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Q05907 (GLNA_PYRFU) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 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:PF0450
OrganismPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) [Reference proteome] [HAMAP]
Taxonomic identifier186497 [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
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 – 439439Glutamine synthetase
PRO_0000153209

Amino acid modifications

Modified residue3581O-AMP-tyrosine By similarity

Experimental info

Sequence conflict2031K → G in AAA71968. Ref.1
Sequence conflict2321M → L in AAA71968. Ref.1
Sequence conflict3511A → S in AAA71968. Ref.1
Sequence conflict3701I → L in AAA71968. Ref.1
Sequence conflict3761S → N in AAA71968. Ref.1
Sequence conflict3821E → G in AAA71968. Ref.1
Sequence conflict3971A → S in AAA71968. Ref.1
Sequence conflict421 – 4266MPKDTK → IPPDTE in AAA71968. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q05907 [UniParc].

Last modified April 3, 2002. Version 2.
Checksum: 96563A8E9A0E0892

FASTA43950,183
        10         20         30         40         50         60 
MNISVSMNKF DSKIKFVQLV FVDINGMPKG MEIPASRLEE AVTDGISFDG SSVPGFQGIE 

        70         80         90        100        110        120 
DSDLVFKADP DTYVEVPWDN VARVYGFIYK DNKPYGADPR GILKRALEEL EKEGYKAYIG 

       130        140        150        160        170        180 
PEPEFYLFKK NGTWELEIPD VGGYFDILTL DKARDIRREI AEYMPSFGLI PEVLHHEVGK 

       190        200        210        220        230        240 
AQHEIDFRYD EALKTADNIV SFKYITKAVA EMHGLYATFM PKPLFGFPGN GMHLHISLWK 

       250        260        270        280        290        300 
DGENVFMGEE GLSEIALHFI GGILKHAKAL TAVTNPTVNS YKRLVPSYEA PVYISWGYRN 

       310        320        330        340        350        360 
RSALIRVPAF WGKGARIEYR CPDPSANPYF AFAAVLKAGL DGIKHKIDPF AYVEENVYEM 

       370        380        390        400        410        420 
SEEKRKELGI ETLPGSLGEA LEELEKDKVV KEALGDAYKN FINYKWKEWE SYLEYLEEKH 

       430 
MPKDTKKVTE WELERYFFL 

« Hide

References

« Hide 'large scale' references
[1]"Evolutionary relationships of bacterial and archaeal glutamine synthetase genes."
Brown J.R., Masuchi Y., Robb F.T., Doolittle W.F.
J. Mol. Evol. 38:566-576(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
[2]"Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences."
Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T.
Genetics 152:1299-1305(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L12410 Genomic DNA. Translation: AAA71968.1.
AE009950 Genomic DNA. Translation: AAL80574.1.
RefSeqNP_578179.1. NC_003413.1.

3D structure databases

ProteinModelPortalQ05907.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING186497.PF0450.

Proteomic databases

PRIDEQ05907.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL80574; AAL80574; PF0450.
GeneID1468291.
KEGGpfu:PF0450.

Phylogenomic databases

eggNOGCOG0174.
HOGENOMHOG000005156.
KOK01915.
OMAPNIAFKN.
ProtClustDBCLSK491907.

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_PYRFU
AccessionPrimary (citable) accession number: Q05907
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: April 3, 2002
Last modified: October 16, 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