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P46033 (GLNA1_FRAAL) 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:glnA
OrganismFrankia alni
Taxonomic identifier1859 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesFrankineaeFrankiaceaeFrankia

Protein attributes

Sequence length474 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.

Miscellaneous

Two forms of glutamine synthetase (GSI and GSII) can be found in this nitrogen fixing bacteria, GSI is a typical prokaryotic glutamine synthetase whereas GSII is similar to the eukaryotic enzyme.

Sequence similarities

Belongs to the glutamine synthetase family.

Ontologies

Keywords
   Biological processNitrogen fixation
   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: UniProtKB-KW

   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 – 474474Glutamine synthetase 1
PRO_0000153221

Amino acid modifications

Modified residue4021O-AMP-tyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
P46033 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: FE1DB19AC1735652

FASTA47453,952
        10         20         30         40         50         60 
MFTKAEDVLR YIRDEDVQFI DVRFCDLPGI MQHFTIPTQV FAESVFTDGL MFDGSSIRGF 

        70         80         90        100        110        120 
QAIHESDMLL LPDPQTAFVD PFREHKTLAM TFFIHDPITK EQYSRDPRNI AKKAETYLRG 

       130        140        150        160        170        180 
TSIADTAYFG PEAEFYIFDD VRYDYNPYGS MHHVDSVEAA WNTSRKEEGG NLGYKPRFKG 

       190        200        210        220        230        240 
GYFPVPPTDH FTDLRSEMTR VLYETGITVE MQHHEVGTAG QAEIDIRYDT LLKTADNLML 

       250        260        270        280        290        300 
YKYVIRNVAR SRGKTVTFMP KPLFEDNGSG MHVHSSLWKD GEPLFYSPNG YGGLSDTARY 

       310        320        330        340        350        360 
YIGGLLHHAP ALLAFTNPTT NSYRRLVPGY EAPVNLVYSA RNRSACCRIP LGGDSPKAKR 

       370        380        390        400        410        420 
VEFRVPDPSC NPYLAFAAML MAGLDGIRNK IDPPDPIDKD LYELPPDELA AVPQVPGSLE 

       430        440        450        460        470 
KVLDALEADN DFLREGDVFT TDLIETWLEY KRLNEVDAIR LRPHPYEFTL YYDI 

« Hide

References

[1]"Close linkage of genes encoding glutamine synthetases I and II in Frankia alni CpI1."
Hosted T.J., Rochefort D.A., Benson D.R.
J. Bacteriol. 175:3679-3684(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: CpI1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L10631 Genomic DNA. No translation available.
PIRA40598.

3D structure databases

ProteinModelPortalP46033.
SMRP46033. Positions 6-474.
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_FRAAL
AccessionPrimary (citable) accession number: P46033
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
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