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 24-JUL-2007, entry version 34. 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 2/2. 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; AE010299; AAM06649.1; -; Genomic_DNA. DR GenomeReviews; AE010299_GR; MA_3279. DR KEGG; mac:MA3279; -. DR BioCyc; MACE188937:MA3279-MONOMER; -. DR GO; GO:0003883; F:CTP synthase activity; IEA:HAMAP. DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:HAMAP. 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; PS51273; GATASE_TYPE_1; 1. PE 3: Inferred from homology; KW Complete proteome; Glutamine amidotransferase; Ligase; KW Pyrimidine biosynthesis. FT CHAIN 1 534 CTP synthase. FT /FTId=PRO_0000138259. FT DOMAIN 289 530 Glutamine amidotransferase type-1. FT REGION 1 252 Aminator domain. FT ACT_SITE 379 379 Nucleophile (By similarity). FT ACT_SITE 503 503 By similarity. FT ACT_SITE 505 505 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 //