GLN11_ORYSJ
ID GLN11_ORYSJ Reviewed; 356 AA.
AC P14656; Q0DXS9; Q6Z753;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Glutamine synthetase cytosolic isozyme 1-1 {ECO:0000305};
DE EC=6.3.1.2 {ECO:0000269|PubMed:15574840};
DE AltName: Full=Glutamate--ammonia ligase GLN1;1 {ECO:0000305};
DE Short=OsGLN1;1 {ECO:0000303|PubMed:15574840};
DE AltName: Full=Glutamine synthetase shoot isozyme {ECO:0000305};
DE AltName: Full=OsGS1;1 {ECO:0000303|Ref.2};
GN Name=GLN1-1 {ECO:0000305}; Synonyms=RGS28 {ECO:0000303|PubMed:2577497};
GN OrderedLocusNames=Os02g0735200 {ECO:0000312|EMBL:BAS80796.1},
GN LOC_Os02g50240 {ECO:0000305};
GN ORFNames=OsJ_08295 {ECO:0000312|EMBL:EAZ24534.1},
GN P0487D09.8 {ECO:0000312|EMBL:BAD15892.1};
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=Shoot;
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 [GENOMIC DNA / MRNA].
RC STRAIN=cv. Sasanishiki;
RA Kojima S., Hanzawa S., Hayakawa T., Hayashi M., Yamaya T.;
RT "Nucleotide sequence of a genomic DNA and a cDNA encoding cytosolic
RT glutamine synthetase in Sasanishiki, a seading cultivar of rice (Oryza
RT sativa L) in northern Japan.";
RL (er) Plant Gene Register PGR00-048(2000).
RN [3]
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 [4]
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 [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [8]
RP PROTEIN SEQUENCE OF 204-213.
RC STRAIN=cv. Nipponbare; TISSUE=Callus;
RX PubMed=14681440; DOI=10.1093/nar/gkh020;
RA Komatsu S., Kojima K., Suzuki K., Ozaki K., Higo K.;
RT "Rice proteome database based on two-dimensional polyacrylamide gel
RT electrophoresis: its status in 2003.";
RL Nucleic Acids Res. 32:D388-D392(2004).
RN [9]
RP DEVELOPMENTAL STAGE.
RX PubMed=12060286; DOI=10.1034/j.1399-3054.2001.1130314.x;
RA Sakurai N., Katayama Y., Yamaya T.;
RT "Overlapping expression of cytosolic glutamine synthetase and phenylalanine
RT ammonia-lyase in immature leaf blades of rice.";
RL Physiol. Plantarum 113:400-408(2001).
RN [10]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND
RP INDUCTION.
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 [11]
RP FUNCTION, DISRUPTION PHENOTYPE, AND 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 [12]
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 [13]
RP FUNCTION.
RX PubMed=21255162; DOI=10.1111/j.1365-313x.2011.04506.x;
RA Kusano M., Tabuchi M., Fukushima A., Funayama K., Diaz C., Kobayashi M.,
RA Hayashi N., Tsuchiya Y.N., Takahashi H., Kamata A., Yamaya T., Saito K.;
RT "Metabolomics data reveal a crucial role of cytosolic glutamine synthetase
RT 1;1 in coordinating metabolic balance in rice.";
RL Plant J. 66:456-466(2011).
RN [14]
RP INDUCTION.
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 [15]
RP INDUCTION.
RX PubMed=23743654; DOI=10.1007/s00299-013-1464-8;
RA Lee H.J., Abdula S.E., Jang D.W., Park S.H., Yoon U.H., Jung Y.J.,
RA Kang K.K., Nou I.S., Cho Y.G.;
RT "Overexpression of the glutamine synthetase gene modulates oxidative stress
RT response in rice after exposure to cadmium stress.";
RL Plant Cell Rep. 32:1521-1529(2013).
RN [16]
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 [17]
RP FUNCTION.
RX PubMed=32024696; DOI=10.1104/pp.19.01118;
RA Kusano M., Fukushima A., Tabuchi-Kobayashi M., Funayama K., Kojima S.,
RA Maruyama K., Yamamoto Y.Y., Nishizawa T., Kobayashi M., Wakazaki M.,
RA Sato M., Toyooka K., Osanai-Kondo K., Utsumi Y., Seki M., Fukai C.,
RA Saito K., Yamaya T.;
RT "Cytosolic GLUTAMINE SYNTHETASE1;1 modulates metabolism and chloroplast
RT development in roots.";
RL Plant Physiol. 182:1894-1909(2020).
CC -!- FUNCTION: High-affinity glutamine synthetase involved in ammonium
CC assimilation (PubMed:15918879, PubMed:21255162). Seems to be a major
CC component of the cytosolic glutamine synthetic pathway in leaf blades
CC (PubMed:15918879, PubMed:21255162). Plays an important role in
CC maintaining carbon and nitrogen metabolic balance during ammonium
CC assimilation in shoots and roots, thus controlling plant growth and
CC development (PubMed:21255162, PubMed:24743556). Plays an important role
CC in maintaining broad range of metabolites and transcripts involved in
CC the maintenance of plant metabolic homeostasis and development of
CC plastid in roots (PubMed:32024696). {ECO:0000269|PubMed:15918879,
CC ECO:0000269|PubMed:21255162, ECO:0000269|PubMed:24743556,
CC ECO:0000269|PubMed:32024696}.
