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P00962 - SYQ_ECOLI

UniProt

P00962 - SYQ_ECOLI

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Protein

Glutamine--tRNA ligase

Gene

glnS

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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
Complete GO annotation...

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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10390. glnS.

Subcellular locationi

Cytoplasm

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

Belongs to the class-I aminoacyl-tRNA synthetase family.Curated

Phylogenomic databases

eggNOGiCOG0008.
HOGENOMiHOG000259232.
InParanoidiP00962.
KOiK01886.
OMAiVTHSICT.
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

        10         20         30         40         50
MSEAEARPTN FIRQIIDEDL ASGKHTTVHT RFPPEPNGYL HIGHAKSICL 
        60         70         80         90        100
NFGIAQDYKG QCNLRFDDTN PVKEDIEYVE SIKNDVEWLG FHWSGNVRYS 
       110        120        130        140        150
SDYFDQLHAY AIELINKGLA YVDELTPEQI REYRGTLTQP GKNSPYRDRS 
       160        170        180        190        200
VEENLALFEK MRAGGFEEGK ACLRAKIDMA SPFIVMRDPV LYRIKFAEHH 
       210        220        230        240        250
QTGNKWCIYP MYDFTHCISD ALEGITHSLC TLEFQDNRRL YDWVLDNITI 
       260        270        280        290        300
PVHPRQYEFS RLNLEYTVMS KRKLNLLVTD KHVEGWDDPR MPTISGLRRR 
       310        320        330        340        350
GYTAASIREF CKRIGVTKQD NTIEMASLES CIREDLNENA PRAMAVIDPV 
       360        370        380        390        400
KLVIENYQGE GEMVTMPNHP NKPEMGSRQV PFSGEIWIDR ADFREEANKQ 
       410        420        430        440        450
YKRLVLGKEV RLRNAYVIKA ERVEKDAEGN ITTIFCTYDA DTLSKDPADG 
       460        470        480        490        500
RKVKGVIHWV SAAHALPVEI RLYDRLFSVP NPGAADDFLS VINPESLVIK 
       510        520        530        540        550
QGFAEPSLKD AVAGKAFQFE REGYFCLDSR HSTAEKPVFN RTVGLRDTWA 

KVGE
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

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

Chemistry

BindingDBiP00962.

2D gel databases

SWISS-2DPAGEP00962.

Proteomic databases

PaxDbiP00962.
PRIDEiP00962.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EchoBASEiEB0385.
EcoGeneiEG10390. glnS.

Phylogenomic databases

eggNOGiCOG0008.
HOGENOMiHOG000259232.
InParanoidiP00962.
KOiK01886.
OMAiVTHSICT.
OrthoDBiEOG6DRPF7.
PhylomeDBiP00962.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP00962.
PROiP00962.

Gene expression databases

GenevestigatoriP00962.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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).
+Additional computationally mapped references.

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: January 7, 2015
This is version 162 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

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 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.