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PYRG_PYRFU
ID   PYRG_PYRFU              Reviewed;         537 AA.
AC   Q8TZY6;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2002, sequence version 2.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=CTP synthase {ECO:0000255|HAMAP-Rule:MF_01227};
DE            EC=6.3.4.2 {ECO:0000255|HAMAP-Rule:MF_01227};
DE   AltName: Full=Cytidine 5'-triphosphate synthase {ECO:0000255|HAMAP-Rule:MF_01227};
DE   AltName: Full=Cytidine triphosphate synthetase {ECO:0000255|HAMAP-Rule:MF_01227};
DE            Short=CTP synthetase {ECO:0000255|HAMAP-Rule:MF_01227};
DE            Short=CTPS {ECO:0000255|HAMAP-Rule:MF_01227};
DE   AltName: Full=UTP--ammonia ligase {ECO:0000255|HAMAP-Rule:MF_01227};
GN   Name=pyrG {ECO:0000255|HAMAP-Rule:MF_01227}; OrderedLocusNames=PF1839;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
CC   -!- FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with
CC       either L-glutamine or ammonia as the source of nitrogen. Regulates
CC       intracellular CTP levels through interactions with the four
CC       ribonucleotide triphosphates. {ECO:0000255|HAMAP-Rule:MF_01227}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-
CC         glutamate + phosphate; Xref=Rhea:RHEA:26426, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:37563, ChEBI:CHEBI:43474, ChEBI:CHEBI:46398,
CC         ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.4.2;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01227};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-glutamine = L-glutamate + NH4(+);
CC         Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01227};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + NH4(+) + UTP = ADP + CTP + 2 H(+) + phosphate;
CC         Xref=Rhea:RHEA:16597, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:37563, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:46398, ChEBI:CHEBI:456216; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01227};
CC   -!- ACTIVITY REGULATION: Allosterically activated by GTP, when glutamine is
CC       the substrate; GTP has no effect on the reaction when ammonia is the
CC       substrate. The allosteric effector GTP functions by stabilizing the
CC       protein conformation that binds the tetrahedral intermediate(s) formed
CC       during glutamine hydrolysis. Inhibited by the product CTP, via
CC       allosteric rather than competitive inhibition. {ECO:0000255|HAMAP-
CC       Rule:MF_01227}.
CC   -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway;
CC       CTP from UDP: step 2/2. {ECO:0000255|HAMAP-Rule:MF_01227}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01227}.
CC   -!- MISCELLANEOUS: CTPSs have evolved a hybrid strategy for distinguishing
CC       between UTP and CTP. The overlapping regions of the product feedback
CC       inhibitory and substrate sites recognize a common feature in both
CC       compounds, the triphosphate moiety. To differentiate isosteric
CC       substrate and product pyrimidine rings, an additional pocket far from
CC       the expected kinase/ligase catalytic site, specifically recognizes the
CC       cytosine and ribose portions of the product inhibitor.
CC       {ECO:0000255|HAMAP-Rule:MF_01227}.
CC   -!- SIMILARITY: Belongs to the CTP synthase family. {ECO:0000255|HAMAP-
CC       Rule:MF_01227}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL81963.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE009950; AAL81963.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_011012979.1; NZ_CP023154.1.
DR   AlphaFoldDB; Q8TZY6; -.
DR   SMR; Q8TZY6; -.
DR   STRING; 186497.PF1839; -.
DR   MEROPS; C26.964; -.
DR   EnsemblBacteria; AAL81963; AAL81963; PF1839.
DR   GeneID; 41713658; -.
DR   KEGG; pfu:PF1839; -.
DR   PATRIC; fig|186497.12.peg.1910; -.
DR   eggNOG; arCOG00063; Archaea.
DR   HOGENOM; CLU_011675_5_0_2; -.
DR   OMA; EFNNAYR; -.
DR   OrthoDB; 14061at2157; -.
DR   PhylomeDB; Q8TZY6; -.
DR   UniPathway; UPA00159; UER00277.
DR   Proteomes; UP000001013; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003883; F:CTP synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004359; F:glutaminase activity; IEA:RHEA.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd03113; CTPS_N; 1.
DR   CDD; cd01746; GATase1_CTP_Synthase; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   HAMAP; MF_01227; PyrG; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR004468; CTP_synthase.
DR   InterPro; IPR017456; CTP_synthase_N.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR033828; GATase1_CTP_Synthase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11550; PTHR11550; 1.
DR   Pfam; PF06418; CTP_synth_N; 1.
DR   Pfam; PF00117; GATase; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00337; PyrG; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Glutamine amidotransferase; Ligase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Pyrimidine biosynthesis; Reference proteome.
FT   CHAIN           1..537
FT                   /note="CTP synthase"
FT                   /id="PRO_0000138266"
FT   DOMAIN          290..532
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   REGION          1..265
FT                   /note="Amidoligase domain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   ACT_SITE        378
FT                   /note="Nucleophile; for glutamine hydrolysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   ACT_SITE        505
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   ACT_SITE        507
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   BINDING         13
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /ligand_note="allosteric inhibitor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   BINDING         13
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   BINDING         14..19
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   BINDING         54
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   BINDING         71
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   BINDING         71
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   BINDING         139
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   BINDING         146..148
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /ligand_note="allosteric inhibitor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   BINDING         186..191
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /ligand_note="allosteric inhibitor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   BINDING         186..191
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   BINDING         222
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /ligand_note="allosteric inhibitor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   BINDING         222
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   BINDING         351
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   BINDING         379..382
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   BINDING         402
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   BINDING         459
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
SQ   SEQUENCE   537 AA;  60608 MW;  032313D941B14012 CRC64;
     MTKYIFVTGG VVSGLGKGIT SASIGLLMKA RGYKTTNIKI DPYINYDAGT MNPYQHGEVF
     VLDDGGEVDL DLGNYERFLD TELTFDHNIT TGKVYSTVIE KERRGEYLGA TVQVIPHITD
     EIKRRIREIA KDYEVVVVEI GGTVGDIESM PFLEAARQMQ LEEGRDNVAF VHVTYVPKLK
     VVGEQKTKPT QHSVKELRSL GIQPDAIVAR SEDPLEEAAR KKISLFTNVP EEAVISAYDV
     EDTYEVPLLL EREGLGKYLT KRLKLEDREP DLKDWEKMVA KYKALTETVE IAIVGKYVKL
     QDSYLSIKEA LKHASVSNEV KVKIRWIEAE DVETHGTKLL EGVDGIIIPG GFGARGAEGK
     IQAIRYAREN DIPFLGICFG FQLTVVEFAR NVLGMKGAHS TEIDPQTPYP VVDLMPEQRN
     LDRLGGTMRL GAYPVKIKKG TLAYSLYNKE LVYERHRHRW EVNPNYIEAL EKAGLVFSGV
     AGDDERRMEI LELPDKRYFI ATQFHPEFKS RPMRPAPVFH GLVRAAKEYK QEKNVTH
 
 
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