ID   GLNA_AGABI              Reviewed;         354 AA.
AC   O00088;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Glutamine synthetase;
DE            Short=GS;
DE            EC=6.3.1.2;
DE   AltName: Full=Glutamate--ammonia ligase;
GN   Name=glnA;
OS   Agaricus bisporus (White button mushroom).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricaceae; Agaricus.
OX   NCBI_TaxID=5341;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Horst H39;
RX   PubMed=9349709; DOI=10.1007/pl00008612;
RA   Kersten M.A.S.H., Mueller Y., Op den Camp H.J.M., Vogels G.D.,
RA   van Griensven L.J.L.D., Visser J., Schaap P.J.;
RT   "Molecular characterization of the glnA gene encoding glutamine synthetase
RT   from the edible mushroom Agaricus bisporus.";
RL   Mol. Gen. Genet. 256:179-186(1997).
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   -!- 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; Y12704; CAA73235.1; -; Genomic_DNA.
DR   AlphaFoldDB; O00088; -.
DR   SMR; O00088; -.
DR   GO; GO:0005737; C:cytoplasm; 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   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Ligase; Nucleotide-binding.
FT   CHAIN           1..354
FT                   /note="Glutamine synthetase"
FT                   /id="PRO_0000153149"
FT   DOMAIN          22..101
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT   DOMAIN          108..354
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
SQ   SEQUENCE   354 AA;  39533 MW;  93CDA55EC287B8A2 CRC64;
     MANTYHNDLL APYLSLDQGD KIQAEYVWID GDGGLRCKTT TVSKKVTDIG QLRIWDFDGS
     STNQAPGHDS DVYLRPAAIF KDPFRGGDNI LVLAETYNND GTPNRTNHRH HAKKVFDEAK
     EHEPWFGLEQ EYTLFDADDQ PYGWPKGGFP GPQGPYYCGA GTGKVFARDL IEAHYRACLY
     AGINISGINA EVMPSQWEFQ VGPCEGISMG DHLWMARYLL VRIAEQWGVK VSFHPKPLKG
     EWNGAGCHTN FSTKAMREAG GMKFIEDAIE KLAKRHDEHI AVYGEDNDLR LTGRHETGHI
     SNFSSGVANR GASIRVPRHV ASQGYGYLED RRPASNIDPY RVTSIIAETT ILDK