GLN14_ARATH
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 03-AUG-2022, entry version 124.
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.AT5G16570.1; -.
DR PaxDb; Q9FMD9; -.
DR PRIDE; Q9FMD9; -.
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; locus:2174175; AT5G16570.
DR eggNOG; KOG0683; Eukaryota.
DR HOGENOM; CLU_036762_1_1_1; -.
DR InParanoid; Q9FMD9; -.
DR OMA; HAVACLY; -.
DR OrthoDB; 784869at2759; -.
DR PhylomeDB; Q9FMD9; -.
DR BioCyc; ARA:AT5G16570-MON; -.
DR BioCyc; MetaCyc:AT5G16570-MON; -.
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 Genevisible; Q9FMD9; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:glutamate-ammonia ligase activity; IDA:TAIR.
DR GO; GO:0006542; P:glutamine biosynthetic process; IBA:GO_Central.
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: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
