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 27-MAR-2024, entry version 120.
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.ENSDARP00000121703; -.
DR iPTMnet; Q6PEI7; -.
DR PaxDb; 7955-ENSDARP00000105255; -.
DR AGR; ZFIN:ZDB-GENE-030131-808; -.
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 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; 3.40.50.880; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR00337; PyrG; 1.
DR PANTHER; PTHR11550; CTP SYNTHASE; 1.
DR PANTHER; PTHR11550:SF0; CTP SYNTHASE-RELATED; 1.
DR Pfam; PF06418; CTP_synth_N; 1.
DR Pfam; PF00117; GATase; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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
//
