ID   GLNA_SACS2              Reviewed;         471 AA.
AC   P23794;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2001, sequence version 2.
DT   25-MAY-2022, entry version 126.
DE   RecName: Full=Glutamine synthetase;
DE            Short=GS;
DE            EC=6.3.1.2;
DE   AltName: Full=Glutamate--ammonia ligase;
GN   Name=glnA; Synonyms=glnA-1; OrderedLocusNames=SSO0366;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1973523; DOI=10.1007/bf00261719;
RA   Sanangelantoni A.M., Barbarini D., di Pasquale G., Cammarano P., Tiboni O.;
RT   "Cloning and nucleotide sequence of an archaebacterial glutamine synthetase
RT   gene: phylogenetic implications.";
RL   Mol. Gen. Genet. 221:187-194(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
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   -!- ACTIVITY REGULATION: The activity of this enzyme is controlled by
CC       adenylation under conditions of abundant glutamine. The fully
CC       adenylated enzyme complex is inactive (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR   EMBL; X53263; CAA37352.1; -; Genomic_DNA.
DR   EMBL; AE006641; AAK40696.1; -; Genomic_DNA.
DR   PIR; A99180; A99180.
DR   PIR; S11899; S11899.
DR   RefSeq; WP_009990668.1; NC_002754.1.
DR   AlphaFoldDB; P23794; -.
DR   SMR; P23794; -.
DR   STRING; 273057.SSO0366; -.
DR   EnsemblBacteria; AAK40696; AAK40696; SSO0366.
DR   GeneID; 44129340; -.
DR   KEGG; sso:SSO0366; -.
DR   PATRIC; fig|273057.12.peg.360; -.
DR   eggNOG; arCOG01909; Archaea.
DR   HOGENOM; CLU_017290_1_2_2; -.
DR   InParanoid; P23794; -.
DR   OMA; VFPWESK; -.
DR   PhylomeDB; P23794; -.
DR   Proteomes; UP000001974; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; 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   GO; GO:0019740; P:nitrogen utilization; 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; IPR004809; Gln_synth_I.
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   TIGRFAMs; TIGR00653; GlnA; 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; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..471
FT                   /note="Glutamine synthetase"
FT                   /id="PRO_0000153214"
FT   DOMAIN          15..99
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT   DOMAIN          107..471
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT   MOD_RES         400
FT                   /note="O-AMP-tyrosine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        162
FT                   /note="S -> T (in Ref. 1; CAA37352)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   471 AA;  53348 MW;  1CC4239287B6C2CD CRC64;
     MPSTAEDVLK FLKENNIKWV DLQFTDVPGR LHHITIPADE FDLESLKTGF GKLDGSSIRG
     FTSIYESDMV LLPVPETMTL IPWSPGVARV LCKVFWGGGK GRFERDPRFI AEEAEKYQTE
     QGYTSYYGPE LEFFMFDKVK LDVSAPQSGT GYKIYAREAP WSDSGTFVIR FKEGYYPAPP
     VDQLMDVRVE IVDTLVKYFG YTIEATHHEV ATAGQGEIDF RFSTLVDTAD KVQTLKYVAK
     NIAAKHGLVV TFMPKPIYGD NGTGMHTHLS LWTKDGKKNL MYDPNDEYAE ISQFGRYVIG
     GLLTHARALS AIVSPTVNSY RRLIPGFEAP VYIAWSKGNR SAVIRVPAYY RGMEKAKRIE
     YRPPDPSTNP YLAFAALLMA ALDGVNKKID PGDPVDENIY HLTPEKRRQL GIKELPRSLN
     EALDELESDK EFLKPVFNSS ILDTYIDLKR DEARSLQGYP HPMELYYYLD S