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Q9KJY8 (PCS_RHIME) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphatidylcholine synthase

Short name=PC synthase
Short name=PCS
EC=2.7.8.24
Alternative name(s):
CDP-diglyceride-choline O-phosphatidyltransferase
Gene names
Name:pcs
Ordered Locus Names:R01672
ORF Names:SMc00247
OrganismRhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti) [Complete proteome] [HAMAP]
Taxonomic identifier266834 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium

Protein attributes

Sequence length241 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Condenses choline with CDP-diglyceride to produce phosphatidylcholine and CMP. Ref.1 Ref.4 Ref.5 Ref.6

Catalytic activity

CDP-diacylglycerol + choline = CMP + phosphatidylcholine. Ref.1 Ref.4 Ref.5 Ref.6

Cofactor

Manganese. Ref.4

Enzyme regulation

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. Ref.4

Subcellular location

Cell inner membrane; Multi-pass membrane protein Ref.6.

Sequence similarities

Belongs to the CDP-alcohol phosphatidyltransferase class-I family.

Biophysicochemical properties

pH dependence:

Optimum pH is 8.0 in cell-free extracts. Activity decreases as pH is raised or lowered. Ref.4

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 241241Phosphatidylcholine synthase
PRO_0000056812

Regions

Topological domain1 – 1515Cytoplasmic Ref.6
Transmembrane16 – 3621Helical; Name=1; Probable
Topological domain37 – 415Periplasmic Probable
Transmembrane42 – 6221Helical; Name=2; Probable
Topological domain63 – 7614Cytoplasmic Probable
Transmembrane77 – 9721Helical; Name= 3; Probable
Topological domain98 – 1003Periplasmic Probable
Transmembrane101 – 12121Helical; Name=4; Probable
Topological domain122 – 13312Cytoplasmic Probable
Transmembrane134 – 15421Helical; Name=5; Probable
Topological domain155 – 1562Periplasmic Ref.6
Transmembrane157 – 17721Helical; Name=6; Probable
Topological domain178 – 18710Cytoplasmic Probable
Transmembrane188 – 20821Helical; Name=7; Probable
Topological domain209 – 2113Periplasmic Probable
Transmembrane212 – 23221Helical; Name=8; Probable
Topological domain233 – 2419Cytoplasmic Ref.6

Experimental info

Mutagenesis201H → A: Loss of enzyme activity. Ref.6
Mutagenesis201H → L: 32% of wild-type enzyme activity. Ref.6
Mutagenesis231T → A: Loss of enzyme activity. Ref.6
Mutagenesis231T → S: 63% of wild-type enzyme activity. Ref.6
Mutagenesis561D → A, E or N: Loss of enzyme activity. Ref.6
Mutagenesis591D → A, E or N: Loss of enzyme activity. Ref.6
Mutagenesis601G → A: Loss of enzyme activity. Ref.6
Mutagenesis771G → A: Strongly reduced enzyme activity. Ref.6
Mutagenesis811D → A: Loss of enzyme activity. Ref.6
Mutagenesis811D → E or N: Strongly reduced enzyme activity. Ref.6
Mutagenesis851D → A, E or N: Loss of enzyme activity. Ref.6
Mutagenesis1231Y → A: Strongly reduced enzyme activity. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Q9KJY8 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 864BC6E353D08D1B

FASTA24127,003
        10         20         30         40         50         60 
MKFFNYRRVP YAEIRAFSVH ILTASGSFLA FLGVVAAAEH RFVDMFWWLG LALLVDGIDG 

        70         80         90        100        110        120 
PIARKVQVKE VLPNWSGDTL DNVIDYVTYV LLPAFALYQS GMIGEPWSFV AAGAIVVSSA 

       130        140        150        160        170        180 
IYYADMGMKT DEYFFSGFPV VWNMVVFTLF VIQASEVTAS IVVFLSVILT FLPINFLHPV 

       190        200        210        220        230        240 
RVKRLRPLNL GIFLVWSVLG MYALLLHFET PPWVVVGVVA TGLYLYVIGF ILQIFPKLGR 


A 

« Hide

References

« Hide 'large scale' references
[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]"Analysis of the chromosome sequence of the legume symbiont Sinorhizobium meliloti strain 1021."
Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J., Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S., Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D. expand/collapse author list , Pohl T., Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C., Thebault P., Vandenbol M., Weidner S., Galibert F.
Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1021.
[3]"The composite genome of the legume symbiont Sinorhizobium meliloti."
Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F., Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G., Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P., Cowie A. expand/collapse author list , Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S., Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I., Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S., Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C., Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R., Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H., Wong K., Yeh K.-C., Batut J.
Science 293:668-672(2001) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF155772 Genomic DNA. Translation: AAF27310.1.
AL591688 Genomic DNA. Translation: CAC46251.1.
RefSeqNP_385778.1. NC_003047.1.

3D structure databases

ProteinModelPortalQ9KJY8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING266834.SMc00247.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC46251; CAC46251; SMc00247.
GeneID1233331.
KEGGsme:SMc00247.
PATRIC23632719. VBISinMel96828_3105.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1183.
HOGENOMHOG000066428.
KOK01004.
OMAFLHPFRV.
OrthoDBEOG6P5ZJN.
ProtClustDBCLSK863002.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-16699.
SMEL266834:GJF6-1713-MONOMER.
BRENDA2.7.8.24. 5715.

Family and domain databases

InterProIPR000462. CDP-OH_P_trans.
IPR026027. PcS.
[Graphical view]
PfamPF01066. CDP-OH_P_transf. 1 hit.
[Graphical view]
PIRSFPIRSF000851. PcS. 1 hit.
ProtoNetSearch...

Entry information

Entry namePCS_RHIME
AccessionPrimary (citable) accession number: Q9KJY8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: October 1, 2000
Last modified: February 19, 2014
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families