ID I1KSQ9_SOYBN Unreviewed; 857 AA.
AC I1KSQ9;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 2.
DT 27-MAR-2024, entry version 66.
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=100810824 {ECO:0000313|EnsemblPlants:KRH43039};
GN ORFNames=GLYMA_08G126700 {ECO:0000313|EMBL:KRH43039.1};
OS Glycine max (Soybean) (Glycine hispida).
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; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EMBL:KRH43039.1};
RN [1] {ECO:0000313|EMBL:KRH43039.1, ECO:0000313|EnsemblPlants:KRH43039}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH43039};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH43039.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EnsemblPlants:KRH43039}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH43039};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRH43039.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH43039.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) 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; CM000841; KRH43039.1; -; Genomic_DNA.
DR RefSeq; XP_003532794.1; XM_003532746.3.
DR AlphaFoldDB; I1KSQ9; -.
DR SMR; I1KSQ9; -.
DR STRING; 3847.I1KSQ9; -.
DR PaxDb; 3847-GLYMA08G13350-1; -.
DR EnsemblPlants; KRH43039; KRH43039; GLYMA_08G126700.
DR GeneID; 100810824; -.
DR Gramene; KRH43039; KRH43039; GLYMA_08G126700.
DR KEGG; gmx:100810824; -.
DR eggNOG; KOG1329; Eukaryota.
DR HOGENOM; CLU_004684_0_0_1; -.
DR InParanoid; I1KSQ9; -.
DR OMA; DDEYCEL; -.
DR OrthoDB; 3014064at2759; -.
DR Proteomes; UP000008827; Chromosome 8.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:InterPro.
DR GO; GO:0009395; P:phospholipid catabolic process; IBA:GO_Central.
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; 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:UP000008827}.
FT DOMAIN 9..156
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 360..395
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 703..730
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 857 AA; 96936 MW; 56D5355E28176A12 CRC64;
MDCHGGICQS SPNREHEGLN EHVFLHGDLD LLIVEAKSLP NLDLSTEAVR KCITMGNMCH
PPFIKGLKTH SGKDKMITSD PYVSVCIAGA TIAQTRVIAN CENPLWDEQF IVPVAHPAQK
LEFLVKDNDL LGAELIGVVE IPVQKIIAGN TINDWFPIIG QYGNCLKPYP ELHISVQYRQ
IGVNRSESIS SGDGKALGVP KTYFPLRKGG SVTLYQDAHL PDGMLPEIPL EGGKVFQQNK
CWEDICHAIL EAHHLIYIIG WSVYHPVRLV REATKPLPSG GELSLGELLK YKSQEGLRVV
MLIWDDRTSH DKFLLKTDGV MQTHDEETKK FFKHSTVHCV LSPRYASNKL SIFKQQVVGT
LFTHHQKCVL VDSLGSGNNR KITAFMGGLD LCDGRYDTPE HRLFRDLDTV FHNDFHNPTF
QLNSNSCAPR QPWHDLHCKI EGPAAYDILT NFEQRWRKAK KWRDFRLKKV TNWHDDALLR
LDRISWIVKP SPCSKGDKSV HVTDEKDPES WNVQIFRSID SGSVKGFPKD VDKAKSQNLL
CGKNLKVDQS IHTAYVRAIR SAERFVYIEN QYFLGSSYHW PSYKNNAGAN HLVPMELALK
IAGKIGANER FCVYIVIPMW PEGVPTSAAV QEILFWQGQT MSMMYKIIAD ALEKAGLSDK
YHPQDYLNFY CLGKREPQST NISPTPNPSE NRALVSVKKF RRFMIYVHAK GMVIDDEYVI
IGSANINQRS LDGSRDTEIA MGAYQPNYTW TEKNAHPRGQ VYGYRMSLWA EHLADLDHCF
TEPHNLECVR HVNKIAKQNW DIYVSEEGNR MRGHLMQYPV KISKDGKVSA LDDYESFPDV
GGKVLGSPNS LPDALTA
//
