ID   GLN12_ORYSJ             Reviewed;         357 AA.
AC   P14654; Q10PS4; Q5NU22; Q8GTZ3;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   27-MAR-2024, entry version 146.
DE   RecName: Full=Glutamine synthetase cytosolic isozyme 1-2 {ECO:0000305};
DE            EC=6.3.1.2 {ECO:0000269|PubMed:15574840};
DE   AltName: Full=Glutamate--ammonia ligase GLN1;2 {ECO:0000305};
DE            Short=OsGLN1;2 {ECO:0000303|PubMed:15574840};
DE   AltName: Full=Glutamine synthetase root isozyme {ECO:0000305};
DE   AltName: Full=OsGS1;2 {ECO:0000312|EMBL:BAD77931.1};
GN   Name=GLN1-2 {ECO:0000305};
GN   Synonyms=GSR, RGS8 {ECO:0000303|PubMed:2577497};
GN   OrderedLocusNames=Os03g0223400 {ECO:0000312|EMBL:BAS83037.1},
GN   LOC_Os03g12290 {ECO:0000312|EMBL:ABF94717.1};
GN   ORFNames=OJ1743A09.19 {ECO:0000312|EMBL:AAN05339.1}, OsJ_09974
GN   {ECO:0000312|EMBL:EEE58620.1};
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Kinmaze; TISSUE=Root;
RX   PubMed=2577497; DOI=10.1007/bf00027323;
RA   Sakamoto A., Ogawa M., Masumura T., Shibata D., Takeba G., Tanaka K.,
RA   Fujii S.;
RT   "Three cDNA sequences coding for glutamine synthetase polypeptides in Oryza
RT   sativa L.";
RL   Plant Mol. Biol. 13:611-614(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND INDUCTION.
RC   STRAIN=cv. Sasanishiki; TISSUE=Root;
RX   PubMed=15574840; DOI=10.1093/pcp/pch190;
RA   Ishiyama K., Inoue E., Tabuchi M., Yamaya T., Takahashi H.;
RT   "Biochemical background and compartmentalized functions of cytosolic
RT   glutamine synthetase for active ammonium assimilation in rice roots.";
RL   Plant Cell Physiol. 45:1640-1647(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16109971; DOI=10.1101/gr.3869505;
RG   The rice chromosome 3 sequencing consortium;
RA   Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA   Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA   Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA   Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA   Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA   Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA   Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA   Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA   Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA   Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA   O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA   Jin W., Lee H.R., Jiang J., Jackson S.;
RT   "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT   and diverged grass species.";
RL   Genome Res. 15:1284-1291(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [6]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RG   The rice full-length cDNA consortium;
RT   "Oryza sativa full length cDNA.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   TISSUE SPECIFICITY.
RX   PubMed=15918879; DOI=10.1111/j.1365-313x.2005.02406.x;
RA   Tabuchi M., Sugiyama K., Ishiyama K., Inoue E., Sato T., Takahashi H.,
RA   Yamaya T.;
RT   "Severe reduction in growth rate and grain filling of rice mutants lacking
RT   OsGS1;1, a cytosolic glutamine synthetase1;1.";
RL   Plant J. 42:641-651(2005).
RN   [10]
RP   INDUCTION.
RX   PubMed=17350935; DOI=10.1093/jxb/erm016;
RA   Tabuchi M., Abiko T., Yamaya T.;
RT   "Assimilation of ammonium ions and reutilization of nitrogen in rice (Oryza
RT   sativa L.).";
RL   J. Exp. Bot. 58:2319-2327(2007).
RN   [11]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=23509111; DOI=10.1093/pcp/pct046;
RA   Funayama K., Kojima S., Tabuchi-Kobayashi M., Sawa Y., Nakayama Y.,
RA   Hayakawa T., Yamaya T.;
RT   "Cytosolic glutamine synthetase1;2 is responsible for the primary
RT   assimilation of ammonium in rice roots.";
RL   Plant Cell Physiol. 54:934-943(2013).
RN   [12]
RP   FUNCTION.
RX   PubMed=24743556; DOI=10.1371/journal.pone.0095581;
RA   Bao A., Zhao Z., Ding G., Shi L., Xu F., Cai H.;
RT   "Accumulated expression level of cytosolic glutamine synthetase 1 gene
RT   (OsGS1;1 or OsGS1;2) alter plant development and the carbon-nitrogen
RT   metabolic status in rice.";
RL   PLoS ONE 9:e95581-e95581(2014).
