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Q05542 (GLNA1_STRVR) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 69. 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 1

EC=6.3.1.2
Alternative name(s):
Glutamate--ammonia ligase I
Glutamine synthetase I
Short name=GSI
Gene names
Name:glnI
Synonyms:glnA
OrganismStreptomyces viridochromogenes
Taxonomic identifier1938 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length469 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.

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 – 469469Glutamine synthetase 1
PRO_0000153269

Amino acid modifications

Modified residue3971O-AMP-tyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q05542 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 2F152E5A5A4283E4

FASTA46952,248
        10         20         30         40         50         60 
MFQNADEAKK LIADEDVKFI DVRFCDLPGV MQHFTIPASA FDPAEELAFD GSSIRGFQAI 

        70         80         90        100        110        120 
HESDMAVRAD LSTARVDPFR RDKTVNINFF IHDPITGEQY SRDPRNVAKK AEAYLASTGI 

       130        140        150        160        170        180 
GDTGYFGPEA EFYVFDSVRL ANSATESFYH IDSEAGAWNT GALENNRGYK VRYKGGYFPV 

       190        200        210        220        230        240 
PPVDHFADLR AQISLELDRA GLQVERHDHE VGTAGQAEIN YKFNTLLAAA DDLQLFKYIV 

       250        260        270        280        290        300 
KNVAWQNGKT ATFMPKPIFG DNGSGMHVHQ SLWTGGQALF YDEAGYAGLS DTARYYMGGI 

       310        320        330        340        350        360 
LKHAPSLLAF TNPTVNSYHR LVPGFEAPVN LVYSQRNRSA AMRIPITGSN PKAKRVEFRA 

       370        380        390        400        410        420 
PDSSGNPYLA FSALLLAGLD GIKNKIEPAE PIDKDLYELA PEEHAGVPQV PTSLPAVLDR 

       430        440        450        460 
LEADHEFLLA GDVFTPDLIE TWIDYKRTNE IAPLQLRPHP YEYEQYYDV 

« Hide

References

[1]"Evolution of the glutamine synthetase gene, one of the oldest existing and functioning genes."
Kumada Y., Benson D.R., Hillemann D., Hosted T.J., Rocheford D.A., Thompson C.J., Wohlleben W., Tateno Y.
Proc. Natl. Acad. Sci. U.S.A. 90:3009-3013(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X70924 Genomic DNA. Translation: CAA50272.1.
PIRS32024.

3D structure databases

ProteinModelPortalQ05542.
SMRQ05542. Positions 3-469.
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 nameGLNA1_STRVR
AccessionPrimary (citable) accession number: Q05542
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: October 16, 2013
This is version 69 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