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Database: UniProt
Entry: A0A158K6R1_9BURK
LinkDB: A0A158K6R1_9BURK
Original site: A0A158K6R1_9BURK 
ID   A0A158K6R1_9BURK        Unreviewed;       183 AA.
AC   A0A158K6R1;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE            EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN   ORFNames=AWB66_05464 {ECO:0000313|EMBL:SAL76685.1};
OS   Caballeronia telluris.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=326475 {ECO:0000313|EMBL:SAL76685.1, ECO:0000313|Proteomes:UP000054717};
RN   [1] {ECO:0000313|EMBL:SAL76685.1, ECO:0000313|Proteomes:UP000054717}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 22936 {ECO:0000313|EMBL:SAL76685.1};
RA   Oliw E.H.;
RL   Submitted (JAN-2016) 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; FCNZ02000030; SAL76685.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A158K6R1; -.
DR   STRING; 326475.AWB66_05464; -.
DR   Proteomes; UP000054717; 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:SAL76685.1};
KW   Hydrolase {ECO:0000313|EMBL:SAL76685.1};
KW   Nuclease {ECO:0000313|EMBL:SAL76685.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054717};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..183
FT                   /note="phospholipase D"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011108641"
FT   DOMAIN          118..145
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
SQ   SEQUENCE   183 AA;  19257 MW;  081D10D2D5C534D5 CRC64;
     MKFRIAVISA ALIGALSFSA TAPAVAADDV QVAFSPNGGA EALVLKTINS ARSSIRVLAY
     SFTAAPVVKA LLAAKHRGVD VAVTVDYKNN IEQDRSGKAA AALNALSYAG VPVRVVRVFP
     IQHSKLIVID QATVETGSYN YSQAAARVNS ENVLVISNRP DIARAYLANW SEVTALGEAY
     RAP
//
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