ID   GLNA_DUNSA              Reviewed;         234 AA.
AC   P11600;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   RecName: Full=Glutamine synthetase;
DE            EC=6.3.1.2;
DE   AltName: Full=Glutamate--ammonia ligase;
DE   Flags: Fragment;
OS   Dunaliella salina (Green alga) (Protococcus salinus).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Dunaliellaceae; Dunaliella.
OX   NCBI_TaxID=3046;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Long Z., Nelson N.;
RL   Submitted (MAY-1989) to the EMBL/GenBank/DDBJ databases.
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: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01331}.
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DR   EMBL; X15280; CAA33353.1; -; mRNA.
DR   PIR; S04888; AJDHQ.
DR   AlphaFoldDB; P11600; -.
DR   SMR; P11600; -.
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:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR   Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 1.
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   PANTHER; PTHR20852; GLUTAMINE SYNTHETASE; 1.
DR   PANTHER; PTHR20852:SF93; GLUTAMINE SYNTHETASE CYTOSOLIC ISOZYME 1-4; 1.
DR   Pfam; PF00120; Gln-synt_C; 1.
DR   SMART; SM01230; Gln-synt_C; 1.
DR   SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR   PROSITE; PS00181; GLNA_ATP; 1.
DR   PROSITE; PS51987; GS_CATALYTIC; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Ligase; Nucleotide-binding.
FT   CHAIN           <1..234
FT                   /note="Glutamine synthetase"
FT                   /id="PRO_0000153171"
FT   DOMAIN          1..234
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT   REGION          126..157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        128..147
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
SQ   SEQUENCE   234 AA;  26224 MW;  D5EB25319131DDF6 CRC64;
     KAQEPWFGIE QEYTLLNSVT KWPLGWPKGG YPAGQGPYYC SVGAGRSIGR DIPEVHYRCC
     LHAGIQISGV NGEVLPSQWE YQVGPVEGIA MGDQMWMSRY LMYRVAELFN VEVTFDPKPI
     PGDWNGSGGH VNFSNRQPES PPAGKQSRSS AKKLGKRHRW HIAAYGEGNE RRLTGKHETS
     SMNDFSWGVA NRGCSIRVGR MVPVEKCGYY EDRRPSSNLD PYVVTRLLVE TTLL
//