ID A0A1J4NHT8_9GAMM Unreviewed; 546 AA. AC A0A1J4NHT8; DT 15-FEB-2017, integrated into UniProtKB/TrEMBL. DT 15-FEB-2017, sequence version 1. DT 27-SEP-2017, entry version 6. 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 ORFNames=BK820_02695 {ECO:0000313|EMBL:OIJ38842.1}; OS Acinetobacter sp. LCT-H3. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=1914307 {ECO:0000313|EMBL:OIJ38842.1, ECO:0000313|Proteomes:UP000186913}; RN [1] {ECO:0000313|EMBL:OIJ38842.1, ECO:0000313|Proteomes:UP000186913} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LCT-H3 {ECO:0000313|EMBL:OIJ38842.1, RC ECO:0000313|Proteomes:UP000186913}; RA Huang B.; RT "Draft genome sequence of strain LCT isolated from the Shenzhou X RT spacecraft of China."; RL Submitted (OCT-2016) 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: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:OIJ38842.1}. 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; MODX01000003; OIJ38842.1; -; Genomic_DNA. DR RefSeq; WP_071320020.1; NZ_MODX01000003.1. DR UniPathway; UPA00159; UER00277. DR Proteomes; UP000186913; Unassembled WGS sequence. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003883; F:CTP synthase activity; IEA:UniProtKB-UniRule. 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:UP000186913}; 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}. FT DOMAIN 292 544 Glutamine amidotransferase type-1. FT {ECO:0000259|PROSITE:PS51273}. FT NP_BIND 14 19 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 382 385 L-glutamine binding. {ECO:0000256|HAMAP- FT Rule:MF_01227}. FT ACT_SITE 381 381 Nucleophile; for glutamine hydrolysis. FT {ECO:0000256|HAMAP-Rule:MF_01227}. FT ACT_SITE 517 517 {ECO:0000256|HAMAP-Rule:MF_01227}. FT ACT_SITE 519 519 {ECO:0000256|HAMAP-Rule:MF_01227}. FT METAL 71 71 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01227}. FT METAL 140 140 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01227}. FT BINDING 13 13 Allosteric inhibitor CTP; alternate. FT {ECO:0000256|HAMAP-Rule:MF_01227}. FT BINDING 13 13 UTP; alternate. {ECO:0000256|HAMAP-Rule: FT MF_01227}. FT BINDING 71 71 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 354 354 L-glutamine; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_01227}. FT BINDING 405 405 L-glutamine. {ECO:0000256|HAMAP-Rule: FT MF_01227}. FT BINDING 472 472 L-glutamine; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01227}. SQ SEQUENCE 546 AA; 60862 MW; 5379150A85318374 CRC64; MTHFIFVTGG VVSSLGKGIS AASVAALLEA RGLKVTMVKM DPYINVDPGT MSPFQHGEVF VTEDGAETDL DLGYYERFLR RAKMTKLNNF TSGRVYQDVL NKERRGDYLG GTVQVIPHIT DNIKERVLRA GEGYDVAIVE IGGTVGDIES LPFMESVRQL MVELGHKRTM LMHLTLLPYI KSAAELKTKP TQHSVKELLS IGIQPDILIC RTEHDVDADT TRKIALFTNV EARAVVVCKD ARTIYQIPRT FYEQNVDDLI CERFGYNDLP EADLTDWDNV VEALLNPEYT VRVAMVGKYV ELPDAYKSVN EALLHAGIQN RVKVQIDYVN AEELESQDVS EVLKDADAIL VPGGFGERGT EGKMQAIKYA RENGVPFLGI CLGMQLAVIE YARNVAGIAD ATSTEFNRST KSPLIGLITE WLDERGEVQQ RSVDSDLGGT MRLGAQKSEL VPGTKTAAVY GSDEIIERHR HRYEMNNRYI PVLEEKGMKI SGYSPVQHLV ETVEIPEHPW FIAVQFHPEF TSSPRDGHPL FAGFIDAAKK KHQKAQ //