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Protein

Glutamyl-Q tRNA(Asp) synthetase

Gene

gluQ

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2-cyclopenten-1-yl) moiety of the queuosine in position 34 of the tRNA(Asp), the wobble position of the QUC anticodon. Does not transfer glutamate to either tRNA(Glu) or tRNA(Gln). The incapacity of the glutamylated tRNA(Asp) to bind elongation factor Tu suggests that it is not involved in ribosomal protein biosynthesis.3 Publications

Cofactori

Zn2+Note: Binds 1 zinc ion per subunit.

Kineticsi

  1. KM=0.15 µM for tRNA(Asp)
  2. KM=3000 µM for glutamate

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei55Glutamate1 Publication1
    Metal bindingi111Zinc1
    Metal bindingi113Zinc1
    Metal bindingi125Zinc1
    Metal bindingi129Zinc1
    Binding sitei182Glutamate1 Publication1
    Binding sitei200Glutamate1 Publication1
    Binding sitei241ATPBy similarity1

    GO - Molecular functioni

    • ATP binding Source: EcoCyc
    • glutamate-tRNA ligase activity Source: GO_Central
    • RNA binding Source: GO_Central
    • zinc ion binding Source: EcoCyc

    GO - Biological processi

    • glutamyl-tRNA aminoacylation Source: GO_Central
    • tRNA wobble base modification Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Aminoacyl-tRNA synthetase, Ligase

    Keywords - Ligandi

    ATP-binding, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    BioCyciEcoCyc:EG11362-MONOMER.
    ECOL316407:JW5892-MONOMER.
    MetaCyc:EG11362-MONOMER.
    BRENDAi6.1.1.B3. 2026.
    SABIO-RKP27305.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamyl-Q tRNA(Asp) synthetase (EC:6.1.1.-)
    Short name:
    Glu-Q-RSs
    Gene namesi
    Name:gluQ
    Synonyms:yadB
    Ordered Locus Names:b0144, JW5892
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11362. gluQ.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00002083001 – 308Glutamyl-Q tRNA(Asp) synthetaseAdd BLAST308

    Proteomic databases

    PaxDbiP27305.
    PRIDEiP27305.

    Interactioni

    Protein-protein interaction databases

    BioGridi4259736. 6 interactors.
    DIPiDIP-11180N.
    MINTiMINT-1218773.
    STRINGi511145.b0144.

    Structurei

    Secondary structure

    1308
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi17 – 20Combined sources4
    Helixi30 – 45Combined sources16
    Beta strandi49 – 54Combined sources6
    Helixi59 – 61Combined sources3
    Helixi66 – 76Combined sources11
    Helixi88 – 90Combined sources3
    Helixi92 – 104Combined sources13
    Beta strandi108 – 111Combined sources4
    Helixi115 – 120Combined sources6
    Turni128 – 132Combined sources5
    Beta strandi140 – 143Combined sources4
    Beta strandi151 – 154Combined sources4
    Turni155 – 157Combined sources3
    Beta strandi158 – 161Combined sources4
    Helixi164 – 168Combined sources5
    Beta strandi172 – 174Combined sources3
    Helixi182 – 192Combined sources11
    Beta strandi197 – 201Combined sources5
    Helixi202 – 204Combined sources3
    Turni205 – 207Combined sources3
    Helixi208 – 218Combined sources11
    Beta strandi224 – 228Combined sources5
    Beta strandi230 – 232Combined sources3
    Beta strandi236 – 240Combined sources5
    Helixi254 – 263Combined sources10
    Helixi272 – 274Combined sources3
    Helixi277 – 286Combined sources10
    Helixi290 – 292Combined sources3
    Beta strandi297 – 299Combined sources3
    Helixi301 – 303Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1NZJX-ray1.50A11-308[»]
    4A91X-ray1.75A11-308[»]
    ProteinModelPortaliP27305.
    SMRiP27305.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP27305.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni19 – 23Glutamate binding5

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Motifi22 – 32"HIGH" regionAdd BLAST11
    Motifi238 – 242"KMSKS" region5

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4106F3G. Bacteria.
    COG0008. LUCA.
    HOGENOMiHOG000252723.
    InParanoidiP27305.
    KOiK01894.
    PhylomeDBiP27305.

