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P08282 (GLNA1_PEA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 76. 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 nodule isozyme

EC=6.3.1.2
Alternative name(s):
Cytosolic GS1
Glutamate--ammonia ligase
Gene names
Name:GS1
OrganismPisum sativum (Garden pea)
Taxonomic identifier3888 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

Protein attributes

Sequence length355 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine.

Subunit structure

Homooctamer.

Subcellular location

Cytoplasm.

Miscellaneous

In pea there are distinct isozymes in leaves, roots and nodules.

Irreversibly inhibited by the herbicide L-phosphinothricin (PPT).

This root isozyme is responsible for the assimilation of ammonia fixed by bacteroids.

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 – 355355Glutamine synthetase nodule isozyme
PRO_0000153188

Sequences

Sequence LengthMass (Da)Tools
P08282 [UniParc].

Last modified July 1, 1989. Version 2.
Checksum: 2AB833FAD7AA3687

FASTA35538,928
        10         20         30         40         50         60 
MSLSDLINLD LSGTTEKIIA EYIWIGGSGL DLRCKARTLP GPVTDPSELP KWNYDGSSTG 

        70         80         90        100        110        120 
QAPGQDSEVI LYPQAIFKDP FRRGNHILVM CDAYSPAGEP IPTNKRHAAA KVFSHPDVVA 

       130        140        150        160        170        180 
EETWYGIEQE YTLLQKDINW PLGWPAGGYP GPQGPYYCSV GADKAFGRDV VEAHYKACLF 

       190        200        210        220        230        240 
AGINISGING EVMPGQWEFQ VGPSVGISAG DEIWVARYIL ERITEVAGVV LTFDPKPIKG 

       250        260        270        280        290        300 
DWNGAGAHTN YSTKSMREDG GYEIIKKAIE KLGKRLPEHI SAYGEGNERR LTGKHETADI 

       310        320        330        340        350 
NTFSWGVANR GASVRVGRDT EKEGKGYFED RRPASNMDPY VVTSMIAETT ILLKP 

« Hide

References

[1]"Chloroplast and cytosolic glutamine synthetase are encoded by homologous nuclear genes which are differentially expressed in vivo."
Tingey S.V., Tsai F., Edwards J., Walker E.L., Coruzzi G.M.
J. Biol. Chem. 263:9651-9657(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Glutamine synthetase genes of pea encode distinct polypeptides which are differentially expressed in leaves, roots and nodules."
Tingey S.V., Walker E.L., Coruzzi G.M.
EMBO J. 6:1-9(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 97-355.
Strain: cv. Sparkle.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M20663 mRNA. Translation: AAA33669.1.
X05515 mRNA. Translation: CAA29058.1.
PIRAJPMQ1. B28089.

3D structure databases

ProteinModelPortalP08282.
SMRP08282. Positions 3-354.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP08282.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.30.590.10. 1 hit.
InterProIPR008147. Gln_synt_beta.
IPR014746. Gln_synth/guanido_kin_cat_dom.
IPR008146. Gln_synth_cat_dom.
IPR027303. Gln_synth_gly_rich_site.
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.
PROSITEPS00180. GLNA_1. 1 hit.
PS00181. GLNA_ATP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLNA1_PEA
AccessionPrimary (citable) accession number: P08282
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: July 1, 1989
Last modified: February 19, 2014
This is version 76 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families