ID   PYRG_BORA1              Reviewed;         550 AA.
AC   Q2KZF8;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 27.
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=BAV1165;
OS   Bordetella avium (strain 197N).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16885469; DOI=10.1128/JB.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D.,
RA   King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D.,
RA   Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R.,
RA   Squares S., Woodward J., Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella
RT   avium with those of B. bronchiseptica, B. pertussis, and B.
RT   parapertussis reveals extensive diversity in surface structures
RT   associated with host interaction.";
RL   J. Bacteriol. 188:6002-6015(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; AM167904; CAJ48773.1; -; Genomic_DNA.
DR   RefSeq; YP_785687.1; -.
DR   GeneID; 6265201; -.
DR   GenomeReviews; AM167904_GR; BAV1165.
DR   KEGG; bav:BAV1165; -.
DR   NMPDR; fig|521.1.peg.2293; -.
DR   HOGENOM; Q2KZF8; -.
DR   OMA; Q2KZF8; 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    550       CTP synthase.
FT                                /FTId=PRO_0000266072.
FT   DOMAIN      295    545       Glutamine amidotransferase type-1.
FT   REGION        1    257       Aminator domain.
FT   ACT_SITE    383    383       Nucleophile (By similarity).
FT   ACT_SITE    518    518       By similarity.
FT   ACT_SITE    520    520       By similarity.
SQ   SEQUENCE   550 AA;  60655 MW;  7945F56D0AF90FC9 CRC64;
     MTKYVFVTGG VVSSLGKGIA AASLAAILES RGLQVTLLKL DPYINVDPGT MSPFQHGEVF
     VTEDGAETDL DLGHYERFIS TKMRRVNNFT TGQIYESVLR KERRGDYLGK TVQVIPHITN
     EIQDFVARGA DSAWQGNTDV AIVEIGGTVG DIESLPFLEA ARQMSLRMGR NSAAFVHLTL
     VPYIASAGEL KTKPTQHSVQ KLREIGIYPN ALLCRADRRI PDDERAKISM FSNVPLDAVI
     SVWDVDSIYK IPAMLHQQGV DNIVCEALGL TPPPADLSMW DNLVDALEHP QHEVTIGMVG
     KYVDLTESYK SLSEALVHAG IHTRSKVKIE YIDSEDIEAR GTEQLKHLDA ILVPGGFGKR
     GTEGKIAAIR YARENGVPYL GICLGMQLAV IEFARHVAGL GGANSTEFDP SAPHPVVALI
     TEWMDREGKV EKRDTNSDLG GTMRKGAQRC PIKPGTLAQS IYGDDVNERH RHRYEVNNVY
     VPRLEAAGLV ISARTPTENL PEMMELPNHP WFVGVQFHPE FTSTPRDGHP LFSSYIRAAL
     ESKNRRDPQA
//