ID   PYRG_CHLTA              Reviewed;         539 AA.
AC   Q3KMH9;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   16-JUN-2009, entry version 28.
DE   RecName: Full=CTP synthase;
DE            EC=6.3.4.2;
DE   AltName: Full=UTP--ammonia ligase;
DE   AltName: Full=CTP synthetase;
GN   Name=pyrG; OrderedLocusNames=CTA_0201;
OS   Chlamydia trachomatis (strain A/HAR-13 / ATCC VR-571B).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydia.
OX   NCBI_TaxID=315277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16177312; DOI=10.1128/IAI.73.10.6407-6418.2005;
RA   Carlson J.H., Porcella S.F., McClarty G., Caldwell H.D.;
RT   "Comparative genomic analysis of Chlamydia trachomatis oculotropic and
RT   genitotropic strains.";
RL   Infect. Immun. 73:6407-6418(2005).
CC   -!- FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with
CC       either L-glutamine or ammonia as the source of nitrogen (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + UTP + NH(3) = ADP + phosphate + CTP.
CC   -!- ENZYME REGULATION: Allosterically activated by GTP, when glutamine
CC       is the substrate. Inhibited by CTP (By similarity).
CC   -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo
CC       pathway; CTP from UDP: step 2/2.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SIMILARITY: Belongs to the CTP synthase family.
CC   -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain.
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DR   EMBL; CP000051; AAX50443.1; -; Genomic_DNA.
DR   RefSeq; YP_327991.1; -.
DR   GeneID; 3687227; -.
DR   GenomeReviews; CP000051_GR; CTA_0201.
DR   KEGG; cta:CTA_0201; -.
DR   HOGENOM; Q3KMH9; -.
DR   OMA; Q3KMH9; EFNNAYR.
DR   BioCyc; CTRA315277-1:CTA_0201-MON; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003883; F:CTP synthase activity; IEA:HAMAP.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_01227; -; 1.
DR   InterPro; IPR004468; CTP_synthase.
DR   InterPro; IPR017456; CTP_synthase_N.
DR   InterPro; IPR017926; GATASE_1.
DR   InterPro; IPR000991; GATase_class1_C.
DR   PANTHER; PTHR11550; PyrG_synth; 1.
DR   Pfam; PF06418; CTP_synth_N; 1.
DR   Pfam; PF00117; GATase; 1.
DR   TIGRFAMs; TIGR00337; PyrG; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Glutamine amidotransferase; Ligase;
KW   Nucleotide-binding; Pyrimidine biosynthesis.
FT   CHAIN         1    539       CTP synthase.
FT                                /FTId=PRO_0000266090.
FT   DOMAIN      294    532       Glutamine amidotransferase type-1.
FT   REGION        1    255       Aminator domain.
FT   ACT_SITE    380    380       Nucleophile (By similarity).
FT   ACT_SITE    505    505       By similarity.
FT   ACT_SITE    507    507       By similarity.
SQ   SEQUENCE   539 AA;  60204 MW;  413F7475BCDDD7CE CRC64;
     MSFKSIFLTG GVVSSLGKGL TAASLALLLE RQDLKVAMLK LDPYLNVDPG TMNPYEHGEV
     YVTDDGVETD LDLGHYHRFS SVQLSKYSTA TSGQIYTKVL TKERNGEFLG STVQVIPHVT
     NEIINVIQSC ADHHKPDILI VEIGGTIGDI ESLPFLEAVR QFRCEHPQDC LSIHMTYVPY
     LRAAKEIKTK PTQHSVQNLR SIGISPDVIL CRSEAPLSTE VKRKISLFCN VPEHAVFNAI
     DLERSIYEMP LLLAKENISD FLLNKLGFSP KPLDLSDWQD LVEALCDKER QHVRIGLVGK
     YLEHEDAYKS VFESLFHASV PANCSLELVP IAPESEDLLE QLSQCDGCLI PGGFGTRSWE
     GKISAARYCR ERNIPCFGIC LGMQALVVEY ARNVLDKPLA NSMEINPETP DPVVCMMEGQ
     DSVVKGGTMR LGAYPCRIAP GSLASAAYKT DLVQERHRHR YEVNPSYIER LEEHGLKIAG
     VCPLGELCEI VEIPNHRWML GVQFHPEFLS KLAKPHPLFI EFIRAAKAYS LEKANHEHR
//