ID A0A2I0VG10_9ASPA Unreviewed; 842 AA.
AC A0A2I0VG10;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=PLD1 {ECO:0000313|EMBL:PKU62362.1};
GN ORFNames=MA16_Dca021944 {ECO:0000313|EMBL:PKU62362.1};
OS Dendrobium catenatum.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae;
OC Epidendroideae; Malaxideae; Dendrobiinae; Dendrobium.
OX NCBI_TaxID=906689 {ECO:0000313|EMBL:PKU62362.1, ECO:0000313|Proteomes:UP000233837};
RN [1] {ECO:0000313|EMBL:PKU62362.1, ECO:0000313|Proteomes:UP000233837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=The whole plant {ECO:0000313|EMBL:PKU62362.1};
RX PubMed=26754549; DOI=10.1038/srep19029;
RA Zhang G.Q., Xu Q., Bian C., Tsai W.C., Yeh C.M., Liu K.W., Yoshida K.,
RA Zhang L.S., Chang S.B., Chen F., Shi Y., Su Y.Y., Zhang Y.Q., Chen L.J.,
RA Yin Y., Lin M., Huang H., Deng H., Wang Z.W., Zhu S.L., Zhao X., Deng C.,
RA Niu S.C., Huang J., Wang M., Liu G.H., Yang H.J., Xiao X.J., Hsiao Y.Y.,
RA Wu W.L., Chen Y.Y., Mitsuda N., Ohme-Takagi M., Luo Y.B., Van de Peer Y.,
RA Liu Z.J.;
RT "The Dendrobium catenatum Lindl. genome sequence provides insights into
RT polysaccharide synthase, floral development and adaptive evolution.";
RL Sci. Rep. 6:19029-19029(2016).
RN [2] {ECO:0000313|EMBL:PKU62362.1, ECO:0000313|Proteomes:UP000233837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=The whole plant {ECO:0000313|EMBL:PKU62362.1};
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; KZ503667; PKU62362.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I0VG10; -.
DR STRING; 906689.A0A2I0VG10; -.
DR Proteomes; UP000233837; 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 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:SF73; 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; 1.
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:UP000233837}.
FT DOMAIN 1..147
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 688..715
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 842 AA; 94414 MW; 8E7320F9D499A2B2 CRC64;
MILLHGILHV DILEAKGLQI PFGLPNGATR LSRRWFARRF SWIKRVSSCL PSRLAGDIEN
VLGWAPEAKL YATVDLEKAR VGRTRLMISG DPTNPRWHES FRIYCAHMAE HVIFTLKSDN
PIGATLLGRA YLPVASIINN TLIDSSLDIC GEDLRPLGGR IHVKVRYTAV AGSDMGGWGR
GIPNTFFKQR EGCKVTLYHD AHVDGSFVPR ILLAGGEVFR PGRCWEDMFD AISGARRFIY
VAGWSVYAEI SLVREGQRGQ AGEATLGEML KRKAGEGVRV LMLVWDDRSS VGDLKKDGVM
ATHDQDTAEF FRGSGVHCVL CPRNPDVGES YVQGLEIATM FTHHQKTIIV DYAETAAAEM
GTHRRKGREG VAARRRIVSF LGGIDLCDGR YDTQKHSLFQ TLAREHRNDF HQPNFAGATL
RKGGPREPWH DVHCRVEGAA AWDVLCNFEQ RWRKQGAGDY LLLRLRENDG GLYVLPEEEA
VVASRSDGNA WNVQVFRSID GGAAHSFPDS PKEAAAMGLI TGKDNVIDRS IQDAYINAIR
RAKNFIYIEN QYFLGSSYAW KEEKGIKVED IGALHLIPKE LSLKIVSKIE AGERFAVYVV
VPMWPEGVPE SGSVQAILDW QRRTMEMMYD DVAEALRAKG IAGNVSPSDY LNFFCLGNRE
VKRGGEYEPP ERPEPDSDYS RAQQARRFMI YVHAKMMIVD DEYIVVGSAN INQRSMDGGR
DTEIAMGAYQ PNHLSSSQPA RGQIHGFRLS LWYEHLGMID DTFLRPESKE CVLKVRQNAE
ERWKLYLGVL LYNDLSGHLL SYPISITNNG KIVVSPWMEF FPDTKAKVLG TKSDYLPAIL
TT
//
