ID   GLN14_ARATH             Reviewed;         356 AA.
AC   Q9FMD9;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, entry version 132.
DE   RecName: Full=Glutamine synthetase cytosolic isozyme 1-4 {ECO:0000303|PubMed:14757761};
DE            EC=6.3.1.2 {ECO:0000269|PubMed:14757761, ECO:0000269|PubMed:16338958};
DE   AltName: Full=Glutamate--ammonia ligase GLN1;4 {ECO:0000303|PubMed:14757761};
DE            Short=GLN1;4 {ECO:0000303|PubMed:14757761};
GN   Name=GLN1-4 {ECO:0000303|PubMed:14757761};
GN   OrderedLocusNames=At5g16570 {ECO:0000312|Araport:AT5G16570};
GN   ORFNames=MTG13.1 {ECO:0000312|EMBL:BAB10184.1};
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=9501997; DOI=10.1093/dnares/4.6.401;
RA   Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT   features of the regions of 1,191,918 bp covered by seventeen physically
RT   assigned P1 clones.";
RL   DNA Res. 4:401-414(1997).
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   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, TISSUE
RP   SPECIFICITY, INDUCTION, AND GENE FAMILY.
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   [5]
RP   FUNCTION, MUTAGENESIS OF GLN-49 AND SER-174, BIOPHYSICOCHEMICAL PROPERTIES,
RP   AND CATALYTIC ACTIVITY.
RX   PubMed=16338958; DOI=10.1093/pcp/pci238;
RA   Ishiyama K., Inoue E., Yamaya T., Takahashi H.;
RT   "Gln49 and Ser174 residues play critical roles in determining the catalytic
RT   efficiencies of plant glutamine synthetase.";
RL   Plant Cell Physiol. 47:299-303(2006).
RN   [6]
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).
CC   -!- FUNCTION: High-affinity glutamine synthetase (PubMed:14757761,
CC       PubMed:16338958). May contribute to the homeostatic control of
CC       glutamine synthesis in roots (PubMed:14757761).
CC       {ECO:0000269|PubMed:14757761, ECO:0000269|PubMed:16338958}.
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, ECO:0000269|PubMed:16338958};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.6 mM for glutamate {ECO:0000269|PubMed:14757761};
CC         KM=48 uM for ammonium {ECO:0000269|PubMed:14757761};
CC         KM=120 uM for ammonium {ECO:0000269|PubMed:16338958};
CC         KM=0.67 mM for glutamate {ECO:0000269|PubMed:16338958};
CC         KM=400 uM for ATP {ECO:0000269|PubMed:14757761};
CC         Vmax=79.2 nmol/sec/mg enzyme with glutamate as substrate
CC         {ECO:0000269|PubMed:14757761};
CC         Vmax=65.7 nmol/sec/mg enzyme with ammonium as substrate
CC         {ECO:0000269|PubMed:14757761};
CC         Vmax=73.9 nmol/sec/mg enzyme with ATP as substrate
CC         {ECO:0000269|PubMed:14757761};
CC         Note=Measured at pH 7.8 and 30 degrees Celsius for all experiments
CC         (PubMed:14757761). kcat is 2.96 sec(-1) with ammonium as substrate
CC         (PubMed:16338958). kcat is 4.18 sec(-1) with glutamate as substrate
CC         (PubMed:16338958). {ECO:0000269|PubMed:14757761,
CC         ECO:0000269|PubMed:16338958};
CC   -!- SUBUNIT: Homooctamer (By similarity). Interacts with GRF3.
CC       {ECO:0000250|UniProtKB:P16580, ECO:0000269|PubMed:21094157}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Expressed in the pericycle in the region of lateral
CC       root emergence. {ECO:0000269|PubMed:14757761}.
CC   -!- INDUCTION: Down-regulated by ammonium supply.
CC       {ECO:0000269|PubMed:14757761}.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR   EMBL; AB008270; BAB10184.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED92312.1; -; Genomic_DNA.
DR   EMBL; AY059932; AAL24414.1; -; mRNA.
DR   EMBL; AY128749; AAM91149.1; -; mRNA.
DR   RefSeq; NP_568335.1; NM_121663.3.
DR   AlphaFoldDB; Q9FMD9; -.
DR   SMR; Q9FMD9; -.
DR   BioGRID; 16795; 3.
DR   STRING; 3702.Q9FMD9; -.
DR   PaxDb; 3702-AT5G16570-1; -.
DR   ProteomicsDB; 247394; -.
DR   EnsemblPlants; AT5G16570.1; AT5G16570.1; AT5G16570.
DR   GeneID; 831519; -.
DR   Gramene; AT5G16570.1; AT5G16570.1; AT5G16570.
DR   KEGG; ath:AT5G16570; -.
DR   Araport; AT5G16570; -.
DR   TAIR; AT5G16570; GLN1.
DR   eggNOG; KOG0683; Eukaryota.
DR   HOGENOM; CLU_036762_1_1_1; -.
DR   InParanoid; Q9FMD9; -.
DR   OMA; HKYHIRM; -.
DR   OrthoDB; 1115057at2759; -.
DR   PhylomeDB; Q9FMD9; -.
DR   BioCyc; ARA:AT5G16570-MONOMER; -.
DR   BioCyc; MetaCyc:AT5G16570-MONOMER; -.
DR   BRENDA; 6.3.1.2; 399.
DR   SABIO-RK; Q9FMD9; -.
DR   PRO; PR:Q9FMD9; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FMD9; baseline and differential.
DR   GO; GO:0005829; C:cytosol; NAS:TAIR.
DR   GO; GO:0009536; C:plastid; HDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004356; F:glutamine synthetase activity; IDA:TAIR.
DR   GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
DR   GO; GO:0042128; P:nitrate assimilation; TAS:TAIR.
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:SF93; GLUTAMINE SYNTHETASE CYTOSOLIC ISOZYME 1-4; 1.
DR   Pfam; PF00120; Gln-synt_C; 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; Q9FMD9; AT.
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:0000250|UniProtKB:Q56WN1"
FT   CHAIN           2..356
FT                   /note="Glutamine synthetase cytosolic isozyme 1-4"
FT                   /id="PRO_0000239820"
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          37..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..65
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q56WN1"
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"
FT   MUTAGEN         49
FT                   /note="Q->K: 6-fold decrease in affinity for ammonium and
FT                   catalytic efficiency; when associated with A-174."
FT                   /evidence="ECO:0000269|PubMed:16338958"
FT   MUTAGEN         174
FT                   /note="S->A: 6-fold decrease in affinity for ammonium and
FT                   catalytic efficiency; when associated with K-49."
FT                   /evidence="ECO:0000269|PubMed:16338958"
SQ   SEQUENCE   356 AA;  38987 MW;  A8F39CE8835592D4 CRC64;
     MSSLADLINL DLSDSTDQII AEYIWIGGSG LDMRSKARTL PGPVTDPSQL PKWNYDGSST
     GQAPGDDSEV IIYPQAIFKD PFRRGNNILV MCDAYTPAGE PIPTNKRHAA AKIFEDPSVV
     AEETWYGIEQ EYTLLQKDIK WPVGWPVGGF PGPQGPYYCG VGADKAFGRD IVDSHYKACL
     YAGINVSGTN GEVMPGQWEF QVGPTVGIAA ADQVWVARYI LERITELAGV VLSLDPKPIP
     GDWNGAGAHT NYSTKSMRED GGYEVIKKAI EKLGLRHKEH IAAYGEGNER RLTGKHETAD
     INTFLWGVAN RGASIRVGRD TEQAGKGYFE DRRPASNMDP YTVTSMIAES TILWKP
//