ID   GLNA_CRYNJ              Reviewed;         358 AA.
AC   P0CN84; D3NQ34; Q55ZS0; Q5KP31; Q96UG9;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=Glutamine synthetase;
DE            Short=GS;
DE            EC=6.3.1.2;
DE   AltName: Full=Glutamate--ammonia ligase;
GN   Name=GLN1; Synonyms=FGS; OrderedLocusNames=CNA04370;
OS   Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS   MYA-565) (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=214684;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=309 CAP 67;
RA   Biondo C., Beninati C., Delfino D., Mancuso G., Midiri A., Tomaselli G.,
RA   Teti G.;
RT   "Immunostimulating glutamine synthetase.";
RL   Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEC21 / ATCC MYA-565;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
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   ---------------------------------------------------------------------------
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; AJ414581; CAD10037.1; -; mRNA.
DR   EMBL; AE017341; AAW40974.1; -; Genomic_DNA.
DR   EMBL; AE017341; AAW40975.1; -; Genomic_DNA.
DR   RefSeq; XP_566793.1; XM_566793.1.
DR   RefSeq; XP_566794.1; XM_566794.1.
DR   AlphaFoldDB; P0CN84; -.
DR   SMR; P0CN84; -.
DR   STRING; 5207.AAW40975; -.
DR   PaxDb; P0CN84; -.
DR   PRIDE; P0CN84; -.
DR   EnsemblFungi; AAW40974; AAW40974; CNA04370.
DR   EnsemblFungi; ALO60332; ALO60332; CNA04370.
DR   GeneID; 3253352; -.
DR   VEuPathDB; FungiDB:CNA04370; -.
DR   eggNOG; KOG0683; Eukaryota.
DR   HOGENOM; CLU_036762_1_1_1; -.
DR   InParanoid; P0CN84; -.
DR   OMA; DRRPNAN; -.
DR   OrthoDB; 784869at2759; -.
DR   Proteomes; UP000002149; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004356; F:glutamate-ammonia ligase activity; IBA:GO_Central.
DR   GO; GO:0006542; P:glutamine biosynthetic process; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..358
FT                   /note="Glutamine synthetase"
FT                   /id="PRO_0000153154"
FT   DOMAIN          25..104
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT   DOMAIN          111..358
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT   CONFLICT        219
FT                   /note="A -> P (in Ref. 1; CAD10037)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   358 AA;  39516 MW;  F159AE2CAA305ACB CRC64;
     MSQLIATKRV DLLAPYLALD QGSRVQAEYI WIDAEGGIRS KTMTLDKAPS SVADLKEWNF
     DGSSTNQAPA DNSDVFLRPV AIFKDPFRGG ANILVLCECY DNDGTPNKSN YRAHCKKVMD
     AAKDTEPWFG LEQEYTLFDA DGQVFGWPKN GFPGPQGPYY CGVGAGKVFA RDFIEAHYRA
     CLYAGIKISG INAEVMPSQW EFQVGPCTGI EMGDHLWMAR FLLLRIGEEW GITPSLHPKP
     LKGDWNGAGC HSNYSTKDMR TPGKGMAAIE DAIKKLEKKH LEHIAVYGED NDLRLTGKHE
     TASMTTFSAG VANRGASIRI PRHVGAQGYG YLEDRRPASN VDPYRVTAIL VETTVLNN