ID   PCY1_PLAFK              Reviewed;         370 AA.
AC   P49587;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Choline-phosphate cytidylyltransferase;
DE            EC=2.7.7.15;
DE   AltName: Full=CTP:phosphocholine cytidylyltransferase;
DE            Short=CCT;
DE            Short=CT;
DE   AltName: Full=Phosphorylcholine transferase;
GN   Name=CTP;
OS   Plasmodium falciparum (isolate K1 / Thailand).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=5839;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7588775; DOI=10.1111/j.1432-1033.1995.062_1.x;
RA   Yeo H.-J., Sri Widada J., Mercereau-Puijalon O., Vial H.J.;
RT   "Molecular cloning of CTP:phosphocholine cytidylyltransferase from
RT   Plasmodium falciparum.";
RL   Eur. J. Biochem. 233:62-72(1995).
CC   -!- FUNCTION: Controls phosphatidylcholine synthesis.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CTP + H(+) + phosphocholine = CDP-choline + diphosphate;
CC         Xref=Rhea:RHEA:18997, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:37563, ChEBI:CHEBI:58779, ChEBI:CHEBI:295975;
CC         EC=2.7.7.15;
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis;
CC       phosphatidylcholine from phosphocholine: step 1/2.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the asexual intraerythrocytic stages.
CC   -!- SIMILARITY: Belongs to the cytidylyltransferase family. {ECO:0000305}.
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DR   EMBL; X84041; CAA58860.1; -; Genomic_DNA.
DR   PIR; S68187; S68187.
DR   AlphaFoldDB; P49587; -.
DR   SMR; P49587; -.
DR   PRIDE; P49587; -.
DR   BRENDA; 2.7.7.15; 4889.
DR   UniPathway; UPA00753; UER00739.
DR   GO; GO:0004105; F:choline-phosphate cytidylyltransferase activity; IEA:UniProtKB-EC.
DR   CDD; cd02174; CCT; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   InterPro; IPR041723; CCT.
DR   InterPro; IPR004821; Cyt_trans-like.
DR   InterPro; IPR045049; Pcy1-like.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR10739; PTHR10739; 1.
DR   Pfam; PF01467; CTP_transf_like; 1.
DR   TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
PE   2: Evidence at transcript level;
KW   Lipid biosynthesis; Lipid metabolism; Nucleotidyltransferase;
KW   Phospholipid biosynthesis; Phospholipid metabolism; Transferase.
FT   CHAIN           1..370
FT                   /note="Choline-phosphate cytidylyltransferase"
FT                   /id="PRO_0000208459"
FT   REGION          17..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..44
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..73
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         99..107
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000250"
FT   BINDING         137
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000250"
FT   BINDING         137
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         166
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         183..184
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000250"
FT   BINDING         188
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000250"
FT   BINDING         229..233
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   370 AA;  42630 MW;  B2E457D09B0B6FB6 CRC64;
     MDSSNYFHDC KTMLSEHNES IESSNNDING KQKEHIKKGN SENQDVDPDT NPDAVPDDDD
     DDDDNSNDES EYESSQMDSE KNKGSIKNSK NVVIYADGVY DMLHLGHMKQ LEQAKKLFEN
     TTLIVGVTSD NETKLFKGQV VQTLEERTET LKHIRWVDEI ISPCPWVVTP EFLEKYKIDY
     VAHDDIPYAN NQKKKKKKKS KGKSFSFDEE NEDIYAWLKR AGKFKATQRT EGVSTTDLIV
     RILKNYEDYI ERSLQRGIHP NELNIGVTKA QSIKMKKNLI RWGEKVTDEL TKVTLTDKPL
     GTDFDQGVEN LQVKFKELFK IWKNASNKLI TDFTRKLEAT SYLTSIQNII DYEIENDDYA
     SSNFDDETSS