    Family and domain databases

    Gene3Di3.40.50.620. 2 hits.
    HAMAPiMF_01428. Glu_Q_tRNA_synth. 1 hit.
    InterProiIPR022380. Glu-Q_TRNA(Asp)_Synthase.
    IPR000924. Glu/Gln-tRNA-synth.
    IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view]
    PfamiPF00749. tRNA-synt_1c. 1 hit.
    [Graphical view]
    PRINTSiPR00987. TRNASYNTHGLU.
    TIGRFAMsiTIGR03838. queuosine_YadB. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P27305-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MLPPYFLFKE MTDTQYIGRF APSPSGELHF GSLIAALGSY LQARARQGRW
    60 70 80 90 100
    LVRIEDIDPP REVPGAAETI LRQLEHYGLH WDGDVLWQSQ RHDAYREALA
    110 120 130 140 150
    WLHEQGLSYY CTCTRARIQS IGGIYDGHCR VLHHGPDNAA VRIRQQHPVT
    160 170 180 190 200
    QFTDQLRGII HADEKLARED FIIHRRDGLF AYNLAVVVDD HFQGVTEIVR
    210 220 230 240 250
    GADLIEPTVR QISLYQLFGW KVPDYIHLPL ALNPQGAKLS KQNHAPALPK
    260 270 280 290 300
    GDPRPVLIAA LQFLGQQAEA HWQDFSVEQI LQSAVKNWRL TAVPESAIVN

    STFSNASC
    Length:308
    Mass (Da):34,868
    Last modified:November 24, 2009 - v6
    Checksum:i69BA4A164AB4363C
    GO

    Sequence cautioni

    The sequence AAA23686 differs from that shown. Reason: Frameshift at several positions.Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00096 Genomic DNA. Translation: AAC73255.3.
    AP009048 Genomic DNA. Translation: BAB96721.2.
    X64595 Genomic DNA. No translation available.
    M34945 Genomic DNA. Translation: AAA23686.1. Sequence problems.
    PIRiH64737.
    RefSeqiNP_414686.3. NC_000913.3.

    Genome annotation databases

    EnsemblBacteriaiAAC73255; AAC73255; b0144.
    BAB96721; BAB96721; BAB96721.
    GeneIDi944846.
    KEGGiecj:JW5892.
    eco:b0144.
    PATRICi32115395. VBIEscCol129921_0149.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00096 Genomic DNA. Translation: AAC73255.3.
    AP009048 Genomic DNA. Translation: BAB96721.2.
    X64595 Genomic DNA. No translation available.
    M34945 Genomic DNA. Translation: AAA23686.1. Sequence problems.
    PIRiH64737.
    RefSeqiNP_414686.3. NC_000913.3.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1NZJX-ray1.50A11-308[»]
    4A91X-ray1.75A11-308[»]
    ProteinModelPortaliP27305.
    SMRiP27305.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4259736. 6 interactors.
    DIPiDIP-11180N.
    MINTiMINT-1218773.
    STRINGi511145.b0144.

    Proteomic databases

    PaxDbiP27305.
    PRIDEiP27305.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC73255; AAC73255; b0144.
    BAB96721; BAB96721; BAB96721.
    GeneIDi944846.
    KEGGiecj:JW5892.
    eco:b0144.
    PATRICi32115395. VBIEscCol129921_0149.

    Organism-specific databases

    EchoBASEiEB1337.
    EcoGeneiEG11362. gluQ.

    Phylogenomic databases

    eggNOGiENOG4106F3G. Bacteria.
    COG0008. LUCA.
    HOGENOMiHOG000252723.
    InParanoidiP27305.
    KOiK01894.
    PhylomeDBiP27305.

    Enzyme and pathway databases

    BioCyciEcoCyc:EG11362-MONOMER.
    ECOL316407:JW5892-MONOMER.
    MetaCyc:EG11362-MONOMER.
    BRENDAi6.1.1.B3. 2026.
    SABIO-RKP27305.

    Miscellaneous databases

    EvolutionaryTraceiP27305.
    PROiP27305.

    Family and domain databases

    Gene3Di3.40.50.620. 2 hits.
    HAMAPiMF_01428. Glu_Q_tRNA_synth. 1 hit.
    InterProiIPR022380. Glu-Q_TRNA(Asp)_Synthase.
    IPR000924. Glu/Gln-tRNA-synth.
    IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view]
    PfamiPF00749. tRNA-synt_1c. 1 hit.
    [Graphical view]
    PRINTSiPR00987. TRNASYNTHGLU.
    TIGRFAMsiTIGR03838. queuosine_YadB. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiGLUQ_ECOLI
    AccessioniPrimary (citable) accession number: P27305
    Secondary accession number(s): P75662
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: November 24, 2009
    Last modified: November 2, 2016
    This is version 146 of the entry and version 6 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.