ID   PYRG_BAUCH              Reviewed;         543 AA.
AC   Q1LTN7;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 25.
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=BCI_0222;
OS   Baumannia cicadellinicola subsp. Homalodisca coagulata.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Baumannia.
OX   NCBI_TaxID=374463;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16729848; DOI=10.1371/journal.pbio.0040188;
RA   Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L.,
RA   Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L.,
RA   Moran N.A., Eisen J.A.;
RT   "Metabolic complementarity and genomics of the dual bacterial
RT   symbiosis of sharpshooters.";
RL   PLoS Biol. 4:1079-1092(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; CP000238; ABF13830.1; -; Genomic_DNA.
DR   RefSeq; YP_588677.1; -.
DR   SMR; Q1LTN7; 1-539.
DR   GeneID; 4056160; -.
DR   GenomeReviews; CP000238_GR; BCI_0222.
DR   KEGG; bci:BCI_0222; -.
DR   HOGENOM; Q1LTN7; -.
DR   OMA; Q1LTN7; 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    543       CTP synthase.
FT                                /FTId=PRO_0000266067.
FT   DOMAIN      291    538       Glutamine amidotransferase type-1.
FT   REGION        1    253       Aminator domain.
FT   ACT_SITE    379    379       Nucleophile (By similarity).
FT   ACT_SITE    511    511       By similarity.
FT   ACT_SITE    513    513       By similarity.
SQ   SEQUENCE   543 AA;  60718 MW;  D2665CA19382B0B3 CRC64;
     MKTNYIFVTG GVVSSLGKGI AVASLAAILE ARGLKVTIMK LDPYINVDPG TISPIQHGEV
     FVTEDGAETD LDLGHYERFI RTKMSRRNNF TTGRIYFDVL HKERRGDYLG ATIQVIPHIT
     NTIKQRIIEC GEGHDVVLVE IGGTVGDIES LPFLEAIRQM AGEVGRDHTL YMHLTLVPYI
     KAAGEVKTKP TQHSVKELLS IGIQPDVLIC RSDRAVPSNE RAKIALFCNV SEKAVISLKD
     VDSIYKIPAL LKSQYLDDYI CERFSLKCPK ANLSEWEQVI YQQANPVGEV TVGIVGKYID
     LPDAYKSVIE ALHHAGLKNR IAVNICLIHS QDVETRSVKI LQDLDAILIP GGFGYRGVEG
     KIMTAQYARE KQIPYLGICL GMQVAIVEFA RHVAGMPEAN STEFVSDCKY PVVALITEWY
     EENNNRKLSN LGGTMRLGSQ PCKLTYGSLA YQIYGKTIIM ERHRHRYEVN NMLLKQIEAA
     GLRVAGLSED YKLVEMIEYP AHPWFIASQF HPEFNSTPRD GHPLFTGFIK AASEYQKKQL
     NKM
//