ID   GLNA_AMAMU              Reviewed;         354 AA.
AC   Q8X169;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 2.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Glutamine synthetase;
DE            Short=GS;
DE            EC=6.3.1.2;
DE   AltName: Full=Glutamate--ammonia ligase;
GN   Name=GLN1;
OS   Amanita muscaria (Fly agaric).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Amanitaceae; Amanita.
OX   NCBI_TaxID=41956;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Nehls U., Kleber R., Hampp R.;
RT   "Glutamine synthetase in Amanita muscaria.";
RL   Submitted (JAN-2002) 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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAD22045.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AJ428992; CAD22045.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; Q8X169; -.
DR   SMR; Q8X169; -.
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   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Ligase; Nucleotide-binding.
FT   CHAIN           1..354
FT                   /note="Glutamine synthetase"
FT                   /id="PRO_0000153150"
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;  39337 MW;  10C9AC87BCF5257E CRC64;
     MANQYHNDLL APYLALDQGG KFHAEYVWID GDGGLRSKTT TVDQKVTDIS QLRVWDFDGS
     STNQAPSGNS DVYLRPSAIF KDPFRGGENI LVLSETYNND GTPNRTNHRH HTAKVMELAK
     DEIPWFGIEQ EYTLFDADGS PYGWPKGGFP GPQGPYYCGA GTGKVFARDL IEAHYRACLY
     AGVNISGINA EVMPSQWEFQ VGPCEGISMG DHLWMARYLL IRVAEQWGVK VSFHPKPLQG
     DWNGAGAHTN YSTLAMREPG GMKYIEAAIE KLAKRHDEHI AVYGEDNEMR LTGRHETGHI
     GTFSSGVANR GASIRVPRHV ANKGYGYLED RRPASNIDPY RVTGIIIETT ILDK