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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: 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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10390. glnS.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
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 – 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.
InParanoidiP00962.
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

        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:
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.
InParanoidi P00962.
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

« 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).

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 29, 2014
This is version 160 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