PYRG1_CRIGR
ID PYRG1_CRIGR Reviewed; 447 AA.
AC P50547;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 97.
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;
DE Flags: Fragment;
GN Name=CTPS1;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung;
RX PubMed=7657337;
RA Zhai C., Skaanild M.T., Chu E.H.;
RT "Cloning and sequencing of CTP synthetase cDNA from Chinese hamster
RT cells.";
RL Hua Xi Yi Ke Da Xue Xue Bao 26:45-49(1995).
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. This enzyme and its product, CTP, play a crucial role in
CC the proliferation of activated lymphocytes and therefore in immunity.
CC {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 -!- ACTIVITY REGULATION: Activated by GTP and inhibited by CTP.
CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway;
CC CTP from UDP: step 2/2. {ECO:0000250|UniProtKB:P17812}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P70698}. Note=Mainly cytosolic but when active
CC detected in long filamentous structures (By similarity). Co-localizes
CC with TNK2 in the cytosolic filaments (By similarity).
CC {ECO:0000250|UniProtKB:P17812, ECO:0000250|UniProtKB:P70698}.
CC -!- SIMILARITY: Belongs to the CTP synthase family. {ECO:0000305}.
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DR EMBL; S79193; AAB35189.2; -; mRNA.
DR EMBL; L29453; AAA36969.1; -; mRNA.
DR AlphaFoldDB; P50547; -.
DR SMR; P50547; -.
DR STRING; 10029.XP_007618857.1; -.
DR eggNOG; KOG2387; Eukaryota.
DR UniPathway; UPA00159; UER00277.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003883; F:CTP synthase activity; ISS:UniProtKB.
DR GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0042100; P:B cell proliferation; ISS:UniProtKB.
DR GO; GO:0006241; P:CTP biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0042098; P:T cell proliferation; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Cytoplasm; Glutamine amidotransferase; Immunity;
KW Ligase; Nucleotide-binding; Pyrimidine biosynthesis.
FT CHAIN <1..>447
FT /note="CTP synthase 1"
FT /id="PRO_0000138274"
FT DOMAIN 261..>447
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 360
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT MOD_RES 61
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P17812"
FT NON_TER 1
FT NON_TER 447
SQ SEQUENCE 447 AA; 50744 MW; 166072828D3DFBE5 CRC64;
DPYINIDAGT FSPYEHGEVF VLDDGGEVDL DLGNYERFLD IRLTKDNNLT TGKIYQYVIN
KERKGDYLGK TVHVVPHITD AIQRWVMRQA LIPVDEDGLE PQVCVIELGG TVGDIESMPF
IEAFRQFQFK VKRENFCNIH VSLVPQPSST GEQKTKPTQN SVRELRGLGL SPDLVVCRCS
NPLDTSVKEK ISMFCHVEPE QVICVHDVSS IYRVPLLLEE QGVVDYFLRS LELPIERQSR
KMLMKWKEMA DRYDRLLETC SIALVGKYTK LSDSYASVIK ALEHSALAIN HKLEIKYIDS
TDLEPSTLQE EPVRYHEAWQ KLCSAHGVLV PGGFGVRGTE GKIQAIAWAR KQKKPFLGVC
LGMQLAVVEF SRNVLGWQDA NSTEFDPKTS HPVVIDMPEH NPGQMGGTMR LGKSRTLFQT
KNSVMSKLYG DTDYLEERHR HRFEVNP