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Glutamine synthetase cytosolic isozyme 1-2 (EC 6.3.1.2) (Glutamate--ammonia ligase GLN1;2) (GLN1;2)

 GLN12_ARATH             Reviewed;         356 AA.
Q8LCE1; Q9C8C7;
13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
13-JUN-2006, sequence version 2.
30-AUG-2017, entry version 103.
RecName: Full=Glutamine synthetase cytosolic isozyme 1-2;
EC=6.3.1.2;
AltName: Full=Glutamate--ammonia ligase GLN1;2;
Short=GLN1;2;
Name=GLN1-2; Synonyms=GSR2; OrderedLocusNames=At1g66200;
ORFNames=F15E12.14;
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=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(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., Troukhan M., Alexandrov N., Lu Y.-P., Flavell R.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[5]
INDUCTION.
PubMed=10444084; DOI=10.1104/pp.120.4.1015;
Miller J.D., Arteca R.N., Pell E.J.;
"Senescence-associated gene expression during ozone-induced leaf
senescence in Arabidopsis.";
Plant Physiol. 120:1015-1024(1999).
[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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19376835; DOI=10.1104/pp.109.138677;
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
Grossmann J., Gruissem W., Baginsky S.;
"Large-scale Arabidopsis phosphoproteome profiling reveals novel
chloroplast kinase substrates and phosphorylation networks.";
Plant Physiol. 150:889-903(2009).
[9]
INTERACTION WITH GRF3.
PubMed=21094157; DOI=10.1016/j.febslet.2010.11.025;
Shin R., Jez J.M., Basra A., Zhang B., Schachtman D.P.;
"14-3-3 proteins fine-tune plant nutrient metabolism.";
FEBS Lett. 585:143-147(2011).
[10]
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=3.8 mM for glutamate {ECO:0000269|PubMed:14757761};
KM=2450 uM for ammonium {ECO:0000269|PubMed:14757761};
KM=1100 uM for ATP {ECO:0000269|PubMed:14757761};
Vmax=65.7 nmol/sec/mg enzyme with glutamate as substrate
{ECO:0000269|PubMed:14757761};
Vmax=65.7 nmol/sec/mg enzyme with ammonium as substrate
{ECO:0000269|PubMed:14757761};
Vmax=66.6 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 (By similarity). Interacts with GRF3.
{ECO:0000250|UniProtKB:P16580, ECO:0000269|PubMed:21094157}.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=1;
Comment=A number of isoforms are produced. According to EST
sequences.;
Name=1;
IsoId=Q8LCE1-1; Sequence=Displayed;
-!- TISSUE SPECIFICITY: Expressed in the pericycle of all root
tissues. {ECO:0000269|PubMed:14757761}.
-!- INDUCTION: By ammonium supply under nitrogen-limited condition.
Induced by sucrose, glucose, fructose, and during leaf senescence.
{ECO:0000269|PubMed:10444084, ECO:0000269|PubMed:10482686,
ECO:0000269|PubMed:14757761}.
-!- SIMILARITY: Belongs to the glutamine synthetase family.
{ECO:0000305}.
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EMBL; AC026480; AAG51310.1; -; Genomic_DNA.
EMBL; CP002684; AEE34474.1; -; Genomic_DNA.
EMBL; AY091101; AAM14052.1; -; mRNA.
EMBL; AY122962; AAM67495.1; -; mRNA.
EMBL; AY086653; AAM63710.1; -; mRNA.
PIR; H96686; H96686.
PIR; S18602; S18602.
RefSeq; NP_176794.1; NM_105291.4. [Q8LCE1-1]
UniGene; At.47484; -.
UniGene; At.74857; -.
ProteinModelPortal; Q8LCE1; -.
SMR; Q8LCE1; -.
BioGrid; 28156; 3.
IntAct; Q8LCE1; 1.
STRING; 3702.AT1G66200.3; -.
iPTMnet; Q8LCE1; -.
PaxDb; Q8LCE1; -.
PRIDE; Q8LCE1; -.
DNASU; 842935; -.
EnsemblPlants; AT1G66200.1; AT1G66200.1; AT1G66200. [Q8LCE1-1]
GeneID; 842935; -.
Gramene; AT1G66200.1; AT1G66200.1; AT1G66200.
KEGG; ath:AT1G66200; -.
Araport; AT1G66200; -.
eggNOG; KOG0683; Eukaryota.
eggNOG; COG0174; LUCA.
HOGENOM; HOG000061500; -.
InParanoid; Q8LCE1; -.
PhylomeDB; Q8LCE1; -.
Reactome; R-ATH-210455; Astrocytic Glutamate-Glutamine Uptake And Metabolism.
Reactome; R-ATH-70614; Amino acid synthesis and interconversion (transamination).
SABIO-RK; Q8LCE1; -.
PRO; PR:Q8LCE1; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q8LCE1; baseline and differential.
Genevisible; Q8LCE1; AT.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004356; F:glutamate-ammonia ligase activity; IEA:UniProtKB-EC.
GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
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; Alternative splicing; ATP-binding; Complete proteome;
Cytoplasm; Ligase; Nitrogen fixation; Nucleotide-binding;
Phosphoprotein; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895}.
CHAIN 2 356 Glutamine synthetase cytosolic isozyme 1-
2.
/FTId=PRO_0000239819.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22223895}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000244|PubMed:19376835}.
MOD_RES 48 48 Phosphoserine.
{ECO:0000250|UniProtKB:Q43127}.
CONFLICT 290 290 R -> L (in Ref. 4; AAM63710).
{ECO:0000305}.
SEQUENCE 356 AA; 39207 MW; 19D19BF1388E5192 CRC64;
MSLLADLVNL DISDNSEKII AEYIWVGGSG MDMRSKARTL PGPVTDPSKL PKWNYDGSST
GQAPGQDSEV ILYPQAIFKD PFRRGNNILV MCDAYTPAGE PIPTNKRHAA AEIFANPDVI
AEVPWYGIEQ EYTLLQKDVN WPLGWPIGGF PGPQGPYYCS IGADKSFGRD IVDAHYKASL
YAGINISGIN GEVMPGQWEF QVGPSVGISA ADEIWIARYI LERITEIAGV VVSFDPKPIP
GDWNGAGAHT NYSTKSMREE GGYEIIKKAI EKLGLRHKEH ISAYGEGNER RLTGHHETAD
INTFLWGVAN RGASIRVGRD TEKEGKGYFE DRRPASNMDP YVVTSMIAET TLLWNP


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