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Glutamine synthetase cytosolic isozyme 1-3 (GS1) (EC 6.3.1.2) (Glutamate--ammonia ligase GLN1;3) (GLN1;3)

 GLN13_ARATH             Reviewed;         354 AA.
Q9LVI8; Q5PNX0; Q84W44;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
07-JUN-2017, entry version 115.
RecName: Full=Glutamine synthetase cytosolic isozyme 1-3;
Short=GS1;
EC=6.3.1.2;
AltName: Full=Glutamate--ammonia ligase GLN1;3;
Short=GLN1;3;
Name=GLN1-3; OrderedLocusNames=At3g17820; ORFNames=MEB5.4;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10819329; DOI=10.1093/dnares/7.2.131;
Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
features of the regions of 4,504,864 bp covered by sixty P1 and TAC
clones.";
DNA Res. 7:131-135(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
"Arabidopsis ORF clones.";
Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
[6]
INDUCTION.
PubMed=10482686; DOI=10.1104/pp.121.1.301;
Oliveira I.C., Coruzzi G.M.;
"Carbon and amino acids reciprocally modulate the expression of
glutamine synthetase in Arabidopsis.";
Plant Physiol. 121:301-310(1999).
[7]
BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=14757761; DOI=10.1074/jbc.M313710200;
Ishiyama K., Inoue E., Watanabe-Takahashi A., Obara M., Yamaya T.,
Takahashi H.;
"Kinetic properties and ammonium-dependent regulation of cytosolic
isoenzymes of glutamine synthetase in Arabidopsis.";
J. Biol. Chem. 279:16598-16605(2004).
[8]
MUTAGENESIS OF LYS-49 AND ALA-174.
PubMed=16338958; DOI=10.1093/pcp/pci238;
Ishiyama K., Inoue E., Yamaya T., Takahashi H.;
"Gln49 and Ser174 residues play critical roles in determining the
catalytic efficiencies of plant glutamine synthetase.";
Plant Cell Physiol. 47:299-303(2006).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
-!- FUNCTION: Low-affinity glutamine synthetase. May contribute to the
homeostatic control of glutamine synthesis in roots.
-!- CATALYTIC ACTIVITY: ATP + L-glutamate + NH(3) = ADP + phosphate +
L-glutamine.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=3.9 mM for glutamate {ECO:0000269|PubMed:14757761};
KM=1210 uM for ammonium {ECO:0000269|PubMed:14757761};
KM=850 uM for ATP {ECO:0000269|PubMed:14757761};
Vmax=162 nmol/sec/mg enzyme with glutamate as substrate
{ECO:0000269|PubMed:14757761};
Vmax=93.9 nmol/sec/mg enzyme with ammonium as substrate
{ECO:0000269|PubMed:14757761};
Vmax=100 nmol/sec/mg enzyme with ATP as substrate
{ECO:0000269|PubMed:14757761};
Note=Measured at pH 7.8 and 30 degrees Celsius for all
experiments.;
-!- SUBUNIT: Homooctamer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- TISSUE SPECIFICITY: Expressed in the pericycle in the region of
mature root. {ECO:0000269|PubMed:14757761}.
-!- INDUCTION: By sucrose, glucose and fructose. Down-regulated by
ammonium supply. {ECO:0000269|PubMed:10482686,
ECO:0000269|PubMed:14757761}.
-!- SIMILARITY: Belongs to the glutamine synthetase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB019230; BAB02705.1; -; Genomic_DNA.
EMBL; CP002686; AEE76011.1; -; Genomic_DNA.
EMBL; BT004249; AAO42253.1; -; mRNA.
EMBL; AY088312; AAM65851.1; -; mRNA.
EMBL; BT020327; AAV85682.1; -; mRNA.
EMBL; BT020432; AAW28559.1; -; mRNA.
RefSeq; NP_188409.1; NM_112663.3.
UniGene; At.26821; -.
ProteinModelPortal; Q9LVI8; -.
SMR; Q9LVI8; -.
BioGrid; 6383; 2.
STRING; 3702.AT3G17820.1; -.
iPTMnet; Q9LVI8; -.
PaxDb; Q9LVI8; -.
PRIDE; Q9LVI8; -.
DNASU; 821050; -.
EnsemblPlants; AT3G17820.1; AT3G17820.1; AT3G17820.
GeneID; 821050; -.
Gramene; AT3G17820.1; AT3G17820.1; AT3G17820.
KEGG; ath:AT3G17820; -.
Araport; AT3G17820; -.
TAIR; locus:2088580; AT3G17820.
eggNOG; KOG0683; Eukaryota.
eggNOG; COG0174; LUCA.
HOGENOM; HOG000061500; -.
InParanoid; Q9LVI8; -.
KO; K01915; -.
OMA; GSWEFQV; -.
OrthoDB; EOG09360CB0; -.
PhylomeDB; Q9LVI8; -.
BRENDA; 6.3.1.2; 399.
Reactome; R-ATH-210455; Astrocytic Glutamate-Glutamine Uptake And Metabolism.
Reactome; R-ATH-70614; Amino acid synthesis and interconversion (transamination).
SABIO-RK; Q9LVI8; -.
PRO; PR:Q9LVI8; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; Q9LVI8; baseline and differential.
Genevisible; Q9LVI8; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0005829; C:cytosol; TAS:TAIR.
GO; GO:0022626; C:cytosolic ribosome; IDA:TAIR.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0042788; C:polysomal ribosome; IDA:CAFA.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005507; F:copper ion binding; IDA:TAIR.
GO; GO:0004356; F:glutamate-ammonia ligase activity; IDA:TAIR.
GO; GO:0003735; F:structural constituent of ribosome; IDA:CAFA.
GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
GO; GO:0042128; P:nitrate assimilation; TAS:TAIR.
GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
GO; GO:0042255; P:ribosome assembly; IC:CAFA.
Gene3D; 3.30.590.10; -; 1.
InterPro; IPR008147; Gln_synt_b-grasp.
InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
InterPro; IPR008146; Gln_synth_cat_dom.
InterPro; IPR027303; Gln_synth_gly_rich_site.
InterPro; IPR027302; Gln_synth_N_conserv_site.
Pfam; PF00120; Gln-synt_C; 1.
Pfam; PF03951; Gln-synt_N; 1.
SMART; SM01230; Gln-synt_C; 1.
SUPFAM; SSF54368; SSF54368; 1.
PROSITE; PS00180; GLNA_1; 1.
PROSITE; PS00181; GLNA_ATP; 1.
1: Evidence at protein level;
Acetylation; ATP-binding; Complete proteome; Cytoplasm; Ligase;
Nucleotide-binding; Phosphoprotein; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895}.
CHAIN 2 354 Glutamine synthetase cytosolic isozyme 1-
3.
/FTId=PRO_0000153168.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22223895}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000250|UniProtKB:Q8LCE1}.
MOD_RES 48 48 Phosphoserine.
{ECO:0000250|UniProtKB:Q43127}.
MUTAGEN 49 49 K->Q: 3-fold increase in affinity for
ammonium and catalytic efficiency.
{ECO:0000269|PubMed:16338958}.
MUTAGEN 174 174 A->S: 4-fold increase in affinity for
ammonium and catalytic efficiency.
{ECO:0000269|PubMed:16338958}.
CONFLICT 85 85 G -> D (in Ref. 3; AAO42253).
{ECO:0000305}.
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


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