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Database: UniProt
Entry: Q9ZQW1_WHEAT
LinkDB: Q9ZQW1_WHEAT
Original site: Q9ZQW1_WHEAT 
ID   Q9ZQW1_WHEAT            Unreviewed;       239 AA.
AC   Q9ZQW1;
DT   01-MAY-1999, integrated into UniProtKB/TrEMBL.
DT   01-MAY-1999, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=CDP-diacylglycerol--serine O-phosphatidyltransferase {ECO:0000256|ARBA:ARBA00017171};
DE            EC=2.7.8.8 {ECO:0000256|ARBA:ARBA00013174};
DE   AltName: Full=Phosphatidylserine synthase {ECO:0000256|ARBA:ARBA00032361};
GN   Name=pS232 {ECO:0000313|EMBL:AAD10497.1};
OS   Triticum aestivum (Wheat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4565 {ECO:0000313|EMBL:AAD10497.1};
RN   [1] {ECO:0000313|EMBL:AAD10497.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ET3 {ECO:0000313|EMBL:AAD10497.1};
RX   PubMed=10066765; DOI=10.1074/jbc.274.11.7082;
RA   Delhaize E., Hebb D.M., Richards K.D., Lin J.M., Ryan P.R., Gardner R.C.;
RT   "Cloning and expression of a wheat (Triticum aestivum L.)
RT   phosphatidylserine synthase cDNA. Overexpression in plants alters the
RT   composition of phospholipids.";
RL   J. Biol. Chem. 274:7082-7088(1999).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a CDP-1,2-diacyl-sn-glycerol + L-serine = a 1,2-diacyl-sn-
CC         glycero-3-phospho-L-serine + CMP + H(+); Xref=Rhea:RHEA:16913,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:33384, ChEBI:CHEBI:57262,
CC         ChEBI:CHEBI:58332, ChEBI:CHEBI:60377; EC=2.7.8.8;
CC         Evidence={ECO:0000256|ARBA:ARBA00000287};
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|RuleBase:RU003750}.
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DR   EMBL; U91983; AAD10497.1; -; mRNA.
DR   AlphaFoldDB; Q9ZQW1; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IEA:InterPro.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.120.1760; -; 1.
DR   InterPro; IPR004533; CDP-diaglyc--ser_O-PTrfase.
DR   InterPro; IPR016271; CDP-diaglyc--ser_O-PTrfase_fun.
DR   InterPro; IPR000462; CDP-OH_P_trans.
DR   InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
DR   InterPro; IPR048254; CDP_ALCOHOL_P_TRANSF_CS.
DR   NCBIfam; TIGR00473; pssA; 1.
DR   PANTHER; PTHR14269; CDP-DIACYLGLYCEROL--GLYCEROL-3-PHOSPHATE 3-PHOSPHATIDYLTRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR14269:SF61; CDP-DIACYLGLYCEROL--SERINE O-PHOSPHATIDYLTRANSFERASE; 1.
DR   Pfam; PF01066; CDP-OH_P_transf; 1.
DR   PIRSF; PIRSF000852; Phosphatidylserine_synth_fun; 1.
DR   PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1.
PE   2: Evidence at transcript level;
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW   Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003750};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        47..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        76..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        114..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        142..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        176..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   239 AA;  26181 MW;  9256990FC465B2F4 CRC64;
     MSKRATRSVS GGLDKEPRLP TSQKQKTLLS ADVGHFSLVR ALHMADLITL MNGFCGVMSV
     FSSLRYCLGA PDNHSNVWLA LYFLPFGLFF DFFDGKVARW RNKSSLMGQE LDSLADLISF
     GVAPAMVAFS IGLRTFADTV GLTFFVLCGL TRLARFNVTV AVLPKDATGK SKYFEGTPIP
     TSLVLDGVMA YWVYNGLILD NVPFGVLAEG TMLEVHPAVL LFMIHGCLMT SKTIRIPKP
//
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