ID A0A453EBG0_AEGTS Unreviewed; 655 AA.
AC A0A453EBG0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
OS Aegilops tauschii subsp. strangulata (Goatgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX NCBI_TaxID=200361 {ECO:0000313|EnsemblPlants:AET3Gv20283800.12, ECO:0000313|Proteomes:UP000015105};
RN [1] {ECO:0000313|Proteomes:UP000015105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX PubMed=25035499; DOI=10.1126/science.1250092;
RG International Wheat Genome Sequencing Consortium,;
RA Marcussen T., Sandve S.R., Heier L., Spannagl M., Pfeifer M.,
RA Jakobsen K.S., Wulff B.B., Steuernagel B., Mayer K.F., Olsen O.A.;
RT "Ancient hybridizations among the ancestral genomes of bread wheat.";
RL Science 345:1250092-1250092(2014).
RN [2] {ECO:0000313|Proteomes:UP000015105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX PubMed=29158546; DOI=10.1038/s41477-017-0067-8;
RA Zhao G., Zou C., Li K., Wang K., Li T., Gao L., Zhang X., Wang H., Yang Z.,
RA Liu X., Jiang W., Mao L., Kong X., Jiao Y., Jia J.;
RT "The Aegilops tauschii genome reveals multiple impacts of transposons.";
RL Nat. Plants 3:946-955(2017).
RN [3] {ECO:0000313|EnsemblPlants:AET3Gv20283800.12}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2019) to UniProtKB.
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SIMILARITY: Belongs to the phospholipase D family. C2-PLD subfamily.
CC {ECO:0000256|ARBA:ARBA00010683}.
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DR AlphaFoldDB; A0A453EBG0; -.
DR EnsemblPlants; AET3Gv20283800.12; AET3Gv20283800.12; AET3Gv20283800.
DR Gramene; AET3Gv20283800.12; AET3Gv20283800.12; AET3Gv20283800.
DR Proteomes; UP000015105; Chromosome 3D.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 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; IPR015679; PLipase_D_fam.
DR PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR PANTHER; PTHR18896:SF115; PHOSPHOLIPASE D ALPHA 2; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00614; PLDc; 1.
DR SMART; SM00239; C2; 1.
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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022963};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000015105}.
FT DOMAIN 1..94
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 294..332
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 655 AA; 74436 MW; 1842E5A8357D5F67 CRC64;
FVEGIEETVG VGKGSSKLYA TIDLEKARVG RTRMLGNEPV NPRWYESFHI YCAHLAADVI
FTMKADNAIG ATLIGRAYLP VGELLGGEEI DRWLEICDDN REPVGESKIH VKLQYFGVDK
DRNWARGVRS VKFPGVPYTF FSQRQGCNVR LYQDAHVPDN FIPKIPLADG KNYEPARCWE
DIFDAISNAQ HLIYITGWSV HTEITLIRDT NRPKPGGDVT LGELLKRKAS EGVRVLMLVW
DDRTSVGLLK RDGLMATHDE ETANYFQGTD VHCVLCPRNP DDSGSIVQDL QISTMFTHHQ
KIVCVDDALP SQGSEQRRIL SFVGGIDLCD GRYDTQYHSL FRTLDTVHHD DFHQPNFATA
SITKGGPREP WHDIHSRLEG PIAWDVLYNF EQRWRKQGGK DLLVQLRDLS DIIIPPSPVM
FPEDRDTWNV QLFRSIDGGA AFGFPDTPEE AARAGLVSGK DQIIDRSIQD AYINAIRRAK
DFIYIENQYF LGSSYCWKPE GIKPEEIGAL HVIPKELSLK IVSKIEAGER FTVYVVVPMW
PEGMPESASV QAILDWQRRT MEMMYTDITQ ALEAKGIEAN PKEYLTFFCL GNREVKQDGE
YEPQEQPEPD TDYVRAQEAR RFMIYVHTKM MIGTPSVLLT VGCIIFQYQG FEWVA
//
