ID   PLD_CORUL               Reviewed;         307 AA.
AC   Q59332;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Phospholipase D {ECO:0000250|UniProtKB:P20626};
DE            Short=PLD {ECO:0000250|UniProtKB:P20626};
DE            EC=3.1.4.- {ECO:0000250|UniProtKB:P20626};
DE   AltName: Full=Choline phosphatase;
DE   AltName: Full=Sphingomyelinase D {ECO:0000250|UniProtKB:P20626};
DE            Short=SMaseD {ECO:0000250|UniProtKB:P20626};
DE            EC=3.1.4.41 {ECO:0000250|UniProtKB:P20626};
DE   Flags: Precursor;
GN   Name=pld;
OS   Corynebacterium ulcerans.
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=65058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 739;
RX   PubMed=7737503; DOI=10.1016/0378-1119(95)00002-n;
RA   McNamara P.J., Cuevas W.A., Songer J.G.;
RT   "Toxic phospholipases D of Corynebacterium pseudotuberculosis, C. ulcerans
RT   and Arcanobacterium haemolyticum: cloning and sequence homology.";
RL   Gene 156:113-118(1995).
CC   -!- FUNCTION: Virulence factor affecting bacterial dissemination and
CC       survival within the host. Has magnesium-dependent catalytic activity
CC       toward sphingomyelin (SM) and acyl- and alkyl-lysophosphatidylcholine
CC       (LPC), but not toward sphingosylphosphorylcholine (SPC) and
CC       phosphatidylcholine (PC). Lysophosphatidic acid (LPA), assumed to
CC       result from LPC hydrolysis, evokes pathophysiological responses after
CC       LPA receptor internalization. Shows hemolytic activity.
CC       {ECO:0000250|UniProtKB:P20626}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a sphingomyelin + H2O = an N-acylsphing-4-enine 1-phosphate +
CC         choline + H(+); Xref=Rhea:RHEA:20984, ChEBI:CHEBI:15354,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17636,
CC         ChEBI:CHEBI:57674; EC=3.1.4.41;
CC         Evidence={ECO:0000250|UniProtKB:P20626};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = 1-(9Z-
CC         octadecenoyl)-sn-glycero-3-phosphate + choline + H(+);
CC         Xref=Rhea:RHEA:38915, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:28610, ChEBI:CHEBI:74544;
CC         Evidence={ECO:0000250|UniProtKB:P20626};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-O-hexadecyl-sn-glycero-3-phosphocholine + H2O = 1-O-
CC         hexadecyl-sn-glycero-3-phosphate + choline + H(+);
CC         Xref=Rhea:RHEA:41143, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:64496, ChEBI:CHEBI:77580;
CC         Evidence={ECO:0000250|UniProtKB:P20626};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P20626};
CC   -!- SIMILARITY: Belongs to the sphingomyelinase D/phospholipase D family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L16585; AAB68401.1; -; Genomic_DNA.
DR   RefSeq; WP_023634800.1; NZ_UFXR01000001.1.
DR   AlphaFoldDB; Q59332; -.
DR   SMR; Q59332; -.
DR   STRING; 65058.Cul210931_0042; -.
DR   eggNOG; ENOG502ZB0H; Bacteria.
DR   GO; GO:0050290; F:sphingomyelin phosphodiesterase D activity; IEA:UniProtKB-EC.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.190; -; 1.
DR   InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR   InterPro; IPR016674; SMase_D/PLipase_D.
DR   PIRSF; PIRSF016632; Phospholipase_actinobac/fun; 1.
DR   SUPFAM; SSF51695; SSF51695; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Lipid degradation; Lipid metabolism; Signal; Virulence.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000250|UniProtKB:P20626"
FT   CHAIN           25..307
FT                   /note="Phospholipase D"
FT                   /id="PRO_0000022067"
FT   ACT_SITE        44
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   307 AA;  33681 MW;  A315E3B2827A8732 CRC64;
     MKKKVVLFLS IIMGILFPVG NAVATPVSHD AASTGNRPVY AIAHRVLTTQ GVDDAVAIGA
     NALEIDFTAW RGGWWADHDG IPTSAGATAE AIFKHIAEKR NQGANITFTW LDIKNPDYCT
     DPHSVCSINA LRDLARKYLE PAGVRVLYGF YKTVGGPGWK TITSDLRDNE AVALSGPTRD
     VLNDFAKAGD KILTKQKIAD YGYYDINQGF GDCYGDGNKT CDQLRKSSEA RDQGKLGKTF
     GWTITTGQDD RVNDLLGKAH VDGMIFGFKV THFYRHADTE NSFKAIKTWV DKHSDTHHLA
     TAADNPW