ID A0A0E0K803_ORYPU Unreviewed; 828 AA.
AC A0A0E0K803;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
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 Oryza punctata (Red rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4537 {ECO:0000313|EnsemblPlants:OPUNC03G01400.1};
RN [1] {ECO:0000313|EnsemblPlants:OPUNC03G01400.1}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OPUNC03G01400.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) 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; A0A0E0K803; -.
DR STRING; 4537.A0A0E0K803; -.
DR EnsemblPlants; OPUNC03G01400.1; OPUNC03G01400.1; OPUNC03G01400.
DR Gramene; OPUNC03G01400.1; OPUNC03G01400.1; OPUNC03G01400.
DR eggNOG; KOG1329; Eukaryota.
DR HOGENOM; CLU_004684_0_0_1; -.
DR OMA; LYRQGQC; -.
DR Proteomes; UP000026962; Chromosome 3.
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:SF61; PHOSPHOLIPASE D; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF12357; PLD_C; 1.
DR Pfam; PF00614; PLDc; 2.
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:UP000026962}.
FT DOMAIN 6..142
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 342..377
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 674..701
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 828 AA; 92472 MW; D363992E0D5415A8 CRC64;
MEVVWPHGSM WGSSSASRRA VMLHGSLDIW IHEARNLPNM DIVSKTVGDF LGTKKKKAAS
GAMTSDPYVT VQLASATVAR TYVVTDDENP VWAQHFLVPV AHEAPTVHFL VKDSDVFGAE
LIGEVVVPTE QLEAGEHVEG VYPVLDAAGK PCAPGAVLRL SVQYIPVARL TMYHHGVTPG
PDFAGVPNTY FPLRRGGRVT LYQDAHVPEG SLPEIRLGNG ARYRQGQCWH DVYDAISQAR
RLIYITGWSV FHTIHLVRDG GGGGGSLGDL LKRKSQEGVR VLLLVWDDPT SRNVLGIQME
GYMGTRDEET RRFFKHSSVQ ILLCPRSAGK RHSWVKQQET GTIFTHHQKT VILDADAGNH
KRKIVAFVGG LDLCGGRYDT PTHPLFRSLQ TLHKEDYYNP NFAVVDAQGP REPWHDLHSK
IDGPAAYDVL ANFEERWLKA SKRSGVKKLS KANNDTLLWI ERIPDIASID DEVHSSDNDP
ERWDVQIFRS IDSNSVKGFP KDPREATSKN LVCGKNVLID MSVQTAYVNA IRGAQHFIYI
ENQYFIGSSF NWDSHKDVGA NNLIPIEIAL KIANKIYANE RFSAYIVIPM WPEGNPTGAP
TQRILYWQKK TMQMMYEVIH KALKEVGQDN TYEPQDYLNF FCLGNREAGG SPSTCSGSSS
ANNPQDQARK NRRFMVYVHS KGMIVDDEYV IIGSANINQR SMEGTRDTEI AMGAYQPQYT
WANMLSAPRG QIYGYRMSLW AEHIGAVDES FSCPESLECT RQVRHIGEQN WKQFACSEVS
EMRGHLIKYP VSVARDGKVK PLPGCAAFPD LGGNICGKFL PIQENLTI
//
