PGPS1_CRIGR
ID PGPS1_CRIGR Reviewed; 553 AA.
AC Q9Z2Z7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 75.
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 Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC TISSUE=Ovary;
RX PubMed=9880566; DOI=10.1074/jbc.274.3.1828;
RA Kawasaki K., Kuge O., Chang S.-C., Heacock P.N., Rho M., Suzuki K.,
RA Nishijima M., Dowhan W.;
RT "Isolation of a chinese hamster ovary (CHO) cDNA encoding
RT phosphatidylglycerophosphate (PGP) synthase, expression of which corrects
RT the mitochondrial abnormalities of a PGP synthase-defective mutant of CHO-
RT K1 cells.";
RL J. Biol. Chem. 274:1828-1834(1999).
RN [2]
RP SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP AND ACTIVITY REGULATION.
RX PubMed=11171073; DOI=10.1042/0264-6021:3540009;
RA Kawasaki K., Kuge O., Yamakawa Y., Nishijima M.;
RT "Purification of phosphatidylglycerophosphate synthase from Chinese hamster
RT ovary cells.";
RL Biochem. J. 354:9-15(2001).
CC -!- FUNCTION: Functions in the biosynthesis of the anionic phospholipids
CC phosphatidylglycerol and cardiolipin. {ECO:0000269|PubMed:9880566}.
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:11171073, ECO:0000269|PubMed:9880566};
CC -!- ACTIVITY REGULATION: Activated by calcium and magnesium and inhibited
CC by other bivalent cations. {ECO:0000269|PubMed:11171073}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=288 uM for CDP-diacylglycerol {ECO:0000269|PubMed:11171073};
CC Vmax=13.6 umol/min/mg enzyme {ECO:0000269|PubMed:11171073};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylglycerol biosynthesis;
CC phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11171073}.
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-II
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB016930; BAA37113.1; -; mRNA.
DR RefSeq; NP_001233637.1; NM_001246708.1.
DR AlphaFoldDB; Q9Z2Z7; -.
DR SMR; Q9Z2Z7; -.
DR STRING; 10029.NP_001233637.1; -.
DR SwissLipids; SLP:000000226; -.
DR Ensembl; ENSCGRT00001024102; ENSCGRP00001019858; ENSCGRG00001019173.
DR GeneID; 100689449; -.
DR KEGG; cge:100689449; -.
DR CTD; 9489; -.
DR eggNOG; KOG3964; Eukaryota.
DR GeneTree; ENSGT00390000002373; -.
DR OrthoDB; 1358866at2759; -.
DR BRENDA; 2.7.8.5; 1309.
DR UniPathway; UPA00084; UER00503.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:BHF-UCL.
DR GO; GO:0005739; C:mitochondrion; IDA:BHF-UCL.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IDA:BHF-UCL.
DR GO; GO:0008444; F:CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase activity; IDA:BHF-UCL.
DR GO; GO:0032049; P:cardiolipin biosynthetic process; IMP:BHF-UCL.
DR GO; GO:0046339; P:diacylglycerol metabolic process; IDA:BHF-UCL.
DR GO; GO:0006655; P:phosphatidylglycerol biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IDA:HGNC-UCL.
DR InterPro; IPR016270; PGS1.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR PANTHER; PTHR12586; PTHR12586; 1.
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 Phosphoprotein; Repeat; Transferase; Transit peptide.
FT TRANSIT 1..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 26..553
FT /note="CDP-diacylglycerol--glycerol-3-phosphate 3-
FT phosphatidyltransferase, mitochondrial"
FT /id="PRO_0000337106"
FT DOMAIN 212..238
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT DOMAIN 457..490
FT /note="PLD phosphodiesterase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 217
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 219
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 224
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT BINDING 121..128
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BHF7"
SQ 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
