ID   A0A1D9NYZ4_9FIRM        Unreviewed;       536 AA.
AC   A0A1D9NYZ4;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   20-JUN-2018, entry version 8.
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|EMBL:AOZ95145.1, ECO:0000313|Proteomes:UP000179284}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB2003 {ECO:0000313|EMBL:AOZ95145.1,
RC   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
RT   hungatei 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: ATP + UTP + L-glutamine = ADP + phosphate +
CC       CTP + L-glutamate. {ECO:0000256|HAMAP-Rule:MF_01227,
CC       ECO:0000256|SAAS:SAAS00710710}.
CC   -!- ENZYME REGULATION: Allosterically activated by GTP, when glutamine
CC       is the substrate; GTP has no effect on the reaction when ammonia
CC       is the substrate. The allosteric effector GTP functions by
CC       stabilizing the protein conformation that binds the tetrahedral
CC       intermediate(s) formed during glutamine hydrolysis. Inhibited by
CC       the product CTP, via allosteric rather than competitive
CC       inhibition. {ECO:0000256|HAMAP-Rule:MF_01227}.
CC   -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo
CC       pathway; CTP from UDP: step 2/2. {ECO:0000256|HAMAP-Rule:MF_01227,
CC       ECO:0000256|SAAS:SAAS00710815}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01227,
CC       ECO:0000256|SAAS:SAAS00710816}.
CC   -!- MISCELLANEOUS: CTPSs have evolved a hybrid strategy for
CC       distinguishing between UTP and CTP. The overlapping regions of the
CC       product feedback inhibitory and substrate sites recognize a common
CC       feature in both compounds, the triphosphate moiety. To
CC       differentiate isosteric substrate and product pyrimidine rings, an
CC       additional pocket far from the expected kinase/ligase catalytic
CC       site, specifically recognizes the cytosine and ribose portions of
CC       the product inhibitor. {ECO:0000256|HAMAP-Rule:MF_01227}.
CC   -!- SIMILARITY: Belongs to the CTP synthase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01227, ECO:0000256|SAAS:SAAS00710794}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of 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   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|HAMAP-Rule:MF_01227,
KW   ECO:0000256|SAAS:SAAS00710699};
KW   Complete proteome {ECO:0000313|Proteomes:UP000179284};
KW   Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01227,
KW   ECO:0000256|PROSITE-ProRule:PRU00605, ECO:0000256|SAAS:SAAS00710676};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01227,
KW   ECO:0000256|SAAS:SAAS00710762};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01227,
KW   ECO:0000256|SAAS:SAAS00710689};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01227,
KW   ECO:0000256|SAAS:SAAS00710675};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01227,
KW   ECO:0000256|SAAS:SAAS00710810};
KW   Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01227,
KW   ECO:0000256|SAAS:SAAS00710748};
KW   Reference proteome {ECO:0000313|Proteomes:UP000179284}.
FT   DOMAIN      293    535       Glutamine amidotransferase type-1.
FT                                {ECO:0000259|PROSITE:PS51273}.
FT   NP_BIND      15     20       ATP. {ECO:0000256|HAMAP-Rule:MF_01227}.
FT   NP_BIND     149    151       Allosteric inhibitor CTP.
FT                                {ECO:0000256|HAMAP-Rule:MF_01227}.
FT   NP_BIND     189    194       Allosteric inhibitor CTP; alternate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01227}.
FT   NP_BIND     189    194       UTP; alternate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01227}.
FT   REGION        1    268       Amidoligase domain. {ECO:0000256|HAMAP-
FT                                Rule:MF_01227}.
FT   REGION      383    386       L-glutamine binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01227}.
FT   ACT_SITE    382    382       Nucleophile. {ECO:0000256|PROSITE-
FT                                ProRule:PRU00605}.
FT   ACT_SITE    382    382       Nucleophile; for glutamine hydrolysis.
FT                                {ECO:0000256|HAMAP-Rule:MF_01227}.
FT   ACT_SITE    508    508       {ECO:0000256|HAMAP-Rule:MF_01227,
FT                                ECO:0000256|PROSITE-ProRule:PRU00605}.
FT   ACT_SITE    510    510       {ECO:0000256|HAMAP-Rule:MF_01227,
FT                                ECO:0000256|PROSITE-ProRule:PRU00605}.
FT   METAL        72     72       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01227}.
FT   METAL       142    142       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01227}.
FT   BINDING      14     14       Allosteric inhibitor CTP; alternate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01227}.
FT   BINDING      14     14       UTP; alternate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01227}.
FT   BINDING      72     72       ATP. {ECO:0000256|HAMAP-Rule:MF_01227}.
FT   BINDING     225    225       Allosteric inhibitor CTP; alternate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01227}.
FT   BINDING     225    225       UTP; alternate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01227}.
FT   BINDING     243    243       ATP. {ECO:0000256|HAMAP-Rule:MF_01227}.
FT   BINDING     355    355       L-glutamine; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01227}.
FT   BINDING     406    406       L-glutamine. {ECO:0000256|HAMAP-Rule:
FT                                MF_01227}.
FT   BINDING     463    463       L-glutamine; via amide nitrogen.
FT                                {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
//