ID   PYRG_CHLFF              Reviewed;         539 AA.
AC   Q254V9;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
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=CF0407;
OS   Chlamydophila felis (strain Fe/C-56).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydophila.
OX   NCBI_TaxID=264202;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16766509; DOI=10.1093/dnares/dsi027;
RA   Azuma Y., Hirakawa H., Yamashita A., Cai Y., Rahman M.A., Suzuki H.,
RA   Mitaku S., Toh H., Goto S., Murakami T., Sugi K., Hayashi H.,
RA   Fukushi H., Hattori M., Kuhara S., Shirai M.;
RT   "Genome sequence of the cat pathogen, Chlamydophila felis.";
RL   DNA Res. 13:15-23(2006).
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; AP006861; BAE81179.1; -; Genomic_DNA.
DR   RefSeq; YP_515324.1; -.
DR   GeneID; 3958889; -.
DR   GenomeReviews; AP006861_GR; CF0407.
DR   KEGG; cfe:CF0407; -.
DR   HOGENOM; Q254V9; -.
DR   OMA; Q254V9; EFNNAYR.
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_0000266092.
FT   DOMAIN      294    533       Glutamine amidotransferase type-1.
FT   REGION        1    255       Aminator domain.
FT   ACT_SITE    380    380       Nucleophile (By similarity).
FT   ACT_SITE    506    506       By similarity.
FT   ACT_SITE    508    508       By similarity.
SQ   SEQUENCE   539 AA;  60092 MW;  C0C15A926AB660B6 CRC64;
     MSFKCIFLTG GVVSSLGKGL TAASLALLLE RQSLKVSMLK LDPYLNVDPG TMNPYEHGEV
     YVTNDGIETD LDLGHYHRFS SVKLSKYSTA TSGQIYARVI KKEREGVYLG STVQVIPHIT
     NEIIEVILEC ARENQPDVLI VEIGGTVGDI ESLPFLEAIR QFRYEHAENC FSIHMTYVPY
     LKAAGEVKTK PTQHSVQSLR SIGIIPDAIL CRSESSLSPD VKKKISLFCN VPNNAVFNVV
     DIEHSIYEMP LMLSQENIST FITEKLGLFT KQEDLSDWKT LVERLRNPSL DKVRIGLVGK
     YVQHKDAYKS VFEALTHAAL SLNSSVEILP LDSEDPHFLE TLEQCDGCLV PGGFGSRGWE
     GKITAAKLCR ERGIPYFGIC LGMQVLVVEY ARNVLRLEKA NSTEMDAETP DPVICMMDGQ
     ASLVATGGTM RLGAYPCLIS PGTKVHEAYG ESEVMERHRH RYEVNFDYVQ QFKDFGLNVV
     GTCPQQGLCE IVEIENHPWM IGVQFHPEFL SKLIAPHPLF VGFIQAAILY SRNKSYVQA
//