ID Q5D9V9_SCHJA Unreviewed; 212 AA.
AC Q5D9V9;
DT 29-MAR-2005, integrated into UniProtKB/TrEMBL.
DT 29-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=CDP-diacylglycerol--inositol 3-phosphatidyltransferase {ECO:0000256|ARBA:ARBA00013212, ECO:0000256|PIRNR:PIRNR000848};
DE EC=2.7.8.11 {ECO:0000256|ARBA:ARBA00013212, ECO:0000256|PIRNR:PIRNR000848};
OS Schistosoma japonicum (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6182 {ECO:0000313|EMBL:AAW27397.1};
RN [1] {ECO:0000313|EMBL:AAW27397.1}
RP NUCLEOTIDE SEQUENCE.
RA Han Z.;
RT "The full-length cDNA sequences of Schistosoma japonicum genes.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AAW27397.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16617374; DOI=10.1371/journal.ppat.0020029;
RA Liu F., Lu J., Hu W., Wang S.Y., Cui S.J., Chi M., Yan Q., Wang X.R.,
RA Song H.D., Xu X.N., Wang J.J., Zhang X.L., Zhang X., Wang Z.Q., Xue C.L.,
RA Brindley P.J., McManus D.P., Yang P.Y., Feng Z., Chen Z., Han Z.G.;
RT "New perspectives on host-parasite interplay by comparative transcriptomic
RT and proteomic analyses of Schistosoma japonicum.";
RL PLoS Pathog. 2:268-281(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a CDP-1,2-diacyl-sn-glycerol + myo-inositol = a 1,2-diacyl-sn-
CC glycero-3-phospho-(1D-myo-inositol) + CMP + H(+);
CC Xref=Rhea:RHEA:11580, ChEBI:CHEBI:15378, ChEBI:CHEBI:17268,
CC ChEBI:CHEBI:57880, ChEBI:CHEBI:58332, ChEBI:CHEBI:60377; EC=2.7.8.11;
CC Evidence={ECO:0000256|PIRNR:PIRNR000848};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {ECO:0000256|PIRNR:PIRNR000848, ECO:0000256|RuleBase:RU003750}.
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DR EMBL; AY815665; AAW27397.1; -; mRNA.
DR AlphaFoldDB; Q5D9V9; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003881; F:CDP-diacylglycerol-inositol 3-phosphatidyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.1760; -; 1.
DR InterPro; IPR000462; CDP-OH_P_trans.
DR InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
DR InterPro; IPR048254; CDP_ALCOHOL_P_TRANSF_CS.
DR InterPro; IPR014387; CDP_diag_ino_3_P_euk.
DR PANTHER; PTHR15362:SF4; CDP-DIACYLGLYCEROL--INOSITOL 3-PHOSPHATIDYLTRANSFERASE; 1.
DR PANTHER; PTHR15362; PHOSPHATIDYLINOSITOL SYNTHASE; 1.
DR Pfam; PF01066; CDP-OH_P_transf; 1.
DR PIRSF; PIRSF000848; CDP_diag_ino_3_P; 1.
DR PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1.
PE 2: Evidence at transcript level;
KW Lipid biosynthesis {ECO:0000256|PIRNR:PIRNR000848};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|PIRNR:PIRNR000848};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR000848};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209,
KW ECO:0000256|PIRNR:PIRNR000848};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264,
KW ECO:0000256|PIRNR:PIRNR000848};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000848};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 136..158
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 164..182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 212 AA; 24427 MW; 6FEC4BD65F8868B8 CRC64;
MGVFLFVPNI IGYIRIILLF QACYFMRINC ELTLLTYIIS CFLDAVDGYA ARALNQSTKF
GAMLDMIVDR CSTMCLLACL TYFYPSYMLF FQFTMIVDIA SHWLHVHSSI LSGKSSHKSI
NLNDNRFLKL YYTNRVILFL MCAGNELFYT LLYVYHFYPG PKVFSFGLYN LMIYLTAPIA
FLKMSISLIQ LFASCVNMAS LDELERSNNK AN
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