ID D8A490_ECOMS Unreviewed; 545 AA. AC D8A490; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 30-NOV-2016, entry version 42. DE RecName: Full=CTP synthase {ECO:0000256|HAMAP-Rule:MF_01227, ECO:0000256|SAAS:SAAS00638782}; DE EC=6.3.4.2 {ECO:0000256|HAMAP-Rule:MF_01227, ECO:0000256|SAAS:SAAS00638793}; DE AltName: Full=Cytidine 5'-triphosphate synthase {ECO:0000256|HAMAP-Rule:MF_01227}; DE AltName: Full=Cytidine triphosphate synthetase {ECO:0000256|HAMAP-Rule:MF_01227}; DE AltName: Full=UTP--ammonia ligase {ECO:0000256|HAMAP-Rule:MF_01227}; GN Name=pyrG {ECO:0000256|HAMAP-Rule:MF_01227, GN ECO:0000313|EMBL:EFK22050.1}; GN ORFNames=HMPREF9530_01328 {ECO:0000313|EMBL:EFK22050.1}; OS Escherichia coli (strain MS 21-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=749527 {ECO:0000313|EMBL:EFK22050.1, ECO:0000313|Proteomes:UP000005688}; RN [1] {ECO:0000313|EMBL:EFK22050.1, ECO:0000313|Proteomes:UP000005688} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MS 21-1 {ECO:0000313|EMBL:EFK22050.1, RC ECO:0000313|Proteomes:UP000005688}; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JUN-2010) 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. Regulates CC intracellular CTP levels through interactions with the four CC ribonucleotide triphosphates. {ECO:0000256|HAMAP-Rule:MF_01227}. CC -!- CATALYTIC ACTIVITY: ATP + UTP + L-glutamine = ADP + phosphate + CC CTP + L-glutamate. {ECO:0000256|HAMAP-Rule:MF_01227, CC ECO:0000256|SAAS:SAAS00638784}. CC -!- ENZYME REGULATION: Allosterically activated by GTP, when glutamine CC is the substrate; GTP has no effect on the reaction when ammonia CC is the substrate. The allosteric effector GTP functions by CC stabilizing the protein conformation that binds the tetrahedral CC intermediate(s) formed during glutamine hydrolysis. Inhibited by CC the product CTP, via allosteric rather than competitive CC inhibition. {ECO:0000256|HAMAP-Rule:MF_01227}. CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo CC pathway; CTP from UDP: step 2/2. {ECO:0000256|HAMAP-Rule:MF_01227, CC ECO:0000256|SAAS:SAAS00638787}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01227, CC ECO:0000256|SAAS:SAAS00638797}. CC -!- MISCELLANEOUS: CTPSs have evolved a hybrid strategy for CC distinguishing between UTP and CTP. The overlapping regions of the CC product feedback inhibitory and substrate sites recognize a common CC feature in both compounds, the triphosphate moiety. To CC differentiate isosteric substrate and product pyrimidine rings, an CC additional pocket far from the expected kinase/ligase catalytic CC site, specifically recognizes the cytosine and ribose portions of CC the product inhibitor. {ECO:0000256|HAMAP-Rule:MF_01227}. CC -!- SIMILARITY: Belongs to the CTP synthase family. CC {ECO:0000256|HAMAP-Rule:MF_01227, ECO:0000256|SAAS:SAAS00638789}. CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain. CC {ECO:0000256|HAMAP-Rule:MF_01227}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFK22050.1}. 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; ADTR01000124; EFK22050.1; -; Genomic_DNA. DR RefSeq; WP_000210878.1; NZ_GG772656.1. DR ProteinModelPortal; D8A490; -. DR SMR; D8A490; -. DR EnsemblBacteria; EFK22050; EFK22050; HMPREF9530_01328. DR PATRIC; 41827339; VBIEscCol155740_1230. DR UniPathway; UPA00159; UER00277. DR Proteomes; UP000005688; Unassembled WGS sequence. