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P13499 (GLNA_RHOCA) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 76. 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
OrganismRhodobacter capsulatus (Rhodopseudomonas capsulata)
Taxonomic identifier1061 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

Protein attributes

Sequence length438 AA.
Sequence statusFragment.
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 – ›438›438Glutamine synthetase
PRO_0000153255

Amino acid modifications

Modified residue3971O-AMP-tyrosine By similarity

Experimental info

Non-terminal residue4381

Sequences

Sequence LengthMass (Da)Tools
P13499 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 07B81EBF6534991F

FASTA43848,391
        10         20         30         40         50         60 
MSAVKKALDL MKAEEVEYVD IRFCDPRGKL QHVTLIADLV DEDFFEEGFM FDGSSIAGWK 

        70         80         90        100        110        120 
SIDQSDMKLI PDASSVYIDP FYAEKTMCVH CNVVEPDTAE AYSRDPRIAL KAEAYLKASG 

       130        140        150        160        170        180 
IGDVAYFGPE AEFFIFDDVR YSVTPAKVAY QIDAEAAAWN TDAEVEMGNL AHRAGHKGGY 

       190        200        210        220        230        240 
FPVNPVDEAQ DLRGEMLSTM KRMGMKVDKH HHEVATCQHE LGLIFGGLTE QADNILKYKY 

       250        260        270        280        290        300 
VIHNVAHAYG KTVTFMPKPM KGDNGSGMHV NMSIWKDGKP LFAGDKYADL SQEALYFIGG 

       310        320        330        340        350        360 
ILKHAKALNA LTNPGTNSYK RLIPGFEAPV LRAYSARNRS GCVRIPWTES PKAKRVEARF 

       370        380        390        400        410        420 
PDPSANPYLA FAALLMAGLD GIKNKIDPGP ASDKDLYDLP PEELAAIPTV CGSLREALTE 

       430 
LEKDHDFLLA GDVFTKDQ 

« Hide

References

[1]"Inactivation, sequence, and lacZ fusion analysis of a regulatory locus required for repression of nitrogen fixation genes in Rhodobacter capsulatus."
Kranz R.G., Pace V.M., Caldicott I.M.
J. Bacteriol. 172:53-62(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-130.
[2]"Regulation of the glnBA operon of Rhodobacter capsulatus."
Borghese R., Wall J.D.
J. Bacteriol. 177:4549-4552(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 31-438.
Strain: ATCC 33303 / B10.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U25953 Genomic DNA. Translation: AAA87025.1.
M28244 Genomic DNA. Translation: AAA26123.1.

3D structure databases

ProteinModelPortalP13499.
SMRP13499. Positions 3-437.
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_RHOCA
AccessionPrimary (citable) accession number: P13499
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: October 1, 1996
Last modified: October 16, 2013
This is version 76 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