ID   A0A7C3VW67_9RHOB        Unreviewed;       547 AA.
AC   A0A7C3VW67;
DT   02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT   02-DEC-2020, sequence version 1.
DT   19-JAN-2022, 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=ENK28_07920 {ECO:0000313|EMBL:HGG05371.1};
OS   Aliiroseovarius sp.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Aliiroseovarius; unclassified Aliiroseovarius.
OX   NCBI_TaxID=1872442 {ECO:0000313|EMBL:HGG05371.1, ECO:0000313|Proteomes:UP000542975};
RN   [1] {ECO:0000313|EMBL:HGG05371.1, ECO:0000313|Proteomes:UP000542975}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HyVt-562 {ECO:0000313|EMBL:HGG05371.1};
RX   PubMed=31911466;
RA   Zhou Z., Liu Y., Xu W., Pan J., Luo Z.H., Li M.;
RT   "Genome- and Community-Level Interaction Insights into Carbon Utilization
RT   and Element Cycling Functions of Hydrothermarchaeota in Hydrothermal
RT   Sediment.";
RL   mSystems 5:e00795-e00719(2020).
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   -!- 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:HGG05371.1}.
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DR   EMBL; DRPQ01000270; HGG05371.1; -; Genomic_DNA.
DR   UniPathway; UPA00159; UER00277.
DR   Proteomes; UP000542975; 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; 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.
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}.
FT   DOMAIN          3..265
FT                   /note="CTP_synth_N"
FT                   /evidence="ECO:0000259|Pfam:PF06418"
FT   DOMAIN          302..538
FT                   /note="GATase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   NP_BIND         14..19
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   NP_BIND         146..148
FT                   /note="CTP; allosteric inhibitor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   NP_BIND         186..191
FT                   /note="CTP; allosteric inhibitor; alternate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   NP_BIND         186..191
FT                   /note="UTP; alternate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   REGION          1..265
FT                   /note="Amidoligase domain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   REGION          381..384
FT                   /note="L-glutamine binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   ACT_SITE        380
FT                   /note="Nucleophile; for glutamine hydrolysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   ACT_SITE        519
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   ACT_SITE        521
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   METAL           71
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   METAL           139
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   BINDING         13
FT                   /note="CTP; allosteric inhibitor; alternate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   BINDING         13
FT                   /note="UTP; alternate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   BINDING         71
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   BINDING         222
FT                   /note="CTP; allosteric inhibitor; alternate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   BINDING         222
FT                   /note="UTP; alternate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   BINDING         240
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   BINDING         353
FT                   /note="L-glutamine; via carbonyl oxygen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   BINDING         404
FT                   /note="L-glutamine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
FT   BINDING         474
FT                   /note="L-glutamine; via amide nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01227"
SQ   SEQUENCE   547 AA;  60640 MW;  6EE650D83B9242BA CRC64;
     MARYIFITGG VVSSLGKGLT SAALGALLQA RGFSVRLRKL DPYLNVDPGT MSPFEHGEVF
     VTDDGAETDL DLGHYERFTG VSARASDSVS SGRIYSTVLE KERRGDYLGK TIQVIPHVTN
     EIKDFINVGD DEVDFMLCEI GGTVGDIEAL PFFEAIRQFS QDKAPGQCLF MHLTLVPFIA
     AAGELKTKPT QHSVKELRSI GIAPDILVCR SEHEIPEKER AKIAQFCNVR PASVIPAYDL
     KSIYEAPMAY HRVGLDQAVL DAFQISPAPK PDLSRWRDVE DRIHNAEGEV RVAIVGKYTS
     HTDAYKSIAE ALTHGGMANK VRVKAKWVDS EVFENEDPAP YLQGFHAILV PGGFGERGTE
     GKIRAAQFAR ERNIPYLGIC LGMQMAVIEA ARNLAGIDDA GSEEFDHESG KKRFTPVVYH
     LKEWVQGNYT VRRKQSDDKG GTMRLGAYTA ALADGSKVAE VYGATSIEER HRHRYEVDVK
     YREALEKQGL IFSGMSPDGK LPEIVEWQDH PWFIGVQFHP ELKSKPFAPA PLFADFIRAA
     KEVERLV
//