ID PYRG_METAC STANDARD; PRT; 534 AA. AC Q8TKW5; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE CTP synthase (EC 6.3.4.2) (UTP--ammonia ligase) (CTP synthetase). GN PYRG OR MA3279. OS Methanosarcina acetivorans. OC Archaea; Euryarchaeota; Euryarchaeota orders incertae sedis; OC Methanosarcinales; Methanosarcinaceae; Methanosarcina. OX NCBI_TaxID=2214; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=C2A / ATCC 35395 / DSM 2834; RX MEDLINE=21929760; PubMed=11932238; 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., 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: Pyrimidine biosynthesis; conversion of UMP to CTP; third CC (last) 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; AE011031; AAM06649.1; -. DR HAMAP; MF_01227; -; 1. DR InterPro; IPR000991; GATase_1. DR InterPro; IPR004468; PyrG. DR Pfam; PF00117; GATase; 1. DR TIGRFAMs; TIGR00337; PyrG; 1. DR PROSITE; PS00442; GATASE_TYPE_I; 1. KW Pyrimidine biosynthesis; Ligase; Glutamine amidotransferase; KW Complete proteome. FT DOMAIN 1 298 AMINATOR DOMAIN. FT DOMAIN 299 534 GLUTAMINE AMIDOTRANSFERASE. FT ACT_SITE 379 379 GATASE (BY SIMILARITY). FT ACT_SITE 503 503 GATASE (BY SIMILARITY). FT ACT_SITE 505 505 GATASE (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 //