ID G8JBF8_9ORYZ Unreviewed; 790 AA.
AC G8JBF8;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=22 {ECO:0000313|EMBL:AER41636.1};
OS Oryza officinalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4535 {ECO:0000313|EMBL:AER41636.1};
RN [1] {ECO:0000313|EMBL:AER41636.1}
RP NUCLEOTIDE SEQUENCE.
RA Yang L., Li B., Sui Y., Chen J., Shi J., Chen M.;
RT "Comparative Sequence Analysis Revealed Gene Movement of Ghd7 in the Grass
RT Genomes.";
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
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; JN873133; AER41636.1; -; Genomic_DNA.
DR AlphaFoldDB; G8JBF8; -.
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:SF153; PHOSPHOLIPASE D; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF12357; PLD_C; 1.
DR Pfam; PF00614; PLDc; 1.
DR PIRSF; PIRSF036470; PLD_plant; 2.
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}.
FT DOMAIN 1..144
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 302..337
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 636..663
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 790 AA; 89653 MW; 9C6E8302C4F09F24 CRC64;
MGKHSAESGT SMLLHGDLDI QIMEAKCLPN MDLMTERMRK CFTGYGACST ECGKSDPHPD
VRKIITSDPY VSVCLSGATV AQTRVIANSE NPKWDEHFYV QVAHSVSRVE FHVKDNDVFG
AELIGVASVP VEDIIPGDTV SGWFPISGQY SNPMKASPEL HLSIQYKPIE QNPLYKDGVG
SDSCQSIGVP NAYFPLRKGG MVTLYQDAHV PDDFCPKIEI DGGRVYEQNK CWEDICHAMA
EAHHLIYIIG WSLYHPVKLD GLMHTHDEEA RKFFRHSGVH CVLAPRYASN KLSIFKQQVV
GTLFTHHQKC VIVDTQATGN NRKITAFIGG LDLCDGRYDT PEHRLFKDLD TIFKDDFHNP
TFQVNKSGPR QPWHDLHCKI EGPAAYDILT NFEQRWRKSA KWKVSVRRAV SWHHDTLVKL
NRMSWIVSPS ADELNAHVCD QDDPENWHVQ IFRSIDSGSV KGFPKLVQEA ESQNLVCAKN
LQIDKSIHNA YVKAIRSAQH YIYIENQYFI GSSYYWSSNR SAGAENLIPI ELAIKIARKI
KARERFAAYI VIPMWPEGNP TTAAMQEILF WQGQTMSMMY KIVADALRKE GLDDTHPQDY
LNFYCLGKRE VSNDVSTTSH SNENSPLRLV QKFKRFMIYV HSKGMIVDDE YVLIGSANIN
QRSMDGSRDT EIAMGAYQPH YSWAGGKKAP RGQVYGYRMS LWAEHLGTVE ECFRWPHSME
CVRQVNEMAE ENWARYLSPE MVNMRGHLMR YPINVDRDGR VGPVRGYECF PDVGGKVLGT
HSSLPNALTT
//
