GLN11_ARATH
ID GLN11_ARATH Reviewed; 356 AA.
AC Q56WN1; Q9FHR0;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Glutamine synthetase cytosolic isozyme 1-1;
DE EC=6.3.1.2 {ECO:0000269|PubMed:14757761};
DE AltName: Full=Glutamate--ammonia ligase GLN1;1 {ECO:0000303|PubMed:14757761};
DE Short=GLN1;1 {ECO:0000303|PubMed:14757761};
GN Name=GLN1-1; OrderedLocusNames=At5g37600; ORFNames=K12B20.50;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 145-356.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INDUCTION.
RX PubMed=10482686; DOI=10.1104/pp.121.1.301;
RA Oliveira I.C., Coruzzi G.M.;
RT "Carbon and amino acids reciprocally modulate the expression of glutamine
RT synthetase in Arabidopsis.";
RL Plant Physiol. 121:301-310(1999).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE
RP SPECIFICITY, AND INDUCTION.
RX PubMed=14757761; DOI=10.1074/jbc.m313710200;
RA Ishiyama K., Inoue E., Watanabe-Takahashi A., Obara M., Yamaya T.,
RA Takahashi H.;
RT "Kinetic properties and ammonium-dependent regulation of cytosolic
RT isoenzymes of glutamine synthetase in Arabidopsis.";
RL J. Biol. Chem. 279:16598-16605(2004).
RN [7]
RP INTERACTION WITH CRK3, PHOSPHORYLATION BY CRK3, INDUCTION BY LEAF
RP SENESCENCE, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=16472779; DOI=10.1016/j.bbrc.2006.01.100;
RA Li R.-J., Hua W., Lu Y.-T.;
RT "Arabidopsis cytosolic glutamine synthetase AtGLN1;1 is a potential
RT substrate of AtCRK3 involved in leaf senescence.";
RL Biochem. Biophys. Res. Commun. 342:119-126(2006).
RN [8]
RP INTERACTION WITH GRF3.
RX PubMed=21094157; DOI=10.1016/j.febslet.2010.11.025;
RA Shin R., Jez J.M., Basra A., Zhang B., Schachtman D.P.;
RT "14-3-3 proteins fine-tune plant nutrient metabolism.";
RL FEBS Lett. 585:143-147(2011).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: High-affinity glutamine synthetase which catalyzes the
CC synthesis of glutamine from ammonium and glutamate (PubMed:14757761).
CC May contribute to the homeostatic control of glutamine synthesis in
CC roots. {ECO:0000269|PubMed:14757761}.
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:14757761};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16170;
CC Evidence={ECO:0000305|PubMed:14757761};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.1 mM for glutamate {ECO:0000269|PubMed:14757761};
CC KM=10 uM for ammonium {ECO:0000269|PubMed:14757761};
CC KM=300 uM for ATP {ECO:0000269|PubMed:14757761};
CC Vmax=29.3 nmol/sec/mg enzyme with glutamate as substrate
CC {ECO:0000269|PubMed:14757761};
CC Vmax=27.4 nmol/sec/mg enzyme with ammonium as substrate
CC {ECO:0000269|PubMed:14757761};
CC Vmax=21.4 nmol/sec/mg enzyme with ATP as substrate
CC {ECO:0000269|PubMed:14757761};
CC Note=The KM value for ammonium is smaller than 10 uM. Measured at pH
CC 7.8 and 30 degrees Celsius for all experiments.;
CC -!- SUBUNIT: Homooctamer (By similarity). Interacts with CRK3 and GRF3.
CC {ECO:0000250|UniProtKB:P16580, ECO:0000269|PubMed:16472779,
CC ECO:0000269|PubMed:21094157}.
CC -!- INTERACTION:
CC Q56WN1; Q9ZUZ2: CRK3; NbExp=7; IntAct=EBI-1538766, EBI-1538748;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16472779}.
CC -!- TISSUE SPECIFICITY: Expressed in root tips, root hairs and epidermis.
CC Ubiquitously expressed with higher levels in siliques and roots.
