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Q9HU65 (GLNA_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:PA5119
OrganismPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP]
Taxonomic identifier208964 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length469 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine. UniProtKB P0A9C5

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. UniProtKB P0A9C5

Subunit structure

Oligomer of 12 subunits arranged in the form of two hexagons By similarity. UniProtKB P0A9C5

Subcellular location

Cytoplasm By similarity UniProtKB P0A9C5.

Sequence similarities

Belongs to the glutamine synthetase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Direct protein sequencing
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

Chain1 – 469469Glutamine synthetase
PRO_0000153251

Amino acid modifications

Modified residue3981O-AMP-tyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9HU65 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: DED83E755B3CD225

FASTA46951,945
        10         20         30         40         50         60 
MSYKSHQLIK DHDVKWVDLR FTDTKGKQQH VTMPARDALD DEFFEAGKMF DGSSIAGWKG 

        70         80         90        100        110        120 
IEASDMILMP DDSTAVLDPF TEEPTLILVC DIIEPSTMQG YERDPRNIAK RAEEYLKSTG 

       130        140        150        160        170        180 
IGDTVFVGPE PEFFIFDEVK FKSDISGSMF KIFSEQASWN TDADIESGNK GHRPGVKGGY 

       190        200        210        220        230        240 
FPVPPVDHDH EIRTAMCNAL EEMGLVVEVH HHEVATAGQN EIGVKFNTLV AKADEVQTLK 

       250        260        270        280        290        300 
YCVHNVADAY GKTVTFMPKP LYGDNGSGMH VHMSISKDGK NTFAGEGYAG LSETALYFIG 

       310        320        330        340        350        360 
GIIKHGKALN GFTNPSTNSY KRLVPGFEAP VMLAYSARNR SASIRIPYVS SPKARRIEAR 

       370        380        390        400        410        420 
FPDPAANPYL AFAALLMAGL DGIQNKIHPG DAADKNLYDL PPEEAKEIPQ VCGSLKEALE 

       430        440        450        460 
ELDKGRAFLT KGGVFTDEFI DAYIELKSEE EIKVRTFVHP LEYDLYYSV 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen."
Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. expand/collapse author list , Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.
Nature 406:959-964(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[2]"Biofouling in water treatment systems: effect of membrane properties on biofilm formation."
Liddor M.
Thesis (2005), Ben-Gurion University, Israel
Cited for: PROTEIN SEQUENCE OF 37-59; 118-140; 142-150; 152-170; 178-193; 432-447 AND 456-469.
Strain: ATCC 33467 / type 1 smooth and ATCC 33468 / type 2 mucoid.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE004091 Genomic DNA. Translation: AAG08504.1.
PIRG83005.
RefSeqNP_253806.1. NC_002516.2.

3D structure databases

ProteinModelPortalQ9HU65.
SMRQ9HU65. Positions 8-469.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING208964.PA5119.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG08504; AAG08504; PA5119.
GeneID877688.
KEGGpae:PA5119.
PATRIC19845073. VBIPseAer58763_5365.

Organism-specific databases

PseudoCAPPA5119.

Phylogenomic databases

eggNOGCOG0174.
HOGENOMHOG000005157.
KOK01915.
OMADMLLMPI.
OrthoDBEOG6B360N.
PhylomeDBQ9HU65.

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...

Entry information

Entry nameGLNA_PSEAE
AccessionPrimary (citable) accession number: Q9HU65
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 74 of the entry and version 1 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