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Q9CLP2 (GLNA_PASMU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 73. 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
Ordered Locus Names:PM1175
OrganismPasteurella multocida (strain Pm70) [Complete proteome] [HAMAP]
Taxonomic identifier272843 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaePasteurella

Protein attributes

Sequence length472 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 – 472472Glutamine synthetase
PRO_0000153249

Amino acid modifications

Modified residue4021O-AMP-tyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9CLP2 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 0DEFBE7ED69E8BB0

FASTA47252,581
        10         20         30         40         50         60 
MSDTTAIANV FKLIEEYDIK FVLLRFTDIK GKEHGVSLPV NLVDEDLFED GKMFDGSSVE 

        70         80         90        100        110        120 
GWKAINKADM LLMPMPETAV VDPFAQIPTL SLRCSIYEPS TMQSYDRDPR SIAIRAENYM 

       130        140        150        160        170        180 
RSTGIADEAL FGPEPEFFLF DDVRFDVSMN RSSYSVDDIE AAWNTNKKYE DGNNAYRPLK 

       190        200        210        220        230        240 
KGGYCAVAPI DSAHDIRSEM CLILEEMGLV IEAHHHEVAT AGQNEIATRF NTLTTKADET 

       250        260        270        280        290        300 
QIYKYVVQNV AYEHGKTACF MPKPITGDNG SGMHCNMSLS KDGKNVFQGD KYAGLSETAL 

       310        320        330        340        350        360 
YYIGGIIKHA KALNAFTNPS TNSYKRLVPG FEAPVLLAYS ASNRSASIRI PAVTNPKAIR 

       370        380        390        400        410        420 
IEARFPDPLA NPYLAFAALL MAGLDGIINK IHPGDAMDKN LYDLPPEELQ NIPAVASSLE 

       430        440        450        460        470 
EALNALEQDY EFLTKGNVFT QAFIDAFITI KRKEVERLNM TPHPVEFEMY YA 

« Hide

References

[1]"Complete genomic sequence of Pasteurella multocida Pm70."
May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.
Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Pm70.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE004439 Genomic DNA. Translation: AAK03259.1.
RefSeqNP_246112.1. NC_002663.1.

3D structure databases

ProteinModelPortalQ9CLP2.
SMRQ9CLP2. Positions 9-472.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272843.PM1175.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK03259; AAK03259; PM1175.
GeneID1244522.
KEGGpmu:PM1175.
PATRIC22871603. VBIPasMul88067_1186.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0174.
HOGENOMHOG000005157.
KOK01915.
OMARAHHEVG.
OrthoDBEOG6B360N.
ProtClustDBCLSK870384.

Enzyme and pathway databases

BioCycPMUL272843:GC8W-1225-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.
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_PASMU
AccessionPrimary (citable) accession number: Q9CLP2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 2, 2001
Last sequence update: June 1, 2001
Last modified: November 13, 2013
This is version 73 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