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Database: UniProt
Entry: G2FWB4_9FIRM
LinkDB: G2FWB4_9FIRM
Original site: G2FWB4_9FIRM 
ID   G2FWB4_9FIRM            Unreviewed;       340 AA.
AC   G2FWB4;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE            EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN   ORFNames=DOT_4017 {ECO:0000313|EMBL:EGW38073.1};
OS   Desulfosporosinus sp. OT.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfosporosinus.
OX   NCBI_TaxID=913865 {ECO:0000313|EMBL:EGW38073.1, ECO:0000313|Proteomes:UP000004928};
RN   [1] {ECO:0000313|EMBL:EGW38073.1, ECO:0000313|Proteomes:UP000004928}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OT {ECO:0000313|EMBL:EGW38073.1,
RC   ECO:0000313|Proteomes:UP000004928};
RX   PubMed=21994931; DOI=10.1128/JB.06018-11;
RA   Abicht H.K., Mancini S., Karnachuk O.V., Solioz M.;
RT   "Genome Sequence of Desulfosporosinus sp. OT, an Acidophilic Sulfate-
RT   Reducing Bacterium from Copper Mining Waste in Norilsk, Northern Siberia.";
RL   J. Bacteriol. 193:6104-6105(2011).
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:EGW38073.1}.
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DR   EMBL; AGAF01000178; EGW38073.1; -; Genomic_DNA.
DR   RefSeq; WP_009621506.1; NZ_AGAF01000178.1.
DR   AlphaFoldDB; G2FWB4; -.
DR   PATRIC; fig|913865.3.peg.3703; -.
DR   eggNOG; COG1502; Bacteria.
DR   OrthoDB; 1792714at2; -.
DR   Proteomes; UP000004928; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR   InterPro; IPR025202; PLD-like_dom.
DR   PANTHER; PTHR43856; CARDIOLIPIN HYDROLASE; 1.
DR   PANTHER; PTHR43856:SF1; MITOCHONDRIAL CARDIOLIPIN HYDROLASE; 1.
DR   Pfam; PF13091; PLDc_2; 2.
DR   SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
FT   DOMAIN          58..166
FT                   /note="Phospholipase D-like"
FT                   /evidence="ECO:0000259|Pfam:PF13091"
FT   DOMAIN          213..335
FT                   /note="Phospholipase D-like"
FT                   /evidence="ECO:0000259|Pfam:PF13091"
SQ   SEQUENCE   340 AA;  38151 MW;  01B93AF722BE512D CRC64;
     MSKRRFVFSI LFLPLFSILL LSGCSFKIPK LAPKVAPISK LPAEALFIDK DAIYNRTIAL
     IESAQTSIYV EQAEFDDPRL IQLLLTKSRS GIDVRILLDQ WQKVNHGTLD LLKSQNVSIQ
     FYPAQKGQID HTKYMIIDQS RAIIYGPPWT ASGLLAHDLA VELSGRSAWK TATLFSKDWE
     FTTTFPLTVA KTSLLPEDNI VLALNANVKQ QLTEQILTST KSIWIENSEI TEPDLKQSLI
     DAAAKGRDVR IIVNQTNANK TSDTLAELKE NGVHIRYYPK QPDLGMNLAI FDNSSFILSS
     SGWTFNSFVT NHEFSITVPS PTASDKLGQV FNQDWERSID
//
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