ID A0A1I0XZI0_9RHOB Unreviewed; 241 AA.
AC A0A1I0XZI0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Phosphatidylcholine synthase {ECO:0000256|ARBA:ARBA00015623, ECO:0000256|PIRNR:PIRNR000851};
DE Short=PC synthase {ECO:0000256|PIRNR:PIRNR000851};
DE Short=PCS {ECO:0000256|PIRNR:PIRNR000851};
DE EC=2.7.8.24 {ECO:0000256|ARBA:ARBA00013195, ECO:0000256|PIRNR:PIRNR000851};
DE AltName: Full=CDP-diglyceride-choline O-phosphatidyltransferase {ECO:0000256|ARBA:ARBA00033321, ECO:0000256|PIRNR:PIRNR000851};
GN ORFNames=SAMN05421688_2651 {ECO:0000313|EMBL:SFB06047.1};
OS Poseidonocella pacifica.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Poseidonocella.
OX NCBI_TaxID=871651 {ECO:0000313|EMBL:SFB06047.1, ECO:0000313|Proteomes:UP000198796};
RN [1] {ECO:0000313|EMBL:SFB06047.1, ECO:0000313|Proteomes:UP000198796}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29316 {ECO:0000313|EMBL:SFB06047.1,
RC ECO:0000313|Proteomes:UP000198796};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Condenses choline with CDP-diglyceride to produce
CC phosphatidylcholine and CMP. {ECO:0000256|ARBA:ARBA00037468,
CC ECO:0000256|PIRNR:PIRNR000851}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a CDP-1,2-diacyl-sn-glycerol + choline = a 1,2-diacyl-sn-
CC glycero-3-phosphocholine + CMP + H(+); Xref=Rhea:RHEA:14597,
CC ChEBI:CHEBI:15354, ChEBI:CHEBI:15378, ChEBI:CHEBI:57643,
CC ChEBI:CHEBI:58332, ChEBI:CHEBI:60377; EC=2.7.8.24;
CC Evidence={ECO:0000256|ARBA:ARBA00000958,
CC ECO:0000256|PIRNR:PIRNR000851};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936,
CC ECO:0000256|PIRNR:PIRNR000851};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429, ECO:0000256|PIRNR:PIRNR000851}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004429,
CC ECO:0000256|PIRNR:PIRNR000851}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {ECO:0000256|PIRNR:PIRNR000851}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FOJU01000004; SFB06047.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0XZI0; -.
DR STRING; 871651.SAMN05421688_2651; -.
DR Proteomes; UP000198796; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050520; F:phosphatidylcholine synthase activity; IEA:UniProtKB-EC.
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; IPR026027; PcS.
DR Pfam; PF01066; CDP-OH_P_transf; 1.
DR PIRSF; PIRSF000851; PcS; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519,
KW ECO:0000256|PIRNR:PIRNR000851};
KW Cell membrane {ECO:0000256|PIRNR:PIRNR000851};
KW Lipid biosynthesis {ECO:0000256|PIRNR:PIRNR000851};
KW Lipid metabolism {ECO:0000256|PIRNR:PIRNR000851};
KW Manganese {ECO:0000256|PIRNR:PIRNR000851};
KW Membrane {ECO:0000256|PIRNR:PIRNR000851, ECO:0000256|SAM:Phobius};
KW Phospholipid biosynthesis {ECO:0000256|PIRNR:PIRNR000851};
KW Phospholipid metabolism {ECO:0000256|PIRNR:PIRNR000851};
KW Reference proteome {ECO:0000313|Proteomes:UP000198796};
KW Transferase {ECO:0000256|PIRNR:PIRNR000851};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 43..60
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 72..95
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 133..150
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 156..174
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 212..233
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 241 AA; 27131 MW; 2E584A757E0BDDE0 CRC64;
MLRHDRQMTV VSKALAVHLL TATGAVFAML AMLEAAQEDW AMMYLWLVVA FFVDGIDGPL
ARRYDVKTNA PIFDGVLLDL IIDYLTYVFI PAFALFQSGL LPGWTGWLAI IVITYASAMY
FCDCRMKTKD NSFSGFPGCW NMFVIVMFAV EPNFWVILGL VALLSIAMFL PLKFIHPVRT
ERWRMISLPV ALAWTFFAGW AAWVSFHPES WATWGLVGTS LYLASAGILQ QIVPARRGQR
G
//
