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Protein

Phosphatidylcholine synthase

Gene

pcs

Organism
Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Condenses choline with CDP-diglyceride to produce phosphatidylcholine and CMP.4 Publications

Catalytic activityi

CDP-diacylglycerol + choline = CMP + phosphatidylcholine.4 Publications

Cofactori

Mn2+1 Publication

Enzyme regulationi

Activated by CDP-diacylglycerol especially in the presence of Triton X-100 (0.1% w/v) at concentrations where micelles are formed. Maximal activation by Triton X-100 at 0.2% w/v, but higher concentrations become inhibitory. Inhibited by EDTA and high concentrations of choline.1 Publication

pH dependencei

Optimum pH is 8.0 in cell-free extracts. Activity decreases as pH is raised or lowered.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Keywords - Ligandi

Manganese

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16699.
SMEL266834:GJF6-1713-MONOMER.
BRENDAi2.7.8.24. 5347.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylcholine synthase (EC:2.7.8.24)
Short name:
PC synthase
Short name:
PCS
Alternative name(s):
CDP-diglyceride-choline O-phosphatidyltransferase
Gene namesi
Name:pcs
Ordered Locus Names:R01672
ORF Names:SMc00247
OrganismiRhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
Taxonomic identifieri266834 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium
ProteomesiUP000001976 Componenti: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1515Cytoplasmic1 PublicationAdd
BLAST
Transmembranei16 – 3621Helical; Name=1CuratedAdd
BLAST
Topological domaini37 – 415Periplasmic1 Publication
Transmembranei42 – 6221Helical; Name=2CuratedAdd
BLAST
Topological domaini63 – 7614Cytoplasmic1 PublicationAdd
BLAST
Transmembranei77 – 9721Helical; Name= 3CuratedAdd
BLAST
Topological domaini98 – 1003Periplasmic1 Publication
Transmembranei101 – 12121Helical; Name=4CuratedAdd
BLAST
Topological domaini122 – 13312Cytoplasmic1 PublicationAdd
BLAST
Transmembranei134 – 15421Helical; Name=5CuratedAdd
BLAST
Topological domaini155 – 1562Periplasmic1 Publication
Transmembranei157 – 17721Helical; Name=6CuratedAdd
BLAST
Topological domaini178 – 18710Cytoplasmic1 Publication
Transmembranei188 – 20821Helical; Name=7CuratedAdd
BLAST
Topological domaini209 – 2113Periplasmic1 Publication
Transmembranei212 – 23221Helical; Name=8CuratedAdd
BLAST
Topological domaini233 – 2419Cytoplasmic1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi20 – 201H → A: Loss of enzyme activity. 1 Publication
Mutagenesisi20 – 201H → L: 32% of wild-type enzyme activity. 1 Publication
Mutagenesisi23 – 231T → A: Loss of enzyme activity. 1 Publication
Mutagenesisi23 – 231T → S: 63% of wild-type enzyme activity. 1 Publication
Mutagenesisi56 – 561D → A, E or N: Loss of enzyme activity. 1 Publication
Mutagenesisi59 – 591D → A, E or N: Loss of enzyme activity. 1 Publication
Mutagenesisi60 – 601G → A: Loss of enzyme activity. 1 Publication
Mutagenesisi77 – 771G → A: Strongly reduced enzyme activity. 1 Publication
Mutagenesisi81 – 811D → A: Loss of enzyme activity. 1 Publication
Mutagenesisi81 – 811D → E or N: Strongly reduced enzyme activity. 1 Publication
Mutagenesisi85 – 851D → A, E or N: Loss of enzyme activity. 1 Publication
Mutagenesisi123 – 1231Y → A: Strongly reduced enzyme activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 241241Phosphatidylcholine synthasePRO_0000056812Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi266834.SMc00247.

Structurei

3D structure databases

ProteinModelPortaliQ9KJY8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1183.
HOGENOMiHOG000066428.
KOiK01004.
OMAiFLHPFRV.
OrthoDBiEOG6P5ZJN.

