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Protein

Glutamine synthetase

Gene

glnA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 (PubMed:25691471). It catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia (PubMed:24158439). Feedback-inhibited GlnA interacts with and regulates the activity of the transcriptional regulator TnrA (PubMed:11719184, PubMed:12139611). During nitrogen limitation, TnrA is in its DNA-binding active state and turns on the transcription of genes required for nitrogen assimilation (PubMed:11719184, PubMed:12139611, PubMed:25691471). Under conditions of nitrogen excess, feedback-inhibited GlnA forms a stable complex with TnrA, which inhibits its DNA-binding activity (PubMed:11719184, PubMed:12139611, PubMed:25691471). 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 (PubMed:25691471).4 Publications

Catalytic activityi

ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine.2 Publications

Cofactori

Mg2+2 PublicationsNote: Binds 2 Mg2+ ions per subunit.2 Publications

Enzyme regulationi

Completely inhibited by glutamine and partially inhibited by glycine, alanine and AMP (PubMed:4149044, PubMed:24158439). Also inhibited by L-methionine-SR-sulphoximine (Met-Sox) (PubMed:8093698, PubMed:24158439).3 Publications

Kineticsi

  1. KM=0.18 mM for ammonium1 Publication
  2. KM=0.83 mM for hydroxylamine1 Publication
  3. KM=2.3 mM for ATP1 Publication
  4. KM=2.4 mM for ATP1 Publication
  5. KM=12 mM for glutamine1 Publication
  6. KM=24 mM for glutamate1 Publication
  7. KM=27 mM for glutamate1 Publication
  1. Vmax=3.7 µmol/min/mg enzyme1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei62Important for inhibition by glutamine1 Publication1
Metal bindingi132Magnesium 1Combined sources2 Publications1
Metal bindingi134Magnesium 2Combined sources2 Publications1
Binding sitei184ATPBy similarity1
Metal bindingi189Magnesium 2Combined sources2 Publications1
Metal bindingi196Magnesium 2Combined sources2 Publications1
Binding sitei241L-glutamate; via carbonyl oxygenCombined sources2 Publications1
Metal bindingi245Magnesium 1; via pros nitrogenCombined sources2 Publications1
Binding sitei249ATPBy similarity1
Binding sitei298L-glutamateBy similarity1
Binding sitei304L-glutamateBy similarity1
Binding sitei316ATPBy similarity1
Binding sitei316L-glutamateBy similarity1
Binding sitei321ATPBy similarity1
Metal bindingi333Magnesium 1Combined sources2 Publications1
Binding sitei335L-glutamateBy similarity1

GO - Molecular functioni

GO - Biological processi

  • glutamine biosynthetic process Source: CACAO
  • nitrogen fixation Source: InterPro

Keywordsi

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

Enzyme and pathway databases

BioCyciBSUB:BSU17460-MONOMER.
BRENDAi6.3.1.2. 658.
SABIO-RKiP12425.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamine synthetase1 Publication (EC:6.3.1.22 Publications)
Short name:
GS1 Publication
Alternative name(s):
Glutamate--ammonia ligaseCurated
Glutamine synthetase I alphaCurated
Short name:
GSI alphaCurated
Gene namesi
Name:glnA1 Publication
Ordered Locus Names:BSU17460
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

In cells lacking this gene, expression of glnR, tnrA, nasB, nrgAB, gabP and ure genes is derepressed.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi59G → R: Unable to form stable complex with TnrA. In the presence of glutamine, this mutant derepresses amtB-lacZ fusion and glnRA-lacZ fusion. 1 Publication1
Mutagenesisi62R → A: Highly resistant to inhibition by glutamine and AMP. Regulation by TnrA and GlnR is abolished. Only small differences (less than 2-fold) in its steady-state kinetic constants compared with the wild-type. Similar sensitivity to Met-Sox that compared to the wild-ytpe. 1 Publication1
Mutagenesisi190V → A: Unable to form stable complex with TnrA. In the presence of glutamine, this mutant partially relieves expression of the glnRA-lacZ fusion, but has no effect on the TnrA-dependent regulation of amtB-lacZ fusion. Resistant to inhibition by MetSox. 2 Publications1
Mutagenesisi302G → E: Unable to form stable complex with TnrA. In the presence of glutamine, amtB-lacZ fusion is only 4-fold regulated by TnrA, whereas glnRA-lacZ fusion is derepressed. This mutant retains enzymatic specific activity with a 2-fold decrease of the affinity for glutamate and glutamine compared to the wild-type. Slightly less sensitive to inhibition by glutamine. 1 Publication1
Mutagenesisi304E → A: Highly resistant to Met-Sox inhibition. 8- and 2-fold increase of the affinity for glutamate and ATP, respectively. Strong decrease of the affinity for ammonium. 1 Publication1
Mutagenesisi306P → H: Unable to form stable complex with TnrA. In the presence of glutamine, this mutant completely derepresses glnRA-lacZ fusion, whereas amtB-lacZ fusion expression is only partially derepresses. 1 Publication1
Mutagenesisi424E → K: Unable to form stable complex with TnrA. In the presence of glutamine, this mutant derepresses amtB-lacZ fusion and glnRA-lacZ fusion. Although it is defective in regulation, this mutant retains enzymatic specific activity and similar affinity for ATP, glutamate and glutamine compared to the wild-type. Slightly less sensitive to inhibition by glutamine. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001532332 – 444Glutamine synthetaseAdd BLAST443

