ID Q04D47_OENOB Unreviewed; 544 AA.
AC Q04D47;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 120.
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 OrderedLocusNames=OEOE_1786 {ECO:0000313|EMBL:ABJ57625.1};
OS Oenococcus oeni (strain ATCC BAA-331 / PSU-1).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Oenococcus.
OX NCBI_TaxID=203123 {ECO:0000313|EMBL:ABJ57625.1, ECO:0000313|Proteomes:UP000000774};
RN [1] {ECO:0000313|EMBL:ABJ57625.1, ECO:0000313|Proteomes:UP000000774}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-331 / PSU-1 {ECO:0000313|Proteomes:UP000000774};
RX PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA Makarova K., Slesarev A., Wolf Y., Sorokin A., Mirkin B., Koonin E.,
RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA Baldwin K., Lee J.H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J., Hutkins R.,
RA O'Sullivan D., Steele J., Unlu G., Saier M., Klaenhammer T., Richardson P.,
RA Kozyavkin S., Weimer B., Mills D.;
RT "Comparative genomics of the lactic acid bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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:
CC Reaction=ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-
CC glutamate + phosphate; Xref=Rhea:RHEA:26426, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:37563, ChEBI:CHEBI:43474, ChEBI:CHEBI:46398,
CC ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.4.2;
CC Evidence={ECO:0000256|ARBA:ARBA00000314, ECO:0000256|HAMAP-
CC Rule:MF_01227};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + NH4(+) + UTP = ADP + CTP + 2 H(+) + phosphate;
CC Xref=Rhea:RHEA:16597, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:37563, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:46398, ChEBI:CHEBI:456216; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01227};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamine = L-glutamate + NH4(+);
CC Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01227};
CC -!- ACTIVITY REGULATION: Allosterically activated by GTP, when glutamine is
CC the substrate; GTP has no effect on the reaction when ammonia is the
CC substrate. The allosteric effector GTP functions by stabilizing the
CC protein conformation that binds the tetrahedral intermediate(s) formed
CC during glutamine hydrolysis. Inhibited by the product CTP, via
CC allosteric rather than competitive inhibition. {ECO:0000256|HAMAP-
CC Rule:MF_01227}.
CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway;
CC CTP from UDP: step 2/2. {ECO:0000256|ARBA:ARBA00005171,
CC ECO:0000256|HAMAP-Rule:MF_01227}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01227}.
CC -!- MISCELLANEOUS: CTPSs have evolved a hybrid strategy for distinguishing
CC between UTP and CTP. The overlapping regions of the product feedback
CC inhibitory and substrate sites recognize a common feature in both
CC compounds, the triphosphate moiety. To differentiate isosteric
CC substrate and product pyrimidine rings, an additional pocket far from
CC the expected kinase/ligase catalytic site, specifically recognizes the
CC cytosine and ribose portions of the product inhibitor.
CC {ECO:0000256|HAMAP-Rule:MF_01227}.
CC -!- SIMILARITY: Belongs to the CTP synthase family.
CC {ECO:0000256|ARBA:ARBA00007533, ECO:0000256|HAMAP-Rule:MF_01227}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01227}.
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DR EMBL; CP000411; ABJ57625.1; -; Genomic_DNA.
DR RefSeq; WP_002821425.1; NC_008528.1.
DR AlphaFoldDB; Q04D47; -.
DR STRING; 203123.OEOE_1786; -.
DR MEROPS; C26.964; -.
DR KEGG; ooe:OEOE_1786; -.
DR PATRIC; fig|203123.7.peg.1827; -.
DR eggNOG; COG0504; Bacteria.
DR HOGENOM; CLU_011675_5_0_9; -.
DR UniPathway; UPA00159; UER00277.
DR Proteomes; UP000000774; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003883; F:CTP synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004359; F:glutaminase activity; IEA:RHEA.
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-UniRule.
DR CDD; cd03113; CTPS_N; 1.
DR CDD; cd01746; GATase1_CTP_Synthase; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR00337; PyrG; 1.
DR PANTHER; PTHR11550; CTP SYNTHASE; 1.
DR PANTHER; PTHR11550:SF0; CTP SYNTHASE-RELATED; 1.
DR Pfam; PF06418; CTP_synth_N; 1.
DR Pfam; PF00117; GATase; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01227};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW ECO:0000256|HAMAP-Rule:MF_01227};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01227};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01227};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01227};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01227};
KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975, ECO:0000256|HAMAP-
KW Rule:MF_01227}; Reference proteome {ECO:0000313|Proteomes:UP000000774}.
FT DOMAIN 8..272
FT /note="CTP synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06418"
FT DOMAIN 308..533
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT REGION 1..272
FT /note="Amidoligase domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT ACT_SITE 387
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 387
FT /note="Nucleophile; for glutamine hydrolysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT ACT_SITE 514
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 516
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT BINDING 18
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT BINDING 18
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT BINDING 19..24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT BINDING 59
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT BINDING 76
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT BINDING 76
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT BINDING 146
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT BINDING 153..155
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT BINDING 193..198
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT BINDING 193..198
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT BINDING 229
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT BINDING 229
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT BINDING 360
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT BINDING 388..391
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT BINDING 411
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT BINDING 469
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
SQ SEQUENCE 544 AA; 60106 MW; 6640FEE491720D80 CRC64;
MTDKKQTKYI FVTGGVVSSL GKGIVAASLG RLLKSRGLAV TVQKFDPYLN PDPGTMSPYQ
HGETFVTQDG VETDLDLGHY ERFMDINTNK YSNVTSGKIY QEVIDRERTG DYMGRTVQVI
PHVTDAIKDK IFRGAKESEA DVIITEIGGT IGDIESMAFI EAIRQMKKEV GSDNTFYIHV
SLVPFLRAAG ELKTKPTQHS VHELRGMGIQ PDMIVVRSEK AITDSMKEKL SEFTDVPTEA
IIQSIDSDVL YSVPLNLAAQ NMDQVVLEKL GLGSQPKANL SQWGALVDRI RHLSKEIKIA
LVGKYTDLPD AYISVHEALK HAGYAVDSKI TLKSINSEML TDNNVAEKLA GIDGVIVPGG
FGPRGIEGMI SAIKYARENN IPFFGVCLGM QMASVEFARD AVGMSNANST EMNPDTPYPV
VGLMDSQKKI TKIGGTMRLG SYPAILKAGT KTAEAYNNVS EISERHRHRY EFNNDYREQF
EKAGMVFAGT SPDNSLVEII EYPQNDFFIA VQYHPEFLSR PDRPEGLYAA FIQAALAYEE
KLKD
//
