ID PYRG2_BOVIN Reviewed; 586 AA. AC Q1RMS2; A5D9B0; DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 16-MAY-2006, sequence version 1. DT 16-JUN-2009, entry version 28. DE RecName: Full=CTP synthase 2; DE EC=6.3.4.2; DE AltName: Full=UTP--ammonia ligase 2; DE AltName: Full=CTP synthetase 2; GN Name=CTPS2; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=16305752; DOI=10.1186/1471-2164-6-166; RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.; RT "Characterization of 954 bovine full-CDS cDNA sequences."; RL BMC Genomics 6:166-166(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Hereford; TISSUE=Uterus; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (APR-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. CC Constitutes the rate-limiting enzyme in the synthesis of cytosine CC nucleotides (By similarity). CC -!- CATALYTIC ACTIVITY: ATP + UTP + NH(3) = ADP + phosphate + CTP. 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 http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BT030529; ABQ12969.1; -; mRNA. DR EMBL; BC114742; AAI14743.1; -; mRNA. DR IPI; IPI00687870; -. DR RefSeq; NP_001070434.1; -. DR UniGene; Bt.74451; -. DR Ensembl; ENSBTAG00000017017; Bos taurus. DR GeneID; 767849; -. DR KEGG; bta:767849; -. DR HOVERGEN; Q1RMS2; -. DR OMA; Q1RMS2; KVPVDGN. DR BRENDA; 6.3.4.2; 251. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003883; F:CTP synthase activity; IEA:EC. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:UniProtKB-KW. 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 2: Evidence at transcript level; KW ATP-binding; Glutamine amidotransferase; Ligase; Nucleotide-binding; KW Phosphoprotein; Pyrimidine biosynthesis. FT CHAIN 1 586 CTP synthase 2. FT /FTId=PRO_0000247032. FT DOMAIN 300 554 Glutamine amidotransferase type-1. FT ACT_SITE 399 399 For GATase activity (By similarity). FT ACT_SITE 526 526 For GATase activity (By similarity). FT ACT_SITE 528 528 For GATase activity (By similarity). FT MOD_RES 568 568 Phosphoserine (By similarity). FT MOD_RES 571 571 Phosphoserine (By similarity). FT MOD_RES 574 574 Phosphoserine (By similarity). SQ SEQUENCE 586 AA; 65481 MW; 0A6E65BF35958831 CRC64; MKYILVTGGV ISGIGKGIIA SSIGTILKSC GLRVTAIKID PYINIDAGTF SPYEHGEVFV LNDGGEVDLD LGNYERFLDI NLYKDNNITT GKIYQHVINK ERRGDYLGKT VQVVPHITDA VQEWVMNQAM VPVDGHKEEP QICVIELGGT IGDIEGMPFV EAFRQFQFKA KRENFCNIHV SLVPQPSATG EQKTKPTQNS VRALRGLGLS PDLIVCRSST PIEMAVKEKI SMFCHVNPEQ VICIHDVSST YRVPVLLEEQ GIIKYFKERL DLPIGDSASS LLSKWRNMAD RYERLQKTCS IALVGKYTKL RDCYASVFKA LEHSALAINH KLNLMYIDSI DLEQTTEVED PVKFHEAWQK LCKADGVLVP GGFGIRGTLG KLQAISWARS RKIPFLGVCL GMQLAVIEFA RNCLNLKDAD STEFEPNARV PVVIDMPEHN PGNLGGTMRL GIRRTVFKTE NSILRKLYGD VPFIEERHRH RYEVNPSLIS QLEQKDLSFV GQDVDGERME IIELANHPYF VGVQFHPEFS SRPMKPSPPY LGLLLAATGN LNAYLLQGCK LSSSDRYSDA SDDSFSEPRL AELEIS //