GLN13_ARATH
ID GLN13_ARATH Reviewed; 354 AA.
AC Q9LVI8; Q5PNX0; Q84W44;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 137.
DE RecName: Full=Glutamine synthetase cytosolic isozyme 1-3;
DE Short=GS1;
DE EC=6.3.1.2 {ECO:0000269|PubMed:14757761};
DE AltName: Full=Glutamate--ammonia ligase GLN1;3;
DE Short=GLN1;3;
GN Name=GLN1-3; OrderedLocusNames=At3g17820; ORFNames=MEB5.4;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP CATALYTIC ACTIVITY, FUNCTION, 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 [8]
RP MUTAGENESIS OF LYS-49 AND ALA-174.
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 [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: Low-affinity glutamine synthetase (PubMed:14757761). May
CC contribute to the homeostatic control of glutamine synthesis in roots.
CC {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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.9 mM for glutamate {ECO:0000269|PubMed:14757761};
CC KM=1210 uM for ammonium {ECO:0000269|PubMed:14757761};
CC KM=850 uM for ATP {ECO:0000269|PubMed:14757761};
CC Vmax=162 nmol/sec/mg enzyme with glutamate as substrate
CC {ECO:0000269|PubMed:14757761};
CC Vmax=93.9 nmol/sec/mg enzyme with ammonium as substrate
CC {ECO:0000269|PubMed:14757761};
CC Vmax=100 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 {ECO:0000269|PubMed:14757761};
CC -!- SUBUNIT: Homooctamer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Expressed in the pericycle in the region of mature
CC root. {ECO:0000269|PubMed:14757761}.
CC -!- INDUCTION: By sucrose, glucose and fructose. Down-regulated by ammonium
CC supply. {ECO:0000269|PubMed:10482686, ECO:0000269|PubMed:14757761}.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR EMBL; AB019230; BAB02705.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76011.1; -; Genomic_DNA.
DR EMBL; BT004249; AAO42253.1; -; mRNA.
DR EMBL; AY088312; AAM65851.1; -; mRNA.
DR EMBL; BT020327; AAV85682.1; -; mRNA.
DR EMBL; BT020432; AAW28559.1; -; mRNA.
DR RefSeq; NP_188409.1; NM_112663.3.
DR AlphaFoldDB; Q9LVI8; -.
DR SMR; Q9LVI8; -.
DR BioGRID; 6383; 2.
DR STRING; 3702.AT3G17820.1; -.
DR iPTMnet; Q9LVI8; -.
DR PaxDb; Q9LVI8; -.
DR PRIDE; Q9LVI8; -.
DR ProteomicsDB; 248583; -.
DR DNASU; 821050; -.
DR EnsemblPlants; AT3G17820.1; AT3G17820.1; AT3G17820.
DR GeneID; 821050; -.
DR Gramene; AT3G17820.1; AT3G17820.1; AT3G17820.
DR KEGG; ath:AT3G17820; -.
DR Araport; AT3G17820; -.
DR TAIR; locus:2088580; AT3G17820.
DR eggNOG; KOG0683; Eukaryota.
DR HOGENOM; CLU_036762_0_1_1; -.
DR InParanoid; Q9LVI8; -.
DR OMA; QVWIARF; -.
DR OrthoDB; 784869at2759; -.
DR PhylomeDB; Q9LVI8; -.
DR BRENDA; 6.3.1.2; 399.
DR SABIO-RK; Q9LVI8; -.
DR PRO; PR:Q9LVI8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LVI8; baseline and differential.
DR Genevisible; Q9LVI8; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
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:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0042788; C:polysomal ribosome; IDA:CAFA.
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:0003735; F:structural constituent of ribosome; IDA:CAFA.
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; Nucleotide-binding;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..354
FT /note="Glutamine synthetase cytosolic isozyme 1-3"
FT /id="PRO_0000153168"
FT DOMAIN 19..99
FT /note="GS beta-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT DOMAIN 106..354
FT /note="GS catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
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"
FT MUTAGEN 49
FT /note="K->Q: 3-fold increase in affinity for ammonium and
FT catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:16338958"
FT MUTAGEN 174
FT /note="A->S: 4-fold increase in affinity for ammonium and
FT catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:16338958"
FT CONFLICT 85
FT /note="G -> D (in Ref. 3; AAO42253)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 354 AA; 38595 MW; 750441568FA1D7B9 CRC64;
MSLLSDLVNL NLTDATGKII AEYIWIGGSG MDIRSKARTL PGPVTDPSKL PKWNYDGSST
GQAAGEDSEV ILYPQAIFKD PFRKGNNILV MCDAYTPAGD PIPTNKRHNA AKIFSHPDVA
KEEPWYGIEQ EYTLMQKDVN WPIGWPVGGY PGPQGPYYCG VGADKAIGRD IVDAHYKACL
YAGIGISGIN GEVMPGQWEF QVGPVEGISS GDQVWVARYL LERITEISGV IVSFDPKPVP
GDWNGAGAHC NYSTKTMRND GGLEVIKKAI GKLQLKHKEH IAAYGEGNER RLTGKHETAD
INTFSWGVAN RGASVRVGRD TEKEGKGYFE DRRPASNMDP YVVTSMIAET TILG
