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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
 
 
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