ID   PGPS1_SCHPO             Reviewed;         502 AA.
AC   Q9HDW1;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-FEB-2012, sequence version 2.
DT   03-AUG-2022, entry version 105.
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; ORFNames=SPBP18G5.02;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   REVISION OF GENE MODEL.
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
CC   -!- FUNCTION: Functions in the biosynthesis of the anionic phospholipids
CC       phosphatidylglycerol and cardiolipin. {ECO:0000250}.
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   -!- PATHWAY: Phospholipid metabolism; phosphatidylglycerol biosynthesis;
CC       phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-II
CC       family. {ECO:0000305}.
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DR   EMBL; CU329671; CAC21490.2; -; Genomic_DNA.
DR   RefSeq; NP_595992.2; NM_001021899.2.
DR   AlphaFoldDB; Q9HDW1; -.
DR   SMR; Q9HDW1; -.
DR   BioGRID; 277757; 1.
DR   STRING; 4896.SPBP18G5.02.1; -.
DR   MaxQB; Q9HDW1; -.
DR   PaxDb; Q9HDW1; -.
DR   EnsemblFungi; SPBP18G5.02.1; SPBP18G5.02.1:pep; SPBP18G5.02.
DR   GeneID; 2541243; -.
DR   KEGG; spo:SPBP18G5.02; -.
DR   PomBase; SPBP18G5.02; pgs1.
DR   VEuPathDB; FungiDB:SPBP18G5.02; -.
DR   eggNOG; KOG3964; Eukaryota.
DR   HOGENOM; CLU_030471_1_2_1; -.
DR   InParanoid; Q9HDW1; -.
DR   OMA; YLSTLYI; -.
DR   UniPathway; UPA00084; UER00503.
DR   PRO; PR:Q9HDW1; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005759; C:mitochondrial matrix; IC:PomBase.
DR   GO; GO:0031966; C:mitochondrial membrane; IDA:PomBase.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008444; F:CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase activity; IDA:PomBase.
DR   GO; GO:0032049; P:cardiolipin biosynthetic process; IDA:PomBase.
DR   GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; EXP:PomBase.
DR   GO; GO:0007006; P:mitochondrial membrane organization; IC:PomBase.
DR   InterPro; IPR016270; PGS1.
DR   InterPro; IPR025202; PLD-like_dom.
DR   InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR   PANTHER; PTHR12586; PTHR12586; 1.
DR   Pfam; PF13091; PLDc_2; 1.
DR   SMART; SM00155; PLDc; 2.
PE   3: Inferred from homology;
KW   ATP-binding; Lipid biosynthesis; Lipid metabolism; Mitochondrion;
KW   Nucleotide-binding; Phospholipid biosynthesis; Phospholipid metabolism;
KW   Phosphoprotein; Reference proteome; Repeat; Transferase.
FT   CHAIN           1..502
FT                   /note="CDP-diacylglycerol--glycerol-3-phosphate 3-
FT                   phosphatidyltransferase"
FT                   /id="PRO_0000350817"
FT   DOMAIN          143..169
FT                   /note="PLD phosphodiesterase 1"
FT   DOMAIN          410..443
FT                   /note="PLD phosphodiesterase 2"
FT   ACT_SITE        148
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        150
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        155
FT                   /evidence="ECO:0000255"
FT   BINDING         58..65
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   502 AA;  57676 MW;  0BD5DA52FB39E3F6 CRC64;
     MDEGIEKNIF VNLESQIDGV CPKFYVNVDD IDIIHEPPEF YQRLKKLIKK AQKRIFLSTL
     YIGKEERELI NCLSNALSNN PSLHVHILAD QLRCTRESPG CCSASLLMQL KKKFPDRCEI
     KLYHTPNLRG LRKQLVPHRF NEGWGLQHMK IYGADDNLII SGANLSRDYF TNRKDRYYLF
     SDKGLADFFF KTHFLFSQLS FECIPHLSDS SIQLSSTSPV IPFTLKWNNS CPNPLTNPQE
     FRVAASAKIQ QLLQGNREKF LSRNPSKPLS SVYGSELINQ AGDDNNKPFH KYEESAIVYP
     LFQCVPILTS DVHSTEEKVL SIIGTLLSRK EVNWTLTAGY FNVYPALRKQ LLKSEGIGEV
     IVASQQANGF YRSPGPSKLI PPAYQYIAEQ FLKDSRKKKR NIDVLQWQNK GNTYHAKGFW
     LSTQHHKHPF LTTIGSSNYT SRSQQLDLES TLVVMTQNEK LKRKFSTEIE LIKQHTKPMN
     TCQLEKVPMY VKALTSLMKK KL