ID B2VUU3_PYRTR Unreviewed; 512 AA.
AC B2VUU3;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 57.
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=PTRG_01080 {ECO:0000313|EMBL:EDU40518.1};
OS Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS (Drechslera tritici-repentis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=426418 {ECO:0000313|EMBL:EDU40518.1, ECO:0000313|Proteomes:UP000001471};
RN [1] {ECO:0000313|Proteomes:UP000001471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pt-1C-BFP {ECO:0000313|Proteomes:UP000001471};
RX PubMed=23316438; DOI=10.1534/g3.112.004044;
RA Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT repentis, reveals transduplication and the impact of repeat elements on
RT pathogenicity and population divergence.";
RL G3 (Bethesda) 3:41-63(2013).
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}.
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DR EMBL; DS231615; EDU40518.1; -; Genomic_DNA.
DR RefSeq; XP_001931413.1; XM_001931378.1.
DR AlphaFoldDB; B2VUU3; -.
DR STRING; 426418.B2VUU3; -.
DR EnsemblFungi; EDU40518; EDU40518; PTRG_01080.
DR GeneID; 6339287; -.
DR eggNOG; KOG3964; Eukaryota.
DR HOGENOM; CLU_030471_1_1_1; -.
DR InParanoid; B2VUU3; -.
DR OMA; HKCLAQC; -.
DR OrthoDB; 179003at2759; -.
DR UniPathway; UPA00084; UER00503.
DR Proteomes; UP000001471; Unassembled WGS sequence.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:EnsemblFungi.
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:EnsemblFungi.
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 PIRSF; PIRSF000850; Phospholipase_D_PSS; 3.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 1.
DR PROSITE; PS50035; PLD; 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:UP000001471};
KW Transferase {ECO:0000256|RuleBase:RU365024, ECO:0000313|EMBL:EDU40518.1}.
FT DOMAIN 147..173
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 408..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 512 AA; 56470 MW; 33D84612CD27F866 CRC64;
MAASTPQSQA SMLATITSDL DRIAPRFEMR PEQIEIIQTP AEFYETLKSK ISKAKYRIYL
STLYIGKTEH ELISTIRTAL HDNPNLHVSF LTDALRGTRE TPDPCSASLM SPLISEFGPG
RVEVRLYHTP NLTGLRKSYI PKRINEGWGL QHMKLYGVDD EIIMSGANLS EDYFTNRQDR
YHLFRSKELT DYFAKIHDGV AKLSFDVQPS NKEGSGGYMM DWPKSNVAPS PLDSPSKYKD
AAAKHLAPLL TPANSPTTPS SPSPSPSTTA IYPILSLVPL IPTSTELPAL TSILTHLTTP
PFQNSSWTFT AGYFNMTPSF RRLLLSTRPA TGTVLTAHPH ANGFYGSKGV SGMLPAAYTH
LAKSFLRRVK YEGLSENVVL KEWKKGMVGE KDGWTYHAKG LWVTFPSSAS SSSSTTPPPP
SSAPGEKASQ DPSLAVIGSS NYTKRAYRLD LEANVVIATT DPGLRRRLAQ EVEWLGKYAR
AVDEKVFETP ERKVGLDVRL AMWAVRVLGG AL
//
