ID   PYRG_BLOPB              Reviewed;         548 AA.
AC   Q493N6;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 29.
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=BPEN_161;
OS   Blochmannia pennsylvanicus (strain BPEN).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX   NCBI_TaxID=291272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16077009; DOI=10.1101/gr.3771305;
RA   Degnan P.H., Lazarus A.B., Wernegreen J.J.;
RT   "Genome sequence of Blochmannia pennsylvanicus indicates parallel
RT   evolutionary trends among bacterial mutualists of insects.";
RL   Genome Res. 15:1023-1033(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; CP000016; AAZ40801.1; -; Genomic_DNA.
DR   RefSeq; YP_277674.1; -.
DR   SMR; Q493N6; 1-546.
DR   GeneID; 3563096; -.
DR   GenomeReviews; CP000016_GR; BPEN_161.
DR   KEGG; bpn:BPEN_161; -.
DR   HOGENOM; Q493N6; -.
DR   OMA; Q493N6; EFNNAYR.
DR   BioCyc; CBLO291272:BPEN_161-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    548       CTP synthase.
FT                                /FTId=PRO_0000266071.
FT   DOMAIN      291    543       Glutamine amidotransferase type-1.
FT   REGION        1    253       Aminator domain.
FT   ACT_SITE    380    380       Nucleophile (By similarity).
FT   ACT_SITE    516    516       By similarity.
FT   ACT_SITE    518    518       By similarity.
SQ   SEQUENCE   548 AA;  61301 MW;  57D35AFC0F2C9037 CRC64;
     MRVNYIFVTG GVVSSLGKGI ATASLAAVLE ARGLSVTIIK LDPYINMDPG TISPVQHGEV
     FITEDGAETD LDLGHYERFI RTKMRHHNNF TAGKIYADVL RKERRGDYLG ATIQIIPHVT
     DTIKKWLIAG AFGHDVLLVE IGGTVGDIES LPFLEAIRQM VMEVNREQTL YIHLTLVPFI
     AVSGELKTKP TQHSVKELLS IGIQPDILIC RSDRVISNSE RKKISLFCNV PKQAIIALQD
     VDSIYKIPAL LKDQGLDNYI CKRFNLNCPE ANLSDWEEVI YYQEHPIGEV TVGMVGKYIE
     LVDAYKSVTE ALKHAGIKNR FIVNIRLINS QDVEKLGIEK TLKGLDAILV PGGFGYRGVE
     GKILSAQYAR ENNIPYFGIC LGMQVALIEF ARHVAGMPEA NSTEFVTNCK CPVIALITEC
     KDENGIFITH NDNTNLGGTM RLGNQACYLI KGSLTHQIYG KSTILERHRH RYEVNNMLLK
     HITHAGLSCV GFSKKNNLVE VIEYPNHPWF IGSQFHPEFN STPREGHPLF IGFIKAAIEY
     QHRHNKLI
//