ID S9T6U4_9RALS Unreviewed; 190 AA.
AC S9T6U4;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN ORFNames=C404_29130 {ECO:0000313|EMBL:EPX94419.1};
OS Ralstonia sp. AU12-08.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=1235457 {ECO:0000313|EMBL:EPX94419.1, ECO:0000313|Proteomes:UP000015343};
RN [1] {ECO:0000313|EMBL:EPX94419.1, ECO:0000313|Proteomes:UP000015343}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU12-08 {ECO:0000313|EMBL:EPX94419.1,
RC ECO:0000313|Proteomes:UP000015343};
RX PubMed=24503988;
RA Zhang L., Morrison M., Rickard C.M.;
RT "Draft Genome Sequence of Ralstonia pickettii AU12-08, Isolated from an
RT Intravascular Catheter in Australia.";
RL Genome Announc. 2:e00027-14(2014).
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:EPX94419.1}.
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DR EMBL; ASZV01000064; EPX94419.1; -; Genomic_DNA.
DR RefSeq; WP_004636218.1; NZ_ASZV01000064.1.
DR AlphaFoldDB; S9T6U4; -.
DR GeneID; 61530043; -.
DR PATRIC; fig|1235457.3.peg.5776; -.
DR eggNOG; COG1502; Bacteria.
DR Proteomes; UP000015343; 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 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:EPX94419.1};
KW Hydrolase {ECO:0000313|EMBL:EPX94419.1};
KW Nuclease {ECO:0000313|EMBL:EPX94419.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..190
FT /note="phospholipase D"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004557049"
FT DOMAIN 123..150
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 190 AA; 20778 MW; 1DC8B6F3D6FC62F0 CRC64;
MTPRRLPLFV PGLVLASTVA LSPIGSYAEG VSLQNTGTVT VYFSPAGGAA DAIARSIEAA
HTRVWLAGYE FTHPRIARAL AQAADPRRHV DVRVVLDQEN VRSSYSVATY LAHAGVPVRI
DWTHPRMHQK TVVIDDNIVG LGSMNFTRAG DEKNSENWNV FRGNPQLAQL YAQAFLQLHA
QSTPYQSKGQ
//
