ID A0A1G5DK66_9FIRM Unreviewed; 340 AA.
AC A0A1G5DK66;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=SAMN05660668_01591 {ECO:0000313|EMBL:SCY14957.1};
OS Pseudobutyrivibrio sp. AR14.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Pseudobutyrivibrio.
OX NCBI_TaxID=1520804 {ECO:0000313|EMBL:SCY14957.1, ECO:0000313|Proteomes:UP000198746};
RN [1] {ECO:0000313|EMBL:SCY14957.1, ECO:0000313|Proteomes:UP000198746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR14 {ECO:0000313|EMBL:SCY14957.1,
RC ECO:0000313|Proteomes:UP000198746};
RA de Groot N.N.;
RL Submitted (OCT-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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FMUY01000007; SCY14957.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5DK66; -.
DR OrthoDB; 7191982at2; -.
DR Proteomes; UP000198746; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 57..210
FT /note="Phosphatidylinositol-specific phospholipase C X"
FT /evidence="ECO:0000259|SMART:SM00148"
SQ SEQUENCE 340 AA; 39073 MW; DF5FE6D117410400 CRC64;
MSKGRFFRII CGIMILIISV ILVQVFVSDD NNGGDELGDQ GMQPGYYDPS RWMESLSDDT
YLSEITIPGT HDSAARYVML GYVMRCQDTS IYEQLDNGYR YLDLRIALDK SQKEHRIKLV
HNFANCHVDG GLFSDYLHLE DVTKDIYTFL QKYNDETVIV NFKIEDDEVN VKEIQKLLNQ
EITSNKDYWF TEEYIPTLGE ARGRAVLATR FDDIAGTGVT GLNMIWAEQD NKTPVDIPYE
LYVNDEFRYW VQDRYKYSVE DKYEAVVDGL ENCEADEDTW FLNFVSTSGD GKIGHPKGYA
NSLNGLLMDY SFKENTSYGI IIVDFGNADL AKKIYLTNSF
//