Proteomic databases

PaxDbiP12425.
PRIDEiP12425.

Expressioni

Inductioni

Repressed by GlnR under conditions of nitrogen excess (PubMed:2573733). Repressed by TnrA under conditions of nitrogen limitation.2 Publications

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. This inhibitory effect is the highest when both glutamine and AMP are present.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
tnrAQ456668EBI-6402863,EBI-8507041

Protein-protein interaction databases

DIPiDIP-29670N.
IntActiP12425. 4 interactors.
MINTiMINT-224371.
STRINGi224308.Bsubs1_010100009606.

Structurei

Secondary structure

1444
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 16Combined sources11
Beta strandi20 – 26Combined sources7
Beta strandi28 – 30Combined sources3
Beta strandi32 – 38Combined sources7
Helixi39 – 41Combined sources3
Helixi42 – 46Combined sources5
Beta strandi51 – 53Combined sources3
Helixi54 – 56Combined sources3
Helixi59 – 61Combined sources3
Helixi63 – 65Combined sources3
Beta strandi67 – 80Combined sources14
Helixi81 – 83Combined sources3
Helixi84 – 87Combined sources4
Beta strandi89 – 97Combined sources9
Beta strandi99 – 103Combined sources5
Helixi108 – 121Combined sources14
Beta strandi125 – 133Combined sources9
Beta strandi135 – 140Combined sources6
Beta strandi142 – 144Combined sources3
Beta strandi146 – 151Combined sources6
Turni160 – 162Combined sources3
Beta strandi163 – 165Combined sources3
Helixi166 – 178Combined sources13
Beta strandi183 – 188Combined sources6
Beta strandi194 – 199Combined sources6
Helixi204 – 224Combined sources21
Beta strandi227 – 230Combined sources4
Beta strandi244 – 252Combined sources9
Beta strandi261 – 263Combined sources3
Helixi264 – 266Combined sources3
Helixi269 – 289Combined sources21
Helixi295 – 298Combined sources4
Beta strandi311 – 313Combined sources3
Beta strandi316 – 322Combined sources7
Helixi327 – 329Combined sources3
Beta strandi332 – 334Combined sources3
Helixi343 – 359Combined sources17
Helixi372 – 374Combined sources3
Helixi377 – 383Combined sources7
Helixi392 – 400Combined sources9
Helixi403 – 409Combined sources7
Helixi411 – 430Combined sources20
Helixi434 – 440Combined sources7
Turni441 – 443Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2FWXmodel-A/B/C/D1-444[»]
4LNFX-ray2.95A/B/C/D/E/F/G/H/I/J/K/L2-444[»]
4LNIX-ray2.58A/B/C/D/E/F/G/H/I/J/K/L2-444[»]
4LNKX-ray2.87A/B/C/D/E/F2-444[»]
4LNNX-ray3.10A/B/C/D/E/F/G/H/I/J/K/L2-444[»]
4LNOX-ray2.90A/B/C/D/E/F2-444[»]
4S0RX-ray3.50A/B/C/D/E/F/G/H/I/J/K/L/M/N1-444[»]
ProteinModelPortaliP12425.
SMRiP12425.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni240 – 241L-glutamate bindingBy similarity2

Sequence similaritiesi

Belongs to the glutamine synthetase family.Curated

Phylogenomic databases

eggNOGiENOG4105C5F. Bacteria.
COG0174. LUCA.
HOGENOMiHOG000005156.
InParanoidiP12425.
KOiK01915.
OMAiNIMTFRH.
PhylomeDBiP12425.