RN   [13]
RP   FUNCTION.
RX   PubMed=25429996; DOI=10.1111/tpj.12731;
RA   Ohashi M., Ishiyama K., Kusano M., Fukushima A., Kojima S., Hanada A.,
RA   Kanno K., Hayakawa T., Seto Y., Kyozuka J., Yamaguchi S., Yamaya T.;
RT   "Lack of cytosolic glutamine synthetase1;2 in vascular tissues of axillary
RT   buds causes severe reduction in their outgrowth and disorder of metabolic
RT   balance in rice seedlings.";
RL   Plant J. 81:347-356(2015).
RN   [14]
RP   FUNCTION.
RX   PubMed=28186255; DOI=10.1093/pcp/pcx022;
RA   Ohashi M., Ishiyama K., Kojima S., Kojima M., Sakakibara H., Yamaya T.,
RA   Hayakawa T.;
RT   "Lack of cytosolic glutamine synthetase1;2 activity reduces nitrogen-
RT   dependent biosynthesis of cytokinin required for axillary bud outgrowth in
RT   rice seedlings.";
RL   Plant Cell Physiol. 58:679-690(2017).
CC   -!- FUNCTION: High-affinity glutamine synthetase involved in ammonium
CC       assimilation (Probable). Plays an important role in the primary
CC       assimilation of ammonium taken up by roots (PubMed:23509111). Plays a
CC       role in maintaining nitrogen metabolic balance during ammonium
CC       assimilation, thus controlling plant growth and development
CC       (PubMed:24743556). Reassimilates ammonium generated during
CC       lignification within developing tillers, which is probably required for
CC       the outgrowth of axillary buds (PubMed:25429996). Required for
CC       nitrogen-dependent biosynthesis of cytokinin (PubMed:28186255). Active
CC       cytokinin in axillary bud meristem is required for axillary bud
CC       outgrowth and necessary for tillering (PubMed:28186255).
CC       {ECO:0000269|PubMed:23509111, ECO:0000269|PubMed:24743556,
CC       ECO:0000269|PubMed:25429996, ECO:0000269|PubMed:28186255,
CC       ECO:0000305|PubMed:15574840}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine +
CC         phosphate; Xref=Rhea:RHEA:16169, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.1.2;
CC         Evidence={ECO:0000269|PubMed:15574840};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16170;
CC         Evidence={ECO:0000269|PubMed:15574840};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.1 mM for glutamate {ECO:0000269|PubMed:15574840};
CC         KM=73 uM for ammonium {ECO:0000269|PubMed:15574840};
CC         KM=530 uM for ATP {ECO:0000269|PubMed:15574840};
CC         Vmax=94.7 nmol/sec/mg enzyme with glutamate as substrate
CC         {ECO:0000269|PubMed:15574840};
CC         Vmax=98.1 nmol/sec/mg enzyme with ammonium as substrate
CC         {ECO:0000269|PubMed:15574840};
CC         Vmax=109.1 nmol/sec/mg enzyme with ATP as substrate
CC         {ECO:0000269|PubMed:15574840};
CC         Note=Measured at pH 7.8 and 30 degrees Celsius for all experiments.
CC         {ECO:0000269|PubMed:15574840};
CC   -!- SUBUNIT: Homooctamer. {ECO:0000250|UniProtKB:P16580}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots and at lower levels in leaf
CC       blades and spikelets (rice flower). {ECO:0000269|PubMed:15574840,
CC       ECO:0000269|PubMed:15918879}.
CC   -!- INDUCTION: Induced in roots by ammonium supply.
CC       {ECO:0000269|PubMed:15574840, ECO:0000269|PubMed:17350935}.
CC   -!- DISRUPTION PHENOTYPE: Reduced number of tillers and panicles.
CC       {ECO:0000269|PubMed:23509111}.
CC   -!- MISCELLANEOUS: Plants overexpressing GLN1-2 exhibit a poor plant growth
CC       phenotype and yield, and decreased carbon/nitrogen ratio in the stem
CC       caused by the accumulation of nitrogen in the stem.
CC       {ECO:0000269|PubMed:24743556}.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN05339.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; X14244; CAA32460.1; -; mRNA.
DR   EMBL; AB180688; BAD77931.1; -; mRNA.
DR   EMBL; AC105364; AAN05339.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; DP000009; ABF94717.1; -; Genomic_DNA.
