ID   A0A2A9BQ88_9BACI        Unreviewed;       534 AA.
AC   A0A2A9BQ88;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   29-SEP-2021, entry version 13.
DE   RecName: Full=CTP synthase {ECO:0000256|HAMAP-Rule:MF_01227};
DE            EC=6.3.4.2 {ECO:0000256|HAMAP-Rule:MF_01227};
DE   AltName: Full=Cytidine 5'-triphosphate synthase {ECO:0000256|HAMAP-Rule:MF_01227};
DE   AltName: Full=Cytidine triphosphate synthetase {ECO:0000256|HAMAP-Rule:MF_01227};
DE            Short=CTP synthetase {ECO:0000256|HAMAP-Rule:MF_01227};
DE            Short=CTPS {ECO:0000256|HAMAP-Rule:MF_01227};
DE   AltName: Full=UTP--ammonia ligase {ECO:0000256|HAMAP-Rule:MF_01227};
GN   Name=pyrG {ECO:0000256|HAMAP-Rule:MF_01227};
GN   ORFNames=ATG71_1049 {ECO:0000313|EMBL:PFG04307.1};
OS   Bacillus sp. es.034.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1761763 {ECO:0000313|EMBL:PFG04307.1, ECO:0000313|Proteomes:UP000225138};
RN   [1] {ECO:0000313|EMBL:PFG04307.1, ECO:0000313|Proteomes:UP000225138}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=es.034 {ECO:0000313|Proteomes:UP000225138};
RA   Fredrickson J.;
RT   "Microbial Interactions in Extremophilic Mat Communities.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|ARBA:ARBA00000314, ECO:0000256|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:0000256|HAMAP-
CC       Rule:MF_01227}.
CC   -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway;
CC       CTP from UDP: step 2/2. {ECO:0000256|ARBA:ARBA00005171,
CC       ECO:0000256|HAMAP-Rule:MF_01227}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01227}.
CC   -!- SIMILARITY: Belongs to the CTP synthase family.
CC       {ECO:0000256|ARBA:ARBA00007533, ECO:0000256|HAMAP-Rule:MF_01227}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01227}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PFG04307.1}.
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DR   EMBL; PDIY01000001; PFG04307.1; -; Genomic_DNA.
DR   EnsemblBacteria; PFG04307; PFG04307; ATG71_1049.
DR   UniPathway; UPA00159; UER00277.
DR   Proteomes; UP000225138; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003883; F:CTP synthase activity; IEA:UniProtKB-UniRule.
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-UniRule.
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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01227};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW   ECO:0000256|HAMAP-Rule:MF_01227};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01227};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01227};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01227};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01227};
KW   Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975, ECO:0000256|HAMAP-
KW   Rule:MF_01227}.
FT   DOMAIN          3..267
FT                   /note="CTP_synth_N"
FT                   /evidence="ECO:0000259|Pfam:PF06418"
FT   DOMAIN          302..527
FT                   /note="GATase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   NP_BIND         14..19
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   NP_BIND         148..150
FT                   /note="CTP; allosteric inhibitor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   NP_BIND         188..193
FT                   /note="CTP; allosteric inhibitor; alternate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   NP_BIND         188..193
FT                   /note="UTP; alternate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   REGION          1..267
FT                   /note="Amidoligase domain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   REGION          382..385
FT                   /note="L-glutamine binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   ACT_SITE        381
FT                   /note="Nucleophile; for glutamine hydrolysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   ACT_SITE        507
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   ACT_SITE        509
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   METAL           71
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   METAL           141
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   BINDING         13
FT                   /note="CTP; allosteric inhibitor; alternate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   BINDING         13
FT                   /note="UTP; alternate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   BINDING         54
FT                   /note="L-glutamine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   BINDING         71
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   BINDING         224
FT                   /note="CTP; allosteric inhibitor; alternate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   BINDING         224
FT                   /note="UTP; alternate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   BINDING         242
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   BINDING         354
FT                   /note="L-glutamine; via carbonyl oxygen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   BINDING         405
FT                   /note="L-glutamine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   BINDING         462
FT                   /note="L-glutamine; via amide nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
SQ   SEQUENCE   534 AA;  59856 MW;  C4E22254730EC7C2 CRC64;
     MTKYIFVTGG VVSSLGKGIT AASLGRLLKN RGVSVTIQKF DPYINVDPGT MSPYQHGEVF
     VTDDGAETDL DLGHYERFVD INLTKYSSVT TGKIYSTVLK KERRGDYLGG TVQVIPHITN
     EIKERVYRAG RETNSDVVIT EIGGTVGDIE SLPFLEAIRQ IKSDVGRDNV MYIHCTLIPY
     IKAAGEMKTK PTQHSVKELR SLGIQPNVIV VRTEMPMTQD MKDKIALFCD IDKHAVIEAM
     DADTLYSVPL ALQDQKLDEI TCQHLKLNCH EADMTEWNEL VDRVKNLSRK TRIALVGKYV
     ELQDAYISVV EALRHAGYHF DSDIEVRWLN SELVDNENVA EKLADVDGIL VPGGFGDRGV
     EGKIAATQYA RENKIPFLGI CLGMQLASVE YARNVLGMEG AHSAELNPET PYPVIDLLPE
     QKDIEDLGGT LRLGLYPCKL TKGSKAYAAY DGEVVYERHR HRFEFNNHYR EQMEKAGFIF
     SGTSPDGRLV EIIELSDHPW FVASQFHPEF TSRPTRPQPL FRDFVEASLA YGEK
//