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Q9UY99 (GLNA_PYRAB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 83. 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

Short name=GS
EC=6.3.1.2
Alternative name(s):
Glutamate--ammonia ligase
Gene names
Name:glnA
Ordered Locus Names:PYRAB16090
ORF Names:PAB1292
OrganismPyrococcus abyssi (strain GE5 / Orsay) [Complete proteome] [HAMAP]
Taxonomic identifier272844 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length439 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.

Subcellular location

Cytoplasm Potential.

Sequence similarities

Belongs to the glutamine synthetase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete 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 – 439439Glutamine synthetase
PRO_0000153208

Amino acid modifications

Modified residue3581O-AMP-tyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9UY99 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 62CCFD3970A98AF0

FASTA43949,743
        10         20         30         40         50         60 
MNVSEVKSGA TRSPKFVQLI FVDINGMPKG MEIPASRLQE AIEDGISFDG SSVPGFQGIE 

        70         80         90        100        110        120 
DSDLIFKADP DTYVEVPWDN VARVYGYIYK DGKPYGADPR GVLKRVIEKL AEMGIKAYIG 

       130        140        150        160        170        180 
PEPEFYLFKK NGSWELEIPD VGGYFDILTL DKAKDIKREI AEYMPSFGLV PEVLHHEVGK 

       190        200        210        220        230        240 
AQHEIDFRYD EALKTADNII SFKYIVKAVA EVHGLYATFM PKPIYGMPGN GMHLHISLWK 

       250        260        270        280        290        300 
EGENIFKGEE GLSETALHFI GGLLKHAKAL TAITNPTVNS YKRLVPGYEA PVYISWGYKN 

       310        320        330        340        350        360 
RSALIRVPAF WGNGARIEYR CPDPSANPYF AFAAILMAGL DGIKHKVEPF AYVEENVYEM 

       370        380        390        400        410        420 
DEGKRKELGI DTLPGSLGEA LDELEKDKVV REALGEAYKN FIEYKRKEWE SYLEYLEAKH 

       430 
LPKDTKRVTE WELERYFFI 

« Hide

References

« Hide 'large scale' references
[1]"An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi."
Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O., Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J., Weissenbach J., Zivanovic Y., Forterre P.
Mol. Microbiol. 47:1495-1512(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GE5 / Orsay.
[2]"Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638."
Gao J., Wang J.
Curr. Microbiol. 64:118-129(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: GE5 / Orsay.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ248288 Genomic DNA. Translation: CAB50513.1.
HE613800 Genomic DNA. Translation: CCE71069.1.
PIRC75009.
RefSeqNP_127283.1. NC_000868.1.

3D structure databases

ProteinModelPortalQ9UY99.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272844.PAB1292.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB50513; CAB50513; PAB1292.
GeneID1495898.
KEGGpab:PAB1292.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0174.
HOGENOMHOG000005156.
KOK01915.
OMARRDIDYA.

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.
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.
PS00181. GLNA_ATP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLNA_PYRAB
AccessionPrimary (citable) accession number: Q9UY99
Secondary accession number(s): G8ZJW2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: May 1, 2000
Last modified: May 14, 2014
This is version 83 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