ID   D8A490_ECOLX            Unreviewed;       545 AA.
AC   D8A490;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-JUL-2011, entry version 8.
DE   RecName: Full=CTP synthase;
DE            EC=6.3.4.2;
DE   AltName: Full=CTP synthetase;
DE   AltName: Full=UTP--ammonia ligase;
GN   Name=pyrG; ORFNames=HMPREF9530_01328;
OS   Escherichia coli MS 21-1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=749527;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MS 21-1;
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B.,
RA   Courtney L., Fronick C., Harrison M., Strong C., Farmer C.,
RA   Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C.,
RA   Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M.,
RA   Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (JUN-2010) 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; ADTR01000124; EFK22050.1; -; Genomic_DNA.
DR   ProteinModelPortal; D8A490; -.
DR   SMR; D8A490; 1-545.
DR   PRIDE; D8A490; -.
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; PyrG; 1; -.
DR   InterPro; IPR004468; CTP_synthase.
DR   InterPro; IPR017456; CTP_synthase_N.
DR   InterPro; IPR017926; GATASE_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; Glutamine amidotransferase; Ligase; Nucleotide-binding;
KW   Pyrimidine biosynthesis.
FT   DOMAIN      291    542       Glutamine amidotransferase type-1 (By
FT                                similarity).
FT   REGION        1    253       Aminator domain (By similarity).
FT   ACT_SITE    379    379       Nucleophile (By similarity).
FT   ACT_SITE    515    515       By similarity.
FT   ACT_SITE    517    517       By similarity.
SQ   SEQUENCE   545 AA;  60374 MW;  FBB9E2E18FA355FC CRC64;
     MTTNYIFVTG GVVSSLGKGI AAASLAAILE ARGLNVTIMK LDPYINVDPG TMSPIQHGEV
     FVTEDGAETD LDLGHYERFI RTKMSRRNNF TTGRIYSDVL RKERRGDYLG ATVQVIPHIT
     NAIKERVLEG GEGHDVVLVE IGGTVGDIES LPFLEAIRQM AVEIGREHTL FMHLTLVPYM
     AASGEVKTKP TQHSVKELLS IGIQPDILIC RSDRAVPANE RAKIALFCNV PEKAVISLKD
     VDSIYKIPGL LKSQGLDDYI CKRFSLNCPE ANLSEWEQVI FEEANPVSEV TIGMVGKYIE
     LPDAYKSVIE ALKHGGLKNR VSVNIKLIDS QDVETRGVEI LKGLDAILVP GGFGYRGVEG
     MITTARFARE NNIPYLGICL GMQVALIDYA RHVANMENAN STEFVPDCKY PVVALITEWR
     DENGNVEVRS EKSDLGGTMR LGAQQCQLVD DSLVRQLYNA PTIVERHRHR YEVNNMLLKQ
     IEDAGLRVAG RSGDDQLVEI IEVPNHPWFV ACQFHPEFTS TPRDGHPLFA GFVKAASEFQ
     KRQAK
//