ID A0A452ZS63_AEGTS Unreviewed; 745 AA.
AC A0A452ZS63;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 24.
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};
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:AET1Gv20899000.1, 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:AET1Gv20899000.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2019) to UniProtKB.
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 AlphaFoldDB; A0A452ZS63; -.
DR EnsemblPlants; AET1Gv20899000.1; AET1Gv20899000.1; AET1Gv20899000.
DR Gramene; AET1Gv20899000.1; AET1Gv20899000.1; AET1Gv20899000.
DR Proteomes; UP000015105; Chromosome 1D.
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; SM00155; PLDc; 2.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
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:UP000015105}.
FT DOMAIN 265..303
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 589..616
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 745 AA; 82507 MW; DB985A6B1DD8F474 CRC64;
MVSPSNAPAW NESFHVYCAH DASHIIFTVK ADNTVGATLI GRAYLPTGAA VLAGQRVDQW
LPICDDKRRP LDGGDRIHVQ LRFTDVADDP AARWGAGVGS AAYPGVPRTF FGQRRGCRVR
LYQDAHISDG FAQRVQVTLA GGKPYQPRRC WEDVFEAITN ARRMVYIAGW SVNTDVALVR
DPRKPSSGTL GELLKRKAAE GVRVLMLVWD DRTSLGLGPI RRDGLMATHD EDTATYFRGT
GVRCILCPRN PDQGRSYVQD VETAAMFTHH QKTVIVDSSR NAAANASPGL VSFLGGIDLC
DGRYDTQEHP LFRTLGTTHH KDFHQPNFPG ASISKGGPRE PWHDIHCRVE GPAAWDVLDN
FEQRWRKQGD GDNHLVTLDR GWAAREAVQD ADSWNVQVFR SIDGGAAAGF PEKPEEAALI
GLETGKDHVI ERSIQDAYIH AIRRARDFIY IENQYFLGSS YAWRRDDGVT VEDINALHLI
PKELSLKIVS KIEAGERFAV YVVVPMWPEG VPESGSVQAI LDWQRRTMEM MYKDVALAIQ
AKGIQASPTD YLTFFCLGNR EALSPGEYVP PERPDPDTDY DRAQQARRFM IYVHAKTMIV
DDEYVIVGSA NINQRSMDGG RDSEIAMGAY QPGYLASTNR PARGQVHGLR LALWQEHLGQ
AAAAVDLLQP SSLACVRRVN QAAQQHWDMF ASDAPPQGDL PGHLLAYPIG VSDGGELLET
TAFFPDTKAR VLGNKSTYLP PILTT
//
