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P00962

- SYQ_ECOLI

UniProt

P00962 - SYQ_ECOLI

Protein

Glutamine--tRNA ligase

Gene

glnS

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 159 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-glutaminyl-tRNA(Gln).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei271 – 2711ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-HAMAP
    2. glutamine-tRNA ligase activity Source: EcoCyc

    GO - Biological processi

    1. glutaminyl-tRNA aminoacylation Source: EcoCyc
    2. 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

    BioCyciEcoCyc:GLNS-MONOMER.
    ECOL316407:JW0666-MONOMER.
    MetaCyc:GLNS-MONOMER.
    BRENDAi6.1.1.18. 2026.
    SABIO-RKP00962.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamine--tRNA ligase (EC:6.1.1.18)
    Alternative name(s):
    Glutaminyl-tRNA synthetase
    Short name:
    GlnRS
    Gene namesi
    Name:glnS
    Ordered Locus Names:b0680, JW0666
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10390. glnS.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 554553Glutamine--tRNA ligasePRO_0000195833Add
    BLAST

    Proteomic databases

    PaxDbiP00962.
    PRIDEiP00962.

    2D gel databases

    SWISS-2DPAGEP00962.

    Expressioni

    Gene expression databases

    GenevestigatoriP00962.

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    DIPiDIP-9787N.
    IntActiP00962. 5 interactions.
    MINTiMINT-1227909.
    STRINGi511145.b0680.

    Structurei

    Secondary structure

    1
    554
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi11 – 2111
    Beta strandi29 – 324
    Beta strandi36 – 383
    Helixi42 – 5716
    Beta strandi61 – 666
    Helixi71 – 733
    Helixi76 – 8813
    Beta strandi94 – 963
    Helixi100 – 1034
    Helixi104 – 11613
    Beta strandi119 – 1235
    Helixi127 – 1348
    Beta strandi137 – 1393
    Turni145 – 1484
    Helixi151 – 16212
    Beta strandi172 – 1754
    Helixi184 – 1863
    Beta strandi190 – 1945
    Turni200 – 2023
    Beta strandi207 – 2104
    Helixi212 – 22211
    Beta strandi226 – 2316
    Helixi232 – 2343
    Turni235 – 2373
    Helixi238 – 2469
    Beta strandi255 – 2595
    Beta strandi264 – 2674
    Helixi271 – 2799
    Beta strandi282 – 2843
    Beta strandi291 – 2933
    Helixi294 – 3007
    Helixi304 – 31411
    Helixi325 – 33915
    Beta strandi345 – 35410
    Beta strandi362 – 3687
    Helixi373 – 3753
    Beta strandi377 – 3826
    Beta strandi384 – 3896
    Turni390 – 3923
    Beta strandi393 – 3964
    Beta strandi403 – 4053
    Beta strandi408 – 4125
    Beta strandi417 – 4248
    Beta strandi427 – 4293
    Beta strandi433 – 4364
    Beta strandi460 – 4623
    Beta strandi466 – 4738
    Beta strandi476 – 4805
    Helixi482 – 4843
    Beta strandi485 – 4873
    Helixi488 – 4914
    Beta strandi496 – 5049
    Helixi506 – 5105
    Beta strandi516 – 5194
    Turni520 – 5223
    Beta strandi523 – 5275
    Turni529 – 5313
    Beta strandi534 – 5363
    Beta strandi538 – 5447

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EUQX-ray3.10A1-548[»]
    1EUYX-ray2.60A1-548[»]
    1EXDX-ray2.70A1-548[»]
    1GSGX-ray2.80P2-554[»]
    1GTRX-ray2.50A2-554[»]
    1GTSX-ray2.80A2-554[»]
    1NYLX-ray2.60A9-547[»]
    1O0BX-ray2.70A2-554[»]
    1O0CX-ray2.70A2-554[»]
    1QRSX-ray2.60A2-554[»]
    1QRTX-ray2.70A2-554[»]
    1QRUX-ray3.00A2-554[»]
    1QTQX-ray2.25A2-554[»]
    1ZJWX-ray2.50A2-554[»]
    2RD2X-ray2.60A1-548[»]
    2RE8X-ray2.60A1-548[»]
    4JXXX-ray2.30A2-554[»]
    4JXZX-ray2.40A2-554[»]
    4JYZX-ray2.50A2-554[»]
    ProteinModelPortaliP00962.
    SMRiP00962. Positions 8-549.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00962.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi34 – 4411"HIGH" regionAdd
    BLAST
    Motifi268 – 2725"KMSKS" region

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0008.
    HOGENOMiHOG000259232.
    KOiK01886.
    OMAiSREIYID.
    OrthoDBiEOG6DRPF7.
    PhylomeDBiP00962.

