ID   PYRG_XANOM              Reviewed;         554 AA.
AC   Q2P1K5;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   12-SEP-2018, entry version 84.
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};
GN   OrderedLocusNames=XOO2817;
OS   Xanthomonas oryzae pv. oryzae (strain MAFF 311018).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=342109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAFF 311018;
RA   Ochiai H., Inoue Y., Takeya M., Sasaki A., Kaku H.;
RT   "Genome sequence of Xanthomonas oryzae pv. oryzae suggests
RT   contribution of large numbers of effector genes and insertion
RT   sequences to its race diversity.";
RL   Jpn. Agric. Res. Q. 39:275-287(2005).
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: ATP + UTP + L-glutamine = ADP + phosphate +
CC       CTP + L-glutamate. {ECO:0000255|HAMAP-Rule:MF_01227}.
CC   -!- ACTIVITY REGULATION: Allosterically activated by GTP, when
CC       glutamine is the substrate; GTP has no effect on the reaction when
CC       ammonia 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:0000255|HAMAP-Rule:MF_01227}.
CC   -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo
CC       pathway; CTP from UDP: step 2/2. {ECO:0000255|HAMAP-
CC       Rule:MF_01227}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01227}.
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:0000255|HAMAP-Rule:MF_01227}.
CC   -!- SIMILARITY: Belongs to the CTP synthase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01227}.
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DR   EMBL; AP008229; BAE69572.1; -; Genomic_DNA.
DR   RefSeq; WP_011259532.1; NC_007705.1.
DR   ProteinModelPortal; Q2P1K5; -.
DR   SMR; Q2P1K5; -.
DR   PRIDE; Q2P1K5; -.
DR   EnsemblBacteria; BAE69572; BAE69572; BAE69572.
DR   GeneID; 34179129; -.
DR   KEGG; xom:XOO2817; -.
DR   HOGENOM; HOG000156188; -.
DR   KO; K01937; -.
DR   OMA; EFNNAYR; -.
DR   OrthoDB; POG091H02IX; -.
DR   UniPathway; UPA00159; UER00277.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003883; F:CTP synthase activity; IEA:UniProtKB-EC.
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; 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; Glutamine amidotransferase; Ligase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Pyrimidine biosynthesis.
FT   CHAIN         1    554       CTP synthase.
FT                                /FTId=PRO_0000266266.
FT   DOMAIN      292    545       Glutamine amidotransferase type-1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   NP_BIND      14     19       ATP. {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   NP_BIND     146    148       Allosteric inhibitor CTP.
FT                                {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   NP_BIND     186    191       Allosteric inhibitor CTP; alternate.
FT                                {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   NP_BIND     186    191       UTP; alternate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01227}.
FT   REGION        1    265       Amidoligase domain. {ECO:0000255|HAMAP-
FT                                Rule:MF_01227}.
FT   REGION      381    384       L-glutamine binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01227}.
FT   ACT_SITE    380    380       Nucleophile; for glutamine hydrolysis.
FT                                {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   ACT_SITE    518    518       {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   ACT_SITE    520    520       {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   METAL        71     71       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01227}.
FT   METAL       139    139       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01227}.
FT   BINDING      13     13       Allosteric inhibitor CTP; alternate.
FT                                {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   BINDING      13     13       UTP; alternate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01227}.
FT   BINDING      71     71       ATP. {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   BINDING     222    222       Allosteric inhibitor CTP; alternate.
FT                                {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   BINDING     222    222       UTP; alternate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01227}.
FT   BINDING     353    353       L-glutamine; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01227}.
FT   BINDING     404    404       L-glutamine. {ECO:0000255|HAMAP-
FT                                Rule:MF_01227}.
FT   BINDING     471    471       L-glutamine; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01227}.
SQ   SEQUENCE   554 AA;  61559 MW;  23615CCFCE279B1B CRC64;
     MTPLIFVTGG VVSSLGKGIA AASLASILEA RGLKVTMMKL DPYINVDPGT MSPFQHGEVY
     VTDDGAETDL DLGHYERYVR TRLSRKNSVT TGRIYENVIR KERRGDYLGA TVQVIPHITD
     EIRRCIDEAT AGFDVALIEI GGTVGDIESL PFLEAIRQVR TERGAEKAMF MHLTLVPYIA
     AAGELKTKPT QHSVKELRSI GIQPDVLLCR SEQAVPDSER RKIALFTNVS ERAVISCPDI
     DVLYGMPLEL LRQGLDELVI VQFKLRDKVA AADLSEWAAV VDAVKHPLDE VTIAVVGKYV
     DHQDAYKSVA EALRHGGLRQ RTKVNLKWLE AQDLERSDMA ALQDIDGILV PGGFGDRGFE
     GKVQTSKFAR EHKVPYFGIC YGMQAAVVDY ARHVADLDAA NSTENDRQSP HPVIGLITEW
     RTATGEVEKR DEKSDLGGTM RLGLQEQRLK PGTLARELYG KDVVAERHRH RYEFNNRYRT
     QLEDAGLVIS GKSMDDTLVE VVELPRDTHP WFLACQAHPE FLSTPRDGHP LFIGFVRAAR
     EKKAGGKLLK EARA
//