ID   GLNA_THEKO              Reviewed;         443 AA.
AC   O08467; Q5JJ67;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 2.
DT   27-MAR-2024, entry version 135.
DE   RecName: Full=Glutamine synthetase {ECO:0000303|PubMed:9172372};
DE            Short=GS {ECO:0000303|PubMed:9172372};
DE            EC=6.3.1.2 {ECO:0000269|PubMed:9172372};
DE   AltName: Full=Glutamate--ammonia ligase {ECO:0000305};
DE   AltName: Full=Glutamine synthetase I alpha {ECO:0000305};
DE            Short=GSI alpha {ECO:0000305};
GN   Name=glnA {ECO:0000303|PubMed:9172372}; OrderedLocusNames=TK1796;
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, GENE NAME,
RP   SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND
RP   SUBUNIT.
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=9172372; DOI=10.1128/aem.63.6.2472-2476.1997;
RA   Adul Rahman R.N.Z., Jongsareejit B., Fujiwara S., Imanaka T.;
RT   "Characterization of recombinant glutamine synthetase from the
RT   hyperthermophilic archaeon Pyrococcus sp. strain KOD1.";
RL   Appl. Environ. Microbiol. 63:2472-2476(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
CC   -!- FUNCTION: Carries out the ATP-dependent synthesis of glutamine from
CC       ammonium nitrogen and glutamate. Exhibits both L-gamma-
CC       glutamylhydroxamate synthetase and gamma-glutamyltransferase activities
CC       when using hydroxylamine as substrate; in fact, the enzyme possesses
CC       low biosynthetic activity, suggesting that the reaction is biased
CC       towards the degradation of glutamine under ammonia-rich conditions.
CC       Might play some role in ammonia assimilation under ammonia-starvation
CC       conditions. Can also use GTP instead of ATP in the synthetase reaction,
CC       but not CTP or UTP. {ECO:0000269|PubMed:9172372}.
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:0000269|PubMed:9172372};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + hydroxylamine + L-glutamate = ADP + L-glutamine
CC         hydroxamate + phosphate; Xref=Rhea:RHEA:45804, ChEBI:CHEBI:15429,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:85433, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000269|PubMed:9172372};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:9172372};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:9172372};
CC       Note=Binds 2 Mg(2+) or Mn(2+) ions per subunit.
CC       {ECO:0000250|UniProtKB:P9WN39};
CC   -!- ACTIVITY REGULATION: The activity of this enzyme is not controlled by
CC       adenylation. {ECO:0000305|PubMed:9172372}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=23.5 mM for L-glutamate (at pH 7.8 and 60 degrees Celsius)
CC         {ECO:0000269|PubMed:9172372};
CC         KM=15.2 mM for hydroxylamine (when a high concentration is used, at
CC         pH 7.8 and 60 degrees Celsius) {ECO:0000269|PubMed:9172372};
CC         KM=1.6 mM for hydroxylamine (when a low concentration is used, at pH
CC         7.8 and 60 degrees Celsius) {ECO:0000269|PubMed:9172372};
CC         KM=28 mM for ATP (at pH 7.8 and 60 degrees Celsius)
CC         {ECO:0000269|PubMed:9172372};
CC         KM=5 mM for L-glutamine (at pH 7.2 and 60 degrees Celsius)
CC         {ECO:0000269|PubMed:9172372};
CC         KM=6.3 mM for ADP (at pH 7.2 and 60 degrees Celsius)
CC         {ECO:0000269|PubMed:9172372};
CC         Note=kcat is 2190 min(-1) towards L-glutamate in the synthetase
CC         reaction and 3900 min(-1) towards L-glutamine in the transferase
CC         reaction.;
CC       pH dependence:
CC         Optimum pH is 7.8 for the synthetase reaction and pH 7.2 for the
CC         transferase reaction. {ECO:0000269|PubMed:9172372};
CC       Temperature dependence:
CC         Optimum temperature is 60 degrees Celsius for both transferase and
CC         synthetase activities. {ECO:0000269|PubMed:9172372};
CC   -!- SUBUNIT: Oligomer of 12 subunits arranged in the form of two hexagons.
CC       {ECO:0000269|PubMed:9172372}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR   EMBL; D86222; BAA20530.1; -; Genomic_DNA.
DR   EMBL; AP006878; BAD85985.1; -; Genomic_DNA.
DR   RefSeq; WP_011250747.1; NC_006624.1.
DR   AlphaFoldDB; O08467; -.
DR   SMR; O08467; -.
DR   IntAct; O08467; 1.
DR   MINT; O08467; -.
DR   STRING; 69014.TK1796; -.
DR   EnsemblBacteria; BAD85985; BAD85985; TK1796.
DR   GeneID; 78448327; -.
DR   KEGG; tko:TK1796; -.
DR   PATRIC; fig|69014.16.peg.1752; -.
DR   eggNOG; arCOG01909; Archaea.
DR   HOGENOM; CLU_017290_1_3_2; -.
DR   InParanoid; O08467; -.
DR   OrthoDB; 36124at2157; -.
DR   PhylomeDB; O08467; -.
DR   BRENDA; 6.3.1.2; 5027.
DR   Proteomes; UP000000536; 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   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Ligase; Magnesium; Manganese; Metal-binding;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..443
FT                   /note="Glutamine synthetase"
FT                   /id="PRO_0000153211"
FT   DOMAIN          11..97
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT   DOMAIN          103..443
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT   BINDING         126
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         128
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         176
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         181
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         188
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         233
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P12425"
FT   BINDING         237
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         239..241
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         241
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P77961"
FT   BINDING         287
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         293
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT   BINDING         305
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         305
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         310
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         322
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   BINDING         324
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P9WN39"
FT   CONFLICT        402
FT                   /note="Y -> N (in Ref. 1; BAA20530)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   443 AA;  50308 MW;  94357E45D5F18168 CRC64;
     MNEIKGIERA VQVEVPRPRF LLLAFTDING SLKGMEIPME RYEEAVEDGV SFDGSSIPGF
     EGIEDSDLIF KADPSTYAEI PWEGIGRVYG YIYKGDEPYQ ADPRGILKRV LERLEKEGLK
     AHIGPEPEFY IFKKNGTWEL HIPDSGGYFD LVGLDKAREI RREIALYMPY LGLKPEVLHH
     EVGKAQHEID FRYDEALRTA DNIVSFKHVV KAVAELHGYY ATFMPKPIYG FPGNGMHLHI
     SLWKDGENVF IGEDGLSDTA LHFIGGILKH AKALAALTNP TVNSYKRLVP GYEAPVYISW
     GYRNRSALIR VPAFKGSGAR IEYRCPDPSA NPYLALAGIL MVGLDGIKKK VEPDSYVETN
     VYEMDDAERE RLGIDTLPGS LGEALEELKK DKTVREALGG AYKNFIDYKE REWEEYIEYL
     SSRDIPIDTK KVTEWELERY FYV
//