    Family and domain databases

    Gene3Di1.10.1160.10. 1 hit.
    2.40.240.10. 2 hits.
    3.40.50.620. 2 hits.
    HAMAPiMF_00126. Gln_tRNA_synth.
    InterProiIPR001412. aa-tRNA-synth_I_CS.
    IPR004514. Gln-tRNA-synth.
    IPR022861. Gln_tRNA_ligase_bac.
    IPR000924. Glu/Gln-tRNA-synth.
    IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
    IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
    IPR020059. Glu/Gln-tRNA-synth_Ib_codon-bd.
    IPR020056. Rbsml_L25/Gln-tRNA_synth_b-brl.
    IPR011035. Ribosomal_L25/Gln-tRNA_synth.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view]
    PANTHERiPTHR10119. PTHR10119. 1 hit.
    PfamiPF00749. tRNA-synt_1c. 1 hit.
    PF03950. tRNA-synt_1c_C. 1 hit.
    [Graphical view]
    PRINTSiPR00987. TRNASYNTHGLU.
    SUPFAMiSSF50715. SSF50715. 1 hit.
    TIGRFAMsiTIGR00440. glnS. 1 hit.
    PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P00962-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSEAEARPTN FIRQIIDEDL ASGKHTTVHT RFPPEPNGYL HIGHAKSICL    50
    NFGIAQDYKG QCNLRFDDTN PVKEDIEYVE SIKNDVEWLG FHWSGNVRYS 100
    SDYFDQLHAY AIELINKGLA YVDELTPEQI REYRGTLTQP GKNSPYRDRS 150
    VEENLALFEK MRAGGFEEGK ACLRAKIDMA SPFIVMRDPV LYRIKFAEHH 200
    QTGNKWCIYP MYDFTHCISD ALEGITHSLC TLEFQDNRRL YDWVLDNITI 250
    PVHPRQYEFS RLNLEYTVMS KRKLNLLVTD KHVEGWDDPR MPTISGLRRR 300
    GYTAASIREF CKRIGVTKQD NTIEMASLES CIREDLNENA PRAMAVIDPV 350
    KLVIENYQGE GEMVTMPNHP NKPEMGSRQV PFSGEIWIDR ADFREEANKQ 400
    YKRLVLGKEV RLRNAYVIKA ERVEKDAEGN ITTIFCTYDA DTLSKDPADG 450
    RKVKGVIHWV SAAHALPVEI RLYDRLFSVP NPGAADDFLS VINPESLVIK 500
    QGFAEPSLKD AVAGKAFQFE REGYFCLDSR HSTAEKPVFN RTVGLRDTWA 550
    KVGE 554
    Length:554
    Mass (Da):63,478
    Last modified:January 23, 2007 - v3
    Checksum:iE720164EF990F335
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti549 – 5546WAKVGE → GRK(PubMed:6288695)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V01575 Genomic DNA. Translation: CAA24894.1.
    U00096 Genomic DNA. Translation: AAC73774.1.
    AP009048 Genomic DNA. Translation: BAA35328.1.
    M16470, M16368 Genomic DNA. Translation: AAA69006.1.
    PIRiG64802. SYECQT.
    I41235.
    RefSeqiNP_415206.1. NC_000913.3.
    YP_488960.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73774; AAC73774; b0680.
    BAA35328; BAA35328; BAA35328.
    GeneIDi12932213.
    945310.
    KEGGiecj:Y75_p0659.
    eco:b0680.
    PATRICi32116549. VBIEscCol129921_0707.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V01575 Genomic DNA. Translation: CAA24894.1 .
    U00096 Genomic DNA. Translation: AAC73774.1 .
    AP009048 Genomic DNA. Translation: BAA35328.1 .
    M16470 , M16368 Genomic DNA. Translation: AAA69006.1 .
    PIRi G64802. SYECQT.
    I41235.
    RefSeqi NP_415206.1. NC_000913.3.
    YP_488960.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EUQ X-ray 3.10 A 1-548 [» ]
    1EUY X-ray 2.60 A 1-548 [» ]
    1EXD X-ray 2.70 A 1-548 [» ]
    1GSG X-ray 2.80 P 2-554 [» ]
    1GTR X-ray 2.50 A 2-554 [» ]
    1GTS X-ray 2.80 A 2-554 [» ]
    1NYL X-ray 2.60 A 9-547 [» ]
    1O0B X-ray 2.70 A 2-554 [» ]
    1O0C X-ray 2.70 A 2-554 [» ]
    1QRS X-ray 2.60 A 2-554 [» ]
    1QRT X-ray 2.70 A 2-554 [» ]
    1QRU X-ray 3.00 A 2-554 [» ]
    1QTQ X-ray 2.25 A 2-554 [» ]
    1ZJW X-ray 2.50 A 2-554 [» ]
    2RD2 X-ray 2.60 A 1-548 [» ]
    2RE8 X-ray 2.60 A 1-548 [» ]
    4JXX X-ray 2.30 A 2-554 [» ]
    4JXZ X-ray 2.40 A 2-554 [» ]
    4JYZ X-ray 2.50 A 2-554 [» ]
    ProteinModelPortali P00962.
    SMRi P00962. Positions 8-549.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-9787N.
    IntActi P00962. 5 interactions.
    MINTi MINT-1227909.
    STRINGi 511145.b0680.

