PLD_ARCHD
ID PLD_ARCHD Reviewed; 309 AA.
AC Q59121; D7BPG4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Phospholipase D {ECO:0000250|UniProtKB:P20626};
DE Short=PLD {ECO:0000250|UniProtKB:P20626};
DE Short=PLD-A;
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; OrderedLocusNames=Arch_1099;
OS Arcanobacterium haemolyticum (strain ATCC 9345 / DSM 20595 / CCUG 17215 /
OS LMG 16163 / NBRC 15585 / NCTC 8452 / 11018).
OC Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae;
OC Arcanobacterium.
OX NCBI_TaxID=644284;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8406819; DOI=10.1128/iai.61.10.4310-4316.1993;
RA Cuevas W.A., Songer J.G.;
RT "Arcanobacterium haemolyticum phospholipase D is genetically and
RT functionally similar to Corynebacterium pseudotuberculosis phospholipase
RT D.";
RL Infect. Immun. 61:4310-4316(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9345 / DSM 20595 / CCUG 17215 / LMG 16163 / NBRC 15585 / NCTC
RC 8452 / 11018;
RX PubMed=21304742; DOI=10.4056/sigs.1123072;
RA Yasawong M., Teshima H., Lapidus A., Nolan M., Lucas S.,
RA Glavina Del Rio T., Tice H., Cheng J.F., Bruce D., Detter C., Tapia R.,
RA Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA Mikhailova N., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA Chang Y.J., Jeffries C.D., Rohde M., Sikorski J., Pukall R., Goker M.,
RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Arcanobacterium haemolyticum type strain
RT (11018).";
RL Stand. Genomic Sci. 3:126-135(2010).
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 -!- SEQUENCE CAUTION:
CC Sequence=AAA21882.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=ADH92813.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L16583; AAA21882.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002045; ADH92813.1; ALT_INIT; Genomic_DNA.
DR PIR; I39484; I39484.
DR RefSeq; WP_041640381.1; NC_014218.1.
DR AlphaFoldDB; Q59121; -.
DR EnsemblBacteria; ADH92813; ADH92813; Arch_1099.
DR KEGG; ahe:Arch_1099; -.
DR eggNOG; ENOG502ZB0H; Bacteria.
DR HOGENOM; CLU_059400_0_0_11; -.
DR OMA; WLDLKNP; -.
DR OrthoDB; 697975at2; -.
DR Proteomes; UP000000376; Chromosome.
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; Reference proteome; Signal;
KW Virulence.
FT SIGNAL 1..26
FT /evidence="ECO:0000250|UniProtKB:P20626"
FT CHAIN 27..309
FT /note="Phospholipase D"
FT /id="PRO_0000022065"
FT ACT_SITE 46
FT /evidence="ECO:0000255"
SQ SEQUENCE 309 AA; 34663 MW; C34AC5B947A21725 CRC64;
MKTRKKIALA LSLLTGFMLP IGSAAAAPLA QEQPTTGNRP VYAIAHRVLT KQSVDDAIKI
GANALEIDFT AWRRGWWADH DGLPTSAGDT AEDILKYIAQ KRREGNNITF VWFDIKNPDY
CKDQNSVCSI TKLRDLARQT IEQEGVRALF GFYKTVGGVG WNTIANNLND KEAVALSGRK
DDIMKDFKQY ENKIKPQQRV ADNGYYNLSY GFGGCYRDEN QTCDQLRLAG EERKKGNLGK
TFGWTVSTGQ EYLAADLLNK AEVDGMIFGF KTTYFYDHAD TRNAFAGIKN WVDAHQGTHH
MATNKDIPW
