ID A0A2S4VI39_9BASI Unreviewed; 548 AA.
AC A0A2S4VI39;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
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 ORFNames=PSTT_07064 {ECO:0000313|EMBL:POW09149.1};
OS Puccinia striiformis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=27350 {ECO:0000313|EMBL:POW09149.1, ECO:0000313|Proteomes:UP000239156};
RN [1] {ECO:0000313|EMBL:POW09149.1, ECO:0000313|Proteomes:UP000239156}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-210 {ECO:0000313|EMBL:POW09149.1,
RC ECO:0000313|Proteomes:UP000239156};
RA Xia C.;
RT "Gene loss provides genomic basis for host adaptation in cereal stripe rust
RT fungi.";
RL Submitted (DEC-2017) 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|ARBA:ARBA00001566,
CC ECO:0000256|RuleBase:RU365024};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylglycerol biosynthesis;
CC phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
CC {ECO:0000256|ARBA:ARBA00005042, 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|ARBA:ARBA00010682, 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:POW09149.1}.
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DR EMBL; PKSL01000058; POW09149.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S4VI39; -.
DR VEuPathDB; FungiDB:PSHT_07054; -.
DR VEuPathDB; FungiDB:PSTT_07064; -.
DR UniPathway; UPA00084; UER00503.
DR Proteomes; UP000239156; 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; IPR001736; PLipase_D/transphosphatidylase.
DR PANTHER; PTHR12586:SF1; CDP-DIACYLGLYCEROL--GLYCEROL-3-PHOSPHATE 3-PHOSPHATIDYLTRANSFERASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR12586; CDP-DIACYLGLYCEROL--SERINE O-PHOSPHATIDYLTRANSFERASE; 1.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU365024};
KW Lipid biosynthesis {ECO:0000256|RuleBase:RU365024};
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:UP000239156};
KW Transferase {ECO:0000256|RuleBase:RU365024}.
FT DOMAIN 179..205
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|SMART:SM00155"
FT DOMAIN 431..474
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|SMART:SM00155"
SQ SEQUENCE 548 AA; 63385 MW; 1C8FC48C0C908842 CRC64;
MRFKPTSRPV LRVPQPTNLR RLNHHCTEYR SSAEPRDIDG LVNHLSSNLP YFRSPQDSIK
VLNEPAQFYH EILNLINKAK KRIFIASLYV GKEEINLIEA LGKALETNPD LKLTILVDYL
RTTREHNKPR VQGEICCSAS LLKRLLKTRF GSRVEIRLFH TSELYGTLKK LIPRRFDEGF
GLQHMKIYGS DNDIIMSGAN LSTDYFTNRQ DRYVMLTDQE GLSEYLSELI EITSSISYRL
IEGKGEELEI IWPDSNPCQP PISSRSASQQ FKKIANLLYT EFTDRWRAKS LSLIGDHNHL
HPRIPSVSIF PTLQMSPFKI HHETHLMIPQ LINFVNRPLS SHNHSPPKSK IVLNWTSGYF
SLLREYKKSM LESNGLVQII TASPQANGFY NSKGVSKYIP LAYSYLENLF RTEIRKSNKE
DQILIRRWNR NGWTYHAKGL WINELNKTEP GNKEEEEERC LVNSIGSSNY GRRSAERDLE
CNLFIVLDDP PTLPSHPERS NKTDDCPLSI QLVNELHHLK SHVSNNDQSH QHVGIFVKLF
TRLIRTML
//
