ID   PGPS1_PONAB             Reviewed;         556 AA.
AC   Q5R8K7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   22-FEB-2023, entry version 63.
DE   RecName: Full=CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase, mitochondrial;
DE            EC=2.7.8.5;
DE   AltName: Full=Phosphatidylglycerophosphate synthase 1;
DE            Short=PGP synthase 1;
DE   Flags: Precursor;
GN   Name=PGS1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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   -!- ACTIVITY REGULATION: Activated by calcium and magnesium and inhibited
CC       by other bivalent cations. {ECO:0000250}.
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; CR859745; CAH91903.1; -; mRNA.
DR   RefSeq; NP_001126101.1; NM_001132629.1.
DR   AlphaFoldDB; Q5R8K7; -.
DR   SMR; Q5R8K7; -.
DR   STRING; 9601.ENSPPYP00000009757; -.
DR   GeneID; 100173056; -.
DR   KEGG; pon:100173056; -.
DR   CTD; 9489; -.
DR   eggNOG; KOG3964; Eukaryota.
DR   InParanoid; Q5R8K7; -.
DR   OrthoDB; 179003at2759; -.
DR   UniPathway; UPA00084; UER00503.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008444; F:CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032049; P:cardiolipin biosynthetic process; IEA:InterPro.
DR   CDD; cd09135; PLDc_PGS1_euk_1; 1.
DR   CDD; cd09137; PLDc_PGS1_euk_2; 1.
DR   Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR   InterPro; IPR016270; PGS1.
DR   InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR   PANTHER; PTHR12586:SF1; CDP-DIACYLGLYCEROL--GLYCEROL-3-PHOSPHATE 3-PHOSPHATIDYLTRANSFERASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR12586; CDP-DIACYLGLYCEROL--SERINE O-PHOSPHATIDYLTRANSFERASE; 1.
DR   PIRSF; PIRSF000850; Phospholipase_D_PSS; 1.
DR   SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR   PROSITE; PS50035; PLD; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Lipid biosynthesis; Lipid metabolism; Mitochondrion;
KW   Nucleotide-binding; Phospholipid biosynthesis; Phospholipid metabolism;
KW   Phosphoprotein; Reference proteome; Repeat; Transferase; Transit peptide.
FT   TRANSIT         1..28
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..556
FT                   /note="CDP-diacylglycerol--glycerol-3-phosphate 3-
FT                   phosphatidyltransferase, mitochondrial"
FT                   /id="PRO_0000337108"
FT   DOMAIN          215..241
FT                   /note="PLD phosphodiesterase 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT   DOMAIN          460..493
FT                   /note="PLD phosphodiesterase 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT   ACT_SITE        220
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT   ACT_SITE        222
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT   ACT_SITE        227
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT   BINDING         124..131
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         49
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BHF7"
SQ   SEQUENCE   556 AA;  62701 MW;  9F49F37C7152AF8C CRC64;
     MAVAAAAAAG PVFWRRLLGL LPGRPGLAAL LGRLSDRLGR NRDRQRRRSP WLLLAPLLSP
     AVPQVTSPPC CLCPEGVHRF QWIRNLVPEF GVSSSHVRVL SSPAESFELM KGQIRVAKRR
     VVMASLYLGT GPLEQELVDC LESTLEKSLQ AKFPSNLKVS ILLDFTRGSR GRKNSRTMLL
     PLPQRFPEQV RVSLFHTPHL RGLLRLLIPE RFNETIGLQH IKVYLFDNSV ILSGANLSDS
     YFTNRQDRYV FLQDCAEIAD FFTELVDAVG DVSLQLQGDD TVQVVDGMVH PYKGDRTEYC
     KAANKRVMDV INSARTRQQM LHAQTFHSNS LLTQEDAAAA GDRRPAPDTW IYPLIQMKPF
     EIQIDEIVTE TLLTEAERGA KVYLTTGYFN LTQAYMDLVL GTRAEYQILL ASPEVNGFFG
     AKGVVGAIPA AYVHIERQFY SEVCSLGQQE RVQLQEYWRR GWTFHAKGLW LYLAGSSLPC
     LTLIGSPNFG YRSVHRDLEA QIAIVTENEA LQQQLHQEQE QLYLRSGVVS SATFEQPSRQ
     VKLWVKMVTP LIKNFF
//