ID   P84147_STRSM            Unreviewed;       506 AA.
AC   P84147;
DT   13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2004, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   SubName: Full=Phospholipase D {ECO:0000313|PDB:1V0R};
DE            EC=3.1.4.4 {ECO:0000313|PDB:1V0R};
OS   Streptomyces sp. (strain PMF).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=172564 {ECO:0000313|PDB:1V0R};
RN   [1] {ECO:0007829|PDB:1F0I}
RP   X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 4-504, AND DISULFIDE BONDS.
RX   PubMed=10873862; DOI=10.1016/S0969-2126(00)00150-7;
RA   Leiros I., Secundo F., Zambonelli C., Servi S., Hough E.;
RT   "The first crystal structure of a phospholipase D.";
RL   Structure 8:655-667(2000).
RN   [2] {ECO:0007829|PDB:1V0R, ECO:0007829|PDB:1V0S}
RP   X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS), DISULFIDE BONDS, AND ACTIVE SITE.
RX   PubMed=15165852; DOI=10.1016/j.jmb.2004.04.003;
RA   Leiros I., McSweeney S., Hough E.;
RT   "The reaction mechanism of phospholipase D from Streptomyces sp. strain
RT   PMF. Snapshots along the reaction pathway reveal a pentacoordinate reaction
RT   intermediate and an unexpected final product.";
RL   J. Mol. Biol. 339:805-820(2004).
RN   [3] {ECO:0007829|PDB:8CTP, ECO:0007829|PDB:8CTQ}
RP   X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS), AND DISULFIDE BONDS.
RX   PubMed=37217787; DOI=10.1038/s41557-023-01214-0;
RA   Tei R., Bagde S.R., Fromme J.C., Baskin J.M.;
RT   "Activity-based directed evolution of a membrane editor in mammalian
RT   cells.";
RL   Nat. Chem. 15:1030-1039(2023).
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DR   PDB; 1F0I; X-ray; 1.40 A; A=3-506.
DR   PDB; 1V0R; X-ray; 1.70 A; A=1-506.
DR   PDB; 1V0S; X-ray; 1.75 A; A=1-506.
DR   PDB; 1V0T; X-ray; 1.53 A; A=1-506.
DR   PDB; 1V0U; X-ray; 1.42 A; A=1-506.
DR   PDB; 1V0V; X-ray; 1.70 A; A=1-506.
DR   PDB; 1V0W; X-ray; 1.35 A; A=1-506.
DR   PDB; 1V0Y; X-ray; 1.71 A; A=1-506.
DR   PDB; 8CTP; X-ray; 1.90 A; A=1-506.
DR   PDB; 8CTQ; X-ray; 1.85 A; A=1-506.
DR   PDBsum; 1F0I; -.
DR   PDBsum; 1V0R; -.
DR   PDBsum; 1V0S; -.
DR   PDBsum; 1V0T; -.
DR   PDBsum; 1V0U; -.
DR   PDBsum; 1V0V; -.
DR   PDBsum; 1V0W; -.
DR   PDBsum; 1V0Y; -.
DR   AlphaFoldDB; P84147; -.
DR   SMR; P84147; -.
DR   BindingDB; P84147; -.
DR   DrugBank; DB07898; (2R)-3-[(tetrahydroxyphosphoranyl)oxy]-1,2-propanediyl dibutanoate.
DR   BRENDA; 3.1.4.4; 1284.
DR   EvolutionaryTrace; P84147; -.
DR   GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-EC.
DR   GO; GO:0030572; F:phosphatidyltransferase activity; IEA:UniProt.
DR   GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-EC.
DR   GO; GO:0032049; P:cardiolipin biosynthetic process; IEA:UniProt.
DR   CDD; cd09108; PLDc_PMFPLD_like_1; 1.
DR   CDD; cd09109; PLDc_PMFPLD_like_2; 1.
DR   Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR   InterPro; IPR025202; PLD-like_dom.
DR   InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR   PANTHER; PTHR21248; CARDIOLIPIN SYNTHASE; 1.
DR   PANTHER; PTHR21248:SF22; PHOSPHOLIPASE D; 1.
DR   Pfam; PF13091; PLDc_2; 2.
DR   SMART; SM00155; PLDc; 2.
DR   SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR   PROSITE; PS50035; PLD; 2.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:1F0I, ECO:0007829|PDB:1V0R};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          162..184
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          435..462
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   ACT_SITE        167
FT                   /note="EMO_00115 covalently attached,EMO_00115 covalently
FT                   attached,EMO_00058 nucleofuge,EMO_00054 nucleophile"
FT                   /evidence="ECO:0007829|PDB:1V0Y"
FT   ACT_SITE        440
FT                   /note="EMO_00040 increase nucleophilicity,EMO_00068 proton
FT                   donor,EMO_00066 proton acceptor"
FT                   /evidence="ECO:0007829|PDB:1V0Y"
FT   SITE            199
FT                   /note="EMO_00033 electrostatic stabiliser,EMO_00158
FT                   modifies pKa,EMO_00033 electrostatic stabiliser,EMO_00158
FT                   modifies pKa"
FT                   /evidence="ECO:0007829|PDB:1V0Y"
FT   SITE            465
FT                   /note="EMO_00033 electrostatic stabiliser,EMO_00040
FT                   increase nucleophilicity,EMO_00033 electrostatic
FT                   stabiliser"
FT                   /evidence="ECO:0007829|PDB:1V0Y"
FT   DISULFID        52..58
FT                   /evidence="ECO:0007829|PDB:1F0I, ECO:0007829|PDB:1V0R"
FT   DISULFID        224..243
FT                   /evidence="ECO:0007829|PDB:1F0I, ECO:0007829|PDB:1V0R"
FT   DISULFID        295..341
FT                   /evidence="ECO:0007829|PDB:1F0I, ECO:0007829|PDB:1V0R"
FT   DISULFID        415..504
FT                   /evidence="ECO:0007829|PDB:1F0I, ECO:0007829|PDB:1V0R"
SQ   SEQUENCE   506 AA;  54005 MW;  C7420055940CBF27 CRC64;
     ADSATPHLDA VEQTLRQVSP GLEGDVWERT SGNKLDGSAA DPSDWLLQTP GCWGDDKCAD
     RVGTKRLLAK MTENIGNATR TVDISTLAPF PNGAFQDAIV AGLKESAAKG NKLKVRILVG
     AAPVYHMNVI PSKYRDELTA KLGKAAENIT LNVASMTTSK TAFSWNHSKI LVVDGQSALT
     GGINSWKDDY LDTTHPVSDV DLALTGPAAG SAGRYLDTLW TWTCQNKSNI ASVWFAASGN
     AGCMPTMHKD TNPKASPATG NVPVIAVGGL GVGIKDVDPK STFRPDLPTA SDTKCVVGLH
     DNTNADRDYD TVNPEESALR ALVASAKGHI EISQQDLNAT CPPLPRYDIR LYDALAAKMA
     AGVKVRIVVS DPANRGAVGS GGYSQIKSLS EISDTLRNRL ANITGGQQAA KTAMCSNLQL
     ATFRSSPNGK WADGHPYAQH HKLVSVDSST FYIGSKNLYP SWLQDFGYIV ESPEAAKQLD
     AKLLDPQWKY SQETATVDYA RGICNA
//