ID A0A1B6BIW8_9FIRM Unreviewed; 469 AA.
AC A0A1B6BIW8;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=1-phosphatidylinositol phosphodiesterase {ECO:0000256|ARBA:ARBA00019758};
DE EC=4.6.1.13 {ECO:0000256|ARBA:ARBA00012581};
DE AltName: Full=Phosphatidylinositol diacylglycerol-lyase {ECO:0000256|ARBA:ARBA00030474};
DE AltName: Full=Phosphatidylinositol-specific phospholipase C {ECO:0000256|ARBA:ARBA00030782};
GN ORFNames=F3D3_4317 {ECO:0000313|EMBL:GAU79653.1};
OS Fusibacter sp. 3D3.
OC Bacteria; Bacillota; Clostridia; Eubacteriales;
OC Eubacteriales Family XII. Incertae Sedis; Fusibacter.
OX NCBI_TaxID=1048380 {ECO:0000313|EMBL:GAU79653.1, ECO:0000313|Proteomes:UP000095197};
RN [1] {ECO:0000313|EMBL:GAU79653.1, ECO:0000313|Proteomes:UP000095197}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D3 {ECO:0000313|EMBL:GAU79653.1,
RC ECO:0000313|Proteomes:UP000095197};
RA Serrano A.E., Escudero L.V., Encalada O., Tebes C.J., Fernandez S.,
RA Demergasso C.S.;
RT "Draft genome sequence of Fusibacter ascotence 3D3 isolated from the high
RT arsenic level Ascotan salt flat in northern Chile.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) = 1D-myo-
CC inositol 1,2-cyclic phosphate + a 1,2-diacyl-sn-glycerol;
CC Xref=Rhea:RHEA:17093, ChEBI:CHEBI:17815, ChEBI:CHEBI:57880,
CC ChEBI:CHEBI:58484; EC=4.6.1.13;
CC Evidence={ECO:0000256|ARBA:ARBA00001316};
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:GAU79653.1}.
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DR EMBL; BDHH01000027; GAU79653.1; -; Genomic_DNA.
DR RefSeq; WP_069876390.1; NZ_BDHH01000027.1.
DR AlphaFoldDB; A0A1B6BIW8; -.
DR STRING; 1048380.F3D3_4317; -.
DR OrthoDB; 7191982at2; -.
DR Proteomes; UP000095197; Unassembled WGS sequence.
DR GO; GO:0004436; F:phosphatidylinositol diacylglycerol-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR PANTHER; PTHR13593:SF148; SI:DKEY-152B24.6-RELATED; 1.
DR PANTHER; PTHR13593; UNCHARACTERIZED; 1.
DR Pfam; PF00388; PI-PLC-X; 1.
DR SMART; SM00148; PLCXc; 1.
DR SUPFAM; SSF51695; PLC-like phosphodiesterases; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
PE 4: Predicted;
KW Lyase {ECO:0000313|EMBL:GAU79653.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000095197}.
FT DOMAIN 196..341
FT /note="Phosphatidylinositol-specific phospholipase C X"
FT /evidence="ECO:0000259|SMART:SM00148"
SQ SEQUENCE 469 AA; 53484 MW; 2205BCEE8EC250EF CRC64;
MKYHDNEVYF SCGSKANFTL VNGTYRISSC SITEGQDPKQ KSRSGNLYNF SSDGKLNFQV
GRKASKEVAD WLNRNITIDN STFGHSADEL NFAFLGILRI KLKNLYALGT ETTIEFENIA
IAQGNTSGRN NWWFGGRNCF NTNDNNCVHA IGKADDGTYY CAMIRRGGNA VNTYEVKSVE
KIQPNWMANL NGALKLSQLS IPGTHDSGTK LVQLPATEYR PLGIKIPNMG LARCQNFSIR
AQLYHGIRFL DIRLKYVNHS LMLFHGPYSR CELSFRQVLD WCNHYLHDFK KETILMSVKA
EDGEISDAFR MIMEKYTELF LKSKVIPTLD EARGKIVLFS RINYPDNGIQ LYNGWEENTQ
FAISTKDYTF EIEDHFNINE SIKDNLVQKN IINAAKDMEA AHYYLTFNSL AQLLENTPYL
HSQGLNKKLL LYLKQQGGDE KVGTILMDYY NNHGELGENE LVETIISRN
//
