ID   PYRG_BURTA              Reviewed;         553 AA.
AC   Q2SXC7;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-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=BTH_I1892;
OS   Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 /
OS   CIP 106301).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Palmer N., Dodson R.,
RA   Hickey E.K., Gwinn M.L., Dougherty B., Fleischmann R.D.,
RA   Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J.,
RA   Salzberg S.L., Hanson M., van-Vugt R., Adams M.D., Gocayne J.D.,
RA   Weidman J., Utterback T.R., Watthey L., McDonald L.A., Artiach P.,
RA   Bowman C., Garland S., Fujii C., Cotton M.D., Horst K., Tomb J.-F.,
RA   Roberts K., Hatch B., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000086; ABC37894.1; -; Genomic_DNA.
DR   RefSeq; YP_442422.1; -.
DR   GeneID; 3848784; -.
DR   GenomeReviews; CP000086_GR; BTH_I1892.
DR   KEGG; bte:BTH_I1892; -.
DR   TIGR; BTH_I1892; -.
DR   HOGENOM; Q2SXC7; -.
DR   OMA; Q2SXC7; EFNNAYR.
DR   BioCyc; BTHA271848:BTH_I1892-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    553       CTP synthase.
FT                                /FTId=PRO_0000266086.
FT   DOMAIN      295    547       Glutamine amidotransferase type-1.
FT   REGION        1    257       Aminator domain.
FT   ACT_SITE    383    383       Nucleophile (By similarity).
FT   ACT_SITE    520    520       By similarity.
FT   ACT_SITE    522    522       By similarity.
SQ   SEQUENCE   553 AA;  61095 MW;  5D1CB23AAC3FF8F6 CRC64;
     MTKYVFVTGG VVSSLGKGIA AASLAAILES RGLKVTLLKL DPYINVDPGT MSPFQHGEVF
     VTEDGAETDL DLGHYERFIS TKMRKANNFT TGQIYESVIR KERRGDYLGK TVQVIPHITN
     EIQAFIERGA ASATCGEPDV AIVEIGGTVG DIESLPFLEA ARQMSLRLGR NSACFVHLTL
     VPFIATAGEL KTKPTQHSVQ KLREIGISPH VLLCRADRPI PDDESKKISL FSNVPEDAVI
     SVWDVDSIYK IPQMLHDQGL DRLICEELRL DPQPADLRMW SELVEKLQNP KHEVTIGMVG
     KYVDLTESYK SLIEALRHAS IHTSTKVNIE YIDSEELEAN GTASLAHLDA VLVPGGFGRR
     GTEGKIAAVR YAREAKVPYL GICLGMQLAV IEFARDVVGL KQANSTEFDP NTPERVVALI
     TEWYDREGKV EKRTEDSDLG GTMRLGSQRC PIKPGTLAEA IYGKDVNERH RHRYEVNNRF
     VPQLEAGGLV ISARTPSEDL PEMMELPRAM HPWFVGVQFH PEFTSTPRDG HPLFKSFVQA
     AIACQQARAG AKA
//