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

 GLN11_ARATH             Reviewed;         356 AA.
Q56WN1; Q9FHR0;
13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
13-JUN-2006, sequence version 2.
25-OCT-2017, entry version 92.
RecName: Full=Glutamine synthetase cytosolic isozyme 1-1;
EC=6.3.1.2;
AltName: Full=Glutamate--ammonia ligase GLN1;1;
Short=GLN1;1;
Name=GLN1-1; OrderedLocusNames=At5g37600; ORFNames=K12B20.50;
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=10470850; DOI=10.1093/dnares/6.3.183;
Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
Miyajima N., Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. IX.
Sequence features of the regions of 1,011,550 bp covered by seventeen
P1 and TAC clones.";
DNA Res. 6:183-195(1999).
[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] OF 145-356.
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
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).
[6]
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).
[7]
INTERACTION WITH CRK3, PHOSPHORYLATION BY CRK3, INDUCTION BY LEAF
SENESCENCE, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=16472779; DOI=10.1016/j.bbrc.2006.01.100;
Li R.-J., Hua W., Lu Y.-T.;
"Arabidopsis cytosolic glutamine synthetase AtGLN1;1 is a potential
substrate of AtCRK3 involved in leaf senescence.";
Biochem. Biophys. Res. Commun. 342:119-126(2006).
[8]
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).
[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: High-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=1.1 mM for glutamate {ECO:0000269|PubMed:14757761};
KM=10 uM for ammonium {ECO:0000269|PubMed:14757761};
KM=300 uM for ATP {ECO:0000269|PubMed:14757761};
Vmax=29.3 nmol/sec/mg enzyme with glutamate as substrate
{ECO:0000269|PubMed:14757761};
Vmax=27.4 nmol/sec/mg enzyme with ammonium as substrate
{ECO:0000269|PubMed:14757761};
Vmax=21.4 nmol/sec/mg enzyme with ATP as substrate
{ECO:0000269|PubMed:14757761};
Note=The KM value for ammonium is smaller than 10 uM. Measured
at pH 7.8 and 30 degrees Celsius for all experiments.;
-!- SUBUNIT: Homooctamer (By similarity). Interacts with CRK3 and
GRF3. {ECO:0000250|UniProtKB:P16580, ECO:0000269|PubMed:16472779,
ECO:0000269|PubMed:21094157}.
-!- INTERACTION:
Q9ZUZ2:CRK3; NbExp=7; IntAct=EBI-1538766, EBI-1538748;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16472779}.
-!- TISSUE SPECIFICITY: Expressed in root tips, root hairs and
epidermis. Ubiquitously expressed with higher levels in siliques
and roots. {ECO:0000269|PubMed:14757761,
ECO:0000269|PubMed:16472779}.
-!- INDUCTION: By nitrogen deprivation, sucrose, glucose and fructose.
Down-regulated by ammonium supply. Induced during leaf senescence.
{ECO:0000269|PubMed:10482686, ECO:0000269|PubMed:14757761,
ECO:0000269|PubMed:16472779}.
-!- PTM: Phosphorylated by CRK3. {ECO:0000269|PubMed:16472779}.
-!- SIMILARITY: Belongs to the glutamine synthetase family.
{ECO:0000305}.
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EMBL; AB018107; BAB08306.1; -; Genomic_DNA.
EMBL; CP002688; AED94209.1; -; Genomic_DNA.
EMBL; AF419608; AAL31940.1; -; mRNA.
EMBL; AF428386; AAL16154.1; -; mRNA.
EMBL; AY079113; AAL84997.1; -; mRNA.
EMBL; BT000753; AAN31893.1; -; mRNA.
EMBL; AK222005; BAD94626.1; -; mRNA.
PIR; S18601; S18601.
RefSeq; NP_198576.1; NM_123119.4.
UniGene; At.7003; -.
ProteinModelPortal; Q56WN1; -.
SMR; Q56WN1; -.
BioGrid; 18989; 4.
IntAct; Q56WN1; 2.
MINT; MINT-8062724; -.
STRING; 3702.AT5G37600.1; -.
iPTMnet; Q56WN1; -.
PaxDb; Q56WN1; -.
PRIDE; Q56WN1; -.
EnsemblPlants; AT5G37600.1; AT5G37600.1; AT5G37600.
GeneID; 833738; -.
Gramene; AT5G37600.1; AT5G37600.1; AT5G37600.
KEGG; ath:AT5G37600; -.
Araport; AT5G37600; -.
TAIR; locus:2151739; AT5G37600.
eggNOG; KOG0683; Eukaryota.
eggNOG; COG0174; LUCA.
HOGENOM; HOG000061500; -.
InParanoid; Q56WN1; -.
KO; K01915; -.
OMA; NINTFKW; -.
OrthoDB; EOG09360CB0; -.
PhylomeDB; Q56WN1; -.
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; Q56WN1; -.
PRO; PR:Q56WN1; -.
Proteomes; UP000006548; Chromosome 5.
Genevisible; Q56WN1; AT.
GO; GO:0005618; C:cell wall; 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:0009506; C:plasmodesma; IDA:TAIR.
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:0006542; P:glutamine biosynthetic process; IEA:InterPro.
GO; GO:0010150; P:leaf senescence; IEP:UniProtKB.
GO; GO:0042128; P:nitrate assimilation; TAS:TAIR.
GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
Gene3D; 3.30.590.10; -; 1.
InterPro; IPR008147; Gln_synt_b-grasp.
InterPro; IPR036651; Gln_synt_N.
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.
SUPFAM; SSF55931; SSF55931; 1.
PROSITE; PS00180; GLNA_1; 1.
PROSITE; PS00181; GLNA_ATP; 1.
1: Evidence at protein level;
Acetylation; 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-
1.
/FTId=PRO_0000239818.
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}.
SEQUENCE 356 AA; 39115 MW; AE54FB88287CFE9D CRC64;
MSLVSDLINL NLSDSTDKII AEYIWVGGSG MDMRSKARTL PGPVTDPSQL PKWNYDGSST
GQAPGEDSEV ILYPQAIFKD PFRRGNNILV MCDAYTPAGE PIPTNKRHAA AKVFSNPDVA
AEVPWYGIEQ EYTLLQKDVK WPVGWPIGGY PGPQGPYYCG IGADKSFGRD VVDSHYKACL
YAGINISGIN GEVMPGQWEF QVGPAVGISA ADEIWVARYI LERITEIAGV VVSFDPKPIP
GDWNGAGAHC NYSTKSMREE GGYEIIKKAI DKLGLRHKEH IAAYGEGNER RLTGHHETAD
INTFLWGVAN RGASIRVGRD TEKEGKGYFE DRRPASNMDP YIVTSMIAET TILWNP


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