ID A0A1S3U7P7_VIGRR Unreviewed; 847 AA.
AC A0A1S3U7P7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=LOC106762543 {ECO:0000313|RefSeq:XP_014501999.1};
OS Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3916 {ECO:0000313|Proteomes:UP000087766, ECO:0000313|RefSeq:XP_014501999.1};
RN [1] {ECO:0000313|RefSeq:XP_014501999.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_014501999.1};
RG RefSeq;
RL Submitted (NOV-2023) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_014501999.1; XM_014646513.2.
DR AlphaFoldDB; A0A1S3U7P7; -.
DR STRING; 3916.A0A1S3U7P7; -.
DR GeneID; 106762543; -.
DR KEGG; vra:106762543; -.
DR OrthoDB; 3014064at2759; -.
DR Proteomes; UP000087766; Chromosome 5.
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:SF60; 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; 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:UP000087766}.
FT DOMAIN 1..145
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 350..385
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 693..720
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 847 AA; 96522 MW; 2AF9039CD1CDF8BC CRC64;
MPQKHNTVVY LHGTLDLVIV EARCLPNMDL LSERVRRFFS ALNTCSSSIS GKRKLHRPRP
RHHKIITSDP YVTVCLAGAT VARTRVISNS QSPSWDEHFK IPLAHPAAQV DFFVKDNDMF
GADLIGVVTV SAERILSGEP ISDWFPIIGS FGKQPKPDCA LRLAMKFTRC ENTRLFRSVK
EPDPDRFVVR DSYFPVRHGG AVTLYQDAHV PEAMLPEVEL EEGVMFEHGK CWEDICHAIL
EAHHLVYVVG WSIYHKVRLV REPTKPLPSG GSLNLGELLK YKSQEGLRVL LLVWDDKTSH
SKFFINTTGV MQTHDEETRK FFKHSSVRCL LSPRYASSKL SIFRQQVVGT LFTHHQKCVI
VDTQAHGNNR KITAFIGGLD LCDGRYDTPE HRLFRDKDTV FQDDYHNPSF CAGTKGPRQP
WHDLHCKIEG PAAYDILTNF EQRWRKATRW SELGRKLKRV SHWNDDSLIK LERISWILSP
SESILTDDPE LWVSKEDDPK NWHVQVFRSI DSGSLKGFPK DVFEAESQNL VCAKNLVIDK
SIQTAYIHAI RSAQHFIYIE NQYFVGSSFA WPAYKDAGAD NLIPMELALK IVSKIRSKER
FTVYIVIPMW PEGNPTSASV QEILFWQAQT MQMMYNVIAR ELIVMELDHH PQDYLNFYCL
GNREPLKNYI LSPSSSSPDN GDTISASQKF RRFMIYVHAK GMIVDDEYVI LGSANINQRS
MAGSRDTEIA MGAYQPRHTW GKKKGHPHGQ VYGYRMSLWA EHIGSIQACF KNPESLECVR
SVNSIAEENW RRYTSDDYSP LQGHLIKYPV IINASGKIKS IPGFESFPDV GGKVLGSRSN
LPDALTT
//
