CDS1_ENCCU
ID CDS1_ENCCU Reviewed; 393 AA.
AC Q95ZE3;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Phosphatidate cytidylyltransferase;
DE EC=2.7.7.41;
DE AltName: Full=CDP-DAG synthase;
DE AltName: Full=CDP-DG synthase;
DE AltName: Full=CDP-diacylglycerol synthase;
DE Short=CDS;
DE AltName: Full=CDP-diglyceride pyrophosphorylase;
DE AltName: Full=CDP-diglyceride synthase;
DE AltName: Full=CTP:phosphatidate cytidylyltransferase;
GN Name=CDS1; OrderedLocusNames=ECU05_1250;
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=284813;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11560410; DOI=10.1006/expr.2001.4635;
RA El Alaoui H., Bata J., Peyret P., Vivares C.P.;
RT "Encephalitozoon cuniculi (Microspora): characterization of phospholipid
RT metabolic pathway potentially linked to therapeutics.";
RL Exp. Parasitol. 98:171-179(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(2001).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-
CC diacyl-sn-glycerol + diphosphate; Xref=Rhea:RHEA:16229,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563,
CC ChEBI:CHEBI:58332, ChEBI:CHEBI:58608; EC=2.7.7.41;
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CDS family. {ECO:0000305}.
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DR EMBL; AJ310088; CAC51023.1; -; Genomic_DNA.
DR EMBL; AL590445; CAD26645.1; -; Genomic_DNA.
DR RefSeq; NP_597468.1; NM_001041334.1.
DR AlphaFoldDB; Q95ZE3; -.
DR STRING; 284813.Q95ZE3; -.
DR GeneID; 859134; -.
DR KEGG; ecu:ECU05_1250; -.
DR VEuPathDB; MicrosporidiaDB:ECU05_1250; -.
DR HOGENOM; CLU_023471_1_2_1; -.
DR InParanoid; Q95ZE3; -.
DR OrthoDB; 1072976at2759; -.
DR UniPathway; UPA00557; UER00614.
DR Proteomes; UP000000819; Chromosome V.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004605; F:phosphatidate cytidylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR000374; PC_trans.
DR InterPro; IPR016720; PC_Trfase_euk.
DR PANTHER; PTHR13773; PTHR13773; 1.
DR PIRSF; PIRSF018269; PC_trans_euk; 1.
DR PROSITE; PS01315; CDS; 1.
PE 3: Inferred from homology;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Nucleotidyltransferase;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..393
FT /note="Phosphatidate cytidylyltransferase"
FT /id="PRO_0000090721"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 393 AA; 44467 MW; 34794E225A5D3CFC CRC64;
MAEERKDSEE SPGTYSCSKT LRRRGEITPN GKVRYETTQN KAAGITKTNF FRRLVLSIVM
ISGFCWISVN DKIYSFGLII FLTISIIREI IGITRKSDGR PFHLRTSIIL GLAVPIYSYL
VFPSIMMMYF SRVSKCFLRR LSFVCFYSYV AAFMCFVASL RKGRLKPQLG LFALIHLSTY
TMAIAAKCAI FNLNKGRFWF VFPALLVISN DISAYVVGKS IGKRPLYRLS PKKTLEGFIG
AFIFTTAVGF ALGHLHVNSG FLRDADSEQF QKFMKFTVFG ANVRVQSIYI HIIPFIFVAS
FVAPFSGFLA SALKRAYKKK DFGEAISGHG GIADRMDCQV LIAIFASTYI SSFIYTEERS
VGSVFSLICR NFSHDEIMIL IEMLNRRVES IRK