PGPS1_SACPS
ID PGPS1_SACPS Reviewed; 521 AA.
AC P79001;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase;
DE EC=2.7.8.5;
DE AltName: Full=Phosphatidylglycerophosphate synthase;
DE Short=PGP synthase;
GN Name=PGS1; Synonyms=PEL1, YCLUN3W;
OS Saccharomyces pastorianus (Lager yeast) (Saccharomyces cerevisiae x
OS Saccharomyces eubayanus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=27292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Andersen T., Nilsson-Tillgren T.;
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Essential for the viability of mitochondrial petite mutant.
CC Catalyzes the committed step to the synthesis of the acidic
CC phospholipids (By similarity). {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 -!- 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; Z86109; CAB06796.1; -; Genomic_DNA.
DR AlphaFoldDB; P79001; -.
DR SMR; P79001; -.
DR UniPathway; UPA00084; UER00503.
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 InterPro; IPR016270; PGS1.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR PANTHER; PTHR12586; PTHR12586; 1.
DR Pfam; PF00614; PLDc; 1.
DR SMART; SM00155; PLDc; 2.
DR PROSITE; PS50035; PLD; 1.
PE 3: Inferred from homology;
KW ATP-binding; Lipid biosynthesis; Lipid metabolism; Mitochondrion;
KW Nucleotide-binding; Phospholipid biosynthesis; Phospholipid metabolism;
KW Repeat; Transferase.
FT CHAIN 1..521
FT /note="CDP-diacylglycerol--glycerol-3-phosphate 3-
FT phosphatidyltransferase"
FT /id="PRO_0000056826"
FT DOMAIN 177..203
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 182
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 184
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT BINDING 91..98
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 521 AA; 59354 MW; 1E28ABDDB2231302 CRC64;
MTTRLLQLTR PHYRLLSSPF RKSSIIQRQM SASSPSPANS YLNMITKSLQ HNLQTWFHFE
PNEIDIIESP SHFYDLLKSK ISSSQKRIFI ASLYLGKSET ELIDCISQAL SKNPDLKVSF
LLDGLRGTRE LPSTCSATLL SSLVAKYGSE RVDCRLYKTP AYHGWKKIVV PKRFNEGLGL
QHMKIYGFDN EIILSGANLS NDYFTNRQDR YYLFKSANFA NYYFKLHQLI SSFSYQIVKP
KVAGNVNIIW PDSNPTIEPM KNKRKFLREA SQLLENFLQI SKHNQPISPP GQFSTIVYPI
SQFTPLFPKY NDKSTEKSTI LSLLSNIKNT SISWTFTAGY FNILPEIKAN LLATPVTEAN
VITASPFANG FYQSKGVSSN LPGAYLYLSK KFLQDVSRYN KDQAITLREW QRGVVNKPNG
WSYHAKGIWI SSRDNNDSDS WKPFITVIGS SNYTRRAYSL DLESNALIIT KDEELRNKMK
GELNDLLQYT KPVTLEDFKS DPERHVGTGV KIATSVLGKK L
