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O66514 (GLNA_AQUAE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 82. 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:aq_111
OrganismAquifex aeolicus (strain VF5) [Reference proteome] [HAMAP]
Taxonomic identifier224324 [NCBI]
Taxonomic lineageBacteriaAquificaeAquificalesAquificaceaeAquifex

Protein attributes

Sequence length469 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the glutamine synthetase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete 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

Chain1 – 469469Glutamine synthetase
PRO_0000153228

Amino acid modifications

Modified residue3981O-AMP-tyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
O66514 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 688504C9FD95B056

FASTA46953,294
        10         20         30         40         50         60 
MPKYTPEEVL DLIQKEGVQY VDLRFSDPFG QWQHLTIPAY EISKETFEVG RGFDGSSIRG 

        70         80         90        100        110        120 
WQSINESDML AKPDPNTAFI DPFIEPKTLV MICDIYDPVT GERYGRDTRY IAQKAEQYLK 

       130        140        150        160        170        180 
QTGIGDTAYF GPEAEFFIFD SVEFGTAANY AFWRVDSEEG WWNREVPSSG YKIPHKRGYF 

       190        200        210        220        230        240 
PAPPVDKMMQ LRNEMVSIMS DLGIIVELHH HEVATAGQGE IDIRYDSLLN QADKLFLYKY 

       250        260        270        280        290        300 
IVRMVAAKHG KYATFMAKVL PNDNGSGMHT HFSIWKNGEN LFAGSEYAGL SKTALYAIGG 

       310        320        330        340        350        360 
ILKHGPAIAA FTNPTVNSYH RLVPGYEAPV RLAYSARNRS AAIRIPMYSQ NPKAKRIEVR 

       370        380        390        400        410        420 
FPDATSNPYL AFAAILMAAI DGIENEIDPG EPFDKDIYSL PPEELEGIPQ LPGSLEEALK 

       430        440        450        460 
ALEEDYEFLL KGNVFTEEFI QLWIESKRAE IDELRFIPHP KEFELYWDI 

« Hide

References

[1]"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.
Nature 392:353-358(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VF5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000657 Genomic DNA. Translation: AAC06472.1.
PIRG70310.
RefSeqNP_213074.1. NC_000918.1.

3D structure databases

ProteinModelPortalO66514.
SMRO66514. Positions 5-469.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224324.aq_111.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC06472; AAC06472; aq_111.
GeneID1192525.
KEGGaae:aq_111.
PATRIC20957910. VBIAquAeo85532_0095.

Phylogenomic databases

eggNOGCOG0174.
HOGENOMHOG000005157.
KOK01915.
OMASCRIPYV.
OrthoDBEOG6B360N.

Enzyme and pathway databases

BioCycAAEO224324:GJBH-89-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.
IPR004809. Gln_synth_I.
[Graphical view]
PfamPF00120. Gln-synt_C. 1 hit.
PF03951. Gln-synt_N. 1 hit.
[Graphical view]
SUPFAMSSF54368. SSF54368. 1 hit.
TIGRFAMsTIGR00653. GlnA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGLNA_AQUAE
AccessionPrimary (citable) accession number: O66514
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: May 14, 2014
This is version 82 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