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-JAN-2015, entry version 12. 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=CTP 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:EOM78470.1}; GN ORFNames=Rrhod_0302 {ECO:0000313|EMBL:EOM78470.1}; OS Rhodococcus rhodnii LMG 5362. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Nocardiaceae; Rhodococcus. OX NCBI_TaxID=1273125 {ECO:0000313|EMBL:EOM78470.1}; RN [1] {ECO:0000313|EMBL:EOM78470.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMG 5362 {ECO:0000313|EMBL:EOM78470.1}; 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. CC {ECO:0000256|HAMAP-Rule:MF_01227, ECO:0000256|SAAS:SAAS00037305}. CC -!- CATALYTIC ACTIVITY: ATP + UTP + L-glutamine = ADP + phosphate + CC CTP + L-glutamate. {ECO:0000256|HAMAP-Rule:MF_01227, CC ECO:0000256|SAAS:SAAS00037321}. CC -!- ENZYME REGULATION: Allosterically activated by GTP, when glutamine CC is the substrate. Inhibited by CTP. {ECO:0000256|HAMAP- CC 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:SAAS00037318}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01227}. CC -!- SIMILARITY: Belongs to the CTP synthase family. CC {ECO:0000256|HAMAP-Rule:MF_01227}. CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain. CC {ECO:0000256|HAMAP-Rule:MF_01227}. CC -!- SIMILARITY: Contains glutamine amidotransferase type-1 domain. CC {ECO:0000256|SAAS:SAAS00037304}. CC -!- SIMILARITY: Contains glutamine amidotransferase type-domain. CC {ECO:0000256|SAAS:SAAS00037304}. 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 EnsemblBacteria; EOM78470; EOM78470; Rrhod_0302. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003883; F:CTP synthase activity; IEA:UniProtKB-HAMAP. 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 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; 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:SAAS00037320}; KW Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00037346}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00037306}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00037369}; KW Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01227, KW ECO:0000256|SAAS:SAAS00037390}. FT DOMAIN 306 554 Glutamine amidotransferase type-1. FT {ECO:0000256|HAMAP-Rule:MF_01227}. FT REGION 1 268 Aminator domain. {ECO:0000256|HAMAP-Rule: FT MF_01227}. FT ACT_SITE 396 396 Nucleophile. {ECO:0000256|HAMAP-Rule: FT MF_01227}. FT ACT_SITE 527 527 {ECO:0000256|HAMAP-Rule:MF_01227}. FT ACT_SITE 529 529 {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 //