GLN12_ORYSJ
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 25-MAY-2022, entry version 139.
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}; 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},
GN OsJ_09974 {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; 4530.OS03T0223400-01; -.
DR PaxDb; P14654; -.
DR PRIDE; 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; 784869at2759; -.
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 Genevisible; P14654; OS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004356; F:glutamate-ammonia ligase activity; IBA:GO_Central.
DR GO; GO:0006542; P:glutamine biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.10.20.70; -; 1.
DR InterPro; IPR008147; Gln_synt_b-grasp.
DR InterPro; IPR036651; Gln_synt_N.
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 Pfam; PF00120; Gln-synt_C; 1.
DR Pfam; PF03951; Gln-synt_N; 1.
DR SMART; SM01230; Gln-synt_C; 1.
DR SUPFAM; SSF54368; SSF54368; 1.
DR SUPFAM; SSF55931; SSF55931; 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.
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
