ID   PYRG_ANADE              Reviewed;         555 AA.
AC   Q2IH81;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-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=Adeh_4174;
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Myxococcaceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397;
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., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-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; CP000251; ABC83938.1; -; Genomic_DNA.
DR   RefSeq; YP_467375.1; -.
DR   GeneID; 3887994; -.
DR   GenomeReviews; CP000251_GR; Adeh_4174.
DR   KEGG; ade:Adeh_4174; -.
DR   HOGENOM; Q2IH81; -.
DR   OMA; Q2IH81; EFNNAYR.
DR   BioCyc; ADEH290397:ADEH_4174-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    555       CTP synthase.
FT                                /FTId=PRO_0000266053.
FT   DOMAIN      297    537       Glutamine amidotransferase type-1.
FT   REGION        1    258       Aminator domain.
FT   ACT_SITE    385    385       Nucleophile (By similarity).
FT   ACT_SITE    510    510       By similarity.
FT   ACT_SITE    512    512       By similarity.
SQ   SEQUENCE   555 AA;  61367 MW;  27D67205E2F1C146 CRC64;
     MVKRGKKTKY LFVTGGVVSS LGKGLSAASI GALLENRGLE VQHLKLDPYI NVDPGTMSPF
     QHGEVFVTDD GAETDLDLGH YERFTSAKMT RRNNYTTGRI YQNVIQRERR GEYLGKTVQV
     IPHITDEIKA VIREAAGGAD ILIVEVGGTV GDIESLPFLE AIRQMKYDVG EENAVYAHLT
     LVPFIAAAGE LKTKPTQHSV KELREIGIQP DLLLCRSDRE IPRDMKDKIA LFCNVDPSAV
     FTALDVPSIY EVPLSLHREG LDDKLAELFN IWSRAPRLER WETIVDKVKN PRRGEVRIGI
     VGKYVELHES YKSLNEALVH GGIANDARVK LAFIDSTKLE EGDLSDLDKV DAILVPGGFG
     IRGTEGKILG VKYAREHKVP FFGICLGLQM AVIEMARNVL GLAGANSLEF DEQTPHPVVT
     LMEGQKGVTD KGGTMRLGAY PCALKEGTKA RALYGADLVH ERHRHRFEFN NDYRAQFEAA
     GMVFSGVNPD LGLVEMIELP GQHFVGCQFH PEFRSKPFAP HPLFAGFVKA ALEHRDAQQR
     QPSAEVKKLP VGKNG
//