ID   A0A1D9NYZ4_9FIRM        Unreviewed;       536 AA.
AC   A0A1D9NYZ4;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   07-OCT-2020, entry version 16.
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=bhn_I0109 {ECO:0000313|EMBL:AOZ95145.1};
OS   Butyrivibrio hungatei.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae;
OC   Butyrivibrio.
OX   NCBI_TaxID=185008 {ECO:0000313|EMBL:AOZ95145.1, ECO:0000313|Proteomes:UP000179284};
RN   [1] {ECO:0000313|Proteomes:UP000179284}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB2003 {ECO:0000313|Proteomes:UP000179284};
RA   Palevich N., Kelly W.J., Leahy S.C., Altermann E., Rakonjac J.,
RA   Attwood G.T.;
RT   "The complete genome sequence of the rumen bacterium Butyrivibrio hungatei
RT   MB2003.";
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; CP017831; AOZ95145.1; -; Genomic_DNA.
DR   RefSeq; WP_071174961.1; NZ_CP017831.1.
DR   KEGG; bhu:bhn_I0109; -.
DR   KO; K01937; -.
DR   OrthoDB; 783657at2; -.
DR   UniPathway; UPA00159; UER00277.
DR   Proteomes; UP000179284; Chromosome i.
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; cd01746; GATase1_CTP_Synthase; 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 {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, ECO:0000256|PROSITE-ProRule:PRU00605};
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}; Reference proteome {ECO:0000313|Proteomes:UP000179284}.
FT   DOMAIN          293..535
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51273"
FT   NP_BIND         15..20
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   NP_BIND         149..151
FT                   /note="Allosteric inhibitor CTP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   NP_BIND         189..194
FT                   /note="Allosteric inhibitor CTP; alternate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   NP_BIND         189..194
FT                   /note="UTP; alternate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   REGION          1..268
FT                   /note="Amidoligase domain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   REGION          383..386
FT                   /note="L-glutamine binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   ACT_SITE        382
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        382
FT                   /note="Nucleophile; for glutamine hydrolysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   ACT_SITE        508
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        510
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   METAL           72
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   METAL           142
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   BINDING         14
FT                   /note="Allosteric inhibitor CTP; alternate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   BINDING         14
FT                   /note="UTP; alternate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   BINDING         72
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   BINDING         225
FT                   /note="Allosteric inhibitor CTP; alternate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   BINDING         225
FT                   /note="UTP; alternate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   BINDING         243
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   BINDING         355
FT                   /note="L-glutamine; via carbonyl oxygen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   BINDING         406
FT                   /note="L-glutamine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   BINDING         463
FT                   /note="L-glutamine; via amide nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
SQ   SEQUENCE   536 AA;  60017 MW;  F908E8338E313BCE CRC64;
     MAVKYIFVTG GVVSGLGKGI TAASLGRLLK ARGYKVTMQK FDPYINIDPG TMNPVQHGEV
     FVTEDGTETD LDLGHYERFI DENLDKNSNV TTGKIYWSVL QKERRGDYGG RTVQVIPHIT
     NEIKSKFYRN FTDDETRIAI IEVGGTVGDI ESQPFLEAIR QFQHEVGREN AMLILVSLIP
     YLRCSEEIKT KPTQSAVKTM QGMGLQPDVI VCRTEIELDQ DTKDKIALFC NVPSSHVLNN
     LDLEYLYEAP LAMEKEHLAQ VACECLELDC PEPDLTDWKA MVDTLYSLKH EVKVALVGKY
     TQLHDAYISV VEALKHGGIS NQTAVDIKWV DSEEVNDENV ASYLSDVDGI IVPGGFGDRG
     IEGMISSIKY ARENNVPFLG LCLGMQLAII EFARDVIGYK DAHSIEFDPN TTHPMIALLP
     DQNGVEDIGG TLRLGSYPCV LDKESKAYEL FGSTDITERH RHRYEVNNDY RTVLVQNGMR
     LCGMSPDGRI VEMIELPSND FHMATQAHPE LKSRPNRPHP LFSGFIKASL EHENKR
//