PGPS1_BOVIN
ID PGPS1_BOVIN Reviewed; 556 AA.
AC Q2KJ28;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 92.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BC105551; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BC105551; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001039860.2; NM_001046395.2.
DR RefSeq; XP_005221295.1; XM_005221238.3.
DR RefSeq; XP_005221296.1; XM_005221239.3.
DR RefSeq; XP_005221297.1; XM_005221240.3.
DR RefSeq; XP_005221298.1; XM_005221241.3.
DR RefSeq; XP_005221299.1; XM_005221242.3.
DR RefSeq; XP_010814866.1; XM_010816564.2.
DR RefSeq; XP_015314464.1; XM_015458978.1.
DR RefSeq; XP_015314465.1; XM_015458979.1.
DR AlphaFoldDB; Q2KJ28; -.
DR SMR; Q2KJ28; -.
DR STRING; 9913.ENSBTAP00000000897; -.
DR PaxDb; Q2KJ28; -.
DR PRIDE; Q2KJ28; -.
DR Ensembl; ENSBTAT00000000897; ENSBTAP00000000897; ENSBTAG00000000675.
DR Ensembl; ENSBTAT00000072446; ENSBTAP00000071736; ENSBTAG00000000675.
DR GeneID; 535126; -.
DR KEGG; bta:535126; -.
DR CTD; 9489; -.
DR VEuPathDB; HostDB:ENSBTAG00000000675; -.
DR VGNC; VGNC:32803; PGS1.
DR eggNOG; KOG3964; Eukaryota.
DR GeneTree; ENSGT00390000002373; -.
DR HOGENOM; CLU_030471_1_2_1; -.
DR InParanoid; Q2KJ28; -.
DR OMA; YLSTLYI; -.
DR OrthoDB; 1492at2759; -.
DR TreeFam; TF314768; -.
DR UniPathway; UPA00084; UER00503.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000000675; Expressed in neutrophil and 104 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
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; IBA:GO_Central.
DR GO; GO:0032049; P:cardiolipin biosynthetic process; IBA:GO_Central.
DR InterPro; IPR016270; PGS1.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR PANTHER; PTHR12586; PTHR12586; 1.
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_0000337104"
FT DOMAIN 215..241
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT DOMAIN 419..457
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; 62732 MW; B5BFE926E0906B00 CRC64;
MAAAAAAAAG PVFWRRLLGL LPGRPGLAAL LGRLSDRLGR NPDRRRRRSP WLLLAPLLSP
AVPVVTSPPC CLCAEGVHRF QWIRNLVPEF GVSSSHVRVL SSPAEFFELM KGQIKVAKRR
VVMASLYLGI GPLEQELVDC LESTLEKSLQ AKFPSGLRVS ILLDFTRGSR GRKNSRTMLL
PLLQRFPEQV RVSLFHTPNL RGLLRLLIPE RFNETIGLQH IKVYLFDNNV ILSGANLSDS
YFTNRQDRYV FLQDCPEIAD FFTELVDAVG DVSLQLQGDD TVQMVEGMVH PYKGDRAAYC
RAANKRVMDV INSARMRQQM LHAQTFHSDP LLTQEDAAAA GDRRPAPDTW IYPLIQMKPF
EIQIDEIVTE TLLTEAERGA KVYLTTGYFN LTQAYMDLVL GTRAEYQILL ASPEVNGFFG
AKGVAGAIPA AYVHIERQFY SEVCSLGQQE RVQLQEYWRR DWTFHAKGLW LYLAGSSLPC
LTLIGSPNFG YRSVHRDLEA QIAIVTESRA LQQQLHQEQE QLYRRAGVVS SATFEQPSRQ
VKLWVKMVTP LIKNFF
