ID A0A9D5CQV8_9LILI Unreviewed; 812 AA.
AC A0A9D5CQV8;
DT 03-MAY-2023, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2023, sequence version 1.
DT 18-JUN-2025, entry version 10.
DE RecName: Full=Phospholipase D {ECO:0000256|PIRNR:PIRNR036470};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR036470};
GN ORFNames=J5N97_013247 {ECO:0000313|EMBL:KAJ0977773.1};
OS Dioscorea zingiberensis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Dioscoreales; Dioscoreaceae;
OC Dioscorea.
OX NCBI_TaxID=325984 {ECO:0000313|EMBL:KAJ0977773.1, ECO:0000313|Proteomes:UP001085076};
RN [1] {ECO:0000313|EMBL:KAJ0977773.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Dzin_1.0 {ECO:0000313|EMBL:KAJ0977773.1};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAJ0977773.1};
RA Li Z., Yang C.;
RL Submitted (MAR-2021) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAJ0977773.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Dzin_1.0 {ECO:0000313|EMBL:KAJ0977773.1};
RX PubMed=36204203;
RA Li Y., Tan C., Li Z., Guo J., Li S., Chen X., Wang C., Dai X., Yang H.,
RA Song W., Hou L., Xu J., Tong Z., Xu A., Yuan X., Wang W., Yang Q., Chen L.,
RA Sun Z., Wang K., Pan B., Chen J., Bao Y., Liu F., Qi X., Gang D.R., Wen J.,
RA Li J.;
RT "The genome of Dioscorea zingiberensis sheds light on the biosynthesis,
RT origin and evolution of the medicinally important diosgenin saponins.";
RL Hortic Res 9:0-0(2022).
CC -!- FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal
CC phosphodiesteric bond. Plays an important role in various cellular
CC processes. {ECO:0000256|ARBA:ARBA00056354}.
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}.
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:KAJ0977773.1}.
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DR EMBL; JAGGNH010000003; KAJ0977773.1; -; Genomic_DNA.
DR OrthoDB; 14911at2759; -.
DR Proteomes; UP001085076; Miscellaneous, Linkage group lg03.
DR GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004630; F:phospholipase D activity; IEA:InterPro.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:InterPro.
DR GO; GO:0009395; P:phospholipid catabolic process; IEA:TreeGrafter.
DR CDD; cd04015; C2_plant_PLD; 1.
DR CDD; cd09199; PLDc_pPLDalpha_2; 1.
DR FunFam; 3.30.870.10:FF:000027; Phospholipase D; 1.
DR FunFam; 3.30.870.10:FF:000025; Phospholipase D delta; 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 1; 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|ARBA:ARBA00022837, 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:ARBA00023098};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP001085076};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
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; 92231 MW; 8AA6FA05A9D20CFC CRC64;
MAQILLHGTL HATIFEANSL SDPGRTSGGA PRFLRQIVEG IEDTIGLGKG SSKVYATIDL
EKARVGRTRL ITNEPVNPRW YESFHIYCAH SAASVIFTVK FDNPIGASLV GRAYLPVEEI
LDGEEVDRWL DICDEDRNPV GEAKIHVKLQ YFDVSKDRNW ARGIRSTKFP GVPYTFFSQR
QGCKVSFYQD AHVPDNFIPK IPLADGKYYD PHRCWEDIFD AITNAQHLIY ITGWSVYTEI
TLVRDSNRQK PGGDVKLGDL LKRKASEGVR VLMLVWDDRT SVGLLKKDGL MATHDEETAK
FFEGSDVHCV LCPRNPDDGG SFVQDLQIST MFTHHQKIVV VDHEMPTKSS QQRRIVSFVG
GIDLCDGRYD TQFHSLFRTL DTAHHDDFHQ PNFATASIKK GGPREPWHDI HSRLEGPIAW
DVLFNFEQRW RKQGGKDLLV ELRDLTDIIV PPSPVMFPED RETWNVQLFR SIDGGAAFGF
PETPEDAARA GLVSGKDNII DRSIQDAYIN AIRRAKNFIY IENQYFLGSS FGWKADDIKP
EEIGALHLIP KELSLKIVSK IEAGERFTVY IVVPMWPEGV PESASVQAIL DWQRRTLEMM
YTDIIEALQA KGIEANPKDY LAFFCLGNRE VKKSGEYTPE EQPEPDTDYS RAQEARRFMI
YVHTKMMIVD DEYIIIGSAN INQRSMDGAR DSEIAMGAYQ PYHLTTREPA RGQIHGFRLA
LWYEHLGMLD DVFLQPESVE CVQKVNRIAE KYWDLYSSES LEHDLPGHLL SYPITVTNEG
QVTELPGTEF FPDTKARILG TKTDYLPPIL TT
//
