PCS_RHIME
ID PCS_RHIME Reviewed; 241 AA.
AC Q9KJY8;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Phosphatidylcholine synthase;
DE Short=PC synthase;
DE Short=PCS;
DE EC=2.7.8.24;
DE AltName: Full=CDP-diglyceride-choline O-phosphatidyltransferase;
GN Name=pcs; OrderedLocusNames=R01672; ORFNames=SMc00247;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=1021;
RX PubMed=10858449; DOI=10.1074/jbc.m000844200;
RA Sohlenkamp C., de Rudder K.E.E., Roehrs V., Lopez-Lara I.M., Geiger O.;
RT "Cloning and characterization of the gene for phosphatidylcholine
RT synthase.";
RL J. Biol. Chem. 275:18919-18925(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481430; DOI=10.1073/pnas.161294398;
RA Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT meliloti strain 1021.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=1021;
RX PubMed=10391951; DOI=10.1074/jbc.274.28.20011;
RA de Rudder K.E., Sohlenkamp C., Geiger O.;
RT "Plant-exuded choline is used for rhizobial membrane lipid biosynthesis by
RT phosphatidylcholine synthase.";
RL J. Biol. Chem. 274:20011-20016(1999).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=1021;
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).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TOPOLOGY, AND
RP MUTAGENESIS OF HIS-20; THR-23; ASP-56; ASP-59; GLY-60; GLY-77; ASP-81;
RP ASP-85 AND TYR-123.
RC STRAIN=1021;
RX PubMed=22333179; DOI=10.1016/j.bbalip.2012.01.016;
RA Solis-Oviedo R.L., Martinez-Morales F., Geiger O., Sohlenkamp C.;
RT "Functional and topological analysis of phosphatidylcholine synthase from
RT Sinorhizobium meliloti.";
RL Biochim. Biophys. Acta 1821:573-581(2012).
CC -!- FUNCTION: Condenses choline with CDP-diglyceride to produce
CC phosphatidylcholine and CMP. {ECO:0000269|PubMed:10391951,
CC ECO:0000269|PubMed:10858449, ECO:0000269|PubMed:14663079,
CC ECO:0000269|PubMed:22333179}.
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:10391951, ECO:0000269|PubMed:10858449,
CC ECO:0000269|PubMed:14663079, ECO:0000269|PubMed:22333179};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:10391951};
CC -!- ACTIVITY REGULATION: Activated by CDP-diacylglycerol especially in the
CC presence of Triton X-100 (0.1% w/v) at concentrations where micelles
CC are formed. Maximal activation by Triton X-100 at 0.2% w/v, but higher
CC concentrations become inhibitory. Inhibited by EDTA and high
CC concentrations of choline. {ECO:0000269|PubMed:10391951}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0 in cell-free extracts. Activity decreases as pH is
CC raised or lowered. {ECO:0000269|PubMed:10391951};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:22333179}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:22333179}.
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {ECO:0000305}.
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DR EMBL; AF155772; AAF27310.1; -; Genomic_DNA.
DR EMBL; AL591688; CAC46251.1; -; Genomic_DNA.
DR RefSeq; NP_385778.1; NC_003047.1.
DR RefSeq; WP_003533217.1; NC_003047.1.
DR AlphaFoldDB; Q9KJY8; -.
DR STRING; 266834.SMc00247; -.
DR EnsemblBacteria; CAC46251; CAC46251; SMc00247.
DR GeneID; 61603141; -.
DR KEGG; sme:SMc00247; -.
DR PATRIC; fig|266834.11.peg.3105; -.
DR eggNOG; COG1183; Bacteria.
DR HOGENOM; CLU_086279_0_0_5; -.
DR OMA; FLHPFRV; -.
DR BioCyc; MetaCyc:MON-16699; -.
DR BRENDA; 2.7.8.24; 5347.
DR Proteomes; UP000001976; 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; 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 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Lipid biosynthesis; Lipid metabolism;
KW Manganese; Membrane; Phospholipid biosynthesis; Phospholipid metabolism;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..241
FT /note="Phosphatidylcholine synthase"
FT /id="PRO_0000056812"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:22333179"
FT TRANSMEM 16..36
FT /note="Helical; Name=1"
FT /evidence="ECO:0000305"
FT TOPO_DOM 37..41
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:22333179"
FT TRANSMEM 42..62
FT /note="Helical; Name=2"
FT /evidence="ECO:0000305"
FT TOPO_DOM 63..76
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:22333179"
FT TRANSMEM 77..97
FT /note="Helical; Name= 3"
FT /evidence="ECO:0000305"
FT TOPO_DOM 98..100
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:22333179"
FT TRANSMEM 101..121
FT /note="Helical; Name=4"
FT /evidence="ECO:0000305"
FT TOPO_DOM 122..133
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:22333179"
FT TRANSMEM 134..154
FT /note="Helical; Name=5"
FT /evidence="ECO:0000305"
FT TOPO_DOM 155..156
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:22333179"
FT TRANSMEM 157..177
FT /note="Helical; Name=6"
FT /evidence="ECO:0000305"
FT TOPO_DOM 178..187
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:22333179"
FT TRANSMEM 188..208
FT /note="Helical; Name=7"
FT /evidence="ECO:0000305"
FT TOPO_DOM 209..211
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:22333179"
FT TRANSMEM 212..232
FT /note="Helical; Name=8"
FT /evidence="ECO:0000305"
FT TOPO_DOM 233..241
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:22333179"
FT MUTAGEN 20
FT /note="H->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:22333179"
FT MUTAGEN 20
FT /note="H->L: 32% of wild-type enzyme activity."
FT /evidence="ECO:0000269|PubMed:22333179"
FT MUTAGEN 23
FT /note="T->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:22333179"
FT MUTAGEN 23
FT /note="T->S: 63% of wild-type enzyme activity."
FT /evidence="ECO:0000269|PubMed:22333179"
FT MUTAGEN 56
FT /note="D->A,E,N: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:22333179"
FT MUTAGEN 59
FT /note="D->A,E,N: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:22333179"
FT MUTAGEN 60
FT /note="G->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:22333179"
FT MUTAGEN 77
FT /note="G->A: Strongly reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:22333179"
FT MUTAGEN 81
FT /note="D->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:22333179"
FT MUTAGEN 81
FT /note="D->E,N: Strongly reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:22333179"
FT MUTAGEN 85
FT /note="D->A,E,N: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:22333179"
FT MUTAGEN 123
FT /note="Y->A: Strongly reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:22333179"
SQ SEQUENCE 241 AA; 27003 MW; 864BC6E353D08D1B CRC64;
MKFFNYRRVP YAEIRAFSVH ILTASGSFLA FLGVVAAAEH RFVDMFWWLG LALLVDGIDG
PIARKVQVKE VLPNWSGDTL DNVIDYVTYV LLPAFALYQS GMIGEPWSFV AAGAIVVSSA
IYYADMGMKT DEYFFSGFPV VWNMVVFTLF VIQASEVTAS IVVFLSVILT FLPINFLHPV
RVKRLRPLNL GIFLVWSVLG MYALLLHFET PPWVVVGVVA TGLYLYVIGF ILQIFPKLGR
A