DR   EMBL; AP008209; BAF11338.1; -; Genomic_DNA.
DR   EMBL; AP014959; BAS83037.1; -; Genomic_DNA.
DR   EMBL; CM000140; EEE58620.1; -; Genomic_DNA.
DR   EMBL; AK243037; BAH01417.1; -; mRNA.
DR   PIR; S07469; AJRZQB.
DR   RefSeq; XP_015631679.1; XM_015776193.1.
DR   AlphaFoldDB; P14654; -.
DR   SMR; P14654; -.
DR   STRING; 39947.P14654; -.
DR   PaxDb; 39947-P14654; -.
DR   EnsemblPlants; Os03t0223400-01; Os03t0223400-01; Os03g0223400.
DR   GeneID; 4332108; -.
DR   Gramene; Os03t0223400-01; Os03t0223400-01; Os03g0223400.
DR   KEGG; osa:4332108; -.
DR   eggNOG; KOG0683; Eukaryota.
DR   HOGENOM; CLU_036762_0_1_1; -.
DR   InParanoid; P14654; -.
DR   OMA; QIMGMVE; -.
DR   OrthoDB; 1115057at2759; -.
DR   BRENDA; 6.3.1.2; 8948.
DR   PlantReactome; R-OSA-1119291; Nitrate assimilation.
DR   PlantReactome; R-OSA-1119293; Glutamine biosynthesis I.
DR   PlantReactome; R-OSA-1119443; Ammonia assimilation cycle.
DR   SABIO-RK; P14654; -.
DR   Proteomes; UP000000763; Chromosome 3.
DR   Proteomes; UP000007752; Chromosome 3.
DR   Proteomes; UP000059680; Chromosome 3.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004356; F:glutamine synthetase activity; IBA:GO_Central.
DR   GO; GO:0006542; P:glutamine biosynthetic process; IBA:GO_Central.
DR   Gene3D; 3.10.20.70; Glutamine synthetase, N-terminal domain; 1.
DR   Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 1.
DR   InterPro; IPR008147; Gln_synt_N.
DR   InterPro; IPR036651; Gln_synt_N_sf.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   InterPro; IPR008146; Gln_synth_cat_dom.
DR   InterPro; IPR027303; Gln_synth_gly_rich_site.
DR   InterPro; IPR027302; Gln_synth_N_conserv_site.
DR   PANTHER; PTHR20852; GLUTAMINE SYNTHETASE; 1.
DR   PANTHER; PTHR20852:SF109; GLUTAMINE SYNTHETASE CYTOSOLIC ISOZYME 1-2; 1.
DR   Pfam; PF00120; Gln-synt_C; 1.
DR   Pfam; PF03951; Gln-synt_N; 1.
DR   SMART; SM01230; Gln-synt_C; 1.
DR   SUPFAM; SSF54368; Glutamine synthetase, N-terminal domain; 1.
DR   SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR   PROSITE; PS00180; GLNA_1; 1.
DR   PROSITE; PS00181; GLNA_ATP; 1.
DR   PROSITE; PS51986; GS_BETA_GRASP; 1.
DR   PROSITE; PS51987; GS_CATALYTIC; 1.
DR   Genevisible; P14654; OS.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..357
FT                   /note="Glutamine synthetase cytosolic isozyme 1-2"
FT                   /id="PRO_0000153186"
FT   DOMAIN          19..99
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT   DOMAIN          106..357
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
SQ   SEQUENCE   357 AA;  39258 MW;  2FF5634EDEF2E77E CRC64;
     MANLTDLVNL NLSDCSDKII AEYIWVGGSG IDLRSKARTV KGPITDVSQL PKWNYDGSST
     GQAPGEDSEV ILYPQAIFKD PFRRGDNILV MCDCYTPQGE PIPTNKRHSA AKIFSHPDVV
     AEVPWYGIEQ EYTLLQKDVN WPLGWPVGGF PGPQGPYYCA AGAEKAFGRD IVDAHYKACI
     YAGINISGIN GEVMPGQWEF QVGPSVGIAA ADQVWVARYI LERVTEVAGV VLSLDPKPIP
     GDWNGAGAHT NFSTKSMREP GGYEVIKKAI DKLALRHKEH IAAYGEGNER RLTGRHETAD
     INTFKWGVAN RGASIRVGRD TEKEGKGYFE DRRPASNMDP YVVTGMIAET TLLWKQN
//