ID B5ZP40_RHILW Unreviewed; 242 AA.
AC B5ZP40;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 90.
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};
DE Flags: Precursor;
GN OrderedLocusNames=Rleg2_1714 {ECO:0000313|EMBL:ACI55001.1};
OS Rhizobium leguminosarum bv. trifolii (strain WSM2304).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=395492 {ECO:0000313|EMBL:ACI55001.1, ECO:0000313|Proteomes:UP000008330};
RN [1] {ECO:0000313|EMBL:ACI55001.1, ECO:0000313|Proteomes:UP000008330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM2304 {ECO:0000313|EMBL:ACI55001.1,
RC ECO:0000313|Proteomes:UP000008330};
RX PubMed=21304679; DOI=10.4056/sigs.44642;
RA Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K., Tiwari R.,
RA Malfatti S., Kiss H., Lapidus A., Copeland A., Nolan M., Land M.,
RA Ivanova N., Mavromatis K., Markowitz V., Kyrpides N., Melino V., Denton M.,
RA Yates R., Howieson J.;
RT "Complete genome sequence of Rhizobium leguminosarum bv trifolii strain
RT WSM2304, an effective microsymbiont of the South American clover Trifolium
RT polymorphum.";
RL Stand. Genomic Sci. 2:66-76(2010).
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; CP001191; ACI55001.1; -; Genomic_DNA.
DR RefSeq; WP_003586520.1; NC_011369.1.
DR AlphaFoldDB; B5ZP40; -.
DR STRING; 395492.Rleg2_1714; -.
DR KEGG; rlt:Rleg2_1714; -.
DR eggNOG; COG1183; Bacteria.
DR HOGENOM; CLU_086279_0_0_5; -.
DR Proteomes; UP000008330; Chromosome.
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 Transferase {ECO:0000256|PIRNR:PIRNR000851, ECO:0000313|EMBL:ACI55001.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 107..124
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 133..152
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 158..176
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 214..235
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 242 AA; 27129 MW; 06472B6874DCECD3 CRC64;
MKIFKYKRVP YAEMRAFSVH ILTASGSFLA FLGVVAAAEH RFIDMFWWLG LALLVDGIDG
PIARKVRVKE VLPNWSGDTL DNIIDYVTYV LLPAFALYQS GMIGEPWSFV AAGMIVVSSA
IYYADMGMKT DEYFFSGFPV VWNMIVFTLF VIDASATTAL AVVTVSVVLT FLPINFLHPV
RVKRLRPLNL GVFFLWSALG IFSLLMHFDT PEWALILFIV TGLYLYVIGA VLQFFPALGR
KA
//