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.

P12425-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKYTREDIE KLVKEENVKY IRLQFTDILG TIKNVEIPVS QLGKALDNKV
60 70 80 90 100
MFDGSSIEGF VRIEESDMYL YPDLNTFVIF PWTAEKGKVA RFICDIYNPD
110 120 130 140 150
GTPFEGDPRN NLKRILKEME DLGFSDFNLG PEPEFFLFKL DEKGEPTLEL
160 170 180 190 200
NDKGGYFDLA PTDLGENCRR DIVLELEEMG FEIEASHHEV APGQHEIDFK
210 220 230 240 250
YAGAVRSCDD IQTFKLVVKT IARKHGLHAT FMPKPLFGVN GSGMHCNLSL
260 270 280 290 300
FKNGVNAFFD ENADLQLSET AKHFIAGIVK HATSFTAVTN PTVNSYKRLV
310 320 330 340 350
PGYEAPCYVA WSAQNRSPLI RIPASRGIST RVEVRSVDPA ANPYLALSVL
360 370 380 390 400
LAAGLDGIKN KLEAPAPIDR NIYVMSKEER MENGIVDLPA TLAEALEEFK
410 420 430 440
SNEVMVKALG EHLFEHFIEA KEIEWDMFRT QVHPWEREQY MSQY
Length:444
Mass (Da):50,278
Last modified:January 23, 2007 - v3
Checksum:i83A5657CE1388AB0
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti10E → V in strain: PCI 219. 1
Natural varianti43G → E in strain: PCI 219. 1
Natural varianti253N → D in strain: PCI 219. 1
Natural varianti259F → Y in strain: PCI 219. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22811 Genomic DNA. Translation: AAA83376.1.
D00854 Genomic DNA. Translation: BAA00730.1.
U66480 Genomic DNA. Translation: AAB41080.1.
AL009126 Genomic DNA. Translation: CAB13630.1.
PIRiJT0392. AJBSQS.
RefSeqiNP_389628.1. NC_000964.3.
WP_003231737.1. NZ_JNCM01000035.1.

Genome annotation databases

EnsemblBacteriaiCAB13630; CAB13630; BSU17460.
GeneIDi940020.
KEGGibsu:BSU17460.
PATRICi18975307. VBIBacSub10457_1845.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22811 Genomic DNA. Translation: AAA83376.1.
D00854 Genomic DNA. Translation: BAA00730.1.
U66480 Genomic DNA. Translation: AAB41080.1.
AL009126 Genomic DNA. Translation: CAB13630.1.
PIRiJT0392. AJBSQS.
RefSeqiNP_389628.1. NC_000964.3.
WP_003231737.1. NZ_JNCM01000035.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2FWXmodel-A/B/C/D1-444[»]
4LNFX-ray2.95A/B/C/D/E/F/G/H/I/J/K/L2-444[»]
4LNIX-ray2.58A/B/C/D/E/F/G/H/I/J/K/L2-444[»]
4LNKX-ray2.87A/B/C/D/E/F2-444[»]
4LNNX-ray3.10A/B/C/D/E/F/G/H/I/J/K/L2-444[»]
4LNOX-ray2.90A/B/C/D/E/F2-444[»]
4S0RX-ray3.50A/B/C/D/E/F/G/H/I/J/K/L/M/N1-444[»]
ProteinModelPortaliP12425.
SMRiP12425.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29670N.
IntActiP12425. 4 interactors.
MINTiMINT-224371.
STRINGi224308.Bsubs1_010100009606.

Proteomic databases

PaxDbiP12425.
PRIDEiP12425.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13630; CAB13630; BSU17460.
GeneIDi940020.
KEGGibsu:BSU17460.
PATRICi18975307. VBIBacSub10457_1845.

Phylogenomic databases

eggNOGiENOG4105C5F. Bacteria.
COG0174. LUCA.
HOGENOMiHOG000005156.
InParanoidiP12425.
KOiK01915.
OMAiNIMTFRH.
PhylomeDBiP12425.

Enzyme and pathway databases

BioCyciBSUB:BSU17460-MONOMER.
BRENDAi6.3.1.2. 658.
SABIO-RKiP12425.

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 nameiGLN1A_BACSU
AccessioniPrimary (citable) accession number: P12425
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: March 15, 2017
This is version 143 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. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.