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Database: UniProt
Entry: A0A085JNE0_9GAMM
LinkDB: A0A085JNE0_9GAMM
Original site: A0A085JNE0_9GAMM 
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
//
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