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Q9KJY8

- PCS_RHIME

UniProt

Q9KJY8 - PCS_RHIME

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Protein
Phosphatidylcholine synthase
Gene
pcs, R01672, SMc00247
Organism
Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
Status
Reviewed - 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

Manganese.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

  1. phosphatidylcholine synthase activity Source: UniProtKB-EC
Complete GO annotation...

GO - Biological processi

  1. phospholipid biosynthetic process Source: UniProtKB-KW
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. 5715.

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: Chromosome

Subcellular locationi

Cell inner membrane; Multi-pass membrane protein 1 Publication

Topology

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

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-SubCell
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 synthase
PRO_0000056812Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi266834.SMc00247.

Structurei

3D structure databases

ProteinModelPortaliQ9KJY8.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1183.
HOGENOMiHOG000066428.
KOiK01004.
OMAiYVFVPAY.
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

MKFFNYRRVP YAEIRAFSVH ILTASGSFLA FLGVVAAAEH RFVDMFWWLG    50
LALLVDGIDG PIARKVQVKE VLPNWSGDTL DNVIDYVTYV LLPAFALYQS 100
GMIGEPWSFV AAGAIVVSSA IYYADMGMKT DEYFFSGFPV VWNMVVFTLF 150
VIQASEVTAS IVVFLSVILT FLPINFLHPV RVKRLRPLNL GIFLVWSVLG 200
MYALLLHFET PPWVVVGVVA TGLYLYVIGF ILQIFPKLGR A 241
Length:241
Mass (Da):27,003
Last modified:October 1, 2000 - v1
Checksum:i864BC6E353D08D1B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AF155772 Genomic DNA. Translation: AAF27310.1 .
AL591688 Genomic DNA. Translation: CAC46251.1 .
RefSeqi NP_385778.1. NC_003047.1.
WP_003533217.1. NC_003047.1.

3D structure databases

ProteinModelPortali Q9KJY8.
ModBasei Search...

Protein-protein interaction databases

STRINGi 266834.SMc00247.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAC46251 ; CAC46251 ; SMc00247 .
GeneIDi 1233331.
KEGGi sme:SMc00247.
PATRICi 23632719. VBISinMel96828_3105.

Phylogenomic databases

eggNOGi COG1183.
HOGENOMi HOG000066428.
KOi K01004.
OMAi YVFVPAY.
OrthoDBi EOG6P5ZJN.

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-16699.
SMEL266834:GJF6-1713-MONOMER.
BRENDAi 2.7.8.24. 5715.

Family and domain databases

InterProi IPR000462. CDP-OH_P_trans.
IPR026027. PcS.
[Graphical view ]
Pfami PF01066. CDP-OH_P_transf. 1 hit.
[Graphical view ]
PIRSFi PIRSF000851. PcS. 1 hit.
ProtoNeti Search...

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: September 3, 2014
This is version 73 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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