ID A0A0B4XPC3_9GAMM Unreviewed; 541 AA.
AC A0A0B4XPC3;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=S7S_12670 {ECO:0000313|EMBL:AJD48946.1};
OS Isoalcanivorax pacificus W11-5.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Alcanivoracaceae; Isoalcanivorax.
OX NCBI_TaxID=391936 {ECO:0000313|EMBL:AJD48946.1, ECO:0000313|Proteomes:UP000006764};
RN [1] {ECO:0000313|EMBL:AJD48946.1, ECO:0000313|Proteomes:UP000006764}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W11-5 {ECO:0000313|EMBL:AJD48946.1,
RC ECO:0000313|Proteomes:UP000006764};
RX PubMed=23209202; DOI=10.1128/JB.01845-12;
RA Lai Q., Shao Z.;
RT "Genome sequence of an alkane-degrading bacterium, Alcanivorax pacificus
RT type strain W11-5, isolated from deep sea sediment.";
RL J. Bacteriol. 194:6936-6936(2012).
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};
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DR EMBL; CP004387; AJD48946.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B4XPC3; -.
DR STRING; 391936.S7S_12670; -.
DR KEGG; apac:S7S_12670; -.
DR HOGENOM; CLU_037497_0_0_6; -.
DR Proteomes; UP000006764; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.80.10.50; -; 2.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR PANTHER; PTHR35518:SF2; MAINTENANCE OF TELOMERE CAPPING PROTEIN 6; 1.
DR PANTHER; PTHR35518; MAINTENANCE OF TELOMOERE CAPPING; 1.
DR Pfam; PF00388; PI-PLC-X; 1.
DR Pfam; PF00652; Ricin_B_lectin; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF51695; PLC-like phosphodiesterases; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 4: Predicted;
KW Lectin {ECO:0000313|EMBL:AJD48946.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000006764};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 287..325
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
SQ SEQUENCE 541 AA; 60442 MW; 0BAFA6FA5AC73D3F CRC64;
MLCLLSTAAF ATPVEDFRNS WNYEALAHQR TLEMGEPLGQ TSFQYTHNSY NSVAYQNLGS
YWDPNHQVSV VDQLDLGIRA LELDVHWAYS KLILCHGTSD HTGCSTFDRH FEDGIKEIAT
WLERPENNDQ VILIYIEEHV DSEHDRAVDI LDLHLGDRIY RPGSCRTLPM DITRADMIND
GKQVLLIGGD CSTTRWAQTV FNYGFPTGND SFAPYPLCTI SGRTQQFVQT NLVRIFEDGT
NLSATFGNPP PPTTPQRMAE AMQCNLGIVG LDHLVPFDSR LAAAVWSWGE NEPNNSGGNE
HCAEQRADGR FNDVNCGQSR RAACQADDGS WMVTAASVTW AQAASTCTAE FGSTYQFQVP
RNGFSNQKLK EARDSAGATV VWLNYSDLAS EGEWLPVNYP VVQPPEPPAE PVWRKLRNDH
GRCLDLEDRS TADGTEIHHW SCHGADSQLW WHDPQGRLRA KSAPDKCADV SGSGTSEGTR
VVLWPCHSGD NQVWTRGASN SFRPAHAPHR ALDIKDPLWG NGQRAHLWTF HGGKSQRWSW
D
//
