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P13564 (GLNA2_HORVU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 85. 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 leaf isozyme, chloroplastic

EC=6.3.1.2
Alternative name(s):
GS2
Glutamate--ammonia ligase
OrganismHordeum vulgare (Barley)
Taxonomic identifier4513 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeHordeum

Protein attributes

Sequence length434 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

The light-modulated chloroplast enzyme, encoded by a nuclear gene and expressed primarily in leaves, is responsible for the reassimilation of the ammonia generated by photorespiration.

Catalytic activity

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

Subunit structure

Homooctamer.

Subcellular location

Plastidchloroplast.

Miscellaneous

In barley, there are distinct isozymes in the chloroplast, and cytoplasm.

Sequence similarities

Belongs to the glutamine synthetase family.

Ontologies

Keywords
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
Gene Ontology (GO)
   Biological_processglutamine biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentchloroplast

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

Transit peptide1 – 5454Chloroplast
Chain55 – 434380Glutamine synthetase leaf isozyme, chloroplastic
PRO_0000011178

Experimental info

Sequence conflict9 – 2719GAGGC…EGQDG → AQAVVQAMQCQVGVRGRTA in CAA34131. Ref.2
Sequence conflict411S → R in CAA34131. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P13564 [UniParc].

Last modified November 1, 1990. Version 2.
Checksum: FC47F5685EFC0D1E

FASTA43447,094
        10         20         30         40         50         60 
MQVRRDDDGA GGCAGDAVPG GGEGQDGVPA RQPAGRVWGV SRAARATSGF KVLALGPETT 

        70         80         90        100        110        120 
GVIQRMQQLL DMDTTPFTDK IIAEYIWVGG SGIDLRSKSR TISKPVEDPS ELPKWNYDGS 

       130        140        150        160        170        180 
STGQAPGEDS EVILYPQAIF KDPFRGGNNI LVICDTYTPQ GEPIPTNKRH MAAQIFSDPK 

       190        200        210        220        230        240 
VTSQVPWFGI EQEYTLMQRD VNWPLGWPVG GYPGPQGPYY CAVGSDKSFG RDISDAHYKA 

       250        260        270        280        290        300 
CLYAGIEISG TNGEVMPGQW EYQVGPSVGI DAGDHIWASR YILERITEQA GVVLTLDPKP 

       310        320        330        340        350        360 
IQGDWNGAGC HTNYSTLSMR EDGGFDVIKK AILNLSLRHD LHIAAYGEGN ERRLTGLHET 

       370        380        390        400        410        420 
ASISDFSWGV ANRGCSIRVG RDTEAKGKGY LEDRRPASNM DPYTVTALLA ETTILWEPTL 

       430 
EAEALAAKKL ALKV 

« Hide

References

[1]"A cDNA sequence coding for glutamine synthetase in Hordeum vulgare L."
Stroman P., Baima S., Casadoro G.
Plant Mol. Biol. 15:161-163(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Molecular analysis of barley mutants deficient in chloroplast glutamine synthetase."
Freeman J., Marquez A.J., Wallsgrove R.M., Saarelainen R., Forde B.G.
Plant Mol. Biol. 14:297-311(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-434.
Strain: cv. Maris Mink.
Tissue: Leaf.
[3]"Characterization of a cDNA clone for barley leaf glutamine synthetase."
Baima S., Haegi A., Stroman P., Casadoro G.
Carlsberg Res. Commun. 54:1-9(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 48-434.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X53580 mRNA. Translation: CAA37643.1.
X16000 mRNA. Translation: CAA34131.1.
PIRAJBHQ. S11865.
UniGeneHv.733.

3D structure databases

ProteinModelPortalP13564.
SMRP13564. Positions 66-417.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

GrameneP13564.

Gene expression databases

GenevestigatorP13564.

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 nameGLNA2_HORVU
AccessionPrimary (citable) accession number: P13564
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: November 1, 1990
Last modified: June 11, 2014
This is version 85 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