ID   GLNA_TUBBO              Reviewed;         358 AA.
AC   Q86ZU6;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-NOV-2023, 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   Tuber borchii (White truffle).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Tuberaceae; Tuber.
OX   NCBI_TaxID=42251;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=12683951; DOI=10.1042/bj20030152;
RA   Montanini B., Betti M., Marquez A.J., Balestrini R., Bonfante P.,
RA   Ottonello S.;
RT   "Distinctive properties and expression profiles of glutamine synthetase
RT   from a plant symbiotic fungus.";
RL   Biochem. J. 373:357-368(2003).
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; AF462037; AAP23163.1; -; mRNA.
DR   AlphaFoldDB; Q86ZU6; -.
DR   SMR; Q86ZU6; -.
DR   BRENDA; 6.3.1.2; 7423.
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:0006542; P:glutamine biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.10.20.70; Glutamine synthetase, N-terminal domain; 1.
DR   Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 1.
DR   InterPro; IPR008147; Gln_synt_N.
DR   InterPro; IPR036651; Gln_synt_N_sf.
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   PANTHER; PTHR20852; GLUTAMINE SYNTHETASE; 1.
DR   PANTHER; PTHR20852:SF57; GLUTAMINE SYNTHETASE 2 CYTOPLASMIC; 1.
DR   Pfam; PF00120; Gln-synt_C; 1.
DR   Pfam; PF03951; Gln-synt_N; 1.
DR   SMART; SM01230; Gln-synt_C; 1.
DR   SUPFAM; SSF54368; Glutamine synthetase, N-terminal domain; 1.
DR   SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 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..358
FT                   /note="Glutamine synthetase"
FT                   /id="PRO_0000153164"
FT   DOMAIN          26..105
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT   DOMAIN          112..358
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
SQ   SEQUENCE   358 AA;  39664 MW;  4BF82095152856E0 CRC64;
     MSENSTIVSN TANLVKFLNL DQKGSILAEY IWIDGANGVR SKTKTLFKKP SSVEDLPEWN
     FDGSSTGQAP GEDSDIYLRP VAIFPDPFRM GDNILVLAEC WNADGSPNKF NHRHECAKIM
     EAHKDQKPWF GLEQEYTLFD LYGNPYGWPK GGFPGPQGPY YCGVGTGKVY CRDIVEAHYK
     ACLFAGIKIS GINAEVLPSQ WEFQVGPCVG IEMGDHLWIS RYLLHRVAEE FGVKISFHPK
     PIPGDWNGSG LHTNVSTQAM RDEGGMKAIE EAIQKLSTRH AEHIAVYGDD NTLRLTGRHE
     TGNIDAFSYG VADRGSSIRI PRSCAKEGKG YFEDRRPASN ACPYQITGIM METICGGI
//