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P14654 (GLN12_ORYSJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 cytosolic isozyme 1-2

EC=6.3.1.2
Alternative name(s):
Glutamate--ammonia ligase GLN1;2
Short name=OsGLN1;2
Glutamine synthetase root isozyme
OsGS1;2
Gene names
Name:GLN1-2
Synonyms:GSR, RGS8
Ordered Locus Names:Os03g0223400, LOC_Os03g12290
ORF Names:OJ1743A09.19
OrganismOryza sativa subsp. japonica (Rice) [Reference proteome]
Taxonomic identifier39947 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladeEhrhartoideaeOryzeaeOryza

Protein attributes

Sequence length357 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

High-affinity glutamine synthetase. May play a role in the primary assimilation of ammonium taken up by roots.

Catalytic activity

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

Subunit structure

Homooctamer By similarity.

Subcellular location

Cytoplasm.

Tissue specificity

Expressed in roots and at lower levels in leaf blades and spikelets (rice flower). Ref.2 Ref.4

Induction

By ammonium supply under nitrogen-limited condition. Ref.2

Sequence similarities

Belongs to the glutamine synthetase family.

Biophysicochemical properties

Kinetic parameters:

Measured at pH 7.8 and 30 degrees Celsius for all experiments.

KM=2.1 mM for glutamate Ref.2

KM=73 µM for ammonium

KM=530 µM for ATP

Vmax=94.7 nmol/sec/mg enzyme with glutamate as substrate

Vmax=98.1 nmol/sec/mg enzyme with ammonium as substrate

Vmax=109.1 nmol/sec/mg enzyme with ATP as substrate

Sequence caution

The sequence AAN05339.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processglutamine biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentchloroplast

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

plasmodesma

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

   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 – 357357Glutamine synthetase cytosolic isozyme 1-2
PRO_0000153186

Sequences

Sequence LengthMass (Da)Tools
P14654 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 2FF5634EDEF2E77E

FASTA35739,258
        10         20         30         40         50         60 
MANLTDLVNL NLSDCSDKII AEYIWVGGSG IDLRSKARTV KGPITDVSQL PKWNYDGSST 

        70         80         90        100        110        120 
GQAPGEDSEV ILYPQAIFKD PFRRGDNILV MCDCYTPQGE PIPTNKRHSA AKIFSHPDVV 

       130        140        150        160        170        180 
AEVPWYGIEQ EYTLLQKDVN WPLGWPVGGF PGPQGPYYCA AGAEKAFGRD IVDAHYKACI 

       190        200        210        220        230        240 
YAGINISGIN GEVMPGQWEF QVGPSVGIAA ADQVWVARYI LERVTEVAGV VLSLDPKPIP 

       250        260        270        280        290        300 
GDWNGAGAHT NFSTKSMREP GGYEVIKKAI DKLALRHKEH IAAYGEGNER RLTGRHETAD 

       310        320        330        340        350 
INTFKWGVAN RGASIRVGRD TEKEGKGYFE DRRPASNMDP YVVTGMIAET TLLWKQN 

« Hide

References

« Hide 'large scale' references
[1]"Three cDNA sequences coding for glutamine synthetase polypeptides in Oryza sativa L."
Sakamoto A., Ogawa M., Masumura T., Shibata D., Takeba G., Tanaka K., Fujii S.
Plant Mol. Biol. 13:611-614(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Kinmaze.
Tissue: Root.
[2]"Biochemical background and compartmentalized functions of cytosolic glutamine synthetase for active ammonium assimilation in rice roots."
Ishiyama K., Inoue E., Tabuchi M., Yamaya T., Takahashi H.
Plant Cell Physiol. 45:1640-1647(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, INDUCTION.
Strain: cv. Sasanishiki.
Tissue: Root.
[3]"Sequence, annotation, and analysis of synteny between rice chromosome 3 and diverged grass species."
The rice chromosome 3 sequencing consortium
Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B., Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T., Fadrosh D., Bera J., Weaver B., Jin S. expand/collapse author list , Johri S., Reardon M., Webb K., Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T., Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R., Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J., Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S., Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M., Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M., Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L., O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R., Jin W., Lee H.R., Jiang J., Jackson S.
Genome Res. 15:1284-1291(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Nipponbare.
[4]"Severe reduction in growth rate and grain filling of rice mutants lacking OsGS1;1, a cytosolic glutamine synthetase1;1."
Tabuchi M., Sugiyama K., Ishiyama K., Inoue E., Sato T., Takahashi H., Yamaya T.
Plant J. 42:641-651(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X14244 mRNA. Translation: CAA32460.1.
AB180688 mRNA. Translation: BAD77931.1.
AC105364 Genomic DNA. Translation: AAN05339.1. Sequence problems.
PIRAJRZQB. S07469.
RefSeqNP_001049424.1. NM_001055959.2.
UniGeneOs.12728.

3D structure databases

ProteinModelPortalP14654.
SMRP14654. Positions 4-355.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbP14654.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsOS03T0223400-01; OS03T0223400-01; OS03G0223400.
GeneID4332108.
KEGGosa:4332108.

Organism-specific databases

GrameneP14654.

Phylogenomic databases

eggNOGCOG0174.
HOGENOMHOG000061500.
KOK01915.
OMAKSFGRDV.

Enzyme and pathway databases

BRENDA6.3.1.2. 4460.
SABIO-RKP14654.

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 nameGLN12_ORYSJ
AccessionPrimary (citable) accession number: P14654
Secondary accession number(s): Q5NU22, Q8GTZ3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: May 14, 2014
This is version 98 of the entry and version 1 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

Oryza sativa (rice)

Index of Oryza sativa entries and their corresponding gene designations