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Database: UniProt
Entry: M8A8Q7_TRIUA
LinkDB: M8A8Q7_TRIUA
Original site: M8A8Q7_TRIUA 
ID   M8A8Q7_TRIUA            Unreviewed;       804 AA.
AC   M8A8Q7;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=Phospholipase D {ECO:0000256|PIRNR:PIRNR036470};
DE            EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR036470};
GN   ORFNames=TRIUR3_10079 {ECO:0000313|EMBL:EMS68436.1};
OS   Triticum urartu (Red wild einkorn) (Crithodium urartu).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4572 {ECO:0000313|EMBL:EMS68436.1};
RN   [1] {ECO:0000313|EMBL:EMS68436.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23535596; DOI=10.1038/nature11997;
RA   Ling H.Q., Zhao S., Liu D., Wang J., Sun H., Zhang C., Fan H., Li D.,
RA   Dong L., Tao Y., Gao C., Wu H., Li Y., Cui Y., Guo X., Zheng S., Wang B.,
RA   Yu K., Liang Q., Yang W., Lou X., Chen J., Feng M., Jian J., Zhang X.,
RA   Luo G., Jiang Y., Liu J., Wang Z., Sha Y., Zhang B., Wu H., Tang D.,
RA   Shen Q., Xue P., Zou S., Wang X., Liu X., Wang F., Yang Y., An X., Dong Z.,
RA   Zhang K., Zhang X., Luo M.C., Dvorak J., Tong Y., Wang J., Yang H., Li Z.,
RA   Wang D., Zhang A., Wang J.;
RT   "Draft genome of the wheat A-genome progenitor Triticum urartu.";
RL   Nature 496:87-90(2013).
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|PIRNR:PIRNR036470};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|PIRNR:PIRNR036470};
CC   -!- SIMILARITY: Belongs to the phospholipase D family. C2-PLD subfamily.
CC       {ECO:0000256|PIRNR:PIRNR036470}.
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DR   EMBL; KD006179; EMS68436.1; -; Genomic_DNA.
DR   AlphaFoldDB; M8A8Q7; -.
DR   STRING; 4572.M8A8Q7; -.
DR   eggNOG; KOG1329; Eukaryota.
DR   OMA; GQAHNND; -.
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; 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:SF59; PHOSPHOLIPASE D ALPHA 2; 1.
DR   Pfam; PF12357; PLD_C; 1.
DR   PIRSF; PIRSF036470; PLD_plant; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR   PROSITE; PS50004; C2; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|PIRNR:PIRNR036470};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR036470};
KW   Lipid degradation {ECO:0000256|PIRNR:PIRNR036470};
KW   Lipid metabolism {ECO:0000256|PIRNR:PIRNR036470}.
SQ   SEQUENCE   804 AA;  89478 MW;  A59A63C5287660A7 CRC64;
     MAHLRLHGTI NATILGADNI HDRSRHTGIV PSFLGNIVQG VQETTSLGKG LSRMYAAIYL
     GSACIARTRT IAVPAAGSAR WNEPLRAYCA HHAADVVISV MIEQLGLNDD TVLGRAYLPA
     RELLNANGTT IDRWFDVLGT DRNKLPDGPK IHVQISFRDV ADQGLAWGGG VGDGVVPHTF
     FSQRPGCRVT LYQDAHASAE FDPKIRLDGG GLYKPGRCWE DIYDAISNAR HLVYITAWSM
     FPHITLVRER DGRQETLGEL LKRKAGEGVQ VLLLVWNDIS SIDGLHEVGV MDTRDQLTAK
     YFRGSRVQCV LCPRNWSVRG YILDAKTPVD TVVYSHHQKA ITVDQELPAS SGTLGTGQAH
     NNDFSQINFS DEAATLDKGG PRTPWHDIHA KVEGAAAWDV LHNFEQRWSK QGGGKEHLVD
     LVALEGKVAP SSWPVTLPGD QEAWNVQLFR SIDSISTVGF PDSMEDAYEA GLIQDKHRVF
     ERSIQDAYIH AIRAANSFIY IENQYFAGSS FQWKTHDGID PADVGACQQI PRELSLKIVS
     KIEAGERFAV YVVVPMWSEG TPTGRYRQAM LDNQRRTMAL MYDDIAVALQ AKKIDADPRD
     YLTFFCLGNR EAKSEGEHLP AKHPKDGTDY ARAQKARRFM IYVHSKMMID QLTKYLRSVD
     DEYIVVGSAN LNERSMAGDR DSEIAIGAFQ PHRVNTDAEL AKGHVHGFRM SLWHEHLGKT
     HDDFLRPGSL ECVRRVNKMA DEYWNLYVGD QQLTDDLPGH LLTYPVAVSK AGTVSTLKGF
     EFFPDTKAPV LGKPTGINDY FMSI
//
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