PGPS1_YEAST
ID PGPS1_YEAST Reviewed; 521 AA.
AC P25578; D6VR07; O93974; P25570; P87011;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2003, sequence version 4.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase;
DE EC=2.7.8.5;
DE AltName: Full=Phosphatidylglycerophosphate synthase;
DE Short=PGP synthase;
GN Name=PGS1; Synonyms=PEL1; OrderedLocusNames=YCL004W;
GN ORFNames=YCL003W, YCL3W, YCL4W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8553693; DOI=10.1002/yea.320111302;
RA Janitor M., Jarosch E., Schweyen R., Subik J.;
RT "Molecular characterization of the PEL1 gene encoding a putative
RT phosphatidylserine synthase.";
RL Yeast 11:1223-1231(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=YP501;
RX PubMed=9545322; DOI=10.1074/jbc.273.16.9829;
RA Chang C., Heacock N., Clancey C., Dowhan W.;
RT "The PEL1 gene (renamed PGS1) encodes the phosphatidylglycero-phosphate
RT synthase of Saccharomyces cerevisiae.";
RL J. Biol. Chem. 273:9829-9836(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
RN [4]
RP SEQUENCE REVISION.
RA Gromadka R.;
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP SEQUENCE REVISION.
RA Valles G., Volckaerts G.;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [7]
RP PRELIMINARY NUCLEOTIDE SEQUENCE OF 30-182.
RX PubMed=8252640; DOI=10.1007/bf00336781;
RA Janitor M., Subik J.;
RT "Molecular cloning of the PEL1 gene of Saccharomyces cerevisiae that is
RT essential for the viability of petite mutants.";
RL Curr. Genet. 24:307-312(1993).
RN [8]
RP SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=9799363; DOI=10.1007/s002940050399;
RA Dzugasova V., Obernauerova M., Horvathova K., Vachova M., Zakova M.,
RA Subik J.;
RT "Phosphatidylglycerolphosphate synthase encoded by the PEL1/PGS1 gene in
RT Saccharomyces cerevisiae is localized in mitochondria and its expression is
RT regulated by phospholipid precursors.";
RL Curr. Genet. 34:297-302(1998).
CC -!- FUNCTION: Essential for the viability of mitochondrial petite mutant.
CC Catalyzes the committed step to the synthesis of the acidic
CC phospholipids. {ECO:0000269|PubMed:9545322}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = 1,2-
CC diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + CMP +
CC H(+); Xref=Rhea:RHEA:12593, ChEBI:CHEBI:15378, ChEBI:CHEBI:57597,
CC ChEBI:CHEBI:58332, ChEBI:CHEBI:60110, ChEBI:CHEBI:60377; EC=2.7.8.5;
CC Evidence={ECO:0000269|PubMed:9545322};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylglycerol biosynthesis;
CC phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:9545322,
CC ECO:0000269|PubMed:9799363}.
CC -!- INDUCTION: Repressed by inositol and choline.
CC {ECO:0000269|PubMed:9799363}.
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-II
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA88175.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA88175.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z48162; CAA88175.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AJ012047; CAA09905.1; -; Genomic_DNA.
DR EMBL; X59720; CAC42966.1; -; Genomic_DNA.
DR EMBL; BK006937; DAA07476.1; -; Genomic_DNA.
DR PIR; T11166; T11166.
DR RefSeq; NP_009923.2; NM_001178653.1.
DR AlphaFoldDB; P25578; -.
DR SMR; P25578; -.
DR BioGRID; 30975; 53.
DR DIP; DIP-8753N; -.
DR MINT; P25578; -.
DR STRING; 4932.YCL004W; -.
DR SwissLipids; SLP:000000239; -.
DR iPTMnet; P25578; -.
DR MaxQB; P25578; -.
DR PaxDb; P25578; -.
DR PRIDE; P25578; -.
DR EnsemblFungi; YCL004W_mRNA; YCL004W; YCL004W.
DR GeneID; 850352; -.
DR KEGG; sce:YCL004W; -.
DR SGD; S000000510; PGS1.
DR VEuPathDB; FungiDB:YCL004W; -.
DR eggNOG; KOG3964; Eukaryota.
DR GeneTree; ENSGT00390000002373; -.
DR HOGENOM; CLU_030471_1_1_1; -.
DR InParanoid; P25578; -.
DR OMA; YLSTLYI; -.
DR BioCyc; YEAST:YCL004W-MON; -.
DR UniPathway; UPA00084; UER00503.
DR PRO; PR:P25578; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25578; protein.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008444; F:CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase activity; IMP:SGD.
DR GO; GO:0032049; P:cardiolipin biosynthetic process; IMP:SGD.
DR InterPro; IPR016270; PGS1.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR PANTHER; PTHR12586; PTHR12586; 1.
DR Pfam; PF00614; PLDc; 1.
DR SMART; SM00155; PLDc; 2.
DR PROSITE; PS50035; PLD; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Lipid biosynthesis; Lipid metabolism; Mitochondrion;
KW Nucleotide-binding; Phospholipid biosynthesis; Phospholipid metabolism;
KW Reference proteome; Repeat; Transferase.
FT CHAIN 1..521
FT /note="CDP-diacylglycerol--glycerol-3-phosphate 3-
FT phosphatidyltransferase"
FT /id="PRO_0000056827"
FT DOMAIN 177..203
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT DOMAIN 419..457
FT /note="PLD phosphodiesterase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 182
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 184
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT BINDING 91..98
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 498
FT /note="F -> Y (in Ref. 1; CAA88175)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 521 AA; 59370 MW; BB9BC47182C3F67E CRC64;
MTTRLLQLTR PHYRLLSLPL QKPFNIKRQM SAANPSPFGN YLNTITKSLQ QNLQTCFHFQ
AKEIDIIESP SQFYDLLKTK ILNSQNRIFI ASLYLGKSET ELVDCISQAL TKNPKLKVSF
LLDGLRGTRE LPSACSATLL SSLVAKYGSE RVDCRLYKTP AYHGWKKVLV PKRFNEGLGL
QHMKIYGFDN EVILSGANLS NDYFTNRQDR YYLFKSRNFS NYYFKLHQLI SSFSYQIIKP
MVDGSINIIW PDSNPTVEPT KNKRLFLREA SQLLDGFLKS SKQSLPITAV GQFSTLVYPI
SQFTPLFPKY NDKSTEKRTI LSLLSTITSN AISWTFTAGY FNILPDIKAK LLATPVAEAN
VITASPFANG FYQSKGVSSN LPGAYLYLSK KFLQDVCRYR QDHAITLREW QRGVVNKPNG
WSYHAKGIWL SARDKNDANN WKPFITVIGS SNYTRRAYSL DLESNALIIT RDEELRKKMK
AELDNLLQYT KPVTLEDFQS DPERHVGTGV KIATSILGKK L
