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Q5HGC3 (GLNA_STAAC) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 60. 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

Short name=GS
EC=6.3.1.2
Alternative name(s):
Glutamate--ammonia ligase
Gene names
Name:glnA
Ordered Locus Names:SACOL1329
OrganismStaphylococcus aureus (strain COL) [Complete proteome] [HAMAP]
Taxonomic identifier93062 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length446 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 By similarity.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the glutamine synthetase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
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

Chain1 – 446446Glutamine synthetase
PRO_0000153257

Amino acid modifications

Modified residue3751O-AMP-tyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5HGC3 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: 81713EE654D7E7E6

FASTA44650,841
        10         20         30         40         50         60 
MPKRTFTKDD IRKFAEEENV RYLRLQFTDI LGTIKNVEVP VSQLEKVLDN EMMFDGSSIE 

        70         80         90        100        110        120 
GFVRIEESDM YLHPDLDTWV IFPWTAGQGK VARLICDVYK TDGTPFEGDP RANLKRVLKE 

       130        140        150        160        170        180 
MEDLGFTDFN LGPEPEFFLF KLDEKGEPTL ELNDDGGYFD LAPTDLGENC RRDIVLELED 

       190        200        210        220        230        240 
MGFDIEASHH EVAPGQHEID FKYADAVTAC DNIQTFKLVV KTIARKHNLH ATFMPKPLFG 

       250        260        270        280        290        300 
VNGSGMHFNV SLFKGKENAF FDPNTEMGLT ETAYQFTAGV LKNARGFTAV CNPLVNSYKR 

       310        320        330        340        350        360 
LVPGYEAPCY IAWSGKNRSP LIRVPSSRGL STRIEVRSVD PAANPYMALA AILEAGLDGI 

       370        380        390        400        410        420 
KNKLKVPEPV NQNIYEMNRE EREAVGIQDL PSTLYTALKA MRENEVIKKA LGNHIYNQFI 

       430        440 
NSKSIEWDYY RTQVSEWERD QYMKQY 

« Hide

References

[1]"Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain."
Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H. expand/collapse author list , Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M.
J. Bacteriol. 187:2426-2438(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: COL.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000046 Genomic DNA. Translation: AAW36580.1.
RefSeqYP_186184.1. NC_002951.2.

3D structure databases

ProteinModelPortalQ5HGC3.
SMRQ5HGC3. Positions 6-446.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING93062.SACOL1329.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW36580; AAW36580; SACOL1329.
GeneID3237965.
KEGGsac:SACOL1329.
PATRIC19528889. VBIStaAur112458_1297.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0174.
HOGENOMHOG000005156.
KOK01915.
OMAAEDDVWS.
OrthoDBEOG6B360N.
ProtClustDBCLSK885265.

Enzyme and pathway databases

BioCycSAUR93062:GCEP-1307-MONOMER.

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_STAAC
AccessionPrimary (citable) accession number: Q5HGC3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: February 15, 2005
Last modified: March 19, 2014
This is version 60 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