ID   PYRG_CLOP1              Reviewed;         535 AA.
AC   Q0TNA4;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 23.
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=CPF_2472;
OS   Clostridium perfringens (strain ATCC 13124 / NCTC 8237 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195103;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16825665; DOI=10.1101/gr.5238106;
RA   Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R.,
RA   DeBoy R.T., Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C.,
RA   Haft D.H., Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J.,
RA   Sullivan S.A., Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S.,
RA   Benton J., Radune D., Fisher D.J., Atkins H.S., Hiscox T., Jost B.H.,
RA   Billington S.J., Songer J.G., McClane B.A., Titball R.W., Rood J.I.,
RA   Melville S.B., Paulsen I.T.;
RT   "Skewed genomic variability in strains of the toxigenic bacterial
RT   pathogen, Clostridium perfringens.";
RL   Genome Res. 16:1031-1040(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; CP000246; ABG84508.1; -; Genomic_DNA.
DR   RefSeq; YP_696886.1; -.
DR   GeneID; 4203868; -.
DR   GenomeReviews; CP000246_GR; CPF_2472.
DR   KEGG; cpf:CPF_2472; -.
DR   TIGR; CPF_2472; -.
DR   HOGENOM; Q0TNA4; -.
DR   OMA; Q0TNA4; 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    535       CTP synthase.
FT                                /FTId=PRO_0000266096.
FT   DOMAIN      295    535       Glutamine amidotransferase type-1.
FT   REGION        1    257       Aminator domain.
FT   ACT_SITE    384    384       Nucleophile (By similarity).
FT   ACT_SITE    510    510       By similarity.
FT   ACT_SITE    512    512       By similarity.
SQ   SEQUENCE   535 AA;  59656 MW;  2B6C15683AD14107 CRC64;
     MSKNTKYVFV TGGVVSSLGK GITAASLGRL LKNRGLSVSI QKFDPYLNID PGTMSPYQHG
     EVFVTDDGAE TDLDLGHYER FIDENLTQNS NVTSGRVYWS VISKERKGEY LGGTVQVIPH
     ITNAIKDRVH RVGKERDVDV VITEIGGTIG DIESLPFLEA IRQIKYDVGK ENVCFIHVTL
     VPYLGKAGEL KTKPTQHSVK ELRSIGIQPD IIVCRSEKEL SEDIKKKIGL FCNIDASEVI
     QNLDAEHLYA VPLMLHKEGL DRLVCEKLGL GCRDIDNAEW IDMVHRITHL THTTKIALVG
     KYVELHDAYI SVVEALNHGG LSNDTNVEIE WINAEDVTKE NVDELLSGVD GVLVPGGFGD
     RGVEGKIEAI RWARENKKPF LGICLGMQCA VIEYARNVLG LEGAHSSELN PETPFPVIDL
     MPEQKDVEDL GGTMRLGLYP CKLEDNTFCK DVYASDLIYE RHRHRYEFNN EYRTQLIESG
     LTIAGTSPDG RLVECVEVKD HPWFVAVQYH PELKSRPNRP HPLFVGFVGA ALNNK
//