ID A0A0E0FGX0_ORYNI Unreviewed; 812 AA.
AC A0A0E0FGX0;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Phospholipase D {ECO:0000256|ARBA:ARBA00012027, ECO:0000256|PIRNR:PIRNR036470};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027, ECO:0000256|PIRNR:PIRNR036470};
OS Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4536 {ECO:0000313|EnsemblPlants:ONIVA01G05180.2};
RN [1] {ECO:0000313|EnsemblPlants:ONIVA01G05180.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA01G05180.2};
RA Wing R.A., Hsing Y.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ONIVA01G05180.2}
RP IDENTIFICATION.
RC STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA01G05180.2};
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal
CC phosphodiesteric bond. {ECO:0000256|PIRNR:PIRNR036470}.
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 ECO:0000256|PIRNR:PIRNR036470};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913,
CC ECO:0000256|PIRNR:PIRNR036470};
CC -!- SIMILARITY: Belongs to the phospholipase D family. C2-PLD subfamily.
CC {ECO:0000256|ARBA:ARBA00010683, ECO:0000256|PIRNR:PIRNR036470}.
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DR AlphaFoldDB; A0A0E0FGX0; -.
DR EnsemblPlants; ONIVA01G05180.2; ONIVA01G05180.2; ONIVA01G05180.
DR Gramene; ONIVA01G05180.2; ONIVA01G05180.2; ONIVA01G05180.
DR HOGENOM; CLU_004684_0_0_1; -.
DR Proteomes; UP000006591; 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:SF115; PHOSPHOLIPASE D ALPHA 2; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF12357; PLD_C; 1.
DR Pfam; PF00614; PLDc; 2.
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 Calcium {ECO:0000256|PIRNR:PIRNR036470};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR036470};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR036470};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR036470};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000006591}.
FT DOMAIN 1..130
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 330..368
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 658..685
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 812 AA; 92218 MW; 0D15D7A2E8B31ED0 CRC64;
MAQMLLHGTL HATIFEAASL SNPHRASGSA PKFIRKFVEG IEDTVGVGKG ATKVYSTIDL
EKARVGRTRM ITNEPINPRW YESFHIYCAH MASNVIFTVK IDNPIGATNI GRAYLPVQEL
LNGEEIDRWL DICDNNREPV GESKIHVKLQ YFDVSKDRNW ARGVRSTKYP GVPYTFFSQR
QGCKVTLYQD AHVPDNFIPK IPLADGKNYE PHRCWEDIFD AISNAQHLIY ITGWSVYTKI
TLVRDSNRPK PGGDVTLGEL LKKKASEGVR VLMLVWDDRT SVGLLKRDGL MATHDEETEN
YFHGSDVNCV LCPRNPDDSG SIVQDLSIST MFTHHQKIVV VDHELPNQGS QQRRIVSFVG
GLDLCDGRYD TQYHSLFRTL DSTHHDDFHQ PNFATASIKK GGPREPWHDI HSRLEGPIAW
DVLYNFEQRW RKQGGKDLLL QLRDLSDTII PPSPVMFPED RETWNVQLFR SIDGGAAFGF
PDTPEEAAKA GLVSGKDQII DRSIQDAYIH AIRRAKNFIY IENQYFLGSS YAWKPEGIKP
EDIGALHLIP KELALKVVSK IEAGERFTVY VVVPMWPEGV PESGSVQAIL DWQRRTMEMM
YTDITEALQA KGIEANPKDY LTFFCLGNRE VKQAGEYQPE EQPEADTDYS RAQEARRFMI
YVHTKMMIVD DEYIIIGSAN INQRSMDGAR DSEIAMGGYQ PYHLATRQPA RGQIHGFRMA
LWYEHLGMLD DVFQRPESLE CVQKVNRIAE KYWDMYSSDD LQQDLPGHLL SYPIGVASDG
VVTELPGMEY FPDTRARVLG AKSDYMPPIL TS
//
