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Database: UniProt
Entry: A0A2I0BB84_9ASPA
LinkDB: A0A2I0BB84_9ASPA
Original site: A0A2I0BB84_9ASPA 
ID   A0A2I0BB84_9ASPA        Unreviewed;       901 AA.
AC   A0A2I0BB84;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   24-JAN-2024, entry version 27.
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};
GN   Name=PLDDELTA {ECO:0000313|EMBL:PKA65046.1};
GN   ORFNames=AXF42_Ash019058 {ECO:0000313|EMBL:PKA65046.1};
OS   Apostasia shenzhenica.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae;
OC   Apostasioideae; Apostasia.
OX   NCBI_TaxID=1088818 {ECO:0000313|EMBL:PKA65046.1, ECO:0000313|Proteomes:UP000236161};
RN   [1] {ECO:0000313|EMBL:PKA65046.1, ECO:0000313|Proteomes:UP000236161}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Shenzhen {ECO:0000313|Proteomes:UP000236161};
RC   TISSUE=Stem {ECO:0000313|EMBL:PKA65046.1};
RX   PubMed=28902843; DOI=10.1038/nature23897;
RA   Zhang G.Q., Liu K.W., Li Z., Lohaus R., Hsiao Y.Y., Niu S.C., Wang J.Y.,
RA   Lin Y.C., Xu Q., Chen L.J., Yoshida K., Fujiwara S., Wang Z.W., Zhang Y.Q.,
RA   Mitsuda N., Wang M., Liu G.H., Pecoraro L., Huang H.X., Xiao X.J., Lin M.,
RA   Wu X.Y., Wu W.L., Chen Y.Y., Chang S.B., Sakamoto S., Ohme-Takagi M.,
RA   Yagi M., Zeng S.J., Shen C.Y., Yeh C.M., Luo Y.B., Tsai W.C.,
RA   Van de Peer Y., Liu Z.J.;
RT   "The Apostasia genome and the evolution of orchids.";
RL   Nature 549:379-383(2017).
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   EMBL; KZ451898; PKA65046.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I0BB84; -.
DR   STRING; 1088818.A0A2I0BB84; -.
DR   OrthoDB; 3014064at2759; -.
DR   Proteomes; UP000236161; 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:SF153; 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   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:UP000236161}.
FT   DOMAIN          37..185
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          393..428
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          731..758
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
SQ   SEQUENCE   901 AA;  101655 MW;  F6FE17BF6D2EE28B CRC64;
     MSFLSSSAAS FQPLHLLLRF AGIPLMTFMA PTSDTKSMGN PPPPEAAAKV TFLHGDLEVW
     VREARSLPNM DLLSERMRRC FSVYGKCGAP LLGGGGGGGG GRRKIITSDP YVSVCLAGAT
     VARTRVIPNC EDPKWEEHFC VPVAHPISEI DFHVKDNDVF GAQLIGVVHI PVEKVVSGSS
     LDGWFPVVGH YSHTLKATPE LHVSLSFTPT TDNPLYRDGI GAGPDYLGVP NAYFPLRRGG
     GVTLYQDAHA PEDLLPKIEL EGGRFYEQSR CWEDICHAIL EAHHLIYIVG WSIYHKVRLV
     REPTKPLPNG GNLTLGELLK YKSQEGVRVL MLIWDDKTSH DKFLLRTDGV MHTHDEETRK
     FFRHSSVHCV LAPRYASSKL SIFKQQVSEV VGTLFTHHQK CVLVDTQASG NNRKITAFIG
     GLDLCDGRYD TPEHRLYRDV NTVFENDYHN PTFPVHGQAP RQPWHDLHCK IDGPAAHDIL
     TNFEQRWRKA TKWKDFKLRK VAHWHDDVLL KIERISWILT PSRNESEAHV CEENEPNSWH
     VQIFRSIDSG SVKGFPKHVP EAVTRNLICA KNLTIDKSIH NAYVKAIRSA QQFIYIENQY
     FLGSSYAWPS YKNAGADNLI PMELALKIVS KINAGERFTV YVVIPLWPEG APTAAAMQEI
     LFWQGQTMAM MYKVIGQALQ KSGLSEKYHP EDYLNFYCLG NREPATKETT STIHNSNENS
     AARMAHKFRR FMIYVHAKGM VVDDEYVIIG SANINQRSMD GSRDTEIAMG AYQPHYTWAR
     NGDHPHGQVY GYRMSLWAEH LGRLEDCFRE PHGLECVRRV NQLAEENWKT YVVSEVKEMK
     GHLMRYPIKV ERDGKIGPLP GYESFPDVGG KIDPPPSLGI VAFFSENVVA SFLEQNTRYL
     G
//
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