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Q02154 (GLNA2_RHILP) 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 2

EC=6.3.1.2
Alternative name(s):
Glutamate--ammonia ligase II
Glutamine synthetase II
Short name=GSII
Gene names
Name:glnII
OrganismRhizobium leguminosarum bv. phaseoli
Taxonomic identifier385 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupRhizobium

Protein attributes

Sequence length326 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Enzyme regulation

Transferase activity is inhibited by NH4Cl.

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 termDirect protein sequencing
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

Initiator methionine11Removed Ref.2
Chain2 – 326325Glutamine synthetase 2
PRO_0000153224

Sequences

Sequence LengthMass (Da)Tools
Q02154 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 637AE03B83D1F840

FASTA32636,979
        10         20         30         40         50         60 
MTKFKLEYIW LDGYTPVPNL RGKTQIKEFD EFPTLEQLPL WGFDGSSTMQ AEGSSDCVLK 

        70         80         90        100        110        120 
PVAIYPDPAR TNGALVMCEV MMPDGHAHAS NARATILDDE DAWFGFEQEY FFYQNGRPLG 

       130        140        150        160        170        180 
FPEQGYPAPQ PYYTGVGYSN VGDVAREIVE EHLDLCLAAG INHEGINAEV AKGQWEFQIF 

       190        200        210        220        230        240 
GKGSKKAADQ IWMARYLLQR LTEKYGIDIE YHCKPLGDTD WNGSGMHCNF STKYLREVGG 

       250        260        270        280        290        300 
KEYFEALMAS SDKNLMDHIA VYGPDNDKRL TGKHETAPWN KFSYGVADRG ASIRVPHSFI 

       310        320 
KNDYKGYLED RRPNSQGDPY QIVRRF 

« Hide

References

[1]"Activation of the Rhizobium leguminosarum glnII gene by NtrC is dependent on upstream DNA sequences."
Patriarca E.J., Chiurazzi M., Manco G., Riccio A., Lamberti A., Paolis A., Rossi M., Defez R., Iaccarino M.
Mol. Gen. Genet. 234:337-345(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: LPR1105.
[2]"Dissociation by NH4Cl treatment of the enzymic activities of glutamine synthetase II from Rhizobium leguminosarum biovar viceae."
Manco G., Rossi M., Defez R., Lamberti A., Percuoco G., Iaccarino M.
J. Gen. Microbiol. 138:1453-1460(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-27.
Strain: LPR1105.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X67296 Genomic DNA. Translation: CAA47710.1.
PIRS26216.

3D structure databases

ProteinModelPortalQ02154.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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_RHILP
AccessionPrimary (citable) accession number: Q02154
Secondary accession number(s): Q9R5J0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: October 16, 2013
This is version 69 of the entry and version 3 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