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P10583 (GLNA_AZOBR) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 78. 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
OrganismAzospirillum brasilense
Taxonomic identifier192 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeAzospirillum

Protein attributes

Sequence length468 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
   Biological processNitrogen fixation
   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: UniProtKB-KW

   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 – 468468Glutamine synthetase
PRO_0000153229

Amino acid modifications

Modified residue3981O-AMP-tyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
P10583 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 356AA3803E024F1A

FASTA46851,976
        10         20         30         40         50         60 
MSDISKVFDL IKEHDVKYVD LRFTDPRGKL HHTAQHVSTI DEDVFEDGIM FDGSSIAGWK 

        70         80         90        100        110        120 
AINESDMILQ LDPTTAVMDP FSAQPTLNIL CDVYEPSTGQ PYARCPRGIA KAAEKYMASA 

       130        140        150        160        170        180 
GIADTAYFGP EAEFFVFDDV KFKVEMNKVS YEFDSEEGPY TSDKDYEDGN LGHRPGVKGG 

       190        200        210        220        230        240 
YFPVAPVDSG SDLRAEMLSV LAEMGVPVEK HHHEVAASQH ELGIKFDTLV RTGDNMQYYK 

       250        260        270        280        290        300 
YVVHNVAHAY GKTATFMPKP VFGDNGSGMH MHQSIWKEGQ PLFAGNQYAD LSELALYYIG 

       310        320        330        340        350        360 
GIIKHAKALN AFTNPTTNSY KRLVPGYEAP VLLAYSARNR SASCRIPYVA SPKGKRVEVR 

       370        380        390        400        410        420 
FPDPSANPYL AFAALLMAGL DGIQNKIHPG EAMDKNLYDL PAEELAKVPT VCGSREALDS 

       430        440        450        460 
LKADSAFLQK GDVFTKDMIE SYIDLRTEEL LAFETMPHPI EYKMYYSV 

« Hide

References

[1]"Nucleotide sequence of the Azospirillum brasilense Sp7 glutamine synthetase structural gene."
Bozouklian H., Elmerich C.
Biochimie 68:1181-1187(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 29145 / Sp7 / DSM 1690 / IMET 11303.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M26107 Genomic DNA. Translation: AAA22183.1.
PIRAJKCQB. A24714.

3D structure databases

ProteinModelPortalP10583.
SMRP10583. Positions 7-468.
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_AZOBR
AccessionPrimary (citable) accession number: P10583
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: October 16, 2013
This is version 78 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