ID   GLNA2_HORVU             Reviewed;         434 AA.
AC   P13564;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 2.
DT   25-MAY-2022, entry version 117.
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;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1983297; DOI=10.1007/bf00017735;
RA   Stroman P., Baima S., Casadoro G.;
RT   "A cDNA sequence coding for glutamine synthetase in Hordeum vulgare L.";
RL   Plant Mol. Biol. 15:161-163(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 9-434.
RC   STRAIN=cv. Maris Mink; TISSUE=Leaf;
RX   PubMed=1983286; DOI=10.1007/bf00028767;
RA   Freeman J., Marquez A.J., Wallsgrove R.M., Saarelainen R., Forde B.G.;
RT   "Molecular analysis of barley mutants deficient in chloroplast glutamine
RT   synthetase.";
RL   Plant Mol. Biol. 14:297-311(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 48-434.
RX   PubMed=2473765; DOI=10.1007/bf02910467;
RA   Baima S., Haegi A., Stroman P., Casadoro G.;
RT   "Characterization of a cDNA clone for barley leaf glutamine synthetase.";
RL   Carlsberg Res. Commun. 54:1-9(1989).
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 barley, there are distinct isozymes in the
CC       chloroplast, and cytoplasm.
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; X53580; CAA37643.1; -; mRNA.
DR   EMBL; X16000; CAA34131.1; -; mRNA.
DR   PIR; S11865; AJBHQ.
DR   AlphaFoldDB; P13564; -.
DR   SMR; P13564; -.
DR   PRIDE; P13564; -.
DR   BRENDA; 6.3.1.2; 2687.
DR   SABIO-RK; P13564; -.
DR   ExpressionAtlas; P13564; 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:glutamate-ammonia ligase 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; -; 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; Nucleotide-binding; Plastid;
KW   Transit peptide.
FT   TRANSIT         1..54
FT                   /note="Chloroplast"
FT   CHAIN           55..434
FT                   /note="Glutamine synthetase leaf isozyme, chloroplastic"
FT                   /id="PRO_0000011178"
FT   DOMAIN          81..161
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT   DOMAIN          168..434
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          101..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        9..27
FT                   /note="GAGGCAGDAVPGGGEGQDG -> AQAVVQAMQCQVGVRGRTA (in Ref.
FT                   2; CAA34131)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        41
FT                   /note="S -> R (in Ref. 2; CAA34131)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   434 AA;  47094 MW;  FC47F5685EFC0D1E CRC64;
     MQVRRDDDGA GGCAGDAVPG GGEGQDGVPA RQPAGRVWGV SRAARATSGF KVLALGPETT
     GVIQRMQQLL DMDTTPFTDK IIAEYIWVGG SGIDLRSKSR TISKPVEDPS ELPKWNYDGS
     STGQAPGEDS EVILYPQAIF KDPFRGGNNI LVICDTYTPQ GEPIPTNKRH MAAQIFSDPK
     VTSQVPWFGI EQEYTLMQRD VNWPLGWPVG GYPGPQGPYY CAVGSDKSFG RDISDAHYKA
     CLYAGIEISG TNGEVMPGQW EYQVGPSVGI DAGDHIWASR YILERITEQA GVVLTLDPKP
     IQGDWNGAGC HTNYSTLSMR EDGGFDVIKK AILNLSLRHD LHIAAYGEGN ERRLTGLHET
     ASISDFSWGV ANRGCSIRVG RDTEAKGKGY LEDRRPASNM DPYTVTALLA ETTILWEPTL
     EAEALAAKKL ALKV