ID   PYRG1_DANRE             Reviewed;         591 AA.
AC   Q6PEI7;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=CTP synthase 1 {ECO:0000305};
DE            EC=6.3.4.2 {ECO:0000250|UniProtKB:P17812};
DE   AltName: Full=CTP synthetase 1;
DE   AltName: Full=UTP--ammonia ligase 1;
GN   Name=ctps1; Synonyms=ctps1a, ctpsa;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-571 AND SER-575, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18307296; DOI=10.1021/pr700667w;
RA   Lemeer S., Pinkse M.W.H., Mohammed S., van Breukelen B., den Hertog J.,
RA   Slijper M., Heck A.J.R.;
RT   "Online automated in vivo zebrafish phosphoproteomics: from large-scale
RT   analysis down to a single embryo.";
RL   J. Proteome Res. 7:1555-1564(2008).
CC   -!- FUNCTION: This enzyme is involved in the de novo synthesis of CTP, a
CC       precursor of DNA, RNA and phospholipids. Catalyzes the ATP-dependent
CC       amination of UTP to CTP with either L-glutamine or ammonia as a source
CC       of nitrogen. {ECO:0000250|UniProtKB:P17812}.
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:P17812};
CC   -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway;
CC       CTP from UDP: step 2/2. {ECO:0000250|UniProtKB:P17812}.
CC   -!- SIMILARITY: Belongs to the CTP synthase family. {ECO:0000305}.
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DR   EMBL; BC058048; AAH58048.1; -; mRNA.
DR   AlphaFoldDB; Q6PEI7; -.
DR   SMR; Q6PEI7; -.
DR   STRING; 7955.ENSDARP00000105255; -.
DR   iPTMnet; Q6PEI7; -.
DR   PaxDb; Q6PEI7; -.
DR   ZFIN; ZDB-GENE-030131-808; ctps1a.
DR   eggNOG; KOG2387; Eukaryota.
DR   InParanoid; Q6PEI7; -.
DR   PhylomeDB; Q6PEI7; -.
DR   Reactome; R-DRE-499943; Interconversion of nucleotide di- and triphosphates.
DR   UniPathway; UPA00159; UER00277.
DR   PRO; PR:Q6PEI7; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0097268; C:cytoophidium; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003883; F:CTP synthase activity; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR   GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006241; P:CTP biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0030903; P:notochord development; IMP:ZFIN.
DR   GO; GO:0019856; P:pyrimidine nucleobase biosynthetic process; IBA:GO_Central.
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   1: Evidence at protein level;
KW   ATP-binding; Glutamine amidotransferase; Ligase; Nucleotide-binding;
KW   Phosphoprotein; Pyrimidine biosynthesis; Reference proteome.
FT   CHAIN           1..591
FT                   /note="CTP synthase 1"
FT                   /id="PRO_0000247029"
FT   DOMAIN          300..554
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"
FT   MOD_RES         571
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18307296"
FT   MOD_RES         575
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18307296"
SQ   SEQUENCE   591 AA;  66595 MW;  64D6527F0D11545D CRC64;
     MKYILVTGGV ISGIGKGIIA SSVGTILKSC GLHVTAIKID PYINIDAGTF SPYEHGEVFV
     LDDGGEVDLD LGNYERFLDI RLTKDNNLTT GKIYQSVINK ERRGDYLGKT VQVVPHITDA
     IQEWVMRQAK IPVDDDDVEP QVCVIELGGT VGDIESMPFV EAFRQFQFKV KRENFCNIHV
     SLVPQPSATG EQKTKPTQNS VRELRGLGLS PDLIMCRCST PLDNSVKEKI SMFCHVEPEQ
     VICVHDVSSI YRVPLLLEDQ GVVGYFCRRL NLPIENRPRK MLAKWKEMSD RSDRLLEQCS
     IALVGKYTKF SDSYASVIKA LEHSALAISH KLEVKYVDSA DLEPSMLQEE PVKYHEAWQK
     LCSSDGILVP GGFGVRGTEG KIQAINWARK QKKPFLGVCL GMQLAVCEFA RNMLDWTDAN
     STEFDPETKH PVVIDMPEHN PGQMGGTMRL GKRRTIFKNK SSILRKLYGD VDYVEERHRH
     RFEVNPELKH HFEEKGFRFV GQDVEGERME VIEMDDHPYF VGVQYHPEFT SRPIKPSPPY
     LGLLLAAAGR LQSYLQKGCR LSPRDAYSDR SGSSSPDLEI ADLKLRSIAQ E