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Database: UniProt
Entry: A0A1I2G5Y2_9RHOB
LinkDB: A0A1I2G5Y2_9RHOB
Original site: A0A1I2G5Y2_9RHOB 
ID   A0A1I2G5Y2_9RHOB        Unreviewed;       233 AA.
AC   A0A1I2G5Y2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
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=SAMN04488523_11930 {ECO:0000313|EMBL:SFF12031.1};
OS   Sulfitobacter brevis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Sulfitobacter.
OX   NCBI_TaxID=74348 {ECO:0000313|EMBL:SFF12031.1, ECO:0000313|Proteomes:UP000198977};
RN   [1] {ECO:0000313|EMBL:SFF12031.1, ECO:0000313|Proteomes:UP000198977}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11443 {ECO:0000313|EMBL:SFF12031.1,
RC   ECO:0000313|Proteomes:UP000198977};
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|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; FOMW01000019; SFF12031.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2G5Y2; -.
DR   STRING; 74348.SAMN04488523_11930; -.
DR   OrthoDB; 350520at2; -.
DR   Proteomes; UP000198977; 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; IPR043130; CDP-OH_PTrfase_TM_dom.
DR   InterPro; IPR026027; PcS.
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:UP000198977};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000851, ECO:0000313|EMBL:SFF12031.1};
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..91
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        97..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..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        205..227
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   233 AA;  26536 MW;  A3448676ED727455 CRC64;
     MTIHMRALLV HLFTATGAVF AMLAMLEAVQ EQWDMMFLWL VVAFFVDGID GPLARKFNVK
     KNAPEFDGVL LDLIIDYLTY VFIPAFALFT SGLMDGWSGW FMIIIVTFAS AMYFADTRMK
     TKDNSFAGFP GCWNMLVLVL FALKPDWWVS LILVTILAIT MFLPIKFVHP VRTERWRAVT
     LPMALAWTFF AGWAAWVDFH PQSWAHWGLI VTSLYLVVAG AAQQVIYSDK TRA
//
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