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=1.9 mM for glutamate {ECO:0000269|PubMed:15574840};
CC KM=27 uM for ammonium {ECO:0000269|PubMed:15574840};
CC KM=450 uM for ATP {ECO:0000269|PubMed:15574840};
CC Vmax=190 nmol/sec/mg enzyme with glutamate as substrate
CC {ECO:0000269|PubMed:15574840};
CC Vmax=186.3 nmol/sec/mg enzyme with ammonium as substrate
CC {ECO:0000269|PubMed:15574840};
CC Vmax=170.2 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: Highly expressed in leaf blades, at intermediate
CC levels in spikelets (rice flower) and at lower levels in roots.
CC {ECO:0000269|PubMed:15574840, ECO:0000269|PubMed:15918879}.
CC -!- DEVELOPMENTAL STAGE: Expressed in metaxylem and phloem of parenchyma
CC cells and in sclerenchyma cells of developing leaf blades.
CC {ECO:0000269|PubMed:12060286}.
CC -!- INDUCTION: Induced in roots under nitrogen-limited condition
CC (PubMed:15574840, PubMed:23509111). Down-regulated in roots under
CC ammonium supply (PubMed:17350935). Down-regulated by treatment with
CC cadmium (PubMed:23743654). {ECO:0000269|PubMed:15574840,
CC ECO:0000269|PubMed:17350935, ECO:0000269|PubMed:23509111,
CC ECO:0000269|PubMed:23743654}.
CC -!- DISRUPTION PHENOTYPE: Plants show marked reduction in leaf blades
CC elongation, plant height, panicle size and grain filling.
CC {ECO:0000269|PubMed:15918879}.
CC -!- MISCELLANEOUS: Plants overexpressing GLN1-1 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}.
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DR EMBL; X14245; CAA32461.1; -; mRNA.
DR EMBL; AB037595; BAA95679.1; -; mRNA.
DR EMBL; AB037664; BAA95678.1; -; Genomic_DNA.
DR EMBL; AP004880; BAD15892.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF09959.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS80796.1; -; Genomic_DNA.
DR EMBL; CM000139; EAZ24534.1; -; Genomic_DNA.
DR EMBL; AK061157; BAG87764.1; -; mRNA.
DR EMBL; AK104987; BAG97064.1; -; mRNA.
DR PIR; S07470; AJRZQG.
DR RefSeq; XP_015626102.1; XM_015770616.1.
DR AlphaFoldDB; P14656; -.
DR SMR; P14656; -.
DR IntAct; P14656; 1.
DR STRING; 4530.OS02T0735200-02; -.
DR PaxDb; P14656; -.
DR PRIDE; P14656; -.
DR EnsemblPlants; Os02t0735200-01; Os02t0735200-01; Os02g0735200.
DR EnsemblPlants; Os02t0735200-02; Os02t0735200-02; Os02g0735200.
DR EnsemblPlants; Os02t0735200-03; Os02t0735200-03; Os02g0735200.
DR GeneID; 4330649; -.
DR Gramene; Os02t0735200-01; Os02t0735200-01; Os02g0735200.
DR Gramene; Os02t0735200-02; Os02t0735200-02; Os02g0735200.
DR Gramene; Os02t0735200-03; Os02t0735200-03; Os02g0735200.
DR KEGG; osa:4330649; -.
DR eggNOG; KOG0683; Eukaryota.
DR HOGENOM; CLU_036762_0_1_1; -.
DR InParanoid; P14656; -.
DR OMA; VAMSVSH; -.
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; P14656; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000007752; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR Genevisible; P14656; 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; Direct protein sequencing; Ligase;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..356
FT /note="Glutamine synthetase cytosolic isozyme 1-1"
FT /id="PRO_0000153187"
FT DOMAIN 19..99
FT /note="GS beta-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT DOMAIN 106..356
FT /note="GS catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
SQ SEQUENCE 356 AA; 39201 MW; 7D21F7C31B7CB4DD CRC64;
MASLTDLVNL NLSDTTEKII AEYIWIGGSG MDLRSKARTL SGPVTDPSKL PKWNYDGSST
GQAPGEDSEV ILYPQAIFKD PFRKGNNILV MCDCYTPAGE PIPTNKRHNA AKIFSSPEVA
SEEPWYGIEQ EYTLLQKDIN WPLGWPVGGF PGPQGPYYCG IGADKSFGRD IVDSHYKACL
YAGINISGIN GEVMPGQWEF QVGPSVGISA GDQVWVARYI LERITEIAGV VVSFDPKPIP
GDWNGAGAHT NYSTKSMRND GGYEIIKSAI EKLKLRHKEH ISAYGEGNER RLTGRHETAD
INTFSWGVAN RGASVRVGRE TEQNGKGYFE DRRPASNMDP YIVTSMIAET TIIWKP
