ID   GEP4_SCHPO              Reviewed;         209 AA.
AC   Q9Y7U3;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2012, sequence version 2.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Probable phosphatidylglycerophosphatase, mitochondrial;
DE            EC=3.1.3.27;
DE   AltName: Full=PGP phosphatase;
GN   Name=gep4; ORFNames=SPCC645.02;
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).
RN   [3]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- FUNCTION: Phosphatidylglycerophosphatase involved in the biosynthesis
CC       of cardiolipin (CL), a unique dimeric phosphoglycerolipid predominantly
CC       present in mitochondrial membranes and which has important functions
CC       for cellular energy metabolism, mitochondrial dynamics and the
CC       initiation of apoptotic pathways. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) +
CC         H2O = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + phosphate;
CC         Xref=Rhea:RHEA:33751, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:60110, ChEBI:CHEBI:64716; EC=3.1.3.27;
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylglycerol biosynthesis;
CC       phosphatidylglycerol from CDP-diacylglycerol: step 2/2.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:16823372}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:16823372}; Matrix side
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the GEP4 family. {ECO:0000305}.
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DR   EMBL; CU329672; CAB39898.2; -; Genomic_DNA.
DR   PIR; T41519; T41519.
DR   RefSeq; NP_588111.2; NM_001023101.2.
DR   AlphaFoldDB; Q9Y7U3; -.
DR   STRING; 4896.SPCC645.02.1; -.
DR   MaxQB; Q9Y7U3; -.
DR   PaxDb; Q9Y7U3; -.
DR   EnsemblFungi; SPCC645.02.1; SPCC645.02.1:pep; SPCC645.02.
DR   GeneID; 2539038; -.
DR   KEGG; spo:SPCC645.02; -.
DR   PomBase; SPCC645.02; gep4.
DR   VEuPathDB; FungiDB:SPCC645.02; -.
DR   eggNOG; KOG2961; Eukaryota.
DR   HOGENOM; CLU_056221_3_2_1; -.
DR   InParanoid; Q9Y7U3; -.
DR   OMA; DMLMANM; -.
DR   UniPathway; UPA00084; UER00504.
DR   PRO; PR:Q9Y7U3; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005759; C:mitochondrial matrix; ISO:PomBase.
DR   GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR   GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR   GO; GO:0008962; F:phosphatidylglycerophosphatase activity; ISO:PomBase.
DR   GO; GO:0032049; P:cardiolipin biosynthetic process; ISO:PomBase.
DR   GO; GO:0007006; P:mitochondrial membrane organization; IC:PomBase.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006549; HAD-SF_hydro_IIIA.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR027706; PGP_Pase.
DR   InterPro; IPR010021; PGPP1/Gep4.
DR   PANTHER; PTHR19288:SF25; PTHR19288:SF25; 1.
DR   Pfam; PF09419; PGP_phosphatase; 1.
DR   SUPFAM; SSF56784; SSF56784; 2.
DR   TIGRFAMs; TIGR01662; HAD-SF-IIIA; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Lipid biosynthesis; Lipid metabolism; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Phospholipid biosynthesis;
KW   Phospholipid metabolism; Reference proteome.
FT   CHAIN           1..209
FT                   /note="Probable phosphatidylglycerophosphatase,
FT                   mitochondrial"
FT                   /id="PRO_0000351427"
FT   MOTIF           57..61
FT                   /note="Phosphoryl acceptor"
SQ   SEQUENCE   209 AA;  23992 MW;  DD99C64B73CF1043 CRC64;
     MLINIEGIQA FCQTIRNPRR IIPHATFPTF SQIPCNINYF LEQKFQVPVD IRALVLDKDN
     CITLPNETTI AEAELKKIRE FQNIYGEKNV ILLSNSIGTR KLDPTGELAA HFQQKWNIPV
     VRHSKLKPLC TEELYTYLSN NSHVSSASQI LFIGDRLLTD ITLANIMGSW GVWLTRGVGN
     TTNMMMEVES WLYKRIHTQN PYIPTNRKS