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Protein

Glutamine synthetase

Gene

glnA

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

Functioni

Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia.By similarity

Catalytic activityi

ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine.By similarity

Cofactori

Mg2+By similarityNote: Binds 2 Mg2+ ions per subunit.By similarity

Enzyme regulationi

The activity of this enzyme could be controlled by adenylation under conditions of abundant glutamine.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi130Magnesium 1By similarity1
Metal bindingi132Magnesium 2By similarity1
Binding sitei208ATPBy similarity1
Metal bindingi213Magnesium 2By similarity1
Metal bindingi221Magnesium 2By similarity1
Binding sitei266L-glutamate; via carbonyl oxygenBy similarity1
Metal bindingi270Magnesium 1; via pros nitrogenBy similarity1
Binding sitei274ATPBy similarity1
Binding sitei322L-glutamateBy similarity1
Binding sitei328L-glutamateBy similarity1
Binding sitei340ATPBy similarity1
Binding sitei340L-glutamateBy similarity1
Binding sitei345ATPBy similarity1
Binding sitei353ATPBy similarity1
Metal bindingi358Magnesium 1By similarity1
Binding sitei360L-glutamateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi272 – 274ATPBy similarity3

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • glutamate-ammonia ligase activity Source: EcoCyc
  • identical protein binding Source: IntAct
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • ammonia assimilation cycle Source: EcoCyc
  • glutamine biosynthetic process Source: InterPro
  • nitrogen fixation Source: InterPro
  • nitrogen utilization Source: EcoCyc
  • response to radiation Source: EcoCyc

Keywordsi

Molecular functionLigase
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:GLUTAMINESYN-MONOMER
MetaCyc:GLUTAMINESYN-MONOMER
SABIO-RKP0A9C5

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamine synthetaseBy similarity (EC:6.3.1.2By similarity)
Short name:
GSBy similarity
Alternative name(s):
Glutamate--ammonia ligaseCurated
Glutamine synthetase I betaBy similarity
Short name:
GSI betaBy similarity
Gene namesi
Name:glnABy similarity
Ordered Locus Names:b3870, JW3841
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10383 glnA

Subcellular locationi

  • Cytoplasm By similarity

GO - Cellular componenti

  • cytosol Source: EcoCyc
  • membrane Source: UniProtKB

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3789

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001532352 – 469Glutamine synthetaseAdd BLAST468

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei398O-AMP-tyrosine2 Publications1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP0A9C5
PaxDbiP0A9C5
PRIDEiP0A9C5

2D gel databases

SWISS-2DPAGEP0A9C5

Interactioni

Subunit structurei

Oligomer of 12 subunits arranged in the form of two hexameric ring.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-909063,EBI-909063

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi4262630, 46 interactors
DIPiDIP-9777N
IntActiP0A9C5, 10 interactors
STRINGi316385.ECDH10B_4060

Chemistry databases

BindingDBiP0A9C5

Structurei

3D structure databases

ProteinModelPortaliP0A9C5
SMRiP0A9C5
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni265 – 266L-glutamate bindingBy similarity2

Sequence similaritiesi

Belongs to the glutamine synthetase family.Curated

Phylogenomic databases

eggNOGiENOG4105C5F Bacteria
COG0174 LUCA
HOGENOMiHOG000005157
InParanoidiP0A9C5
KOiK01915
OMAiIEAAWNT
PhylomeDBiP0A9C5

