ID A0A9D5BSZ5_9LILI Unreviewed; 811 AA.
AC A0A9D5BSZ5;
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_001847 {ECO:0000313|EMBL:KAJ0960329.1};
OS Dioscorea zingiberensis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Dioscoreales; Dioscoreaceae;
OC Dioscorea.
OX NCBI_TaxID=325984 {ECO:0000313|EMBL:KAJ0960329.1, ECO:0000313|Proteomes:UP001085076};
RN [1] {ECO:0000313|EMBL:KAJ0960329.1, ECO:0000313|Proteomes:UP001085076}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Dzin_1.0 {ECO:0000313|EMBL:KAJ0960329.1};
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:KAJ0960329.1}.
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DR EMBL; JAGGNH010000089; KAJ0960329.1; -; Genomic_DNA.
DR OrthoDB; 14911at2759; -.
DR Proteomes; UP001085076; Unassembled WGS sequence.
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 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..367
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 657..684
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 811 AA; 92106 MW; 2AF093E736EAB739 CRC64;
MAQILLHGNL HATIFEADSL TNPGRASGSA PRFLRQFVEG IEDTIGIGKG SSKVYATIDL
EKARVGRTRR ISDEPENPRW YEAFHIYCAH FAANVIFTVK FDNAIGASLV GRAYLPVREI
LTSEEVDRWL EICDEKRNPV GSAKIHVKVQ FFDVSQERNW ARGIRSPKYP GVPYTFFSQR
QGCKVSFYQD AHVPDNFFPK IPLADGKYYE PQRCWEDIFD AITNAQHLIY ITGWSVYTEI
TLVRDSRRQR PGGDVTLGEL LKRKASEGVR VLMLVWDDRT SVGLLKKDGL MATHDEETAN
YFLGTDVHCV LCPRNPDDGG SIVQNLQIST MFTHHQKIVV VDHEMPKTSQ QRRIVSFVGG
IDLCDGRYDT QFHSLFRTLD TAHHNDFHQP NFTGASIRKG GPREPWHDIH SKLEGPIAWD
VLYNFEQRWR KQGGKDLLVQ LRDLADIIIP PSPVMFPEDR ETWNVQLFRS IDGGAAFGFP
DTPEGAARVG LVSGKDNIID RSIQDAYINA IRRAKKFIYI ENQYFLGSSF GWKADGIRPE
EVGALHLIPK ELSLKIVSKI EAGERFSVYV VVPMWPEGVP ESASVQAILD WQRRTMEMMY
TDIIEALQAK GIIANPKDYL TFFCLGNREV KTSGEYAPEE QPEPDTDYSK AQQARRFMIY
VHTKMMIVDD EYIIVGSANI NQRSMDGARD SEIAMGAYQP YHLSTKQPAR GHIHGFRMAL
WYEHLGMLDD VFLQPESMDC VHKVNTIADK YWDIYSSDRL DHDLPGHLLS YPIAVTNEGV
VTELPGMECF PDTKARVLGT KTDYLPPILT T
//
