ID   PYRG_ENCCU              Reviewed;         535 AA.
AC   Q8SQI7;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=CTP synthase;
DE            EC=6.3.4.2;
DE   AltName: Full=CTP synthetase;
DE   AltName: Full=UTP--ammonia ligase;
GN   OrderedLocusNames=ECU11_0480;
GN   and
GN   OrderedLocusNames=ECU11_0880;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
CC   -!- FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with
CC       either L-glutamine or ammonia as the source of nitrogen.
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   -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway;
CC       CTP from UDP: step 2/2.
CC   -!- SIMILARITY: Belongs to the CTP synthase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL590450; CAD25958.1; -; Genomic_DNA.
DR   EMBL; AL590450; CAD25998.1; -; Genomic_DNA.
DR   RefSeq; NP_586354.1; NM_001042187.1.
DR   RefSeq; NP_586394.1; NM_001042227.1.
DR   AlphaFoldDB; Q8SQI7; -.
DR   SMR; Q8SQI7; -.
DR   STRING; 284813.Q8SQI7; -.
DR   GeneID; 860007; -.
DR   GeneID; 860047; -.
DR   KEGG; ecu:ECU11_0480; -.
DR   KEGG; ecu:ECU11_0880; -.
DR   VEuPathDB; MicrosporidiaDB:ECU11_0480; -.
DR   VEuPathDB; MicrosporidiaDB:ECU11_0880; -.
DR   HOGENOM; CLU_011675_5_0_1; -.
DR   InParanoid; Q8SQI7; -.
DR   OMA; EFNNAYR; -.
DR   OrthoDB; 810128at2759; -.
DR   UniPathway; UPA00159; UER00277.
DR   Proteomes; UP000000819; Chromosome XI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003883; F:CTP synthase activity; IEA:UniProtKB-EC.
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.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Glutamine amidotransferase; Ligase; Nucleotide-binding;
KW   Pyrimidine biosynthesis; Reference proteome.
FT   CHAIN           1..535
FT                   /note="CTP synthase"
FT                   /id="PRO_0000138277"
FT   DOMAIN          300..535
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        385
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        509
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        511
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   535 AA;  59338 MW;  4137C91625382710 CRC64;
     MKYVIVSGGV ISGVGKGIVS SSIGALLKSR GHVVTHFKID PYLNYNAGRM HPYEHGEVYV
     LDDGHECDMD FGNYERFNGI KLSGANSIPG GRLLHDIVKC EREGSFLGKT LQINPHIIDE
     VIRRIRAVAD TPVESFGGGQ AAVPDVVVVE LGGTVGEYES SIYTEALAKF QYVVGKANCA
     FVSVDYIVEL ETGEQKTKGI QMGCRNFRRF GLNYDIVICR GRREPNMETR RKISTSCWVK
     EENVLGLPNL ESVYLAPMFL EKHGIVEALN RILGLDDKGM DRRMLDIFSM VGRRHRDGVR
     IGIVGKYAPE FDSYTSLVNA LKFSGAHIGV NVEIVWINSE SYSVCDFERC DGVVIPGGFG
     ARGISGKIEA IRHARENGVP LLGICLGYQL SVIEMCRNIL GMSDAFSEEF QPSGKNLVVR
     FISDENGVVD KRLRVGGYGV ELRDGLVKKL YGGVETVRER HRHRFEVAQE KVRGLLQHGV
     RFVGFSSGGK KINVFEVESH PFFVGVQFHP EFNARPDRPH PLITGLVSAS YERSK