Family and domain databases

Gene3Di3.10.20.70, 1 hit
InterProiView protein in InterPro
IPR008147 Gln_synt_b-grasp
IPR036651 Gln_synt_N
IPR014746 Gln_synth/guanido_kin_cat_dom
IPR008146 Gln_synth_cat_dom
IPR027303 Gln_synth_gly_rich_site
IPR004809 Gln_synth_I
IPR001637 Gln_synth_I_adenylation_site
IPR027302 Gln_synth_N_conserv_site
PfamiView protein in Pfam
PF00120 Gln-synt_C, 1 hit
PF03951 Gln-synt_N, 1 hit
SMARTiView protein in SMART
SM01230 Gln-synt_C, 1 hit
SUPFAMiSSF54368 SSF54368, 1 hit
SSF55931 SSF55931, 1 hit
TIGRFAMsiTIGR00653 GlnA, 1 hit
PROSITEiView protein in PROSITE
PS00180 GLNA_1, 1 hit
PS00182 GLNA_ADENYLATION, 1 hit
PS00181 GLNA_ATP, 1 hit

Sequencei

Sequence statusi: Complete.

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

P0A9C5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAEHVLTML NEHEVKFVDL RFTDTKGKEQ HVTIPAHQVN AEFFEEGKMF
60 70 80 90 100
DGSSIGGWKG INESDMVLMP DASTAVIDPF FADSTLIIRC DILEPGTLQG
110 120 130 140 150
YDRDPRSIAK RAEDYLRSTG IADTVLFGPE PEFFLFDDIR FGSSISGSHV
160 170 180 190 200
AIDDIEGAWN SSTQYEGGNK GHRPAVKGGY FPVPPVDSAQ DIRSEMCLVM
210 220 230 240 250
EQMGLVVEAH HHEVATAGQN EVATRFNTMT KKADEIQIYK YVVHNVAHRF
260 270 280 290 300
GKTATFMPKP MFGDNGSGMH CHMSLSKNGV NLFAGDKYAG LSEQALYYIG
310 320 330 340 350
GVIKHAKAIN ALANPTTNSY KRLVPGYEAP VMLAYSARNR SASIRIPVVS
360 370 380 390 400
SPKARRIEVR FPDPAANPYL CFAALLMAGL DGIKNKIHPG EAMDKNLYDL
410 420 430 440 450
PPEEAKEIPQ VAGSLEEALN ELDLDREFLK AGGVFTDEAI DAYIALRREE
460
DDRVRMTPHP VEFELYYSV
Length:469
Mass (Da):51,904
Last modified:January 23, 2007 - v2
Checksum:i0AFC05724CDEBA36
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti90C → S in AAA23879 (PubMed:2874141).Curated1
Sequence conflicti108 – 109IA → MS in AAA23879 (PubMed:2874141).Curated2
Sequence conflicti197C → S in AAA23879 (PubMed:2874141).Curated1
Sequence conflicti228T → I in CAA28806 (PubMed:2882477).Curated1
Sequence conflicti247 – 248AH → VRN in CAA28806 (PubMed:2882477).Curated2
Sequence conflicti305 – 306HA → QP in CAA28806 (PubMed:2882477).Curated2
Sequence conflicti394 – 395DK → KD AA sequence (PubMed:5543675).Curated2
Sequence conflicti394 – 395DK → KD AA sequence (PubMed:4904088).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05173 Genomic DNA Translation: CAA28806.1
M13746 Genomic DNA Translation: AAA23879.1
L19201 Genomic DNA Translation: AAB03004.1
U00096 Genomic DNA Translation: AAC76867.1
AP009048 Genomic DNA Translation: BAE77439.1
J01618 Genomic DNA Translation: AAA98066.1
M10421 Genomic DNA Translation: AAA23882.1
K02176 Genomic DNA Translation: AAA23880.1
PIRiS40815 AJECQ
RefSeqiNP_418306.1, NC_000913.3
WP_001271717.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC76867; AAC76867; b3870
BAE77439; BAE77439; BAE77439
GeneIDi948370
KEGGiecj:JW3841
eco:b3870
PATRICifig|1411691.4.peg.2841

Similar proteinsi

Entry informationi

Entry nameiGLN1B_ECOLI
AccessioniPrimary (citable) accession number: P0A9C5
Secondary accession number(s): P06711, Q2M8G7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: March 28, 2018
This is version 109 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome
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Main funding by: National Institutes of Health