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Protein

Glutamine--tRNA ligase

Gene

glnS

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

Functioni

Catalytic activityi

ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-glutaminyl-tRNA(Gln).UniRule annotation5 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei67L-glutamineUniRule annotationCombined sources3 Publications1
Binding sitei212L-glutamineUniRule annotationCombined sources4 Publications1
Binding sitei231ATPUniRule annotationCombined sources3 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi35 – 37ATPUniRule annotationCombined sources1 Publication3
Nucleotide bindingi41 – 47ATPUniRule annotationCombined sources1 Publication7
Nucleotide bindingi261 – 262ATPUniRule annotationCombined sources3 Publications2
Nucleotide bindingi269 – 271ATPUniRule annotationCombined sources3 Publications3

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • glutamine-tRNA ligase activity Source: EcoCyc

GO - Biological processi

  • glutaminyl-tRNA aminoacylation Source: EcoCyc

Keywordsi

Molecular functionAminoacyl-tRNA synthetase, Ligase
Biological processProtein biosynthesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:GLNS-MONOMER.
MetaCyc:GLNS-MONOMER.
BRENDAi6.1.1.18. 2026.
6.1.1.24. 2026.
SABIO-RKiP00962.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamine--tRNA ligaseUniRule annotation (EC:6.1.1.18UniRule annotation5 Publications)
Alternative name(s):
Glutaminyl-tRNA synthetaseUniRule annotation
Short name:
GlnRSUniRule annotation
Gene namesi
Name:glnSUniRule annotation
Ordered Locus Names:b0680, JW0666
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10390. glnS.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

  • cytosol Source: EcoCyc

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi31R → A or K: Decreased affinity for glutamine and catalytic activity. 1 Publication1
Mutagenesisi230C → R: Decreases catalytic activity 1000-fold, but has no effect on affinity for glutamine. Loss of catalytic activity; when associated with I-256. 1 Publication1
Mutagenesisi256Q → I: Loss of catalytic activity; when associated with R-230. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00001958332 – 554Glutamine--tRNA ligaseAdd BLAST553

Proteomic databases

PaxDbiP00962.
PRIDEiP00962.

2D gel databases

SWISS-2DPAGEiP00962.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

BioGridi4261207. 27 interactors.
DIPiDIP-9787N.
IntActiP00962. 5 interactors.
MINTiMINT-1227909.
STRINGi316385.ECDH10B_0745.

Chemistry databases

BindingDBiP00962.

Structurei

Secondary structure

1554
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi11 – 21Combined sources11
Beta strandi29 – 32Combined sources4
Beta strandi36 – 38Combined sources3
Helixi42 – 57Combined sources16
Beta strandi61 – 66Combined sources6
Helixi71 – 73Combined sources3
Helixi76 – 88Combined sources13
Beta strandi94 – 96Combined sources3
Helixi100 – 103Combined sources4
Helixi104 – 116Combined sources13
Beta strandi119 – 123Combined sources5
Helixi127 – 134Combined sources8
Beta strandi137 – 139Combined sources3
Turni145 – 148Combined sources4
Helixi151 – 162Combined sources12
Beta strandi172 – 175Combined sources4
Helixi184 – 186Combined sources3
Beta strandi190 – 194Combined sources5
Turni200 – 202Combined sources3
Beta strandi207 – 210Combined sources4
Helixi212 – 222Combined sources11
Beta strandi226 – 231Combined sources6
Helixi232 – 234Combined sources3
Turni235 – 237Combined sources3
Helixi238 – 246Combined sources9
Beta strandi255 – 259Combined sources5
Beta strandi264 – 267Combined sources4
Helixi271 – 279Combined sources9
Beta strandi282 – 284Combined sources3
Beta strandi291 – 293Combined sources3
Helixi294 – 300Combined sources7
Helixi304 – 314Combined sources11
Helixi325 – 339Combined sources15
Beta strandi345 – 354Combined sources10
Beta strandi362 – 368Combined sources7
Helixi373 – 375Combined sources3
Beta strandi377 – 382Combined sources6
Beta strandi384 – 389Combined sources6
Turni390 – 392Combined sources3
Beta strandi393 – 396Combined sources4
Beta strandi403 – 405Combined sources3
Beta strandi408 – 412Combined sources5
Beta strandi417 – 424Combined sources8
Beta strandi427 – 429Combined sources3
Beta strandi433 – 436Combined sources4
Beta strandi460 – 462Combined sources3
Beta strandi466 – 473Combined sources8
Beta strandi476 – 480Combined sources5
Helixi482 – 484Combined sources3
Beta strandi485 – 487Combined sources3
Helixi488 – 491Combined sources4
Beta strandi496 – 504Combined sources9
Helixi506 – 510Combined sources5
Beta strandi516 – 519Combined sources4
Turni520 – 522Combined sources3
Beta strandi523 – 527Combined sources5
Turni529 – 531Combined sources3
Beta strandi534 – 536Combined sources3
Beta strandi538 – 544Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00962.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni317 – 324Interaction with tRNAUniRule annotation2 Publications8

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi34 – 44"HIGH" regionUniRule annotationAdd BLAST11
Motifi268 – 272"KMSKS" regionUniRule annotation5

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105CX6. Bacteria.
COG0008. LUCA.
HOGENOMiHOG000259232.
InParanoidiP00962.
KOiK01886.
PhylomeDBiP00962.

Family and domain databases

Gene3Di1.10.1160.10. 1 hit.
2.40.240.10. 2 hits.
3.40.50.620. 3 hits.
HAMAPiMF_00126. Gln_tRNA_synth. 1 hit.
InterProiView protein in InterPro
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.
PfamiView protein in Pfam
PF00749. tRNA-synt_1c. 1 hit.
PF03950. tRNA-synt_1c_C. 1 hit.
PRINTSiPR00987. TRNASYNTHGLU.
SUPFAMiSSF50715. SSF50715. 1 hit.
TIGRFAMsiTIGR00440. glnS. 1 hit.
PROSITEiView protein in PROSITE
PS00178. AA_TRNA_LIGASE_I. 1 hit.

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)DescriptionActionsGraphical viewLength
Sequence conflicti549 – 554WAKVGE → GRK (PubMed:6288695).Curated6

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.
WP_001287154.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73774; AAC73774; b0680.
BAA35328; BAA35328; BAA35328.
GeneIDi945310.
KEGGiecj:JW0666.
eco:b0680.
PATRICifig|1411691.4.peg.1596.

Similar proteinsi

Entry informationi

Entry nameiSYQ_ECOLI
AccessioniPrimary (citable) accession number: P00962
Secondary accession number(s): Q59403
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: August 30, 2017
This is version 182 of the entry and version 3 of the sequence. See 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