    Chemistry

    BindingDBi P00962.

    2D gel databases

    SWISS-2DPAGE P00962.

    Proteomic databases

    PaxDbi P00962.
    PRIDEi P00962.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC73774 ; AAC73774 ; b0680 .
    BAA35328 ; BAA35328 ; BAA35328 .
    GeneIDi 12932213.
    945310.
    KEGGi ecj:Y75_p0659.
    eco:b0680.
    PATRICi 32116549. VBIEscCol129921_0707.

    Organism-specific databases

    EchoBASEi EB0385.
    EcoGenei EG10390. glnS.

    Phylogenomic databases

    eggNOGi COG0008.
    HOGENOMi HOG000259232.
    KOi K01886.
    OMAi SREIYID.
    OrthoDBi EOG6DRPF7.
    PhylomeDBi P00962.

    Enzyme and pathway databases

    BioCyci EcoCyc:GLNS-MONOMER.
    ECOL316407:JW0666-MONOMER.
    MetaCyc:GLNS-MONOMER.
    BRENDAi 6.1.1.18. 2026.
    SABIO-RK P00962.

    Miscellaneous databases

    EvolutionaryTracei P00962.
    PROi P00962.

    Gene expression databases

    Genevestigatori P00962.

    Family and domain databases

    Gene3Di 1.10.1160.10. 1 hit.
    2.40.240.10. 2 hits.
    3.40.50.620. 2 hits.
    HAMAPi MF_00126. Gln_tRNA_synth.
    InterProi IPR001412. aa-tRNA-synth_I_CS.
    IPR004514. Gln-tRNA-synth.
    IPR022861. Gln_tRNA_ligase_bac.
    IPR000924. Glu/Gln-tRNA-synth.
    IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
    IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
    IPR020059. Glu/Gln-tRNA-synth_Ib_codon-bd.
    IPR020056. Rbsml_L25/Gln-tRNA_synth_b-brl.
    IPR011035. Ribosomal_L25/Gln-tRNA_synth.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view ]
    PANTHERi PTHR10119. PTHR10119. 1 hit.
    Pfami PF00749. tRNA-synt_1c. 1 hit.
    PF03950. tRNA-synt_1c_C. 1 hit.
    [Graphical view ]
    PRINTSi PR00987. TRNASYNTHGLU.
    SUPFAMi SSF50715. SSF50715. 1 hit.
    TIGRFAMsi TIGR00440. glnS. 1 hit.
    PROSITEi PS00178. AA_TRNA_LIGASE_I. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Escherichia coli glutaminyl-tRNA synthetase: a single amino acid replacement relaxes rRNA specificity."
      Uemura H., Conley J., Yamao F., Rogers J., Soell D.G.
      Protein Seq. Data Anal. 1:479-485(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Escherichia coli glutaminyl-tRNA synthetase. I. Isolation and DNA sequence of the glnS gene."
      Yamao F., Inokuchi H., Cheung A., Ozeki H., Soell D.G.
      J. Biol. Chem. 257:11639-11643(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    3. "Misaminoacylation by glutaminyl-tRNA synthetase: relaxed specificity in wild-type and mutant enzymes."
      Hoben P., Uemura H., Yamao F., Cheung A., Swanson R., Sumner-Smith M., Soell D.
      Fed. Proc. 43:2972-2976(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    6. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    7. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
      Link A.J., Robison K., Church G.M.
      Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-13.
      Strain: K12 / EMG2.
    8. "Escherichia coli glutaminyl-tRNA synthetase. II. Characterization of the glnS gene product."
      Hoben P., Royal N., Cheung A., Yamao F., Biemann K., Soell D.
      J. Biol. Chem. 257:11644-11650(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-6, CHARACTERIZATION.
      Strain: K12.
    9. "Escherichia coli proteome analysis using the gene-protein database."
      VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
      Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY 2D-GEL.
    10. "Structure of E. coli glutaminyl-tRNA synthetase complexed with tRNA(Gln) and ATP at 2.8-A resolution."
      Rould M.A., Perona J.J., Soell D., Steitz T.A.
      Science 246:1135-1142(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
    11. "Structural basis of anticodon loop recognition by glutaminyl-tRNA synthetase."
      Rould M.A., Perona J.J., Steitz T.A.
      Nature 352:213-218(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    12. "How glutaminyl-tRNA synthetase selects glutamine."
      Rath V.L., Silvian L.F., Beijer B., Sproat B.S., Steitz T.A.
      Structure 6:439-449(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
    13. "Influence of transfer RNA tertiary structure on aminoacylation efficiency by glutaminyl and cysteinyl-tRNA synthetases."
      Sherlin L.D., Bullock T.L., Newberry K.J., Lipman R.S., Hou Y.M., Beijer B., Sproat B.S., Perona J.J.
      J. Mol. Biol. 299:431-446(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).

    Entry informationi

    Entry nameiSYQ_ECOLI
    AccessioniPrimary (citable) accession number: P00962
    Secondary accession number(s): Q59403
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 159 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3