ID   GLNAC_MAIZE             Reviewed;         423 AA.
AC   P25462;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   27-MAR-2024, entry version 144.
DE   RecName: Full=Glutamine synthetase, chloroplastic;
DE            EC=6.3.1.2;
DE   AltName: Full=GS2;
DE   AltName: Full=Glutamate--ammonia ligase;
DE   Flags: Precursor;
GN   Name=GLN2;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Black Mexican Sweet; TISSUE=Leaf;
RX   PubMed=2906306; DOI=10.1093/genetics/120.4.1111;
RA   Snustad D.P., Hunsperger J.P., Chereskin B.M., Messing J.;
RT   "Maize glutamine synthetase cDNAs: isolation by direct genetic selection in
RT   Escherichia coli.";
RL   Genetics 120:1111-1124(1988).
RN   [2]
RP   POSSIBLE FRAMESHIFT ERROR IN SEQUENCE DESCRIBED IN PUBMED:2906306.
RA   Patthey J.-P.;
RL   Unpublished observations (MAY-1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Black Mexican Sweet; TISSUE=Seedling;
RX   PubMed=8106013; DOI=10.1007/bf00029015;
RA   Li M.-G., Villemur R., Hussey P.J., Silflow C.D., Gantt J.S., Snustad D.P.;
RT   "Differential expression of six glutamine synthetase genes in Zea mays.";
RL   Plant Mol. Biol. 23:401-407(1993).
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   -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X65931; CAA46724.1; -; mRNA.
DR   PIR; S39482; S39482.
DR   RefSeq; NP_001105725.1; NM_001112255.1.
DR   AlphaFoldDB; P25462; -.
DR   SMR; P25462; -.
DR   STRING; 4577.P25462; -.
DR   BindingDB; P25462; -.
DR   ChEMBL; CHEMBL2285357; -.
DR   PaxDb; 4577-GRMZM2G098290_P02; -.
DR   MaizeGDB; 61728; -.
DR   eggNOG; KOG0683; Eukaryota.
DR   InParanoid; P25462; -.
DR   OrthoDB; 1115057at2759; -.
DR   BRENDA; 6.3.1.2; 6752.
DR   PRO; PR:P25462; -.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; P25462; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IEA:EnsemblPlants.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004356; F:glutamine synthetase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003729; F:mRNA binding; IEA:EnsemblPlants.
DR   GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
DR   GO; GO:0046686; P:response to cadmium ion; IEA:EnsemblPlants.
DR   Gene3D; 3.10.20.70; Glutamine synthetase, N-terminal domain; 1.
DR   Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 1.
DR   InterPro; IPR008147; Gln_synt_N.
DR   InterPro; IPR036651; Gln_synt_N_sf.
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   PANTHER; PTHR20852; GLUTAMINE SYNTHETASE; 1.
DR   PANTHER; PTHR20852:SF117; GLUTAMINE SYNTHETASE, CHLOROPLASTIC_MITOCHONDRIAL; 1.
DR   Pfam; PF00120; Gln-synt_C; 1.
DR   Pfam; PF03951; Gln-synt_N; 1.
DR   SMART; SM01230; Gln-synt_C; 1.
DR   SUPFAM; SSF54368; Glutamine synthetase, N-terminal domain; 1.
DR   SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 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; Nucleotide-binding; Plastid;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..51
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           52..423
FT                   /note="Glutamine synthetase, chloroplastic"
FT                   /id="PRO_0000011179"
FT   DOMAIN          70..150
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT   DOMAIN          154..423
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT   REGION          89..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   423 AA;  46017 MW;  EC799D71E0BD6C5F CRC64;
     MAQAVVPAMQ CRVGVKAAAG RVWSAGRTRT GRGGASPGFK VMAVSTGSTG VVPRLEQLLN
     MDTTPYTDKV IAEYIWVGGS GIDIRSKSRT ISKPVEDPSE LPKWNYDGSS TGQAPGEDSE
     VILYPQAIFK DPFRGGNNVL VICDTYTPQG EPLPTNKRHR AAQIFSDPKV GEQVPWFGIE
     QEYTLLQKDV NWPLGWPVGG FPGPQGPYYC AVGADKSFGR DISDAHYKAC LYAGINISGT
     NGEVMPGQWE YQVGPSVGIE AGDHIWISRY ILERITEQAG VVLTLDPKPI QGDWNGAGCH
     TNYSTKTMRE DGGFEEIKRA ILNLSLRHDL HISAYGEGNE RRLTGKHETA SIGTFSWGVA
     NRGCSIRVGR DTEAKGKGYL EDRRPASNMD PYIVTGLLAE TTILWQPSLE AEALAAKKLA
     LKV
//