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Database: UniProt
Entry: M8DD29_9BACL
LinkDB: M8DD29_9BACL
Original site: M8DD29_9BACL 
ID   M8DD29_9BACL            Unreviewed;       267 AA.
AC   M8DD29;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-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=I532_01370 {ECO:0000313|EMBL:EMT54214.1};
OS   Brevibacillus borstelensis AK1.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX   NCBI_TaxID=1300222 {ECO:0000313|EMBL:EMT54214.1, ECO:0000313|Proteomes:UP000012081};
RN   [1] {ECO:0000313|EMBL:EMT54214.1, ECO:0000313|Proteomes:UP000012081}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK1 {ECO:0000313|EMBL:EMT54214.1,
RC   ECO:0000313|Proteomes:UP000012081};
RA   Rajan I., PoliReddy D., Sugumar T., Rathinam K., Alqarawi S., Khalil A.B.,
RA   Sivakumar N.;
RT   "Assembly of a new bacterial strain Brevibacillus borstelensis AK1.";
RL   Submitted (MAR-2013) 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   -!- 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:EMT54214.1}.
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DR   EMBL; APBN01000001; EMT54214.1; -; Genomic_DNA.
DR   RefSeq; WP_003385921.1; NZ_APBN01000001.1.
DR   AlphaFoldDB; M8DD29; -.
DR   STRING; 1300222.I532_01370; -.
DR   GeneID; 72733468; -.
DR   PATRIC; fig|1300222.3.peg.292; -.
DR   OrthoDB; 4376109at2; -.
DR   Proteomes; UP000012081; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006793; P:phosphorus metabolic process; IEA:UniProt.
DR   CDD; cd09170; PLDc_Nuc; 1.
DR   Gene3D; 3.40.10.10; DNA Methylphosphotriester Repair Domain; 1.
DR   Gene3D; 3.30.870.10; Endonuclease Chain A; 1.
DR   InterPro; IPR035451; Ada-like_dom_sf.
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; SSF57884; Ada DNA repair protein, N-terminal domain (N-Ada 10); 1.
DR   SUPFAM; SSF56024; Phospholipase D/nuclease; 1.
DR   PROSITE; PS50035; PLD; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000012081};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..267
FT                   /note="phospholipase D"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004095171"
FT   DOMAIN          120..147
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   REGION          195..221
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   267 AA;  28627 MW;  829E33914A855EAF CRC64;
     MRKIFTWILM ALLALSLVGT AIAAAVTSKT ASNKIEWAFT KADQKPENLL ISVINGAQTQ
     LDVAIYSLTH PDIVAAIKEA KKRGVNVRLI TDKQQAGGQS QTEALKILGS AGVPTKINSH
     SGLMHLKMVV ADKKIATTGS FNFSKAASTT NDEILMVLRD ETVAKSFAAE FERMWNDTKG
     FQTVEYRIAQ PGPVKPATAA PAAPANQVQK PAPAASKACD KPIIKGNKNS KIYHVPGGQS
     YDKTTANVEL FCTEAEAQAA GYRKAQK
//
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