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Protein

CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase

Gene

PGS1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Essential for the viability of mitochondrial petite mutant. Catalyzes the committed step to the synthesis of the acidic phospholipids.1 Publication

Catalytic activityi

CDP-diacylglycerol + sn-glycerol 3-phosphate = CMP + 3(3-sn-phosphatidyl)-sn-glycerol 1-phosphate.1 Publication

Pathwayi: phosphatidylglycerol biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes phosphatidylglycerol from CDP-diacylglycerol.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase (PGS1)
  2. Phosphatidylglycerophosphatase GEP4, mitochondrial (GEP4)
This subpathway is part of the pathway phosphatidylglycerol biosynthesis, which is itself part of Phospholipid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes phosphatidylglycerol from CDP-diacylglycerol, the pathway phosphatidylglycerol biosynthesis and in Phospholipid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei182 – 1821PROSITE-ProRule annotation
Active sitei184 – 1841PROSITE-ProRule annotation
Active sitei189 – 1891PROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi91 – 988ATPSequence analysis

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase activity Source: SGD

GO - Biological processi

  • cardiolipin biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:YCL004W-MONOMER.
UniPathwayiUPA00084; UER00503.

Chemistry

SwissLipidsiSLP:000000239.

Names & Taxonomyi

Protein namesi
Recommended name:
CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase (EC:2.7.8.5)
Alternative name(s):
Phosphatidylglycerophosphate synthase
Short name:
PGP synthase
Gene namesi
Name:PGS1
Synonyms:PEL1
Ordered Locus Names:YCL004W
ORF Names:YCL003W, YCL3W, YCL4W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:YCL004W.
SGDiS000000510. PGS1.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 521521CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferasePRO_0000056827Add
BLAST

Proteomic databases

MaxQBiP25578.

PTM databases

iPTMnetiP25578.

Expressioni

Inductioni

Repressed by inositol and choline.1 Publication

Interactioni

Protein-protein interaction databases

BioGridi30975. 48 interactions.
DIPiDIP-8753N.
MINTiMINT-485213.

Structurei

3D structure databases

ProteinModelPortaliP25578.
SMRiP25578. Positions 46-503.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini177 – 20327PLD phosphodiesterase 1PROSITE-ProRule annotationAdd
BLAST
Domaini419 – 45739PLD phosphodiesterase 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 2 PLD phosphodiesterase domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

GeneTreeiENSGT00390000002373.
HOGENOMiHOG000172574.
InParanoidiP25578.
KOiK00995.
OMAiEGWGTWH.
OrthoDBiEOG7Z95XD.

Family and domain databases

InterProiIPR016270. PLipase-D_PtdSer-synthase-type.
IPR001736. PLipase_D/transphosphatidylase.
[Graphical view]
PANTHERiPTHR12586. PTHR12586. 1 hit.
PfamiPF00614. PLDc. 1 hit.
[Graphical view]
PIRSFiPIRSF000850. Phospholipase_D_PSS. 1 hit.
SMARTiSM00155. PLDc. 2 hits.
[Graphical view]
PROSITEiPS50035. PLD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P25578-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTRLLQLTR PHYRLLSLPL QKPFNIKRQM SAANPSPFGN YLNTITKSLQ
60 70 80 90 100
QNLQTCFHFQ AKEIDIIESP SQFYDLLKTK ILNSQNRIFI ASLYLGKSET
110 120 130 140 150
ELVDCISQAL TKNPKLKVSF LLDGLRGTRE LPSACSATLL SSLVAKYGSE
160 170 180 190 200
RVDCRLYKTP AYHGWKKVLV PKRFNEGLGL QHMKIYGFDN EVILSGANLS
210 220 230 240 250
NDYFTNRQDR YYLFKSRNFS NYYFKLHQLI SSFSYQIIKP MVDGSINIIW
260 270 280 290 300
PDSNPTVEPT KNKRLFLREA SQLLDGFLKS SKQSLPITAV GQFSTLVYPI
310 320 330 340 350
SQFTPLFPKY NDKSTEKRTI LSLLSTITSN AISWTFTAGY FNILPDIKAK
360 370 380 390 400
LLATPVAEAN VITASPFANG FYQSKGVSSN LPGAYLYLSK KFLQDVCRYR
410 420 430 440 450
QDHAITLREW QRGVVNKPNG WSYHAKGIWL SARDKNDANN WKPFITVIGS
460 470 480 490 500
SNYTRRAYSL DLESNALIIT RDEELRKKMK AELDNLLQYT KPVTLEDFQS
510 520
DPERHVGTGV KIATSILGKK L
Length:521
Mass (Da):59,370
Last modified:June 27, 2003 - v4
Checksum:iBB9BC47182C3F67E
GO

