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P0A1P6 (GLNA_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamine synthetase

EC=6.3.1.2
Alternative name(s):
Glutamate--ammonia ligase
Gene names
Name:glnA
Ordered Locus Names:STM4007
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length469 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Enzyme regulation

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

Subunit structure

Oligomer of 12 subunits arranged in the form of two hexagons.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the glutamine synthetase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processglutamine biosynthetic process

Inferred from electronic annotation. Source: InterPro

nitrogen fixation

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glutamate-ammonia ligase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 469468Glutamine synthetase
PRO_0000153253

Amino acid modifications

Modified residue3981O-AMP-tyrosine By similarity

Experimental info

Sequence conflict2231A → R in CAA59423. Ref.3
Sequence conflict3921A → P Ref.1
Sequence conflict3921A → P Ref.3
Sequence conflict4481R → P in AAA27134. Ref.1

Secondary structure

............................................................................................. 469
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A1P6 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: CD4303E758871E10

FASTA46951,786
        10         20         30         40         50         60 
MSAEHVLTML NEHEVKFVDL RFTDTKGKEQ HVTIPAHQVN AEFFEEGKMF DGSSIGGWKG 

        70         80         90        100        110        120 
INESDMVLMP DASTAVIDPF FADSTLIIRC DILEPGTLQG YDRDPRSIAK RAEDYLRATG 

       130        140        150        160        170        180 
IADTVLFGPE PEFFLFDDIR FGASISGSHV AIDDIEGAWN SSTKYEGGNK GHRPGVKGGY 

       190        200        210        220        230        240 
FPVPPVDSAQ DIRSEMCLVM EQMGLVVEAH HHEVATAGQN EVATRFNTMT KKADEIQIYK 

       250        260        270        280        290        300 
YVVHNVAHRF GKTATFMPKP MFGDNGSGMH CHMSLAKNGT NLFSGDKYAG LSEQALYYIG 

       310        320        330        340        350        360 
GVIKHAKAIN ALANPTTNSY KRLVPGYEAP VMLAYSARNR SASIRIPVVA SPKARRIEVR 

       370        380        390        400        410        420 
FPDPAANPYL CFAALLMAGL DGIKNKIHPG EAMDKNLYDL PPEEAKEIPQ VAGSLEEALN 

       430        440        450        460 
ALDLDREFLK AGGVFTDEAI DAYIALRREE DDRVRMTPHP VEFELYYSV 

« Hide

References

« Hide 'large scale' references
[1]"Sequence of glutamine synthetase from Salmonella typhimurium and implications for the protein structure."
Janson C.A., Kayne P.S., Almassy R.J., Grunstein M., Eisenberg D.
Gene 46:297-300(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.
[3]Kustu S.G.
Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 133-469.
Strain: LT2.
[4]"Refined atomic model of glutamine synthetase at 3.5-A resolution."
Yamashita M.Y., Almassy R.J., Janson C.A., Cascio D., Eisenberg D.
J. Biol. Chem. 264:17681-17690(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
[5]"The crystal structure of phosphinothricin in the active site of glutamine synthetase illuminates the mechanism of enzymatic inhibition."
Gill H.S., Eisenberg D.
Biochemistry 40:1903-1912(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M14536 Genomic DNA. Translation: AAA27134.1.
AE006468 Genomic DNA. Translation: AAL22846.1.
X85104 Genomic DNA. Translation: CAA59423.1.
PIRAJEBQT. A25818.
RefSeqNP_462887.1. NC_003197.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1F1HX-ray2.67A/B/C/D/E/F/G/H/I/J/K/L2-469[»]
1F52X-ray2.49A/B/C/D/E/F/G/H/I/J/K/L2-469[»]
1FPYX-ray2.89A/B/C/D/E/F/G/H/I/J/K/L2-469[»]
1LGRX-ray2.79A/B/C/D/E/F/G/H/I/J/K/L2-469[»]
2GLSX-ray3.50A/B/C/D/E/F/G/H/I/J/K/L1-469[»]
2LGSX-ray2.80A/B/C/D/E/F/G/H/I/J/K/L2-469[»]
ProteinModelPortalP0A1P6.
SMRP0A1P6. Positions 2-469.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING99287.STM4007.

Chemistry

BindingDBP0A1P6.
ChEMBLCHEMBL5089.
DrugBankDB00131. Adenosine monophosphate.

Proteomic databases

PaxDbP0A1P6.
PRIDEP0A1P6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL22846; AAL22846; STM4007.
GeneID1255533.
KEGGstm:STM4007.
PATRIC32386886. VBISalEnt20916_4223.

Phylogenomic databases

eggNOGCOG0174.
HOGENOMHOG000005157.
KOK01915.
OMADMLLMPI.
OrthoDBEOG6B360N.
PhylomeDBP0A1P6.

Enzyme and pathway databases

BioCycSENT99287:GCTI-4036-MONOMER.

Family and domain databases

Gene3D3.10.20.70. 1 hit.
3.30.590.10. 1 hit.
InterProIPR008147. Gln_synt_beta.
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]
PfamPF00120. Gln-synt_C. 1 hit.
PF03951. Gln-synt_N. 1 hit.
[Graphical view]
SUPFAMSSF54368. SSF54368. 1 hit.
TIGRFAMsTIGR00653. GlnA. 1 hit.
PROSITEPS00180. GLNA_1. 1 hit.
PS00182. GLNA_ADENYLATION. 1 hit.
PS00181. GLNA_ATP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A1P6.
PROP0A1P6.

Entry information

Entry nameGLNA_SALTY
AccessionPrimary (citable) accession number: P0A1P6
Secondary accession number(s): P06201, Q60007
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 67 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references