Reviewed, UniProtKB/Swiss-Prot P25578 (PGPS1_YEAST)

Names and origin

Protein names

Recommended name:
    CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase
    EC=2.7.8.5
Alternative name(s):
    Phosphatidylglycerophosphate synthase
      Short name=PGP synthase

Gene names

Name:	PGS1
Synonyms:	PEL1
Ordered Locus Names:	YCL004W/YCL003W
ORF Names:	YCL4W/YCL3W

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	521 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Essential for the viability of mitochondrial petite mutant. Catalyzes the committed step to the synthesis of the acidic phospholipids. Ref.2
Catalytic activity	CDP-diacylglycerol + sn-glycerol 3-phosphate = CMP + 3(3-sn-phosphatidyl)-sn-glycerol 1-phosphate. Ref.2
Pathway	Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
Subcellular location	Mitochondrion. Ref.2 Ref.7
Induction	Repressed by inositol and choline. Ref.7
Sequence similarities	Belongs to the CDP-alcohol phosphatidyltransferase class-II family. Contains 2 PLD phosphodiesterase domains.
Sequence caution	The sequence CAA88175.1 differs from that shown. Reason: Frameshift at position 503. The sequence described in Ref.3 differs from that shown. Reason: Frameshift at position 503.

Ontologies

Keywords
Biological process	Phospholipid biosynthesis
Cellular component	Mitochondrion
Domain	Repeat
Ligand	ATP-binding Nucleotide-binding
Molecular function	Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	phospholipid biosynthetic process Ref.2 Inferred from mutant phenotype. Source: SGD
Cellular component	mitochondrion Ref.7 Inferred from direct assay. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase activity Ref.2 Inferred from mutant phenotype. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 521	521	CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase		PRO_0000056827
Regions
	Domain	177 – 203	27	PLD phosphodiesterase 1
	Domain	419 – 457	39	PLD phosphodiesterase 2
	Nucleotide binding	91 – 98	8	ATP Potential
Sites
	Active site	182	1	Potential
	Active site	184	1	Potential
	Active site	189	1	Potential
Amino acid modifications
	Modified residue	159	1	Phosphothreonine Ref.8
Experimental info
	Sequence conflict	498	1	F → Y Ref.1
	Sequence conflict	498	1	F → Y Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P25578-1 [UniParc]. Last modified June 27, 2003. Version 4. Checksum: BB9BC47182C3F67E	FASTA	521	59,370
	10 20 30 40 50 60 MTTRLLQLTR PHYRLLSLPL QKPFNIKRQM SAANPSPFGN YLNTITKSLQ QNLQTCFHFQ 70 80 90 100 110 120 AKEIDIIESP SQFYDLLKTK ILNSQNRIFI ASLYLGKSET ELVDCISQAL TKNPKLKVSF 130 140 150 160 170 180 LLDGLRGTRE LPSACSATLL SSLVAKYGSE RVDCRLYKTP AYHGWKKVLV PKRFNEGLGL 190 200 210 220 230 240 QHMKIYGFDN EVILSGANLS NDYFTNRQDR YYLFKSRNFS NYYFKLHQLI SSFSYQIIKP 250 260 270 280 290 300 MVDGSINIIW PDSNPTVEPT KNKRLFLREA SQLLDGFLKS SKQSLPITAV GQFSTLVYPI 310 320 330 340 350 360 SQFTPLFPKY NDKSTEKRTI LSLLSTITSN AISWTFTAGY FNILPDIKAK LLATPVAEAN 370 380 390 400 410 420 VITASPFANG FYQSKGVSSN LPGAYLYLSK KFLQDVCRYR QDHAITLREW QRGVVNKPNG 430 440 450 460 470 480 WSYHAKGIWL SARDKNDANN WKPFITVIGS SNYTRRAYSL DLESNALIIT RDEELRKKMK 490 500 510 520 AELDNLLQYT KPVTLEDFQS DPERHVGTGV KIATSILGKK L

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 8553693] [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: 9545322] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION. Strain: YP501.
[3]	"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: 8252640] [Abstract] Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE.
[4]	"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: 1574125] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	Gromadka R. Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[6]	Valles G., Volckaerts G. Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[7]	"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: 9799363] [Abstract] Cited for: SUBCELLULAR LOCATION, INDUCTION.
[8]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-159, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z48162 Genomic DNA. Translation: CAA88175.1. Frameshift. AJ012047 Genomic DNA. Translation: CAA09905.1. X59720 Genomic DNA. Translation: CAC42966.1.
PIR	T11166.
RefSeq	NP_009923.2.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P25578. 1 interaction.
STRING	P25578.
Genome annotation databases
Ensembl	YCL004W; YCL004W; YCL004W; Saccharomyces cerevisiae. [Genome view]
GeneID	850352.
GenomeReviews	Gene locus YCL004W in contig X59720_GR.
KEGG	sce:YCL004W.
NMPDR	fig|4932.3.peg.645.
Organism-specific databases
CYGD	YCL004w.
SGD	S000000510. PGS1.
Phylogenomic databases
HOGENOM	P25578.
OMA	RQDRYVL.
Enzyme and pathway databases
BRENDA	2.7.8.5. 250.
Gene expression databases
ArrayExpress	P25578.
Genevestigator	P25578.
GermOnline	YCL004W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR016270. PLipase-D_PtdSer-synthase-type. IPR001736. PLipase_D/transphosphatidylase. [Graphical view]
Pfam	PF00614. PLDc. 2 hits. [Graphical view]
PIRSF	PIRSF000850. Phospholipase_D_PSS. 1 hit.
SMART	SM00155. PLDc. 2 hits. [Graphical view]
PROSITE	PS50035. PLD. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	965815.

Entry information

Entry name

PGPS1_YEAST

Accession

Primary (citable) accession number: P25578
Secondary accession number(s): O93974, P25570, P87011

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	June 27, 2003
Last modified:	November 3, 2009
This is version 76 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)