ID A1B079_PARDP Unreviewed; 230 AA.
AC A1B079;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 89.
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 OrderedLocusNames=Pden_0811 {ECO:0000313|EMBL:ABL68923.1};
OS Paracoccus denitrificans (strain Pd 1222).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL68923.1, ECO:0000313|Proteomes:UP000000361};
RN [1] {ECO:0000313|Proteomes:UP000000361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA Richardson P.;
RT "Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222.";
RL Submitted (DEC-2006) 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}.
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DR EMBL; CP000489; ABL68923.1; -; Genomic_DNA.
DR RefSeq; WP_011747151.1; NC_008686.1.
DR AlphaFoldDB; A1B079; -.
DR STRING; 318586.Pden_0811; -.
DR EnsemblBacteria; ABL68923; ABL68923; Pden_0811.
DR GeneID; 75500349; -.
DR KEGG; pde:Pden_0811; -.
DR eggNOG; COG1183; Bacteria.
DR HOGENOM; CLU_086279_0_0_5; -.
DR OrthoDB; 350520at2; -.
DR Proteomes; UP000000361; Chromosome 1.
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:UP000000361};
KW Transferase {ECO:0000256|PIRNR:PIRNR000851, ECO:0000313|EMBL:ABL68923.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 36..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 66..88
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 126..143
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 149..167
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 179..197
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 203..222
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 230 AA; 26036 MW; F7B5CC929855A2BC CRC64;
MNPRLKALAV HLLTATGAVL SMLALLAAVR AEWSQMFFWL VIALIVDGVD GPLARRYHVK
TNWPTYDGVL MDLIIDYLTY VFIPAYALFM SGLLPGWTGW IAIIAITYGS VIYFADTRMK
TRDNSFAGFP ACWNMVVLVL FAIKPDFWLT LVIVVALAIT MFTNVKFIHP MRTERWRAIS
LPVTVAWVGF SVWAVLVDFH PESFARWGLL LSSLWLMFAG LAQQLTERRA
//
