ID   D6YWF4_WADCW            Unreviewed;       538 AA.
AC   D6YWF4;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   11-NOV-2015, entry version 41.
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=CTP 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.
CC       {ECO:0000256|HAMAP-Rule:MF_01227, ECO:0000256|SAAS:SAAS00037305}.
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. Inhibited by CTP. {ECO:0000256|HAMAP-
CC       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   -!- SIMILARITY: Belongs to the CTP synthase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01227}.
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; NC_014225.1.
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; MRLGEYE; -.
DR   BioCyc; WCHO716544:GHGA-1108-MONOMER; -.
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: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:SAAS00037320};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001505};
KW   Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01227,
KW   ECO:0000256|SAAS:SAAS00037346};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01227,
KW   ECO:0000256|SAAS:SAAS00037306};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01227,
KW   ECO:0000256|SAAS:SAAS00037369};
KW   Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01227,
KW   ECO:0000256|SAAS:SAAS00037390};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001505}.
FT   DOMAIN      294    537       Glutamine amidotransferase type-1.
FT                                {ECO:0000256|HAMAP-Rule:MF_01227}.
FT   REGION        1    256       Aminator domain. {ECO:0000256|HAMAP-Rule:
FT                                MF_01227}.
FT   ACT_SITE    384    384       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_01227}.
FT   ACT_SITE    510    510       {ECO:0000256|HAMAP-Rule:MF_01227}.
FT   ACT_SITE    512    512       {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
//