ID   GLNA2_MEDSA             Reviewed;         428 AA.
AC   Q9XQ94;
DT   02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Glutamine synthetase leaf isozyme, chloroplastic;
DE            EC=6.3.1.2;
DE   AltName: Full=GS2;
DE   AltName: Full=Glutamate--ammonia ligase;
DE   Flags: Precursor;
GN   Name=GS2; Synonyms=GLN;
OS   Medicago sativa (Alfalfa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Saranac; TISSUE=Leaf;
RA   Zozaya-Garza M., Sengupta-Gopalan C.;
RT   "Glutamine synthetase gene isolation from an alfalfa leaf cDNA library.";
RL   (er) Plant Gene Register PGR99-054(1999).
CC   -!- FUNCTION: The light-modulated chloroplast enzyme, encoded by a nuclear
CC       gene and expressed primarily in leaves, is responsible for the
CC       reassimilation of the ammonia generated by photorespiration.
CC       {ECO:0000250}.
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- MISCELLANEOUS: Irreversibly inhibited by the herbicide L-
CC       phosphinothricin (PPT). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR   EMBL; AF124244; AAD28443.1; -; mRNA.
DR   AlphaFoldDB; Q9XQ94; -.
DR   SMR; Q9XQ94; -.
DR   PRIDE; Q9XQ94; -.
DR   GO; GO:0009507; C:chloroplast; 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; Chloroplast; Ligase; Nitrogen fixation; Nucleotide-binding;
KW   Plastid; Transit peptide.
FT   TRANSIT         1..49
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000250"
FT   CHAIN           50..428
FT                   /note="Glutamine synthetase leaf isozyme, chloroplastic"
FT                   /id="PRO_0000011180"
FT   DOMAIN          75..155
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT   DOMAIN          159..428
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
SQ   SEQUENCE   428 AA;  47115 MW;  2E37FB1957EA54C3 CRC64;
     MAQILAPSIQ CQTRITKTSP LATPISSKMW SSLVMKQNKK VARSAKFRVM AINSGTINRV
     EDLLNLDITP FTDSIIAEYI WIGGTGIDVR SKSRTISKPV EHPSELPKWN YDGSSTGQAP
     GEDSEVILYP QAIFKDPFRG GNNILVICDA YTPQGEPIPT NKRHKAAEIF SNPKVEAEIP
     WYGIEQEYTL LQTDVKWPLG WPVGGYPGPQ GPYYCAAGAD KSFGRDISDA HYKACLYAGI
     NISGTNGEVM PGQWEYQVGP SVGIEAGDHI WASRYILERI TEQAGVVLTL DPKPIEGDWN
     GAGCHTNYST KSMREDGGFE VIKKAILNLS LRHKVHIEAY GEGNERRLTG KHETASINTF
     SWGVANRGCS IRVGRDTEKN GKGYLEDRRP ASNMDPYVVT ALLAESTLLW EPTLEAEALA
     AQKIALKV