Family and domain databases

InterProiIPR000462. CDP-OH_P_trans.
IPR026027. PcS.
[Graphical view]
PfamiPF01066. CDP-OH_P_transf. 1 hit.
[Graphical view]
PIRSFiPIRSF000851. PcS. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9KJY8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKFFNYRRVP YAEIRAFSVH ILTASGSFLA FLGVVAAAEH RFVDMFWWLG
60 70 80 90 100
LALLVDGIDG PIARKVQVKE VLPNWSGDTL DNVIDYVTYV LLPAFALYQS
110 120 130 140 150
GMIGEPWSFV AAGAIVVSSA IYYADMGMKT DEYFFSGFPV VWNMVVFTLF
160 170 180 190 200
VIQASEVTAS IVVFLSVILT FLPINFLHPV RVKRLRPLNL GIFLVWSVLG
210 220 230 240
MYALLLHFET PPWVVVGVVA TGLYLYVIGF ILQIFPKLGR A
Length:241
Mass (Da):27,003
Last modified:October 1, 2000 - v1
Checksum:i864BC6E353D08D1B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF155772 Genomic DNA. Translation: AAF27310.1.
AL591688 Genomic DNA. Translation: CAC46251.1.
RefSeqiNP_385778.1. NC_003047.1.
WP_003533217.1. NC_003047.1.

Genome annotation databases

EnsemblBacteriaiCAC46251; CAC46251; SMc00247.
GeneIDi1233331.
KEGGisme:SMc00247.
PATRICi23632719. VBISinMel96828_3105.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF155772 Genomic DNA. Translation: AAF27310.1.
AL591688 Genomic DNA. Translation: CAC46251.1.
RefSeqiNP_385778.1. NC_003047.1.
WP_003533217.1. NC_003047.1.

3D structure databases

ProteinModelPortaliQ9KJY8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi266834.SMc00247.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAC46251; CAC46251; SMc00247.
GeneIDi1233331.
KEGGisme:SMc00247.
PATRICi23632719. VBISinMel96828_3105.

Phylogenomic databases

eggNOGiCOG1183.
HOGENOMiHOG000066428.
KOiK01004.
OMAiFLHPFRV.
OrthoDBiEOG6P5ZJN.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16699.
SMEL266834:GJF6-1713-MONOMER.
BRENDAi2.7.8.24. 5347.

Family and domain databases

InterProiIPR000462. CDP-OH_P_trans.
IPR026027. PcS.
[Graphical view]
PfamiPF01066. CDP-OH_P_transf. 1 hit.
[Graphical view]
PIRSFiPIRSF000851. PcS. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of the gene for phosphatidylcholine synthase."
    Sohlenkamp C., de Rudder K.E.E., Roehrs V., Lopez-Lara I.M., Geiger O.
    J. Biol. Chem. 275:18919-18925(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY.
    Strain: 1021.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 1021.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 1021.
  4. "Plant-exuded choline is used for rhizobial membrane lipid biosynthesis by phosphatidylcholine synthase."
    de Rudder K.E., Sohlenkamp C., Geiger O.
    J. Biol. Chem. 274:20011-20016(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
    Strain: 1021.
  5. "Pathways for phosphatidylcholine biosynthesis in bacteria."
    Martinez-Morales F., Schobert M., Lopez-Lara I.M., Geiger O.
    Microbiology 149:3461-3471(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
    Strain: 1021.
  6. "Functional and topological analysis of phosphatidylcholine synthase from Sinorhizobium meliloti."
    Solis-Oviedo R.L., Martinez-Morales F., Geiger O., Sohlenkamp C.
    Biochim. Biophys. Acta 1821:573-581(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF HIS-20; THR-23; ASP-56; ASP-59; GLY-60; GLY-77; ASP-81; ASP-85 AND TYR-123.
    Strain: 1021.

Entry informationi

Entry nameiPCS_RHIME
AccessioniPrimary (citable) accession number: Q9KJY8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: October 1, 2000
Last modified: April 1, 2015
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.