ID   GLNA_LACSA              Reviewed;         358 AA.
AC   P23712;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Glutamine synthetase;
DE            EC=6.3.1.2;
DE   AltName: Full=GS(1);
DE   AltName: Full=Glutamate--ammonia ligase;
OS   Lactuca sativa (Garden lettuce).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Cichorioideae; Cichorieae;
OC   Lactucinae; Lactuca.
OX   NCBI_TaxID=4236;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. New York 515 improved; TISSUE=Seed;
RX   PubMed=1983300; DOI=10.1007/bf00036917;
RA   Sakamoto A., Takeba G., Shibata D., Tanaka K.;
RT   "Phytochrome-mediated activation of the gene for cytosolic glutamine-
RT   synthetase (GS1) during imbibition of photosensitive lettuce seeds.";
RL   Plant Mol. Biol. 15:317-323(1990).
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; X60092; CAA42689.1; -; mRNA.
DR   PIR; S11965; AJLCQB.
DR   AlphaFoldDB; P23712; -.
DR   SMR; P23712; -.
DR   PRIDE; P23712; -.
DR   EnsemblPlants; rna-gnl|WGS:NBSK|LSAT_2X68621_mrna; cds-PLY72546.1; gene-LSAT_2X68621.
DR   Gramene; rna-gnl|WGS:NBSK|LSAT_2X68621_mrna; cds-PLY72546.1; gene-LSAT_2X68621.
DR   OrthoDB; 784869at2759; -.
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..358
FT                   /note="Glutamine synthetase"
FT                   /id="PRO_0000153174"
FT   DOMAIN          19..99
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT   DOMAIN          106..358
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT   REGION          38..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   358 AA;  39470 MW;  789A4E731DDDFBEB CRC64;
     MALLSDLVNL DLSSITDKII AEYIWIGGSG MDLRSKARTL SGPVSDPSEL PKWNYDGSST
     GQAPGEDSEV IIYPQAIFKD PFRRGNHILV MCDAYTPAGE PIPTNKRAAA AKIFSNPEVE
     KEVTWYGIEQ EYTLLQKDTN WPLGWPLGGF PGPQGPYYCG IGADKAFGRD IVDAHYKACL
     YAGVNISGIN GEVMPGQWEF QVGPSVGIAA ADQIWVARYI LERITEIYGV VVSFDPKPIP
     GDWNGAGAHT NYSTKTMREE GGYEVIKKAI EKLGLRHKEH IAAYGEGNER RLTGRHETAD
     INTFLWGVAN RGASIRVGRD TEKEGKGYFE DRRPASNMDP YVVTSMIAET TILWDNKS