ID V7ATN2_PHAVU Unreviewed; 827 AA.
AC V7ATN2;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
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 ORFNames=PHAVU_009G093500g {ECO:0000313|EMBL:ESW09022.1};
OS Phaseolus vulgaris (Kidney bean) (French bean).
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; Phaseolus.
OX NCBI_TaxID=3885 {ECO:0000313|EMBL:ESW09022.1, ECO:0000313|Proteomes:UP000000226};
RN [1] {ECO:0000313|Proteomes:UP000000226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. G19833 {ECO:0000313|Proteomes:UP000000226};
RX PubMed=24908249; DOI=10.1038/ng.3008;
RA Schmutz J., McClean P.E., Mamidi S., Wu G.A., Cannon S.B., Grimwood J.,
RA Jenkins J., Shu S., Song Q., Chavarro C., Torres-Torres M., Geffroy V.,
RA Moghaddam S.M., Gao D., Abernathy B., Barry K., Blair M., Brick M.A.,
RA Chovatia M., Gepts P., Goodstein D.M., Gonzales M., Hellsten U.,
RA Hyten D.L., Jia G., Kelly J.D., Kudrna D., Lee R., Richard M.M.,
RA Miklas P.N., Osorno J.M., Rodrigues J., Thareau V., Urrea C.A., Wang M.,
RA Yu Y., Zhang M., Wing R.A., Cregan P.B., Rokhsar D.S., Jackson S.A.;
RT "A reference genome for common bean and genome-wide analysis of dual
RT domestications.";
RL Nat. Genet. 46:707-713(2014).
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; CM002296; ESW09022.1; -; Genomic_DNA.
DR RefSeq; XP_007137028.1; XM_007136966.1.
DR AlphaFoldDB; V7ATN2; -.
DR STRING; 3885.V7ATN2; -.
DR EnsemblPlants; ESW09022; ESW09022; PHAVU_009G093500g.
DR GeneID; 18619623; -.
DR Gramene; ESW09022; ESW09022; PHAVU_009G093500g.
DR KEGG; pvu:PHAVU_009G093500g; -.
DR eggNOG; KOG1329; Eukaryota.
DR OMA; MRYPIEV; -.
DR OrthoDB; 875955at2759; -.
DR Proteomes; UP000000226; Chromosome 9.
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:SF176; 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:UP000000226}.
FT DOMAIN 1..141
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 339..380
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 670..697
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 644..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..661
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 827 AA; 93982 MW; 30B875DC4D58554A CRC64;
MSRLLHGSLD VTIYEVDTLP TLNDCDFNLC CKGTSRSVRK RVLSQLKSCL FCQCQCQPGS
TQTGLYATVD LDKARVGRTK VLNDERSNTM WNDTFRIYCA HLISHVIFTV KQKDPINATL
IGRAYVPVEQ VMTGNIVDTW VQILDEDLNP IPSDSKIHVK MQFSDVRNDI NWSGGIRSPR
FQGVPHTFFG QRTGCNVTLY QDAHVSDGFE PMIPVSGRKP YEFRKCWEDI YNAISDARHF
IYITGWSVYT EITLIRDPLQ PKRITLGELL KRRAEEGVHV LMLVWDDKTS VPDFKKDGLM
ATHDQETADY FKNTKVNCVL CPRNPDVGRS IVQGLETSTM FTHHQKTIVV DSQVVGPAVG
QRQKRTITSF VGGIDLCDGR YDTQEHPLFS TLDTVHKDDF HQPNFPDASI KKGGPREPWH
DIHCKLEGDV AWDVLSNFQQ RWEKQVGKQL LFPSSMLNQY FVPRSTVATA NDNETWNVQL
FRSIDGGAAF GFPQDPQEAA ELGLVSANNN IIDRSIQDAY INAIRRAQNF IYIENQYFLG
SSYGWKASDI VVEDIGALHL IPKEVSLKIV SKIEAGERFS VYVVIPMWPE GIPESDSVQA
ILDWQRRTME MMYADIAQAI QRTGIEAHPR DYLTFFCLGN REGQKNSNHT PTEAPQPDSD
YSRAQKSRRF MIYVHAKMMI VDDEYIIIGS ANINQRSMDG ARDSEIAVGA FQPRHLACNG
PVRGQIYGFR RALWYEHLGD INDTGIFNNP ESEECIRLVN HLAETNWAAY SDQTFDENGE
FHHLLRYPIE VTNYGTITNL PGLQYFPDTK ARILGSKSEY LPPILTT
//
