ID PYRG_METAC Reviewed; 534 AA. AC Q8TKW5; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 31-OCT-2006, entry version 27. DE CTP synthase (EC 6.3.4.2) (UTP--ammonia ligase) (CTP synthetase). GN Name=pyrG; OrderedLocusNames=MA_3279; OS Methanosarcina acetivorans. OC Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales; OC Methanosarcinaceae; Methanosarcina. OX NCBI_TaxID=2214; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A; RX MEDLINE=21929760; PubMed=11932238; DOI=10.1101/gr.223902; RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., RA FitzHugh W., Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., RA Allen N., Naylor J., Stange-Thomann N., DeArellano K., Johnson R., RA Linton L., McEwan P., McKernan K., Talamas J., Tirrell A., Ye W., RA Zimmer A., Barber R.D., Cann I., Graham D.E., Grahame D.A., Guss A.M., RA Hedderich R., Ingram-Smith C., Kuettner H.C., Krzycki J.A., RA Leigh J.A., Li W., Liu J., Mukhopadhyay B., Reeve J.N., Smith K., RA Springer T.A., Umayam L.A., White O., White R.H., de Macario E.C., RA Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L., Paulsen I.T., RA Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H., Lander E., RA Metcalf W.W., Birren B.; RT "The genome of Methanosarcina acetivorans reveals extensive metabolic RT and physiological diversity."; RL Genome Res. 12:532-542(2002). 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: Nucleotide biosynthesis; CTP biosynthesis; CTP from UDP: CC step 2 [final step]. CC -!- SIMILARITY: Belongs to the CTP synthase family. CC -!- SIMILARITY: Contains 1 type-1 glutamine amidotransferase 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; AE010299; AAM06649.1; -; Genomic_DNA. DR GenomeReviews; AE010299_GR; MA_3279. DR KEGG; mac:MA3279; -. DR BioCyc; MACE188937:MA3279-MONOMER; -. DR HAMAP; MF_01227; -; 1. DR InterPro; IPR000991; GATase_1. DR InterPro; IPR012998; GATase_1_AS. DR InterPro; IPR004468; PyrG_synth. 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; PS00442; GATASE_TYPE_I; 1. KW Complete proteome; Glutamine amidotransferase; Ligase; KW Pyrimidine biosynthesis. FT CHAIN 1 534 CTP synthase. FT /FTId=PRO_0000138259. FT REGION 1 298 Aminator domain. FT REGION 299 534 Glutamine amidotransferase. FT ACT_SITE 379 379 For GATase activity (By similarity). FT ACT_SITE 503 503 For GATase activity (By similarity). FT ACT_SITE 505 505 For GATase activity (By similarity). SQ SEQUENCE 534 AA; 59730 MW; 2AC6AE3C578072DB CRC64; MKYIVVTGGV MSGLGKGITI ASIGRNLKNK GYKVTAIKID PYINIDAGTM SPYQHGEVFV LRDGGEVDLD LGNYERFLDT ELTRDHNLTT GKIYQEVIAK ERRGDYLGKT VQIIPHITNE IKSRIRKVAA RSGADVCLVE IGGTVGDIES MPFLEAVRQM HREEPSENIV FIHVTLVMED LQGEQKTKPS QHSVKELRAL GLSPEVIVTR SKTPLQESAK EKIALFCDVP QELVISAHDA ADIYEVPLEI EEQGLTTRLM KHLKLESSVE DNGWREMVSR MKSTTEEVKL AIVGKYTNLE DSYLSILEAV KHGGIDNGCK VEVNMVEAET LEEDPAEIEK LRQFDGILIP GGFGGRGTEG KMLAIKFARE NDVPFLGICL GMQLAVIEFA RNVVNLENAN STEFDEDTPY PVIDILPEQT GVADMGGTMR LGDYDAILKD GSLATKLYGT NYIVERHRHR YEVNPEFVDR LESFGIVFSG KNKNRMEIAE IPDKRFFFAS QFHPEFRSRP GRPSPPFKGL VRAMCKYNKE KEGQ //