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P22248 (GLNA_AZOVI) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 69. 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
OrganismAzotobacter vinelandii
Taxonomic identifier354 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeAzotobacter

Protein attributes

Sequence length467 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 – 467467Glutamine synthetase
PRO_0000153231

Amino acid modifications

Modified residue3961O-AMP-tyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
P22248 [UniParc].

Last modified August 1, 1991. Version 1.
Checksum: D4EFA6EC895E38AF

FASTA46751,746
        10         20         30         40         50         60 
MSKSLQLIKE HDVKWIDLRF TDTKGKQQHV TMPARDVDDD FFEYGKMFDG SSIAGWKGIE 

        70         80         90        100        110        120 
ASDMILMPDD STAVLDPFTE EPTLIIVCDI IEPSTMQGYD RDPRAIARRA EEYLKSTGIG 

       130        140        150        160        170        180 
DTAFFGPEPE FFIFDEVKYK SDISGSMFKI FSEQAAWNTD ADFEGGNKGH RPGVKGGYFP 

       190        200        210        220        230        240 
VPPVDHDHEI RTAMCNALEE MGLKVEVHHH EVATAGQNEI GVSFNTLVAK ADEVQTLKYC 

       250        260        270        280        290        300 
VHNVADAYGK TVTFMPKPLY GDNGSGMHVH MSIAKDGKNT FAGEGYAGLS DTALYFIGGI 

       310        320        330        340        350        360 
IKHGKALNGF TNPSTNSYKR LVPGFEAPVM LAYSARNRSA SIRIPYVNSP KARRIEARFP 

       370        380        390        400        410        420 
DPSANPYLAF AALLMAGLDG IQNKIHPGDA ADKNLYDLPP EEAKEIPQVC GSLKEALEEL 

       430        440        450        460 
DKGRAFLTKG GVFSDDFIDA YLELKSEEEI KVRTFVHPLE YDLYYSV 

« Hide

References

[1]"Molecular analysis of the Azotobacter vinelandii glnA gene encoding glutamine synthetase."
Toukdarian A., Saunders G., Selman-Sosa G., Santero E., Woodley P., Kennedy C.
J. Bacteriol. 172:6529-6539(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M57275 Genomic DNA. Translation: AAA62673.1.
PIRAJAVQ. A37153.

3D structure databases

ProteinModelPortalP22248.
SMRP22248. Positions 5-467.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP22248.

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_AZOVI
AccessionPrimary (citable) accession number: P22248
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: October 16, 2013
This is version 69 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