ID   GLNA_PINSY              Reviewed;         357 AA.
AC   P52783;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   RecName: Full=Glutamine synthetase cytosolic isozyme;
DE            EC=6.3.1.2;
DE   AltName: Full=GS1;
DE   AltName: Full=Glutamate--ammonia ligase;
OS   Pinus sylvestris (Scotch pine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC   Pinus subgen. Pinus.
OX   NCBI_TaxID=3349;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8102906; DOI=10.1007/bf00027368;
RA   Canton F.R., Garcia-Gutierrez A., Gallardo F., de Vicente A., Canovas F.M.;
RT   "Molecular characterization of a cDNA clone encoding glutamine synthetase
RT   from a gymnosperm, Pinus sylvestris.";
RL   Plant Mol. Biol. 22:819-828(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7506600; DOI=10.1007/bf01089034;
RA   Elmlinger M.W., Bolle C., Batschauer A., Oelmueller R., Mohr H.;
RT   "Coaction of blue light and light absorbed by phytochrome in control of
RT   glutamine synthetase gene expression in Scots pine (Pinus sylvestris L.)
RT   seedlings.";
RL   Planta 192:189-194(1994).
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: 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; X69822; CAA49476.1; -; mRNA.
DR   EMBL; X74429; CAA52448.1; -; mRNA.
DR   PIR; S36195; S36195.
DR   AlphaFoldDB; P52783; -.
DR   SMR; P52783; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004356; F:glutamine synthetase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
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:SF118; GLUTAMINE SYNTHETASE; 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; Cytoplasm; Ligase; Nucleotide-binding.
FT   CHAIN           1..357
FT                   /note="Glutamine synthetase cytosolic isozyme"
FT                   /id="PRO_0000153195"
FT   DOMAIN          20..100
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT   DOMAIN          107..357
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT   CONFLICT        183
FT                   /note="S -> A (in Ref. 2; CAA52448)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        307
FT                   /note="W -> R (in Ref. 2; CAA52448)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   357 AA;  39571 MW;  659B457032DB9F11 CRC64;
     MSSVLTDLLN LDLSDVTEKV IAEYIWIGGS GMDMRSKARS LSGPVSSVKE LPKWNYDGSS
     TGQAQGHDSE VILYPQAIFR DPFRRGKHIL VICDAYSPNG TAIPSNKRAA AAKIFNEKAV
     SDEETWYGLE QEYTLLQKDV KWPLGWPIGG YPGPQGPYYC GVGADKAWGR DIVDAHYKAC
     LYSGINISGI NGEVMPGQWE FQVGPSVGIS AADELWCARF IMERITEKAG VVLSFDPKPI
     EGDWNGAGCH TNYSTKSMRK EGGFEVIKKA IEKLKLRHKE HISAYGEGNE RRLTGRHETA
     DMNTFSWGVA NRGASVRVGR DTEKEGKGYF EDRRPASNMD PYIVTSMIAE TTILWKP
//