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Glutamine synthetase cytosolic isozyme 1-4 (EC 6.3.1.2) (Glutamate--ammonia ligase GLN1;4) (GLN1;4)

 GLN14_ARATH             Reviewed;         356 AA.
Q9FMD9;
13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
25-OCT-2017, entry version 104.
RecName: Full=Glutamine synthetase cytosolic isozyme 1-4;
EC=6.3.1.2;
AltName: Full=Glutamate--ammonia ligase GLN1;4;
Short=GLN1;4;
Name=GLN1-4; OrderedLocusNames=At5g16570; ORFNames=MTG13.1;
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=9501997; DOI=10.1093/dnares/4.6.401;
Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. III.
Sequence features of the regions of 1,191,918 bp covered by seventeen
physically assigned P1 clones.";
DNA Res. 4:401-414(1997).
[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]
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).
[5]
MUTAGENESIS OF GLN-49 AND SER-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).
[6]
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).
-!- 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=0.6 mM for glutamate {ECO:0000269|PubMed:14757761};
KM=48 uM for ammonium {ECO:0000269|PubMed:14757761};
KM=400 uM for ATP {ECO:0000269|PubMed:14757761};
Vmax=79.2 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=73.9 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.
-!- TISSUE SPECIFICITY: Expressed in the pericycle in the region of
lateral root emergence. {ECO:0000269|PubMed:14757761}.
-!- INDUCTION: Down-regulated by ammonium supply.
{ECO:0000269|PubMed:14757761}.
-!- SIMILARITY: Belongs to the glutamine synthetase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB008270; BAB10184.1; -; Genomic_DNA.
EMBL; CP002688; AED92312.1; -; Genomic_DNA.
EMBL; AY059932; AAL24414.1; -; mRNA.
EMBL; AY128749; AAM91149.1; -; mRNA.
RefSeq; NP_568335.1; NM_121663.3.
UniGene; At.24254; -.
ProteinModelPortal; Q9FMD9; -.
SMR; Q9FMD9; -.
BioGrid; 16795; 3.
STRING; 3702.AT5G16570.1; -.
PaxDb; Q9FMD9; -.
PRIDE; Q9FMD9; -.
EnsemblPlants; AT5G16570.1; AT5G16570.1; AT5G16570.
GeneID; 831519; -.
Gramene; AT5G16570.1; AT5G16570.1; AT5G16570.
KEGG; ath:AT5G16570; -.
Araport; AT5G16570; -.
TAIR; locus:2174175; AT5G16570.
eggNOG; KOG0683; Eukaryota.
eggNOG; COG0174; LUCA.
HOGENOM; HOG000061500; -.
InParanoid; Q9FMD9; -.
KO; K01915; -.
OMA; AESTILW; -.
OrthoDB; EOG09360CB0; -.
PhylomeDB; Q9FMD9; -.
BioCyc; ARA:AT5G16570-MONOMER; -.
BioCyc; MetaCyc:AT5G16570-MONOMER; -.
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; Q9FMD9; -.
PRO; PR:Q9FMD9; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q9FMD9; baseline and differential.
Genevisible; Q9FMD9; AT.
GO; GO:0005829; C:cytosol; NAS:TAIR.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004356; F:glutamate-ammonia ligase activity; IDA:TAIR.
GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
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:0000250|UniProtKB:Q56WN1}.
CHAIN 2 356 Glutamine synthetase cytosolic isozyme 1-
4.
/FTId=PRO_0000239820.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:Q56WN1}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000250|UniProtKB:Q8LCE1}.
MOD_RES 48 48 Phosphoserine.
{ECO:0000250|UniProtKB:Q43127}.
MUTAGEN 49 49 Q->K: 6-fold decrease in affinity for
ammonium and catalytic efficiency; when
associated with A-174.
{ECO:0000269|PubMed:16338958}.
MUTAGEN 174 174 S->A: 6-fold decrease in affinity for
ammonium and catalytic efficiency; when
associated with K-49.
{ECO:0000269|PubMed:16338958}.
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


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