ID   PYRG_ALHEH              Reviewed;         540 AA.
AC   Q0A7K2;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
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=Mlg_1841;
OS   Alkalilimnicola ehrlichei (strain MLHE-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Alkalilimnicola.
OX   NCBI_TaxID=187272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T.,
RA   King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T.,
RA   Xie G., Stolz J.F., Richardson P.;
RT   "Complete sequence of Alkalilimnicola ehrilichei MLHE-1.";
RL   Submitted (AUG-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; CP000453; ABI57185.1; -; Genomic_DNA.
DR   RefSeq; YP_742675.1; -.
DR   GeneID; 4269209; -.
DR   GenomeReviews; CP000453_GR; Mlg_1841.
DR   KEGG; aeh:Mlg_1841; -.
DR   NMPDR; fig|187272.6.peg.1752; -.
DR   HOGENOM; Q0A7K2; -.
DR   OMA; Q0A7K2; 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    540       CTP synthase.
FT                                /FTId=PRO_0000266051.
FT   DOMAIN      290    540       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   540 AA;  60166 MW;  7F703139C3127293 CRC64;
     MTRYIFITGG VVSSLGKGIT AASLGTILQA RGLSVSMTKL DPYINVDPGT MSPFQHGEVY
     VTDDGAETDL DLGHYERFVR TTMTRNNNYT TGRIYESVIR KERRGEYLGG TVQVIPHITD
     EIKRSIQQGA DDADIALIEI GGTVGDIESL PFLEAIRQMG AELGRGRCLF MHLTLVPFIG
     AAGEMKTKPT QHSVKELRSI GIQPDILVCR ASQRIPEEER RKIALFTNVE PRAVVSCLDV
     DNIYKIPEVL HRQGLDNIVA EKLGLELPPA SLQDWQRVVE AMQNPEGEVT IAMVGKYVDL
     TDAYMSLNES LRHAGIQTRH RVNIRYIDSE ELEREGTHAL DGVDAVLVPG GFGERGVEGK
     ILAARYARER KVPYLGICLG MQVAVIEYAR NVAGLEGAHS TEFTRHPHHP VIGLITEWMT
     DEGTVEQRSE DSDLGGTMRL GAQPCRLTEG SLARQVYGKD VVEERHRHRY EFNNHYLEAL
     EAAGLRFSGW SHDRKLVEVV EQPDHPWFLA CQFHPEFTST PRDGHPLFAA FVRAAIAHRG
//