ID   GLNA_EMENI              Reviewed;         357 AA.
AC   Q96V52; C8V4Q5; Q5B5M1;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 3.
DT   24-JAN-2024, entry version 108.
DE   RecName: Full=Glutamine synthetase;
DE            Short=GS;
DE            EC=6.3.1.2;
DE   AltName: Full=Glutamate--ammonia ligase;
GN   Name=glnA; ORFNames=AN4159;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11566979; DOI=10.1128/jb.183.20.5826-5833.2001;
RA   Margelis S., D'Souza C., Small A.J., Hynes M.J., Adams T.H., Davis M.A.;
RT   "Role of glutamine synthetase in nitrogen metabolite repression in
RT   Aspergillus nidulans.";
RL   J. Bacteriol. 183:5826-5833(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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=AAK70354.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=EAA59420.1; Type=Erroneous gene model prediction; Evidence={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; AF333968; AAK70354.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AACD01000067; EAA59420.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001302; CBF74586.1; -; Genomic_DNA.
DR   RefSeq; XP_661763.1; XM_656671.1.
DR   AlphaFoldDB; Q96V52; -.
DR   SMR; Q96V52; -.
DR   STRING; 227321.Q96V52; -.
DR   EnsemblFungi; CBF74586; CBF74586; ANIA_04159.
DR   GeneID; 2873585; -.
DR   KEGG; ani:AN4159.2; -.
DR   eggNOG; KOG0683; Eukaryota.
DR   HOGENOM; CLU_036762_1_1_1; -.
DR   InParanoid; Q96V52; -.
DR   OMA; DRRPNAN; -.
DR   OrthoDB; 1115057at2759; -.
DR   Proteomes; UP000000560; Chromosome II.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004356; F:glutamine synthetase activity; IBA:GO_Central.
DR   GO; GO:0006542; P:glutamine biosynthetic process; IBA:GO_Central.
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   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..357
FT                   /note="Glutamine synthetase"
FT                   /id="PRO_0000153156"
FT   DOMAIN          25..104
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT   DOMAIN          111..357
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT   CONFLICT        236
FT                   /note="F -> N (in Ref. 1; AAK70354)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   357 AA;  39714 MW;  3A8D1110050EE9CA CRC64;
     MTDSTNVSNT ENLMKYMSLD QRGSVMAEYI WIDAHGGTRS KTKTLSKAPS SVDELPEWNF
     DGSSTAQAPG DNSDVYLRPV AMYPDPFRRG DNILVLCETW DSDGSPNKFN YRHDCARLME
     THAKEEFWFG LEQEYTLLGP DGWPYGWPKG GFPGAQGPYY CGVGTGKVYC RDIVEAHYRA
     CLYAGVKISG INAEVMPSQW EYQVGPCHGI EMGDHLWISR FLLHRVAEEF GVKISFDPKP
     IKGDWNGAGL HTNVSTTSTR AEGGIKAIES YMKKLEARHV EHIAVYGEGN EERLTGRHET
     GNIDKFSYGV ADRGGSIRIP RQVAKDGKGY FEDRRPASNA DPYQITGIIA ETLCGGL
//