 2065
    Helixi207 – 2126
    Helixi213 – 22210
    Beta strandi229 – 2335
    Beta strandi241 – 2433
    Turni246 – 2494
    Helixi253 – 2586
    Helixi263 – 2719
    Beta strandi273 – 2753
    Helixi285 – 2917
    Helixi294 – 2963
    Helixi306 – 31914
    Helixi322 – 33413
    Turni335 – 3373
    Helixi340 – 3456
    Helixi349 – 3568
    Helixi363 – 3708
    Helixi371 – 3733
    Helixi448 – 4547
    Helixi457 – 4659

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4G6ZX-ray2.05A1-469[»]
    ProteinModelPortaliQ2SX36.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi11 – 2111"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.
    OMAiDSHEHHA.
    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.

    Q2SX36-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTRPVRTRFA PSPTGFIHLG NIRSALYPWA FARKMKGTFV LRIEDTDVER    50
    SSQEAVDAIL EGMAWLGLDY DEGPYYQMQR MDRYREVLAQ MQEKGLVYPC 100
    YMSTEELDAL RERQRAAGEK PRYDGTWRPE PGKVLPEPPA GVAPVLRFRN 150
    PLTGTVAWDD AVKGRVEISN EELDDLVVAR PDGTPMYNFC VVVDDLDMGI 200
    THVIRGDDHV NNTPRQINIL RALGGEVPVY AHLPTVLNEQ GEKMSKRHGA 250
    MSVMGYRDAG YLPEAVLNYL ARLGWSHGDA EIFTREQFVE WFDLEHLGKS 300
    PAQYDHNKLN WLNNHYIKEA DDARLAGLAK PFFAALGIDA GAIEQGPDLV 350
    SVMGLMKDRA STVKEIAENS AMFYRAPAPG ADALAQHVTD AVRPALVEFA 400
    AALKTVEWTK EAIAAALKAV LGAHKLKMPQ LAMPVRLLVA GTTHTPSIDA 450
    VLLLFGRDVV VSRIEAALA 469
    Length:469
    Mass (Da):52,046
    Last modified:January 24, 2006 - v1
    Checksum:iEEE0D68248D730E0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000086 Genomic DNA. Translation: ABC37833.1.
    RefSeqiYP_442513.1. NC_007651.1.

    Genome annotation databases

    EnsemblBacteriaiABC37833; ABC37833; BTH_I1984.
    GeneIDi3850087.
    KEGGibte:BTH_I1984.
    PATRICi19307002. VBIBurTha36512_4795.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000086 Genomic DNA. Translation: ABC37833.1 .
    RefSeqi YP_442513.1. NC_007651.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4G6Z X-ray 2.05 A 1-469 [» ]
    ProteinModelPortali Q2SX36.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 271848.BTH_I1984.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABC37833 ; ABC37833 ; BTH_I1984 .
    GeneIDi 3850087.
    KEGGi bte:BTH_I1984.
    PATRICi 19307002. VBIBurTha36512_4795.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci BTHA271848:GJMY-1985-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. "Bacterial genome adaptation to niches: divergence of the potential virulence genes in three Burkholderia species of different survival strategies."
      Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C., DeShazer D.
      BMC Genomics 6:174-174(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: E264 / ATCC 700388 / DSM 13276 / CIP 106301.

    Entry informationi

    Entry nameiSYE_BURTA
    AccessioniPrimary (citable) accession number: Q2SX36
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2006
    Last sequence update: January 24, 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

    3D-structure, Complete proteome

    Documents

    1. Aminoacyl-tRNA synthetases
      List of aminoacyl-tRNA synthetase entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3