ID   GLNA_HEBCY              Reviewed;         354 AA.
AC   Q96UV5;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Glutamine synthetase;
DE            Short=GS;
DE            EC=6.3.1.2;
DE   AltName: Full=Glutamate--ammonia ligase;
GN   Name=GLN1;
OS   Hebeloma cylindrosporum.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Hymenogastraceae; Hebeloma.
OX   NCBI_TaxID=76867;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=h1;
RA   Rodriguez-Pastrana B., Javelle A., Belleville R., Morel M., Botton B.,
RA   Jacob C., Chalot M., Brun A.;
RT   "Nucleotide sequence and expression of NADP-GDH and GS from the
RT   ectomycorrhizal fungus Hebeloma cylindrosporum.";
RL   Submitted (JUL-2001) 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}.
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DR   EMBL; AF411820; AAK96111.1; -; mRNA.
DR   AlphaFoldDB; Q96UV5; -.
DR   SMR; Q96UV5; -.
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_0000153159"
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;  39225 MW;  DEFEF69A36322241 CRC64;
     MAYRYHNDLL APYLALPQGD KIQAEYVWVD GDGGLRSKTT TVSKKVTDIG SLRIWDFDGS
     STNQAPGHDS DVYLRPAAIF KDPFRGGDNI LVLAETYNSD GTPNRTNFRH HAAKVMEQAK
     EDVPWFGLEQ EYTLFDADGS PYGWPKGGFP GPQGPYYCGA GTGKVFARDL IEAHYRACLY
     SGINISGINA EVMPSQWEFQ VGPCEGISMG DHLWMARYLL VRIAEQWAVK VSFHPKPLQG
     DWNGAGCHTN YSTKAMREPG GMKVIEEAIE KLSKRHDEHI AVYGEDNDLR LTGRHETGHI
     GAFSSGVANR GASIRVPRHV AAQGYGYLED RRPASNIDPY RVTSIIVETT LLNA