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P28786 (GLNA_PROHU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 71. 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
OrganismProteus hauseri
Taxonomic identifier183417 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeProteus

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.

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 – 469469Glutamine synthetase
PRO_0000153250

Amino acid modifications

Modified residue3981O-AMP-tyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
P28786 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: 852EE660D070E61A

FASTA46952,205
        10         20         30         40         50         60 
MSLEHVLSMI EEHKVRYIDL RFTDTRGKEQ HLTIPAHQVN DDFFEEGKMF DGSSIGGWKG 

        70         80         90        100        110        120 
INESDMVLMP DASTAMLDPF FQDPTLIIRC DVLEPGTMQG YDRDPRSISK RAEDYLKSSG 

       130        140        150        160        170        180 
IADTVLFGPE PEFFLFDDIR FKNDISGASY AINDIEAAWN TNTKYEDGNK GHRPMVKGGY 

       190        200        210        220        230        240 
FPLPPVDSSQ DIRSTMCNIM EEMGLVVEAH HHEVATAGQN EVATRFNTMT KKADETQIYK 

       250        260        270        280        290        300 
YVVQNVAHVF GKTATFMPKP LVGDNGSGMH CHMSLSKNGT NLFAGDKYGG LSEMALYYIG 

       310        320        330        340        350        360 
GIIKHARALN AFTNPTTNSY KRLVPGFEAP VMLAYSARNR SASIRIPVVA SMKARRIEVR 

       370        380        390        400        410        420 
FPDPLANPYL AFAAQLMAGL DGITNKIHPG DAMDKNLYDL PPEEAKEIPT VAGSLEEALN 

       430        440        450        460 
ALDADREFLT HGGVFTNDSI DAYLALLRTD VQRVRMAPHP LEFEMYYSA 

« Hide

References

[1]"Cloning, heterologous expression, and sequencing of the Proteus vulgaris glnAntrBC operon and implications of nitrogen control on heterologous urease expression."
Steglitz-Moersdorf U., Moersdorf G., Kaltwasser H.
FEMS Microbiol. Lett. 106:157-164(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 13315 / DSM 30118 / JCM 1668 / NBRC 3851 / NCIMB 4175 / NCTC 4175 / NRRL B-3405.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X68129 Genomic DNA. Translation: CAA48234.1.
PIRS23899.

3D structure databases

ProteinModelPortalP28786.
SMRP28786. Positions 2-468.
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.
IPR001637. Gln_synth_I_adenylation_site.
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.
PS00182. GLNA_ADENYLATION. 1 hit.
PS00181. GLNA_ATP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLNA_PROHU
AccessionPrimary (citable) accession number: P28786
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: June 11, 2014
This is version 71 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