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003883; F:CTP synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-HAMAP. DR CDD; cd01746; GATase1_CTP_Synthase; 1. DR Gene3D; 3.40.50.300; -; 1. DR Gene3D; 3.40.50.880; -; 1. DR HAMAP; MF_01227; PyrG; 1. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR004468; CTP_synthase. DR InterPro; IPR017456; CTP_synthase_N. DR InterPro; IPR017926; GATASE. DR InterPro; IPR033828; GATase1_CTP_Synthase. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR11550; PTHR11550; 1. DR Pfam; PF06418; CTP_synth_N; 1. DR Pfam; PF00117; GATase; 1. DR SUPFAM; SSF52317; SSF52317; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00337; PyrG; 1. DR PROSITE; PS51273; GATASE_TYPE_1; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00638801}; KW Complete proteome {ECO:0000313|Proteomes:UP000005688}; KW Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00638788}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00638786, ECO:0000313|EMBL:EFK22050.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00638781}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00638795}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00638799}; KW Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00638802}. FT DOMAIN 291 542 Glutamine amidotransferase type-1. FT {ECO:0000259|PROSITE:PS51273}. FT NP_BIND 15 20 ATP. {ECO:0000256|HAMAP-Rule:MF_01227}. FT NP_BIND 147 149 Allosteric inhibitor CTP. FT {ECO:0000256|HAMAP-Rule:MF_01227}. FT NP_BIND 187 192 Allosteric inhibitor CTP; alternate. FT {ECO:0000256|HAMAP-Rule:MF_01227}. FT NP_BIND 187 192 UTP; alternate. {ECO:0000256|HAMAP-Rule: FT MF_01227}. FT NP_BIND 239 241 ATP; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01227}. FT REGION 1 266 Amidoligase domain. {ECO:0000256|HAMAP- FT Rule:MF_01227}. FT REGION 380 383 L-glutamine binding. {ECO:0000256|HAMAP- FT Rule:MF_01227}. FT ACT_SITE 379 379 Nucleophile; for glutamine hydrolysis. FT {ECO:0000256|HAMAP-Rule:MF_01227}. FT ACT_SITE 515 515 {ECO:0000256|HAMAP-Rule:MF_01227}. FT ACT_SITE 517 517 {ECO:0000256|HAMAP-Rule:MF_01227}. FT METAL 72 72 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01227}. FT METAL 140 140 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01227}. FT BINDING 14 14 Allosteric inhibitor CTP; alternate. FT {ECO:0000256|HAMAP-Rule:MF_01227}. FT BINDING 14 14 UTP; alternate. {ECO:0000256|HAMAP-Rule: FT MF_01227}. FT BINDING 72 72 ATP. {ECO:0000256|HAMAP-Rule:MF_01227}. FT BINDING 223 223 Allosteric inhibitor CTP; alternate. FT {ECO:0000256|HAMAP-Rule:MF_01227}. FT BINDING 223 223 UTP; alternate. {ECO:0000256|HAMAP-Rule: FT MF_01227}. FT BINDING 352 352 L-glutamine; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_01227}. FT BINDING 403 403 L-glutamine. {ECO:0000256|HAMAP-Rule: FT MF_01227}. FT BINDING 470 470 L-glutamine; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01227}. SQ SEQUENCE 545 AA; 60374 MW; FBB9E2E18FA355FC CRC64; MTTNYIFVTG GVVSSLGKGI AAASLAAILE ARGLNVTIMK LDPYINVDPG TMSPIQHGEV FVTEDGAETD LDLGHYERFI RTKMSRRNNF TTGRIYSDVL RKERRGDYLG ATVQVIPHIT NAIKERVLEG GEGHDVVLVE IGGTVGDIES LPFLEAIRQM AVEIGREHTL FMHLTLVPYM AASGEVKTKP TQHSVKELLS IGIQPDILIC RSDRAVPANE RAKIALFCNV PEKAVISLKD VDSIYKIPGL LKSQGLDDYI CKRFSLNCPE ANLSEWEQVI FEEANPVSEV TIGMVGKYIE LPDAYKSVIE ALKHGGLKNR VSVNIKLIDS QDVETRGVEI LKGLDAILVP GGFGYRGVEG MITTARFARE NNIPYLGICL GMQVALIDYA RHVANMENAN STEFVPDCKY PVVALITEWR DENGNVEVRS EKSDLGGTMR LGAQQCQLVD DSLVRQLYNA PTIVERHRHR YEVNNMLLKQ IEDAGLRVAG RSGDDQLVEI IEVPNHPWFV ACQFHPEFTS TPRDGHPLFA GFVKAASEFQ KRQAK //