GLNA_THEKO
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 03-AUG-2022, entry version 128.
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=28.0 mM for ATP (at pH 7.8 and 60 degrees Celsius)
CC {ECO:0000269|PubMed:9172372};
CC KM=5.0 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; 3233803; -.
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 OMA; PHPHEFE; -.
DR OrthoDB; 47310at2157; -.
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:glutamate-ammonia ligase 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; -; 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 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
