ID   PYRG2_XENLA             Reviewed;         578 AA.
AC   Q6GME1;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=CTP synthase 2;
DE            EC=6.3.4.2;
DE   AltName: Full=CTP synthetase 2;
DE   AltName: Full=UTP--ammonia ligase 2;
GN   Name=ctps2;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with
CC       either L-glutamine or ammonia as the source of nitrogen. Constitutes
CC       the rate-limiting enzyme in the synthesis of cytosine nucleotides (By
CC       similarity). {ECO:0000250}.
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}.
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DR   EMBL; BC074125; AAH74125.1; -; mRNA.
DR   RefSeq; NP_001086048.1; NM_001092579.1.
DR   AlphaFoldDB; Q6GME1; -.
DR   SMR; Q6GME1; -.
DR   GeneID; 444477; -.
DR   KEGG; xla:444477; -.
DR   CTD; 444477; -.
DR   Xenbase; XB-GENE-991295; ctps2.L.
DR   OrthoDB; 810128at2759; -.
DR   UniPathway; UPA00159; UER00277.
DR   Proteomes; UP000186698; Chromosome 2L.
DR   Bgee; 444477; Expressed in muscle tissue and 19 other tissues.
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   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   2: Evidence at transcript level;
KW   ATP-binding; Glutamine amidotransferase; Ligase; Nucleotide-binding;
KW   Pyrimidine biosynthesis; Reference proteome.
FT   CHAIN           1..578
FT                   /note="CTP synthase 2"
FT                   /id="PRO_0000247037"
FT   DOMAIN          300..553
FT                   /note="Glutamine amidotransferase type-1"
FT   ACT_SITE        399
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        526
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        528
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   578 AA;  65119 MW;  33EBB77299DE2168 CRC64;
     MKYILVTGGV ISGVGKGIIA SSIGTILKSC GLRVTAIKID PYINIDAGTF SPYEHGEVFV
     LNDGGEVDLD LGNYERFLDI NLYKDNNITT GKIYQQVINR ERRGDYLGKT VQVVPHITDA
     IQEWVLNQAK VPVDRDQKEP QICVIELGGT IGDIEGMPFI EAFRQFQFKA KRENFCNIHV
     SLVPQPSATG EQKTKPTQNS VRALRGLGLS PDLIVCRSAK PIEMAVKQKI SMFCHVEPEQ
     VIFVHDVSST YRVPILLQEQ GIIKYFKQRL SIPIEDQPST QLFKWKRMAD RYERLLKTCS
     IALVGKYTKL SDCYTSVFKA LEHSALAINH KLNLMYIDSA DLEPSMKAQD PVKYHKAWEE
     LCKAEGILVP GGFGLRGTEG KIQAITWARE RKIPFLGICL GMQLAVVEFA RNILKMTDAN
     STEFDPNTKN PAVIDMPEHH PGDMGGTMRL GSRKTVFKTS ESVVKKLYDN QDFVEERHRH
     RYEVNPELVQ QFEEKGLKFV GQDNEGQRME IIELEGHPYF VGVQFHPEFC SRPMKPSPPY
     LGFMLAASGK LNTYVQNGCK LSPRNSYSEH SDESSSDS