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Q5HPN2 (GLNA_STAEQ) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 59. 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:SERP0876
OrganismStaphylococcus epidermidis (strain ATCC 35984 / RP62A) [Complete proteome] [HAMAP]
Taxonomic identifier176279 [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_0000153265

Amino acid modifications

Modified residue3751O-AMP-tyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5HPN2 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: 63F94D34B734A5D3

FASTA44650,851
        10         20         30         40         50         60 
MPKRSFTKDD IRKFAEEENV RYLRLQFTDI LGTIKNVEVP VSQLEKVLDN EMMFDGSSIE 

        70         80         90        100        110        120 
GFVRIEESDM YLHPDLDTWV IFPWTAGQGK VARLICDVFK TDGTPFEGDP RANLKRVLRR 

       130        140        150        160        170        180 
MEDMGFTDFN 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 FDPEGDLQLT DTAYQFTAGV LKNARGFTAV CNPIVNSYKR 

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

       370        380        390        400        410        420 
ENKLEVPEPV NQNIYEMNRE EREAVGIQDL PSTLYTALKA MRENKSIKNA LGNHIYNQFI 

       430        440 
NSKSIEWDYY RTQVSEWERE QYIKQY 

« 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: ATCC 35984 / RP62A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000029 Genomic DNA. Translation: AAW54283.1.
RefSeqYP_188458.1. NC_002976.3.

3D structure databases

ProteinModelPortalQ5HPN2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING176279.SERP0876.

Proteomic databases

PRIDEQ5HPN2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW54283; AAW54283; SERP0876.
GeneID3241510.
KEGGser:SERP0876.
PATRIC19612625. VBIStaEpi130894_0855.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycSEPI176279:GJJB-902-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_STAEQ
AccessionPrimary (citable) accession number: Q5HPN2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: February 15, 2005
Last modified: November 13, 2013
This is version 59 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