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
//