ID A0A318IX91_9BURK Unreviewed; 613 AA.
AC A0A318IX91;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
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=DFR42_11289 {ECO:0000313|EMBL:PXX38577.1};
OS Undibacterium pigrum.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Undibacterium.
OX NCBI_TaxID=401470 {ECO:0000313|EMBL:PXX38577.1, ECO:0000313|Proteomes:UP000247792};
RN [1] {ECO:0000313|EMBL:PXX38577.1, ECO:0000313|Proteomes:UP000247792}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19792 {ECO:0000313|EMBL:PXX38577.1,
RC ECO:0000313|Proteomes:UP000247792};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAY-2018) 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:PXX38577.1}.
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DR EMBL; QJKB01000012; PXX38577.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A318IX91; -.
DR OrthoDB; 7191982at2; -.
DR Proteomes; UP000247792; 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;
FT DOMAIN 143..298
FT /note="Phosphatidylinositol-specific phospholipase C X"
FT /evidence="ECO:0000259|SMART:SM00148"
SQ SEQUENCE 613 AA; 68510 MW; C3F2F0F7756524D4 CRC64;
MTSTVAVYQH SAKQPERYFY DKLDYNNQDW TAGTLAFGAC ATPVPGTISI YTQVATNPYR
NRFSTQPEAD GEWSQGEFAF YAYTSQQPGT VPIYQHLAAS PARYLYDTLE DGRGIWGAGK
TVFYAAPPLV SWRRHWMGAL IAQTATAPLI TNVNLPGTHD TGTWAVVHEK ASKCQTMDLA
TQLAMGIRFI DIRLYPGTNP ATGQKDLKVW HGPTDCGIWF SDIVATCNQF LDGSLETIVM
SVKLESKEIF NTEFLQILED HFLANTWKIN APATRLFNVE ENAQNILATA GQIVLFRRYE
YDPADPARKH IGIDAAGWPD DDLTRMPTPK PVPKMIQDAY QFAVGTTAGK WAMVNDFLEM
AKADKNDVWY INFSSAAGGA YPSYYSDRVN PHLQEYMEKE VANASPVTKK YGSILMDFPT
PRMIDAIVAS NLYYDNKVLR PHRPYYFAVG STKDYALGQP HKVAGWNYPM AVTDTKVAHV
LIKINGTPGQ EGEIHVGDIV MIQCPQFTND IYIYIESKGS KNGDGIDLFY DQENAPEYGN
KNEVYWRVER NPGDSNQKSI IAPGDNVRFK SVSSTQDQYL CATTNAYLGA VDIKNYNPND
LIAGGFEFYL TVV
//