ID PYRG_METBU Reviewed; 534 AA. AC Q12WH5; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 22-AUG-2006, sequence version 1. DT 16-JUN-2009, entry version 23. 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=Mbur_1282; OS Methanococcoides burtonii (strain DSM 6242). OC Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales; OC Methanosarcinaceae; Methanococcoides. OX NCBI_TaxID=259564; 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 Kadner K., Aerts A., Dehal P., Pitluck S., Martinez M., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., RA Franzmann P., Thomas T., Saunders N., Cavicchioli R., Sowers K., RA Richardson P.; RT "Complete sequence of Methanococcoides burtonii DSM 6242."; RL Submitted (MAR-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 -!- 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; CP000300; ABE52201.1; -; Genomic_DNA. DR RefSeq; YP_565951.1; -. DR GeneID; 3998306; -. DR GenomeReviews; CP000300_GR; Mbur_1282. DR KEGG; mbu:Mbur_1282; -. DR NMPDR; fig|259564.8.peg.1213; -. DR HOGENOM; Q12WH5; -. DR OMA; Q12WH5; YPVVDLM. DR BioCyc; MBUR259564:MBUR_1282-MON; -. 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 1 534 CTP synthase. FT /FTId=PRO_0000266273. 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; 59573 MW; A08872A8BBD4BDE9 CRC64; MKYIIVTGGV MSGLGKGITT ASVGRNLKNK GYKVTAIKID PYINIDAGTM SPYQHGEVYV LKDGGEVDLD LGNYERFLDT ELTRDHNLTT GKIYQTVIDK ERKGEYLGKT VQIIPHITNE IKDRIRRIAA KSGADVCLIE VGGTVGDIES MPFLEAVRQM YREESPENIA LLHVTLVPID SQGDQKTKPT QHSVKELREL GLTPHVIVSR CKKALMESTR SKIALFCDVP VEAVISAHDS ADIYEVPLQL ENEGLSNYLL KKLILKSTLE DTNWEEMVIR MNNCTGNVNV AIVGKYTHLE DSYISIVESL KHGAIEIGCK FEITWFDAES FDDDPSEVEK LNGFDGILVP GGFGERGTEG KMLAIKYARE NNIPYLGLCL GMQLAVIEFA RNVVGLDGAN SSEFDENTPY PVIDLLPEQE DVVDMGATMR LGDYEATLKA GSLAESIYGA SLITERHRHR YEVNPNYVDR IEEHGMIFSG KNKNRMEIAE VPSKDFYFAS QFHPEFKSRP GRPSPPFKAF MGAMLKKSKE KKDQ //