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Protein

Glutamine synthetase

Gene

glnA

Organism
Clostridium saccharobutylicum
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Glutamine synthetase (GS) is an unusual multitasking protein that functions as an enzyme, a transcription coregulator, and a chaperone in ammonium assimilation and in the regulation of genes involved in nitrogen metabolism. It catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia. Feedback-inhibited GlnA also interacts with and regulates the activity of the transcriptional regulator TnrA. During nitrogen limitation, TnrA is in its DNA-binding active state and turns on the transcription of genes required for nitrogen assimilation. Under conditions of nitrogen excess, feedback-inhibited GlnA forms a stable complex with TnrA, which inhibits its DNA-binding activity. In contrast, feedback-inhibited GlnA acts as a chaperone to stabilize the DNA-binding activity of GlnR, which represses the transcription of nitrogen assimilation genes.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

Inhibited by glutamine.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei62Important for inhibition by glutamineBy similarity1
Metal bindingi131Magnesium 1By similarity1
Metal bindingi133Magnesium 2By similarity1
Binding sitei183ATPBy similarity1
Metal bindingi188Magnesium 2By similarity1
Metal bindingi195Magnesium 2By similarity1
Binding sitei240L-glutamate; via carbonyl oxygenBy similarity1
Metal bindingi244Magnesium 1; via pros nitrogenBy similarity1
Binding sitei248ATPBy similarity1
Binding sitei297L-glutamateBy similarity1
Binding sitei303L-glutamateBy similarity1
Binding sitei315ATPBy similarity1
Binding sitei315L-glutamateBy similarity1
Binding sitei320ATPBy similarity1
Metal bindingi332Magnesium 1By similarity1
Binding sitei334L-glutamateBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamine synthetase1 Publication (EC:6.3.1.2By similarity)
Short name:
GS1 Publication
Alternative name(s):
Glutamate--ammonia ligaseBy similarity
Glutamine synthetase I alphaBy similarity
Short name:
GSI alphaBy similarity
Gene namesi
Name:glnA1 Publication
OrganismiClostridium saccharobutylicum
Taxonomic identifieri169679 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Subcellular locationi

  • Cytoplasm By similarity

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001532341 – 443Glutamine synthetaseAdd BLAST443

Interactioni

Subunit structurei

Oligomer of 12 subunits arranged in the form of two hexagons. In its feedback-inhibited form, interacts with TnrA in order to block its DNA-binding activity.By similarity

Structurei

3D structure databases

ProteinModelPortaliP10656.
SMRiP10656.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni239 – 240L-glutamate bindingBy similarity2

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.
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.
PS00181. GLNA_ATP. 1 hit.

Sequencei

Sequence statusi: Complete.

P10656-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKYTKEDII NLVKENGVKF IRLQFTDIFG TLKNVAITDK QLEKALDNEC
60 70 80 90 100
MFDGSSIDGF VRIEESDMNL RPNLDSFVIF PWRPQQGKVA RLICDVYKPD
110 120 130 140 150
GTPFEGDPRH VLKRANADAK ELGYTMNVGP ECEFFLFETD ENGRATTNTQ
160 170 180 190 200
DKAGYFDLAP TDLGENARRD MTLALEEMGF EIEASHHEVA EGQNEIDFKY
210 220 230 240 250
GDALTTADNI MTFKLVVKSI AQRHGLHASF MPKPIFGING SGMHVNMSLF
260 270 280 290 300
KDGKNAFVDE NDKNGLSKVA YQFIAGLLKN IKGMAAVTNP LVNSYKRLVP
310 320 330 340 350
GYEAPVYLAW SCKNRTALIR VPAARGAGTR VELRCPDPSS NPYLVLACLL
360 370 380 390 400
QAGLDGIKNN LQPPAEVEAN IFAMTEQERK ENGIDNLPNN LYEAVNYMKE
410 420 430 440
NELAKKALGD HVYGNYVAGK AAEWDDYRTK VHDWELENYL NKY
Length:443
Mass (Da):49,682
Last modified:July 1, 1989 - v1
Checksum:iEDE5BF44495151FC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M18966 Genomic DNA. Translation: AAA23241.1.
PIRiA28676. AJCLQA.

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.

Entry informationi

Entry nameiGLN1A_CLOSA
AccessioniPrimary (citable) accession number: P10656
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: March 15, 2017
This is version 83 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Was originally thought to originate from C.acetobutylicum.Curated
Lacks the tyrosine conserved in bacteria and other archaea, involved in feedback inhibition.Curated