PYRG_UREPA
ID PYRG_UREPA Reviewed; 542 AA.
AC Q9PQK7;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Putative CTP synthase {ECO:0000250|UniProtKB:P0A7E5, ECO:0000305};
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};
GN Name=pyrG {ECO:0000250|UniProtKB:P0A7E5}; OrderedLocusNames=UU284;
OS Ureaplasma parvum serovar 3 (strain ATCC 700970).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX NCBI_TaxID=273119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700970;
RX PubMed=11048724; DOI=10.1038/35037619;
RA Glass J.I., Lefkowitz E.J., Glass J.S., Heiner C.R., Chen E.Y.,
RA Cassell G.H.;
RT "The complete sequence of the mucosal pathogen Ureaplasma urealyticum.";
RL Nature 407:757-762(2000).
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}.
CC -!- CAUTION: Lacks the conserved cysteine and histidine residues
CC potentially involved in the active site of the GAT domain.
CC {ECO:0000305}.
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DR EMBL; AF222894; AAF30693.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9PQK7; -.
DR SMR; Q9PQK7; -.
DR STRING; 273119.UU284; -.
DR EnsemblBacteria; AAF30693; AAF30693; UU284.
DR KEGG; uur:UU284; -.
DR eggNOG; COG0504; Bacteria.
DR HOGENOM; CLU_011675_5_0_14; -.
DR OMA; EFNNAYR; -.
DR UniPathway; UPA00159; UER00277.
DR Proteomes; UP000000423; Chromosome.
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 CDD; cd03113; CTPS_N; 1.
DR CDD; cd01746; GATase1_CTP_Synthase; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.40.50.880; -; 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.
PE 3: Inferred from homology;
KW ATP-binding; Glutamine amidotransferase; Ligase; Magnesium; Metal-binding;
KW Nucleotide-binding; Pyrimidine biosynthesis; Reference proteome.
FT CHAIN 1..542
FT /note="Putative CTP synthase"
FT /id="PRO_0000138245"
FT DOMAIN 310..542
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000250|UniProtKB:P0A7E5"
FT REGION 1..277
FT /note="Amidoligase domain"
FT /evidence="ECO:0000250|UniProtKB:P0A7E5"
FT ACT_SITE 517
FT /evidence="ECO:0000250|UniProtKB:P0A7E5"
FT BINDING 23
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000250|UniProtKB:P0A7E5"
FT BINDING 23
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:P0A7E5"
FT BINDING 24..29
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P0A7E5"
FT BINDING 81
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P0A7E5"
FT BINDING 81
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0A7E5"
FT BINDING 151
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0A7E5"
FT BINDING 158..160
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000250|UniProtKB:P0A7E5"
FT BINDING 198..203
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000250|UniProtKB:P0A7E5"
FT BINDING 198..203
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:P0A7E5"
FT BINDING 234
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000250|UniProtKB:P0A7E5"
FT BINDING 234
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:P0A7E5"
SQ SEQUENCE 542 AA; 61347 MW; 155F079EFD8C73B4 CRC64;
MEIDLMKHIQ KTKFIFVTGG VYSSLGKGVS ASSIGRILVE LGYSVAMQKL DPYLNIDPTY
LSPLQHGEVF VTKDGKEADL DLGTYERFIN ADLNKYASVT SGKIYYEILT KERENGFDGK
TVQTIPHVTS AVIDYIKKIK DSLKTDFIIV EIGGTIGDIE SLPFIEAISQ FKTIYGVNNV
MFIHCSPLIY IEKVGELKTK PTQHSVKTLR SLGINLDLLL LRTNQKLDEV TIKKLAWSCG
LDIDMIFAAY DVESVYLLPN VLFEQGIHKT ILDFFSLPLK NDNINSWIDF TDKITTFKKH
NLVIGLVGKY VELPDAYKSV LASLELAAIE LNIDLKIKYI QPQNLNENNI NEELKKINGI
VIPSIAGSIK GWPGALLAAS YARKNNIPFL AVGTGVNIGI GEFINNVLKL PIEFINLGNG
DFSFLKDAFV KNEIENYRIG EYCSNIQANT ITSQIYLKQN QLNERHRHHF EFNNHYINNY
FLNQNWKIGA ISVDNNYIDV LEYTKNHFYV LTIFNPEYTS KPSKANPYFI NLLKMSLKIK
ES
