Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O08467 (GLNA_THEKO) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 88. 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:TK1796
OrganismThermococcus kodakaraensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1)) [Reference proteome] [HAMAP]
Taxonomic identifier69014 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaeThermococcus

Protein attributes

Sequence length443 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
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 – 443443Glutamine synthetase
PRO_0000153211

Amino acid modifications

Modified residue3621O-AMP-tyrosine By similarity

Experimental info

Sequence conflict4021Y → N in BAA20530. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O08467 [UniParc].

Last modified March 29, 2005. Version 2.
Checksum: 94357E45D5F18168

FASTA44350,308
        10         20         30         40         50         60 
MNEIKGIERA VQVEVPRPRF LLLAFTDING SLKGMEIPME RYEEAVEDGV SFDGSSIPGF 

        70         80         90        100        110        120 
EGIEDSDLIF KADPSTYAEI PWEGIGRVYG YIYKGDEPYQ ADPRGILKRV LERLEKEGLK 

       130        140        150        160        170        180 
AHIGPEPEFY IFKKNGTWEL HIPDSGGYFD LVGLDKAREI RREIALYMPY LGLKPEVLHH 

       190        200        210        220        230        240 
EVGKAQHEID FRYDEALRTA DNIVSFKHVV KAVAELHGYY ATFMPKPIYG FPGNGMHLHI 

       250        260        270        280        290        300 
SLWKDGENVF IGEDGLSDTA LHFIGGILKH AKALAALTNP TVNSYKRLVP GYEAPVYISW 

       310        320        330        340        350        360 
GYRNRSALIR VPAFKGSGAR IEYRCPDPSA NPYLALAGIL MVGLDGIKKK VEPDSYVETN 

       370        380        390        400        410        420 
VYEMDDAERE RLGIDTLPGS LGEALEELKK DKTVREALGG AYKNFIDYKE REWEEYIEYL 

       430        440 
SSRDIPIDTK KVTEWELERY FYV 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of recombinant glutamine synthetase from the hyperthermophilic archaeon Pyrococcus sp. strain KOD1."
Adul Rahman R.N.Z., Jongsareejit B., Fujiwara S., Imanaka T.
Appl. Environ. Microbiol. 63:2472-2476(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC BAA-918 / JCM 12380 / KOD1.
[2]"Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes."
Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.
Genome Res. 15:352-363(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-918 / JCM 12380 / KOD1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D86222 Genomic DNA. Translation: BAA20530.1.
AP006878 Genomic DNA. Translation: BAD85985.1.
RefSeqYP_184209.1. NC_006624.1.

3D structure databases

ProteinModelPortalO08467.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO08467. 1 interaction.
MINTMINT-8377176.
STRING69014.TK1796.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD85985; BAD85985; TK1796.
GeneID3233803.
KEGGtko:TK1796.

Phylogenomic databases

eggNOGCOG0174.
HOGENOMHOG000005156.
KOK01915.
OMAAEDDVWS.
ProtClustDBCLSK491907.

Enzyme and pathway databases

BioCycTKOD69014:GH72-1833-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.
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_THEKO
AccessionPrimary (citable) accession number: O08467
Secondary accession number(s): Q5JJ67
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: March 29, 2005
Last modified: November 13, 2013
This is version 88 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