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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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei55 – 551Glutamate1 Publication
    Metal bindingi111 – 1111Zinc
    Metal bindingi113 – 1131Zinc
    Metal bindingi125 – 1251Zinc
    Metal bindingi129 – 1291Zinc
    Binding sitei182 – 1821Glutamate1 Publication
    Binding sitei200 – 2001Glutamate1 Publication
    Binding sitei241 – 2411ATPBy similarity

    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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    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)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 308308Glutamyl-Q tRNA(Asp) synthetasePRO_0000208300Add
    BLAST

    Proteomic databases

    PaxDbiP27305.

    Interactioni

    Protein-protein interaction databases

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

    Structurei

    Secondary structure

    1
    308
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi17 – 204Combined sources
    Helixi30 – 4516Combined sources
    Beta strandi49 – 546Combined sources
    Helixi59 – 613Combined sources
    Helixi66 – 7611Combined sources
    Helixi88 – 903Combined sources
    Helixi92 – 10413Combined sources
    Beta strandi108 – 1114Combined sources
    Helixi115 – 1206Combined sources
    Turni128 – 1325Combined sources
    Beta strandi140 – 1434Combined sources
    Beta strandi151 – 1544Combined sources
    Turni155 – 1573Combined sources
    Beta strandi158 – 1614Combined sources
    Helixi164 – 1685Combined sources
    Beta strandi172 – 1743Combined sources
    Helixi182 – 19211Combined sources
    Beta strandi197 – 2015Combined sources
    Helixi202 – 2043Combined sources
    Turni205 – 2073Combined sources
    Helixi208 – 21811Combined sources
    Beta strandi224 – 2285Combined sources
    Beta strandi230 – 2323Combined sources
    Beta strandi236 – 2405Combined sources
    Helixi254 – 26310Combined sources
    Helixi272 – 2743Combined sources
    Helixi277 – 28610Combined sources
    Helixi290 – 2923Combined sources
    Beta strandi297 – 2993Combined sources
    Helixi301 – 3033Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NZJX-ray1.50A11-308[»]
    4A91X-ray1.75A11-308[»]
    ProteinModelPortaliP27305.
    SMRiP27305. Positions 13-304.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP27305.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni19 – 235Glutamate binding

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi22 – 3211"HIGH" regionAdd
    BLAST
    Motifi238 – 2425"KMSKS" region

    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
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NZJX-ray1.50A11-308[»]
    4A91X-ray1.75A11-308[»]
    ProteinModelPortaliP27305.
    SMRiP27305. Positions 13-304.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

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

    Proteomic databases

    PaxDbiP27305.

    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: September 7, 2016
    This is version 144 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.