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CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase, mitochondrial (EC 2.7.8.5) (Phosphatidylglycerophosphate synthase 1) (PGP synthase 1)

 PGPS1_CRIGR             Reviewed;         553 AA.
Q9Z2Z7;
20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
27-SEP-2017, entry version 56.
RecName: Full=CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase, mitochondrial;
EC=2.7.8.5;
AltName: Full=Phosphatidylglycerophosphate synthase 1;
Short=PGP synthase 1;
Flags: Precursor;
Name=PGS1;
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Cricetidae; Cricetinae; Cricetulus.
NCBI_TaxID=10029;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
TISSUE=Ovary;
PubMed=9880566; DOI=10.1074/jbc.274.3.1828;
Kawasaki K., Kuge O., Chang S.-C., Heacock P.N., Rho M., Suzuki K.,
Nishijima M., Dowhan W.;
"Isolation of a chinese hamster ovary (CHO) cDNA encoding
phosphatidylglycerophosphate (PGP) synthase, expression of which
corrects the mitochondrial abnormalities of a PGP synthase-defective
mutant of CHO-K1 cells.";
J. Biol. Chem. 274:1828-1834(1999).
[2]
SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
PROPERTIES, AND ENZYME REGULATION.
PubMed=11171073; DOI=10.1042/0264-6021:3540009;
Kawasaki K., Kuge O., Yamakawa Y., Nishijima M.;
"Purification of phosphatidylglycerophosphate synthase from Chinese
hamster ovary cells.";
Biochem. J. 354:9-15(2001).
-!- FUNCTION: Functions in the biosynthesis of the anionic
phospholipids phosphatidylglycerol and cardiolipin.
{ECO:0000269|PubMed:9880566}.
-!- CATALYTIC ACTIVITY: CDP-diacylglycerol + sn-glycerol 3-phosphate =
CMP + 3(3-sn-phosphatidyl)-sn-glycerol 1-phosphate.
{ECO:0000269|PubMed:11171073, ECO:0000269|PubMed:9880566}.
-!- ENZYME REGULATION: Activated by calcium and magnesium and
inhibited by other bivalent cations.
{ECO:0000269|PubMed:11171073}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=288 uM for CDP-diacylglycerol {ECO:0000269|PubMed:11171073};
Vmax=13.6 umol/min/mg enzyme {ECO:0000269|PubMed:11171073};
-!- PATHWAY: Phospholipid metabolism; phosphatidylglycerol
biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step
1/2.
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11171073}.
-!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase
class-II family. {ECO:0000305}.
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EMBL; AB016930; BAA37113.1; -; mRNA.
RefSeq; NP_001233637.1; NM_001246708.1.
ProteinModelPortal; Q9Z2Z7; -.
SwissLipids; SLP:000000226; -.
GeneID; 100689449; -.
KEGG; cge:100689449; -.
CTD; 9489; -.
HOVERGEN; HBG057228; -.
KO; K00995; -.
BRENDA; 2.7.8.5; 1309.
UniPathway; UPA00084; UER00503.
GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
GO; GO:0005743; C:mitochondrial inner membrane; TAS:BHF-UCL.
GO; GO:0005739; C:mitochondrion; IDA:BHF-UCL.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005509; F:calcium ion binding; IDA:BHF-UCL.
GO; GO:0008444; F:CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase activity; IDA:BHF-UCL.
GO; GO:0032049; P:cardiolipin biosynthetic process; IMP:BHF-UCL.
GO; GO:0046339; P:diacylglycerol metabolic process; IDA:BHF-UCL.
GO; GO:0006655; P:phosphatidylglycerol biosynthetic process; IDA:BHF-UCL.
GO; GO:0008654; P:phospholipid biosynthetic process; IDA:HGNC.
InterPro; IPR016270; PGS1.
InterPro; IPR001736; PLipase_D/transphosphatidylase.
PANTHER; PTHR12586; PTHR12586; 1.
PROSITE; PS50035; PLD; 1.
1: Evidence at protein level;
ATP-binding; Lipid biosynthesis; Lipid metabolism; Mitochondrion;
Nucleotide-binding; Phospholipid biosynthesis;
Phospholipid metabolism; Phosphoprotein; Repeat; Transferase;
Transit peptide.
TRANSIT 1 25 Mitochondrion. {ECO:0000255}.
CHAIN 26 553 CDP-diacylglycerol--glycerol-3-phosphate
3-phosphatidyltransferase, mitochondrial.
/FTId=PRO_0000337106.
DOMAIN 212 238 PLD phosphodiesterase 1.
{ECO:0000255|PROSITE-ProRule:PRU00153}.
DOMAIN 457 490 PLD phosphodiesterase 2.
{ECO:0000255|PROSITE-ProRule:PRU00153}.
NP_BIND 121 128 ATP. {ECO:0000255}.
ACT_SITE 217 217 {ECO:0000255|PROSITE-ProRule:PRU00153}.
ACT_SITE 219 219 {ECO:0000255|PROSITE-ProRule:PRU00153}.
ACT_SITE 224 224 {ECO:0000255|PROSITE-ProRule:PRU00153}.
MOD_RES 46 46 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BHF7}.
SEQUENCE 553 AA; 62369 MW; B5422CF157995A28 CRC64;
MAAPAAGPVF WRRLLGLLPG RPGLAALLGR LSDRLGRSRE RRRRRSPWLL LAPLLSPTVP
QVTSPPCCLC PEGVHRFQWI RNLVPEFGVS SSHVRVLSSP AEFFELLKGQ IKMAKRRVVM
ASLYLGTGPL EQELVDCLES SLEKSLQSKF PSDLKVSILL DFTRGSRGRK NSRTMLLPLL
QRFPEHVRVS LFHTPNLRGL LRLLIPERFN ETIGLQHIKV YLFDNNVVLS GANLSDSYFT
NRQDRYVFLQ DCAEIADFFT ELVDAVGDVS LQLQGDDTVD VVDGMVHPYK GDRAAYCRAA
NKRVMDVIHS ARTRQQLLHA QTFHSDSLLS QEEAAAAGDR RPAPDTWIYP LIQMKPFEIQ
IDEIVTETLL TEAERGAKVF LTTGYFNLTQ AYMDLVLGTR AEYQILLASP EVNGFFGAKG
VAGAIPAAYV HIERQFYGEV CGLGQQDRVQ LQEYWRTGWT FHAKGLWLYL AGSSLPCLTL
IGSPNFGYRS VHRDLEAQIA IVTESRALQQ QLHQEQEQLY LRSSVVTSAT FEQPGRQVKL
WVKMVTPLIK NFF


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