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Database: UniProt
Entry: A0A0X3TXN8_9RHOB
LinkDB: A0A0X3TXN8_9RHOB
Original site: A0A0X3TXN8_9RHOB 
ID   A0A0X3TXN8_9RHOB        Unreviewed;       239 AA.
AC   A0A0X3TXN8;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=AVO45_05010 {ECO:0000313|EMBL:KUJ80414.1};
OS   Ruegeria marisrubri.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Ruegeria.
OX   NCBI_TaxID=1685379 {ECO:0000313|EMBL:KUJ80414.1, ECO:0000313|Proteomes:UP000053791};
RN   [1] {ECO:0000313|EMBL:KUJ80414.1, ECO:0000313|Proteomes:UP000053791}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZGT118 {ECO:0000313|EMBL:KUJ80414.1,
RC   ECO:0000313|Proteomes:UP000053791};
RA   Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL   Submitted (DEC-2015) 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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KUJ80414.1}.
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DR   EMBL; LQBQ01000012; KUJ80414.1; -; Genomic_DNA.
DR   RefSeq; WP_068345642.1; NZ_LQBQ01000012.1.
DR   AlphaFoldDB; A0A0X3TXN8; -.
DR   STRING; 1685379.AVO45_05010; -.
DR   OrthoDB; 350520at2; -.
DR   Proteomes; UP000053791; 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:UP000053791};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000851};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        66..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        97..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        179..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        205..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   239 AA;  26880 MW;  E79ECF27902AD7E8 CRC64;
     MTPQIKALAV HLLTATGAVF AMLAMLAAVE EKWSLMYLWL VVSFMVDGVD GPLARHYHVK
     TYAPEFDGVL LDLIIDYLTY VFIPAYALFK SGLMDGWTGW FAIIVITFAS AMYFADTRMK
     TKDNSFSGFP GCWNMVVIVI FALQPNFYVS LSLVTLLAVA MFLPLKFIHP VRTERWRNLS
     LPMAFAWTFF AGWAAWVDFD PQSWAHWGLV LTSVYLVSAG IAQQLIPERG ISRKAKGAQ
//
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