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
//