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P19064 (GLNA_BACCE) 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
OrganismBacillus cereus
Taxonomic identifier1396 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length444 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

Not regulated by post-translational modification and not subject to feedback inhibition.

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
   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: InterPro

   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.1
Chain2 – 444443Glutamine synthetase
PRO_0000153232

Amino acid modifications

Modified residue3731O-AMP-tyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
P19064 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 75A4A2525A445FF7

FASTA44450,195
        10         20         30         40         50         60 
MARYTKEDIF RLAKEENVKY IRLQFTDLLG VIKNVEIPVS QLTKALDNKM MFDGSSIEGF 

        70         80         90        100        110        120 
VRIEESDMYL YPDLDTWVIF PWTAEKGKVA RLICDIYNAD GTPFEGDPRN NLKRVLKEME 

       130        140        150        160        170        180 
ALGFSDFNLG PEPEFFLFKV DEKGNPTLEL NDNGGYFDLA PMDLGENCRR DIVLELEEMG 

       190        200        210        220        230        240 
FEIEASHHEV APGQHEIDFK YANAIRSCDD IQTFKLVVKT IARKHGLHAT FMPKPLYGVN 

       250        260        270        280        290        300 
GSGMHCNLSL FKNGENVFYD QNGDLQLSDD ARHFIAGILK HAPAFTAVAN PTVNSYKRLV 

       310        320        330        340        350        360 
PGYEAPCYVA WSAQNRSPLV RIPASRGIST RVEVRSVDPA ANPYLVMATL LAAGLDGIKN 

       370        380        390        400        410        420 
KLTPPAAVDR NIYVMTKEER EEAGIVDLPA TLAQALVTLQ SNEVISNALG DHLLEHFIEA 

       430        440 
KEFEWDIFRT QVHQWERDQY MSLY 

« Hide

References

[1]"Nucleotide sequence of the glutamine synthetase gene (glnA) and its upstream region from Bacillus cereus."
Nakano Y., Kato C., Tanaka E., Kimura K., Horikoshi K.
J. Biochem. 106:209-215(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-19.
Strain: IFO 3131.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D00513 Genomic DNA. Translation: BAA00403.1.
PIRAJBSQU. JU0075.

3D structure databases

ProteinModelPortalP19064.
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_BACCE
AccessionPrimary (citable) accession number: P19064
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: October 16, 2013
This is version 76 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