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Protein

Glutamine synthetase

Gene

glnA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

Keywordsi

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

Enzyme and pathway databases

BioCyciEcoCyc:GLUTAMINESYN-MONOMER.
MetaCyc:GLUTAMINESYN-MONOMER.
SABIO-RKiP0A9C5.

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: UniProtKB
  • 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-2DPAGEiP0A9C5.

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. 12 interactors.
DIPiDIP-9777N.
IntActiP0A9C5. 10 interactors.
STRINGi511145.b3870.

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.
PhylomeDBiP0A9C5.

Family and domain databases

Gene3Di3.10.20.70. 1 hit.
3.30.590.10. 1 hit.
InterProiView protein in InterPro
IPR008147. Gln_synt_b-grasp.
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.
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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliP0A9C5.
SMRiP0A9C5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262630. 12 interactors.
DIPiDIP-9777N.
IntActiP0A9C5. 10 interactors.
STRINGi511145.b3870.

Chemistry databases

BindingDBiP0A9C5.
ChEMBLiCHEMBL3789.

2D gel databases

SWISS-2DPAGEiP0A9C5.

Proteomic databases

EPDiP0A9C5.
PaxDbiP0A9C5.
PRIDEiP0A9C5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EchoBASEiEB0378.
EcoGeneiEG10383. glnA.

Phylogenomic databases

eggNOGiENOG4105C5F. Bacteria.
COG0174. LUCA.
HOGENOMiHOG000005157.
InParanoidiP0A9C5.
KOiK01915.
PhylomeDBiP0A9C5.

Enzyme and pathway databases

BioCyciEcoCyc:GLUTAMINESYN-MONOMER.
MetaCyc:GLUTAMINESYN-MONOMER.
SABIO-RKiP0A9C5.

Miscellaneous databases

PROiPR:P0A9C5.

Family and domain databases

Gene3Di3.10.20.70. 1 hit.
3.30.590.10. 1 hit.
InterProiView protein in InterPro
IPR008147. Gln_synt_b-grasp.
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.
TIGRFAMsiTIGR00653. GlnA. 1 hit.
PROSITEiView protein in PROSITE
PS00180. GLNA_1. 1 hit.
PS00182. GLNA_ADENYLATION. 1 hit.
PS00181. GLNA_ATP. 1 hit.
ProtoNetiSearch...

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: June 7, 2017
This is version 103 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

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.