ID A0A085JNE0_9GAMM Unreviewed; 177 AA.
AC A0A085JNE0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 22.
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:KFD21986.1};
GN ORFNames=GTPT_0560 {ECO:0000313|EMBL:KFD21986.1};
OS Tatumella ptyseos ATCC 33301.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Tatumella.
OX NCBI_TaxID=1005995 {ECO:0000313|EMBL:KFD21986.1, ECO:0000313|Proteomes:UP000028602};
RN [1] {ECO:0000313|EMBL:KFD21986.1, ECO:0000313|Proteomes:UP000028602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33301 {ECO:0000313|EMBL:KFD21986.1,
RC ECO:0000313|Proteomes:UP000028602};
RA Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.;
RT "ATOL: Assembling a taxonomically balanced genome-scale reconstruction of
RT the evolutionary history of the Enterobacteriaceae.";
RL Submitted (MAY-2014) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFD21986.1}.
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DR EMBL; JMPR01000010; KFD21986.1; -; Genomic_DNA.
DR RefSeq; WP_038010816.1; NZ_JMPR01000010.1.
DR AlphaFoldDB; A0A085JNE0; -.
DR eggNOG; COG1502; Bacteria.
DR OrthoDB; 5294698at2; -.
DR Proteomes; UP000028602; Unassembled WGS sequence.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
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 SUPFAM; SSF56024; Phospholipase D/nuclease; 1.
DR PROSITE; PS50035; PLD; 1.
PE 3: Inferred from homology;
KW Endonuclease {ECO:0000313|EMBL:KFD21986.1};
KW Hydrolase {ECO:0000313|EMBL:KFD21986.1};
KW Nuclease {ECO:0000313|EMBL:KFD21986.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000028602};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..177
FT /note="phospholipase D"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001793566"
FT DOMAIN 111..138
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 177 AA; 19687 MW; 8E36B1EA9184B3B3 CRC64;
MKKTILCIAG ILCSSVMFSA TAAEPSVDVG FSPEGSARTL VLETIASARS SIRMLSYSFT
APDIMRALAD ARRRGVDVKI VVDERGNRSK SSIAAMNFIV NSGIPLRTDH HYPIQHDKVI
IVDGQTVETG SFNYTASAER RNSENVVVIR NLPSLARTYL LHWQERWDYG QDYQSVY
//