ID A0A088QGM9_9CORY Unreviewed; 275 AA.
AC A0A088QGM9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Phosphatidylcholine synthase {ECO:0000256|ARBA:ARBA00015623};
DE EC=2.7.8.24 {ECO:0000256|ARBA:ARBA00013195};
DE AltName: Full=CDP-diglyceride-choline O-phosphatidyltransferase {ECO:0000256|ARBA:ARBA00033321};
GN ORFNames=DR71_943 {ECO:0000313|EMBL:AIN82448.1};
OS Corynebacterium sp. ATCC 6931.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1487956 {ECO:0000313|EMBL:AIN82448.1, ECO:0000313|Proteomes:UP000029247};
RN [1] {ECO:0000313|EMBL:AIN82448.1, ECO:0000313|Proteomes:UP000029247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6931 {ECO:0000313|Proteomes:UP000029247};
RA Bishop-Lilly K.A., Broomall S.M., Chain P.S., Chertkov O., Coyne S.R.,
RA Daligault H.E., Davenport K.W., Erkkila T., Frey K.G., Gibbons H.S., Gu W.,
RA Jaissle J., Johnson S.L., Koroleva G.I., Ladner J.T., Lo C.-C.,
RA Minogue T.D., Munk C., Palacios G.F., Redden C.L., Rosenzweig C.N.,
RA Scholz M.B., Teshima H., Xu Y.;
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP008913; AIN82448.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A088QGM9; -.
DR STRING; 1487956.DR71_943; -.
DR KEGG; coa:DR71_943; -.
DR eggNOG; COG1183; Bacteria.
DR HOGENOM; CLU_086279_0_0_11; -.
DR Proteomes; UP000029247; 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:UniProt.
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 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022519};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000029247};
KW Transferase {ECO:0000313|EMBL:AIN82448.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 44..68
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 113..132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 138..155
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 219..236
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 275 AA; 29665 MW; 68D779E4ADCEA4CB CRC64;
MNATIRSDNA SSAVADNSAA VSTANTDAAI TAATFTRFTR RQHVIAWAVH AFTLTGLVWA
TLAVVALLES RPHWMWLWLG IALVVDGVDG NMARKHHIKE VVPWFNGAVV DNIVDYLTWT
AIPAAFMVMY LPLGPRPLAI SLIILVLVSS MFCYANEAAK SGDYYFVGFP AAWNIVAVLL
WVWNAPMAVC IAAIFIFSAM TLVPLHYTHP FRVERGRIAN IAATFIWIIS TGTLIAGETT
AASLSSTAVH GLVAVNVAAG AWLIIGGVRR SLSGR
//