CC {ECO:0000269|PubMed:14757761, ECO:0000269|PubMed:16472779}.
CC -!- INDUCTION: By nitrogen deprivation, sucrose, glucose and fructose.
CC Down-regulated by ammonium supply. Induced during leaf senescence.
CC {ECO:0000269|PubMed:10482686, ECO:0000269|PubMed:14757761,
CC ECO:0000269|PubMed:16472779}.
CC -!- PTM: Phosphorylated by CRK3. {ECO:0000269|PubMed:16472779}.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR EMBL; AB018107; BAB08306.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94209.1; -; Genomic_DNA.
DR EMBL; AF419608; AAL31940.1; -; mRNA.
DR EMBL; AF428386; AAL16154.1; -; mRNA.
DR EMBL; AY079113; AAL84997.1; -; mRNA.
DR EMBL; BT000753; AAN31893.1; -; mRNA.
DR EMBL; AK222005; BAD94626.1; -; mRNA.
DR PIR; S18601; S18601.
DR RefSeq; NP_198576.1; NM_123119.4.
DR AlphaFoldDB; Q56WN1; -.
DR SMR; Q56WN1; -.
DR BioGRID; 18989; 4.
DR IntAct; Q56WN1; 2.
DR STRING; 3702.AT5G37600.1; -.
DR iPTMnet; Q56WN1; -.
DR PaxDb; Q56WN1; -.
DR PRIDE; Q56WN1; -.
DR ProteomicsDB; 248581; -.
DR EnsemblPlants; AT5G37600.1; AT5G37600.1; AT5G37600.
DR GeneID; 833738; -.
DR Gramene; AT5G37600.1; AT5G37600.1; AT5G37600.
DR KEGG; ath:AT5G37600; -.
DR Araport; AT5G37600; -.
DR TAIR; locus:2151739; AT5G37600.
DR eggNOG; KOG0683; Eukaryota.
DR HOGENOM; CLU_036762_0_1_1; -.
DR InParanoid; Q56WN1; -.
DR OMA; RHEQHIA; -.
DR OrthoDB; 784869at2759; -.
DR PhylomeDB; Q56WN1; -.
DR BRENDA; 6.3.1.2; 399.
DR SABIO-RK; Q56WN1; -.
DR PRO; PR:Q56WN1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q56WN1; baseline and differential.
DR Genevisible; Q56WN1; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0022626; C:cytosolic ribosome; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR GO; GO:0004356; F:glutamate-ammonia ligase activity; IDA:TAIR.
DR GO; GO:0006542; P:glutamine biosynthetic process; IBA:GO_Central.
DR GO; GO:0010150; P:leaf senescence; IEP:UniProtKB.
DR GO; GO:0042128; P:nitrate assimilation; TAS:TAIR.
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 Acetylation; ATP-binding; Cytoplasm; Ligase; Nitrogen fixation;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..356
FT /note="Glutamine synthetase cytosolic isozyme 1-1"
FT /id="PRO_0000239818"
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"
FT REGION 36..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8LCE1"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q43127"
SQ SEQUENCE 356 AA; 39115 MW; AE54FB88287CFE9D CRC64;
MSLVSDLINL NLSDSTDKII AEYIWVGGSG MDMRSKARTL PGPVTDPSQL PKWNYDGSST
GQAPGEDSEV ILYPQAIFKD PFRRGNNILV MCDAYTPAGE PIPTNKRHAA AKVFSNPDVA
AEVPWYGIEQ EYTLLQKDVK WPVGWPIGGY PGPQGPYYCG IGADKSFGRD VVDSHYKACL
YAGINISGIN GEVMPGQWEF QVGPAVGISA ADEIWVARYI LERITEIAGV VVSFDPKPIP
GDWNGAGAHC NYSTKSMREE GGYEIIKKAI DKLGLRHKEH IAAYGEGNER RLTGHHETAD
INTFLWGVAN RGASIRVGRD TEKEGKGYFE DRRPASNMDP YIVTSMIAET TILWNP
