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

P36687 (GLNA_PYRWO) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 67. 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 1

EC=6.3.1.2
Alternative name(s):
Glutamate--ammonia ligase
Glutamine synthetase I
Short name=GSI
Gene names
Name:glnA
OrganismPyrococcus woesei
Taxonomic identifier2262 [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.

Sequence similarities

Belongs to the glutamine synthetase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
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 1
PRO_0000153212

Amino acid modifications

Modified residue3581O-AMP-tyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
P36687 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: C503B43B790BD25C

FASTA43950,066
        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 GMHLHISLSK 

       250        260        270        280        290        300 
DGENVFMGEE GLSEIALHFI GGILKHAKAL IAVTNPTVNS YKRLVPGYEA 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

[1]"Cloning and sequencing of the gene encoding glutamine synthetase I from the archaeum Pyrococcus woesei: anomalous phylogenies inferred from analysis of archaeal and bacterial glutamine synthetase I sequences."
Tiboni O., Cammarano P., Sanangelantoni A.M.
J. Bacteriol. 175:2961-2969(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X60161 Genomic DNA. Translation: CAA42730.1.
PIRA36911.

3D structure databases

ProteinModelPortalP36687.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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_PYRWO
AccessionPrimary (citable) accession number: P36687
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: October 16, 2013
This is version 67 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