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Database: UniProt
Entry: E3DFD0_ERWSE
LinkDB: E3DFD0_ERWSE
Original site: E3DFD0_ERWSE 
ID   E3DFD0_ERWSE            Unreviewed;       175 AA.
AC   E3DFD0;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE            EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN   OrderedLocusNames=EJP617_05020 {ECO:0000313|EMBL:ADP10183.1};
OS   Erwinia sp. (strain Ejp617).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=215689 {ECO:0000313|EMBL:ADP10183.1, ECO:0000313|Proteomes:UP000006865};
RN   [1] {ECO:0000313|EMBL:ADP10183.1, ECO:0000313|Proteomes:UP000006865}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ejp617 {ECO:0000313|EMBL:ADP10183.1,
RC   ECO:0000313|Proteomes:UP000006865};
RX   PubMed=21075933; DOI=10.1128/JB.01246-10;
RA   Park D.H., Thapa S.P., Choi B.S., Kim W.S., Hur J.H., Cho J.M., Lim J.S.,
RA   Choi I.Y., Lim C.K.;
RT   "Complete genome sequence of Japanese Erwinia strain Ejp617, a bacterial
RT   shoot blight pathogen of pear.";
RL   J. Bacteriol. 193:586-587(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-
CC         sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:14445,
CC         ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57643, ChEBI:CHEBI:58608; EC=3.1.4.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00000798};
CC   -!- SIMILARITY: Belongs to the phospholipase D family.
CC       {ECO:0000256|ARBA:ARBA00008664}.
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DR   EMBL; CP002124; ADP10183.1; -; Genomic_DNA.
DR   RefSeq; WP_012666958.1; NC_017445.1.
DR   AlphaFoldDB; E3DFD0; -.
DR   STRING; 215689.EJP617_05020; -.
DR   KEGG; erj:EJP617_05020; -.
DR   PATRIC; fig|215689.3.peg.537; -.
DR   HOGENOM; CLU_080814_3_0_6; -.
DR   OMA; VICDNEM; -.
DR   Proteomes; UP000006865; Chromosome.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0006796; P:phosphate-containing compound metabolic process; IEA:UniProt.
DR   CDD; cd09170; PLDc_Nuc; 1.
DR   Gene3D; 3.30.870.10; Endonuclease Chain A; 1.
DR   InterPro; IPR025202; PLD-like_dom.
DR   InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR   PANTHER; PTHR43856; CARDIOLIPIN HYDROLASE; 1.
DR   PANTHER; PTHR43856:SF1; MITOCHONDRIAL CARDIOLIPIN HYDROLASE; 1.
DR   Pfam; PF13091; PLDc_2; 1.
DR   SMART; SM00155; PLDc; 1.
DR   SUPFAM; SSF56024; Phospholipase D/nuclease; 1.
DR   PROSITE; PS50035; PLD; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..175
FT                   /note="phospholipase D"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003167675"
FT   DOMAIN          109..136
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
SQ   SEQUENCE   175 AA;  18998 MW;  0A9380837D3A1BA1 CRC64;
     MRKSIFFVLA IIMSPPAVAT DAPEISVGFS PSAGQAALQI VLSTINGAEQ SIDIAAYSFT
     SHPIAAALIA AQNRGVSVRL VADAKANNDK YTAVTFLTNQ DVPVRLNAQY IFMHNKFMVI
     DSNTVQTGSF NYTSNAAKRN AENVLLVRNA PALAAMYQQE FNRLWSESQG FDSLY
//
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