ID   PYRG_CHRSD              Reviewed;         548 AA.
AC   Q1QZX9;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-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=Csal_0617;
OS   Chromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB
OS   13768).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Chromohalobacter.
OX   NCBI_TaxID=290398;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Saunders E., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Csonka L.N.,
RA   O'Conner K., Vreeland R.H., Oren A., Vargas C., Nieto J., Arahal D.R.,
RA   Goodner B., Wheeler C., Hall P., Ewing A., Benson L., McBeath D.,
RA   Canovas D., Richardson P.;
RT   "Complete sequence of Chromohalobacter salexigens DSM 3043.";
RL   Submitted (MAR-2006) 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; CP000285; ABE57979.1; -; Genomic_DNA.
DR   RefSeq; YP_572678.1; -.
DR   GeneID; 4029086; -.
DR   GenomeReviews; CP000285_GR; Csal_0617.
DR   KEGG; csa:Csal_0617; -.
DR   NMPDR; fig|290398.4.peg.420; -.
DR   HOGENOM; Q1QZX9; -.
DR   OMA; Q1QZX9; EFNNAYR.
DR   BioCyc; CSAL290398:CSAL_0617-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_0000266095.
FT   DOMAIN      290    541       Glutamine amidotransferase type-1.
FT   REGION        1    252       Aminator domain.
FT   ACT_SITE    378    378       Nucleophile (By similarity).
FT   ACT_SITE    514    514       By similarity.
FT   ACT_SITE    516    516       By similarity.
SQ   SEQUENCE   548 AA;  60663 MW;  F765AC07F2405337 CRC64;
     MTRYIFVTGG VVSSLGKGIA SASLAAILEA RGLKVTILKL DPYINVDPGT MSPFQHGEVF
     VTEDGAETDL DLGHYERFIR TKMTQGNNFT TGRVYEHVLR KERRGDYLGG TVQVIPHITD
     EIKRRVYEGG DGFDVALVEI GGTVGDIESL PFLEATRQIR SEKGANQAIF MHLTLVPYIK
     TAGETKTKPT QHSVKELRSI GIQPDILICR SEVELEESER RKIALFTNVE ERAVVPLQDA
     DTIYRIPLML HEHGLDDIIC DKLRIEADEV DLAEWVRVLD AKLNPLKSVN IAMVGKYMEL
     LDAYKSLNEA LIHAGIQGRV KVNIDYIDSE DIEHHGTERL AGKDAILVPG GFGERGVEGK
     IATARYAREN GVPYLGICLG MQVAVIEYAR HVAGWADANS TEFTHDTQHP VVGLITEWVN
     AEGKIELRDA ASDLGGTMRL GGQVCHLKPG TRAHEAYGLD EITERHRHRF EVNNQFVEAL
     ESAGLVISGK SADHSLVEMI ELPEHPWYVA CQFHPEFTST PRDGHPLFSG FVNAALAYKA
     ARARAQQS
//