PYRG_MYCCC
ID PYRG_MYCCC Reviewed; 99 AA.
AC Q93DW6;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=CTP synthase {ECO:0000250|UniProtKB:P0A7E5};
DE EC=6.3.4.2 {ECO:0000250|UniProtKB:P0A7E5};
DE AltName: Full=Cytidine 5'-triphosphate synthase {ECO:0000250|UniProtKB:P0A7E5};
DE AltName: Full=Cytidine triphosphate synthetase {ECO:0000250|UniProtKB:P0A7E5};
DE Short=CTP synthetase {ECO:0000250|UniProtKB:P0A7E5};
DE Short=CTPS {ECO:0000250|UniProtKB:P0A7E5};
DE AltName: Full=UTP--ammonia ligase {ECO:0000250|UniProtKB:P0A7E5};
DE Flags: Fragment;
GN Name=pyrG {ECO:0000250|UniProtKB:P0A7E5};
OS Mycoplasma capricolum subsp. capripneumoniae.
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=40480;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Gabes;
RX PubMed=11844618; DOI=10.1016/s0378-1135(01)00509-0;
RA Lorenzon S., Wesonga H., Ygesu L., Tekleghiorgis T., Maikano Y., Angaya M.,
RA Hendrikx P., Thiaucourt F.;
RT "Genetic evolution of Mycoplasma capricolum subsp. capripneumoniae strains
RT and molecular epidemiology of contagious caprine pleuropneumonia by
RT sequencing of locus H2.";
RL Vet. Microbiol. 85:111-123(2002).
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:0000250|UniProtKB:P0A7E5}.
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:0000250|UniProtKB:P0A7E5};
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;
CC Evidence={ECO:0000250|UniProtKB:P0A7E5};
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;
CC Evidence={ECO:0000250|UniProtKB:P0A7E5};
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.
CC {ECO:0000250|UniProtKB:P0A7E5}.
CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway;
CC CTP from UDP: step 2/2. {ECO:0000250|UniProtKB:P0A7E5}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P0A7E5}.
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:0000250|UniProtKB:P0A7E5}.
CC -!- SIMILARITY: Belongs to the CTP synthase family. {ECO:0000305}.
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DR EMBL; AF378157; AAK96434.1; -; Genomic_DNA.
DR AlphaFoldDB; Q93DW6; -.
DR SMR; Q93DW6; -.
DR STRING; 40480.BVA24_00695; -.
DR UniPathway; UPA00159; UER00277.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003883; F:CTP synthase activity; IEA:UniProtKB-EC.
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-KW.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR004468; CTP_synthase.
DR InterPro; IPR017926; GATASE.
DR PANTHER; PTHR11550; PTHR11550; 1.
DR Pfam; PF00117; GATase; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW ATP-binding; Glutamine amidotransferase; Ligase; Magnesium; Metal-binding;
KW Nucleotide-binding; Pyrimidine biosynthesis.
FT CHAIN <1..99
FT /note="CTP synthase"
FT /id="PRO_0000138200"
FT DOMAIN <1..99
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 73
FT /evidence="ECO:0000250|UniProtKB:P0A7E5"
FT ACT_SITE 75
FT /evidence="ECO:0000250|UniProtKB:P0A7E5"
FT BINDING 28
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P0A7E5"
FT NON_TER 1
SQ SEQUENCE 99 AA; 11635 MW; F6F0BB50FB084F0D CRC64;
TMVTKLEKDS LVSKLYNSDV ALERHRHRYE FNNKYKKDLE SVGLRFSGIY EEKNLVEVIE
IPSLKFFVAS QFHPEFTSRP NKPTPLFKGF IKAIIENNK
