ID   GLNA_LUPLU              Reviewed;         353 AA.
AC   P52782;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Glutamine synthetase nodule isozyme;
DE            Short=GS;
DE            EC=6.3.1.2;
DE   AltName: Full=Glutamate--ammonia ligase;
OS   Lupinus luteus (European yellow lupine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   genistoids sensu lato; core genistoids; Genisteae; Lupinus.
OX   NCBI_TaxID=3873;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Ventus; TISSUE=Root;
RX   PubMed=7904975; DOI=10.1016/0378-1119(93)90452-9;
RA   Boron L., Legocki A.B.;
RT   "Cloning and characterization of a nodule-enhanced glutamine synthetase-
RT   encoding gene from Lupinus luteus.";
RL   Gene 136:95-102(1993).
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   -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR   EMBL; X71399; CAA50522.1; -; Genomic_DNA.
DR   AlphaFoldDB; P52782; -.
DR   SMR; P52782; -.
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   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Ligase; Nitrogen fixation; Nucleotide-binding.
FT   CHAIN           1..353
FT                   /note="Glutamine synthetase nodule isozyme"
FT                   /id="PRO_0000153177"
FT   DOMAIN          19..99
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT   DOMAIN          106..353
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
SQ   SEQUENCE   353 AA;  38829 MW;  E99CE58C089111C5 CRC64;
     MSVLSDLINL NLSDTTEKII AEYIWVGGSG VDLRSKARTL SGPVNDPSKL PKWNYDGSST
     GQAPGKDSEV ILWPQAIFKD PFRRGNNILV MCDTYTPAGE PIPTNKRHAA AKIFSHPDVV
     AEEPWFGIEQ EYTLLQKDIH WPIGWPLGGF PGPQGPYYCG TGAEKAFGRD IVDSHYKACL
     YAGINISGIN AEVMPGQWEF QVGPSVGISA GDELWVARYI LERITEIAGV VLSLDPKPIP
     GDWNGAGAHT NYSTKSMRND GGYEVIKKAI EKLGKRHNEH IAAYGEGNER RLTGRHETAD
     ISTFFWGVAN RGASIRVGRD TEKEGKGYFE DRRPASNMDP YVVTSMIAET TLL