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P77958 (GLNA1_STRFL) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 67. 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:glnA
OrganismStreptomyces filamentosus (Streptomyces roseosporus)
Taxonomic identifier67294 [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 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 – 469469Glutamine synthetase 1
PRO_0000153268

Amino acid modifications

Modified residue3971O-AMP-tyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
P77958 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 9AE0FF7A6675F792

FASTA46952,514
        10         20         30         40         50         60 
MFQNADEVQK YVADNDVKFI DVRFCDLPGV MQHFTIPAAT FDPAEELAFD GSSIRGFQAI 

        70         80         90        100        110        120 
HESDMALRAD LSTARVDPFR RDKTININFF IHDPITGEQY SRDPRNIAKK AEAYLASTGI 

       130        140        150        160        170        180 
ADTAYFGPEA EFYVFDNVRF QTSANESFYH IDSEAGAWNT GAVENNRGYK VRYKGGYFPA 

       190        200        210        220        230        240 
PPVDHFADLR AEISLELDKN GLQVERQHHE VGTAGQAEIN YKFNTLLAAA DDLMLFKYIV 

       250        260        270        280        290        300 
KNVAWRNGKT ATFMPKPIFG DNGSGMHVHQ SLWQGGSPLF YDEQGYAGLS DTARYYIGGI 

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

       370        380        390        400        410        420 
PDPSSNPYLA FSALLMAGLD GVKNKIEPAE PIDKDLYELA PEEHANVQQV PTSLPAVLDA 

       430        440        450        460 
LEADNEYLQA GGVFTSDLIE TWIDYKRTNE IAPIQLRPHP HEFELYFDI 

« Hide

References

[1]"Mutants of Streptomyces roseosporus that express enhanced recombination within partially homologous genes."
Hosted T.J., Baltz R.H.
Microbiology 142:2803-2813(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: A54145.3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U58138 Genomic DNA. Translation: AAB41959.1.

3D structure databases

ProteinModelPortalP77958.
SMRP77958. 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_STRFL
AccessionPrimary (citable) accession number: P77958
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: October 16, 2013
This is version 67 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