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P04772 (GLNA2_BRADU) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 89. 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 2

EC=6.3.1.2
Alternative name(s):
Glutamate--ammonia ligase II
Glutamine synthetase II
Short name=GSII
Gene names
Name:glnII
Ordered Locus Names:blr4169
OrganismBradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110) [Reference proteome] [HAMAP]
Taxonomic identifier224911 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium

Protein attributes

Sequence length344 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine.

Subunit structure

Homooctamer.

Subcellular location

Cytoplasm.

Miscellaneous

Two forms of glutamine synthetase (GSI and GSII) can be found in this nitrogen fixing bacteria, GSI is a typical prokaryotic glutamine synthetase whereas GSII is similar to the eukaryotic enzyme.

Sequence similarities

Belongs to the glutamine synthetase family.

Ontologies

Keywords
   Biological processNitrogen fixation
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Reference proteome
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 – 344344Glutamine synthetase 2
PRO_0000153220

Experimental info

Sequence conflict37 – 382QL → HV in CAA27779. Ref.1
Sequence conflict326 – 34419ASQIL…KKAVA → VRRS in CAA27779. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P04772 [UniParc].

Last modified February 28, 2003. Version 2.
Checksum: 5462522D03DC51B2

FASTA34438,366
        10         20         30         40         50         60 
MTKYKLEYIW LDGYTPTPNL RGKTQIKEFA SFPTLEQLPL WGFDGSSTQQ AEGHSSDCVL 

        70         80         90        100        110        120 
KPVAVFPDAA RTNGVLVMCE VMMPDGKTPH ASNKRATILD DAGAWFGFEQ EYFFYKDGRP 

       130        140        150        160        170        180 
LGFPTSGYPA PQGPYYTGVG FSNVGDVARK IVEEHLDLCL AAGINHEGIN AEVAKGQWEF 

       190        200        210        220        230        240 
QIFGKGSKKA ADEMWMARYL MLRLTEKYGI DIEFHCKPLG DTDWNGSGMH ANFSTEYMRT 

       250        260        270        280        290        300 
VGGKEYFEAL MAAFDKNLMD HIAVYGPDND KRLTGKHETA PWNKFSYGVA DRGASIRVPH 

       310        320        330        340 
SFVNNGYKGY LEDRRPNSQG DPYQIASQIL KTISSVPTEK KAVA 

« Hide

References

« Hide 'large scale' references
[1]"Apparent eukaryotic origin of glutamine synthetase II from the bacterium Bradyrhizobium japonicum."
Carlson T.A., Chelm B.K.
Nature 322:568-570(1986)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete genomic sequence of nitrogen-fixing symbiotic bacterium Bradyrhizobium japonicum USDA110."
Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.
DNA Res. 9:189-197(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X04187 Genomic DNA. Translation: CAA27779.1.
BA000040 Genomic DNA. Translation: BAC49434.1.
PIRAJZJQ2. A24155.
RefSeqNP_770809.1. NC_004463.1.

3D structure databases

ProteinModelPortalP04772.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224911.blr4169.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC49434; BAC49434; BAC49434.
GeneID1054220.
KEGGbja:blr4169.
PATRIC21191856. VBIBraJap65052_4184.

Phylogenomic databases

eggNOGCOG0174.
HOGENOMHOG000061500.
KOK01915.
OMAYGIDIEF.
OrthoDBEOG6K3ZXS.
ProtClustDBCLSK862960.

Enzyme and pathway databases

BioCycBJAP224911:GJEJ-4195-MONOMER.

Family and domain databases

Gene3D3.30.590.10. 1 hit.
InterProIPR008147. Gln_synt_beta.
IPR014746. Gln_synth/guanido_kin_cat_dom.
IPR008146. Gln_synth_cat_dom.
IPR027303. Gln_synth_gly_rich_site.
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.
PROSITEPS00180. GLNA_1. 1 hit.
PS00181. GLNA_ATP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLNA2_BRADU
AccessionPrimary (citable) accession number: P04772
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: February 28, 2003
Last modified: December 11, 2013
This is version 89 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