ID R7WT62_9NOCA Unreviewed; 595 AA. AC R7WT62; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=CTP synthase {ECO:0000256|HAMAP-Rule:MF_01227}; DE EC=6.3.4.2 {ECO:0000256|HAMAP-Rule:MF_01227}; 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 Short=CTP synthetase {ECO:0000256|HAMAP-Rule:MF_01227}; DE Short=CTPS {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:EOM78470.1}; GN ORFNames=Rrhod_0302 {ECO:0000313|EMBL:EOM78470.1}; OS Rhodococcus rhodnii LMG 5362. OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; OC Rhodococcus. OX NCBI_TaxID=1273125 {ECO:0000313|EMBL:EOM78470.1, ECO:0000313|Proteomes:UP000013525}; RN [1] {ECO:0000313|EMBL:EOM78470.1, ECO:0000313|Proteomes:UP000013525} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMG 5362 {ECO:0000313|EMBL:EOM78470.1, RC ECO:0000313|Proteomes:UP000013525}; RX PubMed=23788540; RA Pachebat J.A., van Keulen G., Whitten M.M., Girdwood S., Del Sol R., RA Dyson P.J., Facey P.D.; RT "Draft Genome Sequence of Rhodococcus rhodnii Strain LMG5362, a RT Symbiont of Rhodnius prolixus (Hemiptera, Reduviidae, Triatominae), RT the Principle Vector of Trypanosoma cruzi."; RL Genome Announc. 1:e00329-13(2013). 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:SAAS00710710}. 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:SAAS00710815}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01227, CC ECO:0000256|SAAS:SAAS00710816}. 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:SAAS00710794}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {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:EOM78470.1}. 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; APMY01000004; EOM78470.1; -; Genomic_DNA. DR RefSeq; WP_010836377.1; NZ_APMY01000004.1. DR EnsemblBacteria; EOM78470; EOM78470; Rrhod_0302. DR PATRIC; fig|1273125.3.peg.301; -. DR OrthoDB; POG091H02IX; -. DR UniPathway; UPA00159; UER00277. DR Proteomes; UP000013525; 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-KW. DR CDD; cd01746; GATase1_CTP_Synthase; 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:SAAS00710699}; KW Complete proteome {ECO:0000313|Proteomes:UP000013525}; KW Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00710676}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00710762}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00710689}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00710675}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00710810}; KW Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00710748}; KW Reference proteome {ECO:0000313|Proteomes:UP000013525}. FT DOMAIN 306 554 Glutamine amidotransferase type-1. FT {ECO:0000259|PROSITE:PS51273}. FT NP_BIND 24 29 ATP. {ECO:0000256|HAMAP-Rule:MF_01227}. FT NP_BIND 162 164 Allosteric inhibitor CTP. FT {ECO:0000256|HAMAP-Rule:MF_01227}. FT NP_BIND 202 207 Allosteric inhibitor CTP; alternate. FT {ECO:0000256|HAMAP-Rule:MF_01227}. FT NP_BIND 202 207 UTP; alternate. {ECO:0000256|HAMAP-Rule: FT MF_01227}. FT REGION 1 281 Amidoligase domain. {ECO:0000256|HAMAP- FT Rule:MF_01227}. FT REGION 397 400 L-glutamine binding. {ECO:0000256|HAMAP- FT Rule:MF_01227}. FT ACT_SITE 396 396 Nucleophile; for glutamine hydrolysis. FT {ECO:0000256|HAMAP-Rule:MF_01227}. FT ACT_SITE 527 527 {ECO:0000256|HAMAP-Rule:MF_01227}. FT ACT_SITE 529 529 {ECO:0000256|HAMAP-Rule:MF_01227}. FT METAL 81 81 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01227}. FT METAL 155 155 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01227}. FT BINDING 23 23 Allosteric inhibitor CTP; alternate. FT {ECO:0000256|HAMAP-Rule:MF_01227}. FT BINDING 23 23 UTP; alternate. {ECO:0000256|HAMAP-Rule: FT MF_01227}. FT BINDING 81 81 ATP. {ECO:0000256|HAMAP-Rule:MF_01227}. FT BINDING 238 238 Allosteric inhibitor CTP; alternate. FT {ECO:0000256|HAMAP-Rule:MF_01227}. FT BINDING 238 238 UTP; alternate. {ECO:0000256|HAMAP-Rule: FT MF_01227}. FT BINDING 256 256 ATP. {ECO:0000256|HAMAP-Rule:MF_01227}. FT BINDING 369 369 L-glutamine; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_01227}. FT BINDING 419 419 L-glutamine. {ECO:0000256|HAMAP-Rule: FT MF_01227}. FT BINDING 480 480 L-glutamine; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01227}. SQ SEQUENCE 595 AA; 64345 MW; F2CCDE88590A76C6 CRC64; MSQSRIHSRT DTKHIFVSGG VASSLGKGLT ASSLGQLLTA RGMRVTMQKL DPYLNVDPGT MNPFQHGEVF VTEDGAETDL DVGHYERFLD RDLSGQANVT TGQVYSTVIA KERRGEYLGD TVQVIPHITD EIKSRILAMG EPDREGIRPD VVITEIGGTV GDIESQPFLE AARQVRHDVG RDNVFFLHVS LVPYLAPSGE LKTKPTQHSV AALRSIGIQP DALILRCDRD VPQSLKSKIA LMCDVDVDGC ISCPDAPSIY DIPKVLHSEG LDAYVVRQLG LPFRDVDWTV WGNLLERVHQ PRETVKIALV GKYVDLPDAY LSVTEALRAG GFGNRAKVEV VWVRSDDVET PAGAAAHLAD VDGILVPGGF GIRGIEGKVG AIRYARARRI PLLGLCLGLQ CVVIEAARSV GLDDANSTEF EPDTTHPVIS TMADQEDVVA GEADLGGTMR LGAYPATLAK GSVVARAYGA EQVSERHRHR YEVNNTYRAR IEKSGLRFSG TSPDGHLVEF VEYAQDEHPF LVATQAHPEL KSRPTRPHPL FAAFVAAALT YKFEERLPVD VHGDDAQSPA PAETDARGDD LAATGAGDVG ETADA //