ID   GLNA_HALSA              Reviewed;         454 AA.
AC   Q9HNI2;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, entry version 122.
DE   RecName: Full=Glutamine synthetase {ECO:0000250|UniProtKB:P12425};
DE            Short=GS {ECO:0000250|UniProtKB:P12425};
DE            EC=6.3.1.2 {ECO:0000250|UniProtKB:P12425};
DE   AltName: Full=Glutamate--ammonia ligase {ECO:0000250|UniProtKB:P12425};
DE   AltName: Full=Glutamine synthetase I alpha {ECO:0000250|UniProtKB:P12425};
DE            Short=GSI alpha {ECO:0000250|UniProtKB:P12425};
GN   Name=glnA {ECO:0000250|UniProtKB:P12425}; OrderedLocusNames=VNG_2093G;
OS   Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS   (Halobacterium halobium).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium; Halobacterium salinarum NRC-34001.
OX   NCBI_TaxID=64091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX   PubMed=11016950; DOI=10.1073/pnas.190337797;
RA   Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA   Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA   Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA   Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA   Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA   Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA   Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA   DasSarma S.;
RT   "Genome sequence of Halobacterium species NRC-1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
CC   -!- FUNCTION: Glutamine synthetase (GS) is an unusual multitasking protein
CC       that functions as an enzyme, a transcription coregulator, and a
CC       chaperone in ammonium assimilation and in the regulation of genes
CC       involved in nitrogen metabolism. It catalyzes the ATP-dependent
CC       biosynthesis of glutamine from glutamate and ammonia. Feedback-
CC       inhibited GlnA also interacts with and regulates the activity of the
CC       transcriptional regulator TnrA. During nitrogen limitation, TnrA is in
CC       its DNA-binding active state and turns on the transcription of genes
CC       required for nitrogen assimilation. Under conditions of nitrogen
CC       excess, feedback-inhibited GlnA forms a stable complex with TnrA, which
CC       inhibits its DNA-binding activity. In contrast, feedback-inhibited GlnA
CC       acts as a chaperone to stabilize the DNA-binding activity of GlnR,
CC       which represses the transcription of nitrogen assimilation genes.
CC       {ECO:0000250|UniProtKB:P12425}.
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         Evidence={ECO:0000250|UniProtKB:P12425};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P12425};
CC       Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P12425};
CC   -!- ACTIVITY REGULATION: Inhibited by glutamine.
CC       {ECO:0000250|UniProtKB:P12425}.
CC   -!- SUBUNIT: Oligomer of 12 subunits arranged in the form of two hexagons.
CC       In its feedback-inhibited form, interacts with TnrA in order to block
CC       its DNA-binding activity. {ECO:0000250|UniProtKB:P12425}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P12425}.
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; AE004437; AAG20238.1; -; Genomic_DNA.
DR   PIR; B84359; B84359.
DR   RefSeq; WP_010903540.1; NC_002607.1.
DR   AlphaFoldDB; Q9HNI2; -.
DR   SMR; Q9HNI2; -.
DR   STRING; 64091.VNG_2093G; -.
DR   PaxDb; 64091-VNG_2093G; -.
DR   GeneID; 68694667; -.
DR   KEGG; hal:VNG_2093G; -.
DR   PATRIC; fig|64091.14.peg.1598; -.
DR   HOGENOM; CLU_017290_1_3_2; -.
DR   InParanoid; Q9HNI2; -.
DR   OrthoDB; 36124at2157; -.
DR   PhylomeDB; Q9HNI2; -.
DR   Proteomes; UP000000554; Chromosome.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR004809; Gln_synth_I.
DR   InterPro; IPR027302; Gln_synth_N_conserv_site.
DR   NCBIfam; TIGR00653; GlnA; 1.
DR   PANTHER; PTHR43785; GAMMA-GLUTAMYLPUTRESCINE SYNTHETASE; 1.
DR   PANTHER; PTHR43785:SF12; GAMMA-GLUTAMYLPUTRESCINE SYNTHETASE PUUA; 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; Magnesium; Metal-binding;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome.
FT   CHAIN           1..454
FT                   /note="Glutamine synthetase"
FT                   /id="PRO_0000153202"
FT   DOMAIN          25..111
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT   DOMAIN          118..454
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT   BINDING         141
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P12425"
FT   BINDING         143
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P12425"
FT   BINDING         193
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         198
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P12425"
FT   BINDING         205
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P12425"
FT   BINDING         249..250
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         250
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P12425"
FT   BINDING         254
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P12425"
FT   BINDING         256..258
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         258
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P77961"
FT   BINDING         308
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT   BINDING         314
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT   BINDING         326
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         326
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         331
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         343
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P12425"
FT   BINDING         345
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT   SITE            71
FT                   /note="Important for inhibition by glutamine"
FT                   /evidence="ECO:0000250|UniProtKB:P12425"
SQ   SEQUENCE   454 AA;  49757 MW;  09C12E8D0B91D538 CRC64;
     MTNGDSSSSA LTDNERAVLD DIEAQGIDFL RLQFTDILGT VKNVSIPAHQ AEKAFTEGIY
     FDGSSIEGFV RIQESDMRLD PDPETFAVLP WRSNGDGGSA RLICDVVDRE GNAFAGGPRQ
     VLKNVLARAD DMGYSVSIGP EPEFFLFEKD DDGNATTTAH DQGGYFDLAP KDLASDIRRE
     IIFTLEAMGF EIEASHHEVA RGQHEINFKY DDALTTADNI ATFRAVVRAV AEQHDVHATF
     MPKPIGEING SGMHSHISLF DEDGENVFAD NDDEFNLSET AYQFMGGVLE HAPAFTAVTN
     PTVNSYKRLV PGYEAPVYIA WSGVNRSALI RVPDAAGVSA RFEIRSPDPS CNPYLALAAV
     IAAGLDGIDT DADPGDAVRE DIYEFDEDKR DAYGIDTLPG HLGDAVTALE SDPVMQDALG
     EHVCEKFAEA KRHEYAEYKA SVSEWETDRY LEKF
//