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PYRG_RHILO
ID   PYRG_RHILO              Reviewed;         542 AA.
AC   Q98MF0;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=CTP synthase {ECO:0000255|HAMAP-Rule:MF_01227};
DE            EC=6.3.4.2 {ECO:0000255|HAMAP-Rule:MF_01227};
DE   AltName: Full=Cytidine 5'-triphosphate synthase {ECO:0000255|HAMAP-Rule:MF_01227};
DE   AltName: Full=Cytidine triphosphate synthetase {ECO:0000255|HAMAP-Rule:MF_01227};
DE            Short=CTP synthetase {ECO:0000255|HAMAP-Rule:MF_01227};
DE            Short=CTPS {ECO:0000255|HAMAP-Rule:MF_01227};
DE   AltName: Full=UTP--ammonia ligase {ECO:0000255|HAMAP-Rule:MF_01227};
GN   Name=pyrG {ECO:0000255|HAMAP-Rule:MF_01227}; OrderedLocusNames=mll0606;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(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:0000255|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:0000255|HAMAP-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:0000255|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:0000255|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:0000255|HAMAP-
CC       Rule:MF_01227}.
CC   -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway;
CC       CTP from UDP: step 2/2. {ECO:0000255|HAMAP-Rule:MF_01227}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01227}.
CC   -!- SIMILARITY: Belongs to the CTP synthase family. {ECO:0000255|HAMAP-
CC       Rule:MF_01227}.
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DR   EMBL; BA000012; BAB48163.1; -; Genomic_DNA.
DR   RefSeq; WP_010909518.1; NC_002678.2.
DR   AlphaFoldDB; Q98MF0; -.
DR   SMR; Q98MF0; -.
DR   STRING; 266835.14021551; -.
DR   MEROPS; C26.964; -.
DR   EnsemblBacteria; BAB48163; BAB48163; BAB48163.
DR   GeneID; 66684015; -.
DR   KEGG; mlo:mll0606; -.
DR   eggNOG; COG0504; Bacteria.
DR   HOGENOM; CLU_011675_5_0_5; -.
DR   OMA; EFNNAYR; -.
DR   UniPathway; UPA00159; UER00277.
DR   Proteomes; UP000000552; 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-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   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; Glutamine amidotransferase; Ligase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Pyrimidine biosynthesis.
FT   CHAIN           1..542
FT                   /note="CTP synthase"
FT                   /id="PRO_0000138214"
FT   DOMAIN          291..541
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   REGION          1..265
FT                   /note="Amidoligase domain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   ACT_SITE        380
FT                   /note="Nucleophile; for glutamine hydrolysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   ACT_SITE        514
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   ACT_SITE        516
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   BINDING         13
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /ligand_note="allosteric inhibitor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   BINDING         13
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   BINDING         14..19
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   BINDING         54
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   BINDING         71
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   BINDING         71
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   BINDING         139
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   BINDING         146..148
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /ligand_note="allosteric inhibitor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   BINDING         186..191
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /ligand_note="allosteric inhibitor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   BINDING         186..191
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   BINDING         222
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /ligand_note="allosteric inhibitor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   BINDING         222
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   BINDING         353
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   BINDING         381..384
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   BINDING         404
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT   BINDING         469
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
SQ   SEQUENCE   542 AA;  60164 MW;  A90E195E953AA552 CRC64;
     MARYVFITGG VVSSLGKGIA AAALGALLQA RGYRARIKKL DPYLNVDPGT MSPYQHGEVF
     VTDDGAETDL DLGHYERFTG RSANQQDNIT TGRIYKNIIE RERRGDYLGA TVQVIPHVTD
     EIKNFVLNGN DDYDFVLCEI GGTVGDIEAM PFLEAIRQLG NDLPRNNAVY VHLTLMPYIP
     TAGELKTKPT QHSVKELRGI GIAPDILLVR ADRAIPKEER RKLSLFCNVR ESAVIQALDV
     PHIYDVPMAY HKEGLDSEVL AAFGIDPAPK PRMEPWQKVS DRIHSPEGEV TIAIVGKYTG
     LKDAYKSLIE ALSHGGLANH VKVKLDWIES EIFEKEDPTP WLEKVHGILV PGGFGERGSE
     GKILAAKFAR ERKVPYFGIC FGMQMACIEA ARSLAGVEHA SSTEFGPTEE PVVGLMTEWL
     KGNMLEKRRE TGDLGGTMRL GAYQADLAKG SKIAEIYGDT QISERHRHRY EVNIDYKERL
     EDCGLVFAGM SPDGVLPETV EYPDHPWFIG VQYHPELKSR PLDPHPLFAS FIEAAVEQSR
     LV
 
 
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