ID   GLNA2_PEA               Reviewed;         430 AA.
AC   P08281;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 2.
DT   25-MAY-2022, entry version 101.
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;
OS   Pisum sativum (Garden pea).
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; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2898472; DOI=10.1016/s0021-9258(19)81566-1;
RA   Tingey S.V., Tsai F., Edwards J., Walker E.L., Coruzzi G.M.;
RT   "Chloroplast and cytosolic glutamine synthetase are encoded by homologous
RT   nuclear genes which are differentially expressed in vivo.";
RL   J. Biol. Chem. 263:9651-9657(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 58-430.
RC   STRAIN=cv. Sparkle;
RX   PubMed=2884100; DOI=10.1002/j.1460-2075.1987.tb04710.x;
RA   Tingey S.V., Walker E.L., Coruzzi G.M.;
RT   "Glutamine synthetase genes of pea encode distinct polypeptides which are
RT   differentially expressed in leaves, roots and nodules.";
RL   EMBO J. 6:1-9(1987).
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   -!- 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: Plastid, chloroplast.
CC   -!- MISCELLANEOUS: In pea there are distinct isozymes in leaves, roots and
CC       nodules.
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; M20664; AAA33653.1; -; mRNA.
DR   EMBL; X05514; CAA29057.1; -; mRNA.
DR   PIR; A28089; AJPMQ2.
DR   AlphaFoldDB; P08281; -.
DR   SMR; P08281; -.
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   CHAIN           50..430
FT                   /note="Glutamine synthetase leaf isozyme, chloroplastic"
FT                   /id="PRO_0000011182"
FT   DOMAIN          77..157
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT   DOMAIN          161..430
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT   REGION          99..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   430 AA;  47346 MW;  AB7EFA4F53970D7E CRC64;
     MAQILAPSTQ WQMRITKTSP CATPITSKMW SSLVMKQTKK VAHSAKFRVM AVNSENGTIN
     RVEDLLNLDI TPFTDSIIAE YIWIGGTGID VRSKSRTISK PVSHPSEVPK WNYDGSSTGQ
     APGEDSEVIL YPQAIFKDPF RGGNNILVVC DAYTPAGEPI PTNKRHRAAE IFSNPKVEAE
     IPWYGIEQEY TLLQTNVKWP LGWPVGGYPG PQGPYYCAAG ADKSFGRDIS DAHYKACIYA
     GINISGTNGE VMPGQWEYQV GPSVGIEAGD HIWASRYILE RITEQAGVVL TLDPKPIEGD
     WNGAGCHTNY STKSMREDGG FEVIKKAILN LSLRHKIHIE AYGEGNERRL TGKHETASIN
     DFSWGVANRG CSIRVGRDTE KNGKGYLEDR RPASNMDPYV VTALLAESTL LWEPTLEAEA
     LAAQKIALKV