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Protein

Glutamine synthetase

Gene

glnA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Enzyme regulationi

The activity of this enzyme is controlled by adenylation under conditions of abundant glutamine. The fully adenylated enzyme complex is inactive (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

  • glutamine biosynthetic process Source: CACAO
  • nitrogen fixation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciBSUB:BSU17460-MONOMER.
BRENDAi6.3.1.2. 658.
SABIO-RKP12425.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamine synthetase (EC:6.3.1.2)
Alternative name(s):
Glutamate--ammonia ligase
Gene namesi
Name:glnA
Ordered Locus Names:BSU17460
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei373O-AMP-tyrosineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP12425.
PRIDEiP12425.

Expressioni

Inductioni

Repressed by GlnR under conditions of nitrogen excess. Repressed by TnrA under conditions of nitrogen limitation.

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.1 Publication

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

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.
InterProiIPR008147. 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.
[Graphical view]
PfamiPF00120. Gln-synt_C. 1 hit.
PF03951. Gln-synt_N. 1 hit.
[Graphical view]
SMARTiSM01230. Gln-synt_C. 1 hit.
[Graphical view]
SUPFAMiSSF54368. SSF54368. 1 hit.
TIGRFAMsiTIGR00653. GlnA. 1 hit.
PROSITEiPS00180. GLNA_1. 1 hit.
PS00182. GLNA_ADENYLATION. 1 hit.
PS00181. GLNA_ATP. 1 hit.
[Graphical view]

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-RKP12425.

Family and domain databases

Gene3Di3.10.20.70. 1 hit.
3.30.590.10. 1 hit.
InterProiIPR008147. 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.
[Graphical view]
PfamiPF00120. Gln-synt_C. 1 hit.
PF03951. Gln-synt_N. 1 hit.
[Graphical view]
SMARTiSM01230. Gln-synt_C. 1 hit.
[Graphical view]
SUPFAMiSSF54368. SSF54368. 1 hit.
TIGRFAMsiTIGR00653. GlnA. 1 hit.
PROSITEiPS00180. GLNA_1. 1 hit.
PS00182. GLNA_ADENYLATION. 1 hit.
PS00181. GLNA_ATP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGLNA_BACSU
AccessioniPrimary (citable) accession number: P12425
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 141 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Elevated Mn2+ concentration reduces sensitivity of GlnA to feedback inhibitors Gln and AMP.

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.