PCS_RHIL3
ID PCS_RHIL3 Reviewed; 242 AA.
AC Q1MGQ9;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Phosphatidylcholine synthase {ECO:0000303|PubMed:14663079, ECO:0000312|EMBL:CAK07860.1};
DE Short=PC synthase {ECO:0000250|UniProtKB:Q9KJY8};
DE Short=PCS {ECO:0000303|PubMed:14663079};
DE EC=2.7.8.24 {ECO:0000269|PubMed:14663079, ECO:0000312|EMBL:CAK07860.1};
DE AltName: Full=CDP-diglyceride-choline O-phosphatidyltransferase {ECO:0000250|UniProtKB:Q9KJY8};
GN Name=pcs {ECO:0000312|EMBL:CAK07860.1}; OrderedLocusNames=RL2370;
OS Rhizobium leguminosarum bv. viciae (strain 3841).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=216596;
RN [1] {ECO:0000312|EMBL:CAK07860.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3841 {ECO:0000312|EMBL:CAK07860.1};
RX PubMed=16640791; DOI=10.1186/gb-2006-7-4-r34;
RA Young J.P.W., Crossman L.C., Johnston A.W.B., Thomson N.R., Ghazoui Z.F.,
RA Hull K.H., Wexler M., Curson A.R.J., Todd J.D., Poole P.S., Mauchline T.H.,
RA East A.K., Quail M.A., Churcher C., Arrowsmith C., Cherevach I.,
RA Chillingworth T., Clarke K., Cronin A., Davis P., Fraser A., Hance Z.,
RA Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA Rabbinowitsch E., Sanders M., Simmonds M., Whitehead S., Parkhill J.;
RT "The genome of Rhizobium leguminosarum has recognizable core and accessory
RT components.";
RL Genome Biol. 7:R34.1-R34.20(2006).
RN [2] {ECO:0000305}
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=3841 {ECO:0000269|PubMed:14663079};
RX PubMed=14663079; DOI=10.1099/mic.0.26522-0;
RA Martinez-Morales F., Schobert M., Lopez-Lara I.M., Geiger O.;
RT "Pathways for phosphatidylcholine biosynthesis in bacteria.";
RL Microbiology 149:3461-3471(2003).
CC -!- FUNCTION: Condenses choline with CDP-diglyceride to produce
CC phosphatidylcholine and CMP. {ECO:0000269|PubMed:14663079}.
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:0000269|PubMed:14663079};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9KJY8};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:Q9KJY8}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9KJY8}.
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {ECO:0000255}.
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DR EMBL; AM236080; CAK07860.1; -; Genomic_DNA.
DR RefSeq; WP_011651942.1; NC_008380.1.
DR AlphaFoldDB; Q1MGQ9; -.
DR SMR; Q1MGQ9; -.
DR STRING; 216596.RL2370; -.
DR EnsemblBacteria; CAK07860; CAK07860; RL2370.
DR KEGG; rle:RL2370; -.
DR eggNOG; COG1183; Bacteria.
DR HOGENOM; CLU_086279_0_0_5; -.
DR OMA; FLHPFRV; -.
DR OrthoDB; 1232102at2; -.
DR Proteomes; UP000006575; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050520; F:phosphatidylcholine synthase activity; IDA:UniProtKB.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Lipid biosynthesis; Lipid metabolism;
KW Manganese; Membrane; Phospholipid biosynthesis; Phospholipid metabolism;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..242
FT /note="Phosphatidylcholine synthase"
FT /id="PRO_0000425223"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9KJY8, ECO:0000255"
FT TRANSMEM 16..36
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..41
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..76
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..97
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..100
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..133
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 155..159
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..187
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..214
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..235
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 236..242
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9KJY8, ECO:0000255"
SQ SEQUENCE 242 AA; 27146 MW; D6D968E0EF418C7C CRC64;
MKIFNYKRVP YAEMRAFSVH ILTASGSFLA FLGVVAAAEH RFIDMFWWLG LALLVDGIDG
PIARKVRVKE VLPNWSGDTL DNIIDYVTYV LLPAFALYQS GMIGEPWSFV AAGMIVVSSA
IYYADMGMKT DEYFFSGFPV VWNMIVFTLF VIDASATTAL TVVIVSVVLT FLPINFLHPV
RVKRLRPLNL GVFFLWSALG IFSLLMHFDT PEWALILFIV TGAYLYVIGA VLQFFPALGR
ET
