ID   GLNA_HALVD              Reviewed;         456 AA.
AC   P43386; D4GZI4;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   13-JUL-2010, sequence version 2.
DT   27-MAR-2024, entry version 116.
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=HVO_0239;
OS   Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS   NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax.
OX   NCBI_TaxID=309800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7916055; DOI=10.1007/bf00175876;
RA   Brown J.R., Masuchi Y., Robb F.T., Doolittle W.F.;
RT   "Evolutionary relationships of bacterial and archaeal glutamine synthetase
RT   genes.";
RL   J. Mol. Evol. 38:566-576(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 /
RC   VKM B-1768 / DS2;
RX   PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA   Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA   Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA   Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT   "The complete genome sequence of Haloferax volcanii DS2, a model
RT   archaeon.";
RL   PLoS ONE 5:E9605-E9605(2010).
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}.
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DR   EMBL; U03029; AAC43489.1; -; Genomic_DNA.
DR   EMBL; CP001956; ADE03696.1; -; Genomic_DNA.
DR   PIR; T47127; T47127.
DR   RefSeq; WP_004045354.1; NZ_AOHU01000107.1.
DR   AlphaFoldDB; P43386; -.
DR   SMR; P43386; -.
DR   STRING; 309800.HVO_0239; -.
DR   PaxDb; 309800-C498_19454; -.
DR   EnsemblBacteria; ADE03696; ADE03696; HVO_0239.
DR   GeneID; 8924457; -.
DR   KEGG; hvo:HVO_0239; -.
DR   eggNOG; arCOG01909; Archaea.
DR   HOGENOM; CLU_017290_1_3_2; -.
DR   OrthoDB; 36124at2157; -.
DR   Proteomes; UP000008243; 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..456
FT                   /note="Glutamine synthetase"
FT                   /id="PRO_0000153203"
FT   DOMAIN          26..113
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT   DOMAIN          120..456
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT   BINDING         143
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P12425"
FT   BINDING         145
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P12425"
FT   BINDING         195
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         200
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P12425"
FT   BINDING         207
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P12425"
FT   BINDING         251..252
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         252
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P12425"
FT   BINDING         256
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P12425"
FT   BINDING         258..260
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         260
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P77961"
FT   BINDING         309
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT   BINDING         315
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT   BINDING         327
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         327
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         332
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         345
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P12425"
FT   BINDING         347
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT   SITE            72
FT                   /note="Important for inhibition by glutamine"
FT                   /evidence="ECO:0000250|UniProtKB:P12425"
FT   CONFLICT        130..131
FT                   /note="RA -> P (in Ref. 1; AAC43489)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        223
FT                   /note="A -> R (in Ref. 1; AAC43489)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        299..308
FT                   /note="VADPTVNSYK -> SLTRRSTPTR (in Ref. 1; AAC43489)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        403..413
FT                   /note="DLGGAVDALEE -> TSAARRRPRR (in Ref. 1; AAC43489)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   456 AA;  50522 MW;  7A3905E9706174EA CRC64;
     MTEDNALTDG GLSDEAQAVI DEIEEKNVDF LRLQFTDILG TVKNVSIPAS QAEKAFTEGI
     YFDGSSIDGF VRIQESDMRL EPDPSTFAVL PWRKKENSAA GRLICDVFNT STGEPFSGDP
     RGVLKRAIER AEELGYDVNV APEPEFFLFE EDEDGRATTV TNDAGGYFDL APKDLASDVR
     RDIIYGLESM GFDIEASHHE VAEGQHEINF TYDDALSTAD NVATFRSVVR AIAAEHDLHA
     TFMPKPIPRI NGSGMHTHIS LFKDGENAFH DGDDEFDLSD TAKSFVAGIL DHAPAITAVA
     DPTVNSYKRL VPGYEAPVYI AWSDRNRSAL IRKPAARTPA ASRIEARFPD PSCNPYLAFA
     ALIHAGLDGV EKGLDCPDPV RENIYEFDEA KREEYGIETL PKDLGGAVDA LEEDEVIQEA
     LGDHVFEKFV EAKRSEFKDY LVDVSQWELD RYLETF
//