ID D6YWF4_WADCW Unreviewed; 538 AA. AC D6YWF4; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 14-DEC-2011, entry version 12. 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; OrderedLocusNames=wcw_1108; OS Waddlia chondrophila (strain ATCC VR-1470 / WSU 86-1044). OC Bacteria; Chlamydiae; Chlamydiales; Waddliaceae; Waddlia. OX NCBI_TaxID=716544; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WSU 86-1044; RX PubMed=20531937; DOI=10.1371/journal.pone.0010890; RA Bertelli C., Collyn F., Croxatto A., Ruckert C., Polkinghorne A., RA Kebbi-Beghdadi C., Goesmann A., Vaughan L., Greub G.; RT "The Waddlia genome: a window into chlamydial biology."; RL PLoS ONE 5:E10890-E10890(2010). 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. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001928; ADI38465.1; -; Genomic_DNA. DR RefSeq; YP_003709471.1; NC_014225.1. DR ProteinModelPortal; D6YWF4; -. DR GeneID; 9278087; -. DR GenomeReviews; CP001928_GR; wcw_1108. DR KEGG; wch:wcw_1108; -. DR PATRIC; 38314204; VBIWadCho156037_1072. 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:HAMAP. 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 KO; K01937; -. 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 DOMAIN 294 537 Glutamine amidotransferase type-1 (By FT similarity). FT REGION 1 256 Aminator domain (By similarity). FT ACT_SITE 384 384 Nucleophile (By similarity). FT ACT_SITE 510 510 By similarity. FT ACT_SITE 512 512 By similarity. SQ SEQUENCE 538 AA; 60421 MW; E21E9942FFB01F74 CRC64; MSTKYIFFTG GVCSSLGKGL TAASTALLLE KKGLRVAMLK LDPYLNVDPG TMNPFQHGEV YVTDDGAETD LDLGHYYRYS NSPLSKASNA TSGQIYNTVI KRERHGDYLG NTVQVIPHIT DEIKRRILNC ARQEDGIDIL IIEIGGTVGD IESLPFLEAI RQFRNENERN CISIHLTYVP YIKAAGEVKT KPTQHSVQSL REIGLYPDII LCRSEMTLPD SVKDKISLFC NVNRKAVIEE VDVEHSIYEV PLELKNQGLD SMIMELLHLE DKEIDMSEWI KIVDTIKNPK GKITVGVVGK YVKHQDAYKS VFEALDHGAL AHGYELEIKR FEADKVLTAA DLEQAFGRCD GYLIPGGFGE RGWEGKIQAA KYCRENKIPY FGICLGMQVM SVEFARNAAK LEDANTTEVD PGTSTPIISL LSEQQQVSDM GGTMRLGAQD CLIEKGSKAF EIYDSEKISE RHRHRYEFNS KYKELMEKAG LRISGKHAET KLCEIVEVED HPWMIGVQFH PEFKSKPTAP HPLFRSFIEA AIKRKTSS //