ID S8EBW0_9LAMI Unreviewed; 846 AA.
AC S8EBW0;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
DE Flags: Fragment;
GN ORFNames=M569_01343 {ECO:0000313|EMBL:EPS73398.1};
OS Genlisea aurea.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lentibulariaceae; Genlisea.
OX NCBI_TaxID=192259 {ECO:0000313|EMBL:EPS73398.1, ECO:0000313|Proteomes:UP000015453};
RN [1] {ECO:0000313|EMBL:EPS73398.1, ECO:0000313|Proteomes:UP000015453}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23855885;
RA Leushkin E.V., Sutormin R.A., Nabieva E.R., Penin A.A., Kondrashov A.S.,
RA Logacheva M.D.;
RT "The miniature genome of a carnivorous plant Genlisea aurea contains a low
RT number of genes and short non-coding sequences.";
RL BMC Genomics 14:476-476(2013).
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SIMILARITY: Belongs to the phospholipase D family. C2-PLD subfamily.
CC {ECO:0000256|ARBA:ARBA00010683}.
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:EPS73398.1}.
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DR EMBL; AUSU01000436; EPS73398.1; -; Genomic_DNA.
DR AlphaFoldDB; S8EBW0; -.
DR OrthoDB; 3014064at2759; -.
DR Proteomes; UP000015453; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-EC.
DR GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-EC.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:InterPro.
DR CDD; cd04015; C2_plant_PLD; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR InterPro; IPR024632; PLipase_D_C.
DR InterPro; IPR015679; PLipase_D_fam.
DR InterPro; IPR011402; PLipase_D_pln.
DR PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR PANTHER; PTHR18896:SF60; PHOSPHOLIPASE D; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF12357; PLD_C; 1.
DR Pfam; PF00614; PLDc; 1.
DR PIRSF; PIRSF036470; PLD_plant; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50035; PLD; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022963};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000015453}.
FT DOMAIN 1..136
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 356..391
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 688..715
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EPS73398.1"
SQ SEQUENCE 846 AA; 96489 MW; 12A7C7F33C61FE4B CRC64;
NNDTIYLHGD LHLKIIEARR LPNMDIVTSH LRRLFAAMTV CRRPTASDNH KHRKKIVTSD
PYVTVCLARA RVARTRIISN SQNPVWNEDF KIPVSHPVSQ VEFEVKDNDV FGADLIGVAS
VSARRIAAGN LIEEWVPLIG AWGKPHKPNS ALRLRIEFTP CSQNPLFLKG ITDDYSLKES
YFPLRHGCSL TLYQDAHLPD GMLPEIPLEN GGNFQHEKCW EDICHAIVEA HHLVYIVGWS
IYHKVRLVRE PTRPLPRGGD LNLGDLLKYK SQEGVRVLLL VWDDKTSHNK FFINTSGVMQ
THDEETKKFF KHSSVTCVLA PRYASSKLSI FKQQACNSWD HTNFYLIYIY MLVVGTIYTH
HQKCVIVDTQ GPGNNRKITA FLGGLDLCDG RYDTPEHRLF RDLDTVFEDD YHNPTFSPGT
KGPRQPWHDL HCKIEGPAAH DVLANFEQRW KKAAKWGRRF KKISHWHDDS LLKVERISWI
NSPSSSTPND HPSLWVCSED DPENWHVQIF RSIDSGSLKG FPKTAQAAEQ QNLVFAKNLV
IDKSIQMAYI QAIRSAQHYI YIENQYFLGS SYAWPSYKNA GADNSIPMEL ALKIASKIKS
KERFAVYIVI PMWPEGSPSS ASVQEILYWQ TQTMQMMYEV IARELKSGGM KDGRPTDYLN
FYCLGNREDR STESSGMVES VSERRGRFMI YVHAKGLIVD DEYVILGSAN INQRSMAGSR
DTEIAMGGYQ PHYTWRRKKK HPVGQVYGYR MSLWAEHLGT VENEERLMEA EDLECVRYVN
QVAESNWRIY TAAKYSRPLQ GHILKYPITV DGDDGKVSPL VGYENFPDVG GKVLGAPSNI
PDALTT
//
