Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P25821 (GLNA_NEIGO) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 65. 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
OrganismNeisseria gonorrhoeae
Taxonomic identifier485 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

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
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_0000153248

Amino acid modifications

Modified residue4011O-AMP-tyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
P25821 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: E1643ED5CF240108

FASTA47251,975
        10         20         30         40         50         60 
MSIKNAVKLI EKSKARFVDL RFTDTKGKQH HFTVPARIVL EGPEEWFENG QAFDGSSIGG 

        70         80         90        100        110        120 
WKGIQASDMQ LRPDASTAFV DPFYDDVTVV ITCDVIDPAD GQGYDRDPRS IARRAEAYLK 

       130        140        150        160        170        180 
SSGIGDTAYF GPEPEFFVFD GVEFETDMHK TRYEITSESG AWASGLHMDG QNTGHRPAVK 

       190        200        210        220        230        240 
GGYAPVAPID CGQDLRSAMV NILEGLGIEV EVHHSEVGTG SQMEIGTRFA TLVKRADQTQ 

       250        260        270        280        290        300 
DMKYVIQNVA HNFGKTATFM PKPIMGDNGS GMHVHQSIWK DGQNLFAGDG YAGLSDTALY 

       310        320        330        340        350        360 
YIGGIIKHAK ALNAITNPST NSYKRLVPHF EAPTKLAYSA KNRSASIRIP SVNSSKARRI 

       370        380        390        400        410        420 
EARFPDPTAN PYLAFAALLM AGLDGIQNKI HPGDPADKNL YDLPPEEDAL VPTVCASLEE 

       430        440        450        460        470 
ALAALKADHE FLLRGGVFSK DWIDSYIAFK EEDVRRIRMA PHPLEFEMYY SL 

« Hide

References

[1]Seifert H.S.
Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M84113 Genomic DNA. Translation: AAB61772.1.

3D structure databases

ProteinModelPortalP25821.
SMRP25821. Positions 2-472.
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_NEIGO
AccessionPrimary (citable) accession number: P25821
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: October 16, 2013
This is version 65 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