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P00962 (SYQ_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 158. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamine--tRNA ligase

EC=6.1.1.18
Alternative name(s):
Glutaminyl-tRNA synthetase
Short name=GlnRS
Gene names
Name:glnS
Ordered Locus Names:b0680, JW0666
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length554 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-glutaminyl-tRNA(Gln). HAMAP-Rule MF_00126

Subunit structure

Monomer.

Subcellular location

Cytoplasm HAMAP-Rule MF_00126.

Sequence similarities

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

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7 Ref.8
Chain2 – 554553Glutamine--tRNA ligase HAMAP-Rule MF_00126
PRO_0000195833

Regions

Motif34 – 4411"HIGH" region HAMAP-Rule MF_00126
Motif268 – 2725"KMSKS" region HAMAP-Rule MF_00126

Sites

Binding site2711ATP By similarity

Experimental info

Sequence conflict549 – 5546WAKVGE → GRK Ref.2

Secondary structure

............................................................................................................ 554
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00962 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: E720164EF990F335

FASTA55463,478
        10         20         30         40         50         60 
MSEAEARPTN FIRQIIDEDL ASGKHTTVHT RFPPEPNGYL HIGHAKSICL NFGIAQDYKG 

        70         80         90        100        110        120 
QCNLRFDDTN PVKEDIEYVE SIKNDVEWLG FHWSGNVRYS SDYFDQLHAY AIELINKGLA 

       130        140        150        160        170        180 
YVDELTPEQI REYRGTLTQP GKNSPYRDRS VEENLALFEK MRAGGFEEGK ACLRAKIDMA 

       190        200        210        220        230        240 
SPFIVMRDPV LYRIKFAEHH QTGNKWCIYP MYDFTHCISD ALEGITHSLC TLEFQDNRRL 

       250        260        270        280        290        300 
YDWVLDNITI PVHPRQYEFS RLNLEYTVMS KRKLNLLVTD KHVEGWDDPR MPTISGLRRR 

       310        320        330        340        350        360 
GYTAASIREF CKRIGVTKQD NTIEMASLES CIREDLNENA PRAMAVIDPV KLVIENYQGE 

       370        380        390        400        410        420 
GEMVTMPNHP NKPEMGSRQV PFSGEIWIDR ADFREEANKQ YKRLVLGKEV RLRNAYVIKA 

       430        440        450        460        470        480 
ERVEKDAEGN ITTIFCTYDA DTLSKDPADG RKVKGVIHWV SAAHALPVEI RLYDRLFSVP 

       490        500        510        520        530        540 
NPGAADDFLS VINPESLVIK QGFAEPSLKD AVAGKAFQFE REGYFCLDSR HSTAEKPVFN 

       550 
RTVGLRDTWA KVGE 

« Hide

References

« Hide 'large scale' references
[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]"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map."
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. expand/collapse author list , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.
DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRSYECQT. G64802.
I41235.
RefSeqNP_415206.1. NC_000913.3.
YP_488960.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP00962.
SMRP00962. Positions 8-549.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-9787N.
IntActP00962. 5 interactions.
MINTMINT-1227909.
STRING511145.b0680.

Chemistry

BindingDBP00962.

2D gel databases

SWISS-2DPAGEP00962.

Proteomic databases

PaxDbP00962.
PRIDEP00962.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73774; AAC73774; b0680.
BAA35328; BAA35328; BAA35328.
GeneID12932213.
945310.
KEGGecj:Y75_p0659.
eco:b0680.
PATRIC32116549. VBIEscCol129921_0707.

Organism-specific databases

EchoBASEEB0385.
EcoGeneEG10390. glnS.

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000259232.
KOK01886.
OMASREIYID.
OrthoDBEOG6DRPF7.
PhylomeDBP00962.

Enzyme and pathway databases

BioCycEcoCyc:GLNS-MONOMER.
ECOL316407:JW0666-MONOMER.
MetaCyc:GLNS-MONOMER.
BRENDA6.1.1.18. 2026.
SABIO-RKP00962.

Gene expression databases

GenevestigatorP00962.

Family and domain databases

Gene3D1.10.1160.10. 1 hit.
2.40.240.10. 2 hits.
3.40.50.620. 2 hits.
HAMAPMF_00126. Gln_tRNA_synth.
InterProIPR001412. 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]
PANTHERPTHR10119. PTHR10119. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
PF03950. tRNA-synt_1c_C. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF50715. SSF50715. 1 hit.
TIGRFAMsTIGR00440. glnS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00962.
PROP00962.

Entry information

Entry nameSYQ_ECOLI
AccessionPrimary (citable) accession number: P00962
Secondary accession number(s): Q59403
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 158 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries