ID   D6YWF4_WADCW            Unreviewed;       538 AA.
AC   D6YWF4;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   02-NOV-2016, entry version 50.
DE   RecName: Full=CTP synthase {ECO:0000256|HAMAP-Rule:MF_01227, ECO:0000256|SAAS:SAAS00037303};
DE            EC=6.3.4.2 {ECO:0000256|HAMAP-Rule:MF_01227, ECO:0000256|SAAS:SAAS00037401};
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   AltName: Full=UTP--ammonia ligase {ECO:0000256|HAMAP-Rule:MF_01227};
GN   Name=pyrG {ECO:0000256|HAMAP-Rule:MF_01227,
GN   ECO:0000313|EMBL:ADI38465.1};
GN   OrderedLocusNames=wcw_1108 {ECO:0000313|EMBL:ADI38465.1};
OS   Waddlia chondrophila (strain ATCC VR-1470 / WSU 86-1044).
OC   Bacteria; Chlamydiae; Chlamydiales; Waddliaceae; Waddlia.
OX   NCBI_TaxID=716544 {ECO:0000313|EMBL:ADI38465.1, ECO:0000313|Proteomes:UP000001505};
RN   [1] {ECO:0000313|EMBL:ADI38465.1, ECO:0000313|Proteomes:UP000001505}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-1470 / WSU 86-1044 {ECO:0000313|Proteomes:UP000001505};
RX   PubMed=20531937; DOI=10.1371/journal.pone.0010890;
RA   Bertelli C., Collyn F., Croxatto A., Ruckert C., Polkinghorne A.,
RA   Kebbi-Beghdadi C., Goesmann A., Vaughan L., Greub G.;
RT   "The Waddlia genome: a window into chlamydial biology.";
RL   PLoS ONE 5:E10890-E10890(2010).
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:SAAS00037321}.
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:SAAS00037318}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01227,
CC       ECO:0000256|SAAS:SAAS00356542}.
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:SAAS00548960}.
CC   -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain.
CC       {ECO:0000256|HAMAP-Rule:MF_01227}.
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DR   EMBL; CP001928; ADI38465.1; -; Genomic_DNA.
DR   RefSeq; WP_013182178.1; NZ_LVEB01000045.1.
DR   ProteinModelPortal; D6YWF4; -.
DR   STRING; 716544.wcw_1108; -.
DR   EnsemblBacteria; ADI38465; ADI38465; wcw_1108.
DR   KEGG; wch:wcw_1108; -.
DR   PATRIC; 38314204; VBIWadCho156037_1072.
DR   eggNOG; ENOG4105C8D; Bacteria.
DR   eggNOG; COG0504; LUCA.
DR   HOGENOM; HOG000077515; -.
DR   KO; K01937; -.
DR   OMA; TMRLGEY; -.
DR   OrthoDB; POG091H02IX; -.
DR   UniPathway; UPA00159; UER00277.
DR   Proteomes; UP000001505; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003883; F:CTP synthase activity; IEA:UniProtKB-HAMAP.
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-HAMAP.
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; 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:SAAS00434461};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001505};
KW   Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01227,
KW   ECO:0000256|SAAS:SAAS00434680};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01227,
KW   ECO:0000256|SAAS:SAAS00434363, ECO:0000313|EMBL:ADI38465.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01227,
KW   ECO:0000256|SAAS:SAAS00615993};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01227,
KW   ECO:0000256|SAAS:SAAS00615990};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01227,
KW   ECO:0000256|SAAS:SAAS00434657};
KW   Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01227,
KW   ECO:0000256|SAAS:SAAS00434336};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001505}.
FT   DOMAIN      294    537       Glutamine amidotransferase type-1.
FT                                {ECO:0000259|PROSITE:PS51273}.
FT   NP_BIND      15     20       ATP. {ECO:0000256|HAMAP-Rule:MF_01227}.
FT   NP_BIND     150    152       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    269       Amidoligase domain. {ECO:0000256|HAMAP-
FT                                Rule:MF_01227}.
FT   REGION      385    388       L-glutamine binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01227}.
FT   ACT_SITE    384    384       Nucleophile; for glutamine hydrolysis.
FT                                {ECO:0000256|HAMAP-Rule:MF_01227}.
FT   ACT_SITE    510    510       {ECO:0000256|HAMAP-Rule:MF_01227}.
FT   ACT_SITE    512    512       {ECO:0000256|HAMAP-Rule:MF_01227}.
FT   METAL        72     72       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01227}.
FT   METAL       143    143       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     357    357       L-glutamine; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01227}.
FT   BINDING     408    408       L-glutamine. {ECO:0000256|HAMAP-Rule:
FT                                MF_01227}.
FT   BINDING     465    465       L-glutamine; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01227}.
SQ   SEQUENCE   538 AA;  60421 MW;  E21E9942FFB01F74 CRC64;
     MSTKYIFFTG GVCSSLGKGL TAASTALLLE KKGLRVAMLK LDPYLNVDPG TMNPFQHGEV
     YVTDDGAETD LDLGHYYRYS NSPLSKASNA TSGQIYNTVI KRERHGDYLG NTVQVIPHIT
     DEIKRRILNC ARQEDGIDIL IIEIGGTVGD IESLPFLEAI RQFRNENERN CISIHLTYVP
     YIKAAGEVKT KPTQHSVQSL REIGLYPDII LCRSEMTLPD SVKDKISLFC NVNRKAVIEE
     VDVEHSIYEV PLELKNQGLD SMIMELLHLE DKEIDMSEWI KIVDTIKNPK GKITVGVVGK
     YVKHQDAYKS VFEALDHGAL AHGYELEIKR FEADKVLTAA DLEQAFGRCD GYLIPGGFGE
     RGWEGKIQAA KYCRENKIPY FGICLGMQVM SVEFARNAAK LEDANTTEVD PGTSTPIISL
     LSEQQQVSDM GGTMRLGAQD CLIEKGSKAF EIYDSEKISE RHRHRYEFNS KYKELMEKAG
     LRISGKHAET KLCEIVEVED HPWMIGVQFH PEFKSKPTAP HPLFRSFIEA AIKRKTSS
//