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Database: UniProt
Entry: O08467
LinkDB: O08467
Original site: O08467 
ID   GLN1A_THEKO             Reviewed;         443 AA.
AC   O08467; Q5JJ67;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 2.
DT   05-JUL-2017, entry version 108.
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
RP   NAME, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
RP   AND SUBUNIT.
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=9172372;
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
RT   Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus
RT   genomes.";
RL   Genome Res. 15:352-363(2005).
CC   -!- FUNCTION: Carries out the ATP-dependent synthesis of glutamine
CC       from ammonium nitrogen and glutamate. Exhibits both L-gamma-
CC       glutamylhydroxamate synthetase and gamma-glutamyltransferase
CC       activities when using hydroxylamine as substrate; in fact, the
CC       enzyme possesses low biosynthetic activity, suggesting that the
CC       reaction is biased towards the degradation of glutamine under
CC       ammonia-rich conditions. Might play some role in ammonia
CC       assimilation under ammonia-starvation conditions. Can also use GTP
CC       instead of ATP in the synthetase reaction, but not CTP or UTP.
CC       {ECO:0000269|PubMed:9172372}.
CC   -!- CATALYTIC ACTIVITY: ATP + L-glutamate + NH(3) = ADP + phosphate +
CC       L-glutamine. {ECO:0000269|PubMed:9172372}.
CC   -!- CATALYTIC ACTIVITY: ATP + L-glutamate + hydroxylamine = ADP +
CC       phosphate + L-gamma-glutamylhydroxamate.
CC       {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   -!- ENZYME REGULATION: The activity of this enzyme is not controlled
CC       by 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,
CC         at pH 7.8 and 60 degrees Celsius) {ECO:0000269|PubMed:9172372};
CC         KM=1.6 mM for hydroxylamine (when a low concentration is used,
CC         at pH 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
CC         and synthetase activities. {ECO:0000269|PubMed:9172372};
CC   -!- SUBUNIT: Oligomer of 12 subunits arranged in the form of two
CC       hexagons. {ECO:0000269|PubMed:9172372}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC       {ECO:0000305}.
DR   EMBL; D86222; BAA20530.1; -; Genomic_DNA.
DR   EMBL; AP006878; BAD85985.1; -; Genomic_DNA.
DR   RefSeq; WP_011250747.1; NC_006624.1.
DR   ProteinModelPortal; O08467; -.
DR   IntAct; O08467; 1.
DR   MINT; MINT-8377176; -.
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   eggNOG; COG0174; LUCA.
DR   HOGENOM; HOG000005156; -.
DR   InParanoid; O08467; -.
DR   KO; K01915; -.
DR   OMA; IEAAWNT; -.
DR   OrthoDB; POG093Z00GE; -.
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   GO; GO:0009399; P:nitrogen fixation; IEA:InterPro.
DR   Gene3D; 3.10.20.70; -; 1.
DR   Gene3D; 3.30.590.10; -; 1.
DR   InterPro; IPR008147; Gln_synt_b-grasp.
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   TIGRFAMs; TIGR00653; GlnA; 1.
DR   PROSITE; PS00180; GLNA_1; 1.
DR   PROSITE; PS00181; GLNA_ATP; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; Cytoplasm; Ligase; Magnesium;
KW   Manganese; Metal-binding; Nucleotide-binding; Reference proteome.
FT   CHAIN         1    443       Glutamine synthetase.
FT                                /FTId=PRO_0000153211.
FT   NP_BIND     239    241       ATP. {ECO:0000250|UniProtKB:P9WN39}.
FT   METAL       126    126       Magnesium 1.
FT                                {ECO:0000250|UniProtKB:P9WN39}.
FT   METAL       128    128       Magnesium 2.
FT                                {ECO:0000250|UniProtKB:P9WN39}.
FT   METAL       181    181       Magnesium 2.
FT                                {ECO:0000250|UniProtKB:P9WN39}.
FT   METAL       188    188       Magnesium 2.
FT                                {ECO:0000250|UniProtKB:P9WN39}.
FT   METAL       237    237       Magnesium 1; via pros nitrogen.
FT                                {ECO:0000250|UniProtKB:P9WN39}.
FT   METAL       322    322       Magnesium 1.
FT                                {ECO:0000250|UniProtKB:P9WN39}.
FT   BINDING     176    176       ATP. {ECO:0000250|UniProtKB:P9WN39}.
FT   BINDING     233    233       L-glutamate; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P12425}.
FT   BINDING     241    241       ATP. {ECO:0000250|UniProtKB:P77961}.
FT   BINDING     287    287       L-glutamate.
FT                                {ECO:0000250|UniProtKB:P9WN39}.
FT   BINDING     293    293       L-glutamate.
FT                                {ECO:0000250|UniProtKB:P0A1P6}.
FT   BINDING     305    305       ATP. {ECO:0000250|UniProtKB:P9WN39}.
FT   BINDING     305    305       L-glutamate.
FT                                {ECO:0000250|UniProtKB:P9WN39}.
FT   BINDING     310    310       ATP. {ECO:0000250|UniProtKB:P9WN39}.
FT   BINDING     324    324       L-glutamate.
FT                                {ECO:0000250|UniProtKB:P9WN39}.
FT   CONFLICT    402    402       Y -> N (in Ref. 1; BAA20530).
FT                                {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
//
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