ID A0A0V1DCN4_TRIBR Unreviewed; 467 AA.
AC A0A0V1DCN4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase {ECO:0000256|RuleBase:RU365024};
DE EC=2.7.8.5 {ECO:0000256|RuleBase:RU365024};
GN Name=PGS1 {ECO:0000313|EMBL:KRY59308.1};
GN ORFNames=T03_15147 {ECO:0000313|EMBL:KRY59308.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY59308.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY59308.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY59308.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Functions in the biosynthesis of the anionic phospholipids
CC phosphatidylglycerol and cardiolipin. {ECO:0000256|RuleBase:RU365024}.
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:0000256|RuleBase:RU365024};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylglycerol biosynthesis;
CC phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
CC {ECO:0000256|RuleBase:RU365024}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|RuleBase:RU365024}.
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-II
CC family. {ECO:0000256|RuleBase:RU365024}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRY59308.1}.
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DR EMBL; JYDI01000013; KRY59308.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1DCN4; -.
DR UniPathway; UPA00084; UER00503.
DR Proteomes; UP000054653; Unassembled WGS sequence.
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; IPR025202; PLD-like_dom.
DR PANTHER; PTHR12586:SF1; CDP-DIACYLGLYCEROL--GLYCEROL-3-PHOSPHATE 3-PHOSPHATIDYLTRANSFERASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR12586; CDP-DIACYLGLYCEROL--SERINE O-PHOSPHATIDYLTRANSFERASE; 1.
DR Pfam; PF13091; PLDc_2; 2.
DR PIRSF; PIRSF000850; Phospholipase_D_PSS; 1.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU365024};
KW Lipid biosynthesis {ECO:0000256|RuleBase:RU365024};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|RuleBase:RU365024};
KW Mitochondrion {ECO:0000256|RuleBase:RU365024};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU365024};
KW Phospholipid biosynthesis {ECO:0000256|RuleBase:RU365024};
KW Phospholipid metabolism {ECO:0000256|RuleBase:RU365024};
KW Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW Transferase {ECO:0000256|RuleBase:RU365024, ECO:0000313|EMBL:KRY59308.1}.
FT DOMAIN 45..192
FT /note="Phospholipase D-like"
FT /evidence="ECO:0000259|Pfam:PF13091"
FT DOMAIN 292..431
FT /note="Phospholipase D-like"
FT /evidence="ECO:0000259|Pfam:PF13091"
SQ SEQUENCE 467 AA; 53730 MW; F4367D25E97DEB0F CRC64;
MLKVVAAKEK NMKEVGVMES IPTFKIRGNN VKIIESPAQF YEQLIVLVSQ SRYRVTLCSL
YIGTGEMERD LIASLRKAMN ANESLKVDIL LDFNRARRGN ENSCTMLSSL KHDYDYRVNV
ALFHSPMLRG PLKKFLSERV NEILGVQHMK VYLFDNFVLI SGSAYNRANL SHDYFTKRQD
RYILIESADL ANFYFDLIRA VSELSFQLNS DSEVILSPSC CHHPFSGSRS RYCQFLNAKI
KAVLSKWSQL HSLTADEDED TIVMPVVQFG AIGLFADREI INLIINNPSP SELFMATGYF
NLAPCYVNAL FESEKSCNLM IASPEANGFH GAEGLSGYVP DVYKNFSESF YRRMINKQVL
NRLQLFEYKR DDWTFHAKGI WLKVYSDNKV NASVIGSTNF GYRSLNRDLE TQIVLFTENE
QLKDQLTKEC DMLFYYCSAF KRPLTTYGNR QVPLFVSFIS RWLRSFL
//
