ID   GLNA_NICPL              Reviewed;         356 AA.
AC   P12424;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Glutamine synthetase;
DE            EC=6.3.1.2;
DE   AltName: Full=Glutamate--ammonia ligase;
OS   Nicotiana plumbaginifolia (Leadwort-leaved tobacco) (Tex-Mex tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4092;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=16665445; DOI=10.1104/pp.84.2.366;
RA   Tingey S.V., Coruzzi G.M.;
RT   "Glutamine synthetase of Nicotiana plumbaginifolia: cloning and in vivo
RT   expression.";
RL   Plant Physiol. 84:366-373(1987).
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   -!- SUBUNIT: Homooctamer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MISCELLANEOUS: Irreversibly inhibited by the herbicide L-
CC       phosphinothricin (PPT).
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR   EMBL; M19055; AAA34066.1; -; mRNA.
DR   PIR; JN0041; JN0041.
DR   AlphaFoldDB; P12424; -.
DR   SMR; P12424; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004356; F:glutamate-ammonia ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
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   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Ligase; Nucleotide-binding.
FT   CHAIN           1..356
FT                   /note="Glutamine synthetase"
FT                   /id="PRO_0000153185"
FT   DOMAIN          19..99
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT   DOMAIN          106..356
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
SQ   SEQUENCE   356 AA;  38893 MW;  306547AA6E7114A0 CRC64;
     MSLLSDLINL NLSDSTEKII AEYIWIGGSG MDLRSKARTL SGPVTDPAKL PKWNYDGSST
     GQAPGEDSEV ILYPQAIFKD PFRRGNNILV MCDAYTPAGE PIPTNKRHAA AKIFSNPDVV
     AEEPWYGIEQ EYTLLQRDIN WPLGWPIGGF PGPQGPYYCG TGADKAFGRD IVDSHYKAYL
     YAGINISGIN GEVMPGQWEF QVGPSVGISA GDEVWVARYI LERIAEIAGV VVSFDPKPIP
     GDWNGAGAHT NYSTKSMRED GGYEVILKAI EKLGLKHKEH IAAYGEGNER RLTGKHETAN
     ISTFKWGVAN RGASVRVGRD TEKAGKGYFE DRRPASNMDP YVVTAMIADT TIIGKS