ID F1CNM9_ECOLX Unreviewed; 187 AA.
AC F1CNM9;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN Name=nuc {ECO:0000313|EMBL:ADY00085.1};
GN ORFNames=RCS60_P0024 {ECO:0000313|EMBL:SPE01930.1};
OS Escherichia coli.
OG Plasmid RCS60_p {ECO:0000313|EMBL:SPE01930.1}, and
OG Plasmid pNDM-HK {ECO:0000313|EMBL:ADY00085.1}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562 {ECO:0000313|EMBL:ADY00085.1};
RN [1] {ECO:0000313|EMBL:ADY00085.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HK-01 {ECO:0000313|EMBL:ADY00085.1};
RC PLASMID=pNDM-HK {ECO:0000313|EMBL:ADY00085.1};
RX PubMed=21445317; DOI=10.1371/journal.pone.0017989;
RA Ho P.L., Lo W.U., Yeung M.K., Lin C.H., Chow K.H., Ang I., Tong A.H.,
RA Bao J.Y., Lok S., Lo J.Y.;
RT "Complete sequencing of pNDM-HK encoding NDM-1 carbapenemase from a
RT multidrug-resistant Escherichia coli strain isolated in Hong Kong.";
RL PLoS ONE 6:E17989-E17989(2011).
RN [2] {ECO:0000313|EMBL:SPE01930.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=676 {ECO:0000313|EMBL:SPE01930.1};
RC PLASMID=RCS60_p {ECO:0000313|EMBL:SPE01930.1};
RA Cohen D.B., Kent A.D.;
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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; HQ451074; ADY00085.1; -; Genomic_DNA.
DR EMBL; LT985279; SPE01930.1; -; Genomic_DNA.
DR RefSeq; WP_004187378.1; NZ_VYQD01000001.1.
DR RefSeq; YP_006952478.1; NC_019063.1.
DR AlphaFoldDB; F1CNM9; -.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-EC.
DR GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-EC.
DR GO; GO:0006793; P:phosphorus 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 Endonuclease {ECO:0000313|EMBL:ADY00085.1};
KW Hydrolase {ECO:0000313|EMBL:ADY00085.1};
KW Nuclease {ECO:0000313|EMBL:ADY00085.1};
KW Plasmid {ECO:0000313|EMBL:ADY00085.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..187
FT /note="phospholipase D"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015090397"
FT DOMAIN 121..148
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 187 AA; 19970 MW; 54FFA94C74491D60 CRC64;
MKKYVLLTLT LIAGAVAANP VTAAGNIAGD VQAQAATEVK TGFSPGGTAL NLVLDSIDHA
QHEILVAAYS LTSRPVAGAL RAAKKRGVSV VVVADRKAND NRYTEVNFLA NNRVAVRIND
NYEAMHDKFM VFDRRAVLTG SFNFSASADS RNAENVVLIS GAPAVTEAYV NEFSRLWGEG
KDVAPRY
//