Sequence cautioni

The sequence CAA88175.1 differs from that shown. Reason: Frameshift at position 503. Curated
The sequence CAA88175.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti498 – 4981F → Y in CAA88175 (PubMed:8553693).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z48162 Genomic DNA. Translation: CAA88175.1. Sequence problems.
AJ012047 Genomic DNA. Translation: CAA09905.1.
X59720 Genomic DNA. Translation: CAC42966.1.
BK006937 Genomic DNA. Translation: DAA07476.1.
PIRiT11166.
RefSeqiNP_009923.2. NM_001178653.1.

Genome annotation databases

EnsemblFungiiCAC42966; CAC42966; CAC42966.
YCL004W; YCL004W; YCL004W.
GeneIDi850352.
KEGGisce:YCL004W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z48162 Genomic DNA. Translation: CAA88175.1. Sequence problems.
AJ012047 Genomic DNA. Translation: CAA09905.1.
X59720 Genomic DNA. Translation: CAC42966.1.
BK006937 Genomic DNA. Translation: DAA07476.1.
PIRiT11166.
RefSeqiNP_009923.2. NM_001178653.1.

3D structure databases

ProteinModelPortaliP25578.
SMRiP25578. Positions 46-503.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi30975. 48 interactions.
DIPiDIP-8753N.
MINTiMINT-485213.

Chemistry

SwissLipidsiSLP:000000239.

PTM databases

iPTMnetiP25578.

Proteomic databases

MaxQBiP25578.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCAC42966; CAC42966; CAC42966.
YCL004W; YCL004W; YCL004W.
GeneIDi850352.
KEGGisce:YCL004W.

Organism-specific databases

EuPathDBiFungiDB:YCL004W.
SGDiS000000510. PGS1.

Phylogenomic databases

GeneTreeiENSGT00390000002373.
HOGENOMiHOG000172574.
InParanoidiP25578.
KOiK00995.
OMAiEGWGTWH.
OrthoDBiEOG7Z95XD.

Enzyme and pathway databases

UniPathwayiUPA00084; UER00503.
BioCyciYEAST:YCL004W-MONOMER.

Miscellaneous databases

NextBioi965815.
PROiP25578.

Family and domain databases

InterProiIPR016270. PLipase-D_PtdSer-synthase-type.
IPR001736. PLipase_D/transphosphatidylase.
[Graphical view]
PANTHERiPTHR12586. PTHR12586. 1 hit.
PfamiPF00614. PLDc. 1 hit.
[Graphical view]
PIRSFiPIRSF000850. Phospholipase_D_PSS. 1 hit.
SMARTiSM00155. PLDc. 2 hits.
[Graphical view]
PROSITEiPS50035. PLD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular characterization of the PEL1 gene encoding a putative phosphatidylserine synthase."
    Janitor M., Jarosch E., Schweyen R., Subik J.
    Yeast 11:1223-1231(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The PEL1 gene (renamed PGS1) encodes the phosphatidylglycero-phosphate synthase of Saccharomyces cerevisiae."
    Chang C., Heacock N., Clancey C., Dowhan W.
    J. Biol. Chem. 273:9829-9836(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
    Strain: YP501.
  3. "The complete DNA sequence of yeast chromosome III."
    Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M.
    , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
    Nature 357:38-46(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Gromadka R.
    Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  5. Valles G., Volckaerts G.
    Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  6. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  7. "Molecular cloning of the PEL1 gene of Saccharomyces cerevisiae that is essential for the viability of petite mutants."
    Janitor M., Subik J.
    Curr. Genet. 24:307-312(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE OF 30-182.
  8. "Phosphatidylglycerolphosphate synthase encoded by the PEL1/PGS1 gene in Saccharomyces cerevisiae is localized in mitochondria and its expression is regulated by phospholipid precursors."
    Dzugasova V., Obernauerova M., Horvathova K., Vachova M., Zakova M., Subik J.
    Curr. Genet. 34:297-302(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INDUCTION.

Entry informationi

Entry nameiPGPS1_YEAST
AccessioniPrimary (citable) accession number: P25578
Secondary accession number(s): D6VR07
, O93974, P25570, P87011
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: June 27, 2003
Last modified: May 11, 2016
This is version 128 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome III
    Yeast (Saccharomyces cerevisiae) chromosome III: entries and gene names

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 one 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.