ID A0A1J7HH06_LUPAN Unreviewed; 811 AA.
AC A0A1J7HH06;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=TanjilG_18197 {ECO:0000313|EMBL:OIW11924.1};
OS Lupinus angustifolius (Narrow-leaved blue lupine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC genistoids sensu lato; core genistoids; Genisteae; Lupinus.
OX NCBI_TaxID=3871 {ECO:0000313|EMBL:OIW11924.1, ECO:0000313|Proteomes:UP000188354};
RN [1] {ECO:0000313|EMBL:OIW11924.1, ECO:0000313|Proteomes:UP000188354}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tanjil {ECO:0000313|Proteomes:UP000188354};
RC TISSUE=Whole plant {ECO:0000313|EMBL:OIW11924.1};
RX PubMed=27557478; DOI=10.1111/pbi.12615;
RA Hane J.K., Ming Y., Kamphuis L.G., Nelson M.N., Garg G., Atkins C.A.,
RA Bayer P.E., Bravo A., Bringans S., Cannon S., Edwards D., Foley R.,
RA Gao L.L., Harrison M.J., Huang W., Hurgobin B., Li S., Liu C.W.,
RA McGrath A., Morahan G., Murray J., Weller J., Jian J., Singh K.B.;
RT "A comprehensive draft genome sequence for lupin (Lupinus angustifolius),
RT an emerging health food: insights into plant-microbe interactions and
RT legume evolution.";
RL Plant Biotechnol. J. 15:318-330(2017).
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; CM007365; OIW11924.1; -; Genomic_DNA.
DR RefSeq; XP_019443381.1; XM_019587836.1.
DR RefSeq; XP_019443382.1; XM_019587837.1.
DR RefSeq; XP_019443383.1; XM_019587838.1.
DR AlphaFoldDB; A0A1J7HH06; -.
DR STRING; 3871.A0A1J7HH06; -.
DR EnsemblPlants; OIW11924; OIW11924; TanjilG_18197.
DR GeneID; 109347779; -.
DR Gramene; OIW11924; OIW11924; TanjilG_18197.
DR KEGG; lang:109347779; -.
DR OMA; PNWGRGI; -.
DR OrthoDB; 3014064at2759; -.
DR Proteomes; UP000188354; Chromosome LG05.
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 CDD; cd09199; PLDc_pPLDalpha_2; 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:SF115; PHOSPHOLIPASE D ALPHA 2; 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:UP000188354}.
FT DOMAIN 1..128
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 329..367
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 657..684
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 811 AA; 92030 MW; ACE6F5A32BCD09FB CRC64;
MAQILLHGNL HATIFEVDRL KSEGGGGGGN FLSKIKQNIE EKVGIGKGVT KLYATIDLEK
ARVGRTRIIE NEENNPKWYE SFHIYCGHSA SNIIFTVKDD NPIGASLIGR AYVPVGEVLD
GEEIDRWVEL LDEDKNPIQQ GSKIHVKLQY FDVGKDLNWA RGIRSAKFPG VPYTFFSQRQ
GCKVTLYQDA HVPDNFVPKI PLSGGKNYEP HRCWEDIFDA ITNAKHMIYI TGWSVYTEIS
LVRDSRRPKQ GGDVTLGELL KKKAGEGVRV LMLVWDDRTS VNLLKKDGLM ATHDEETAQF
FEGTDVHCVL CPRNPDNGGS IVQDLQISTM FTHHQKIVVV DSELPSGASD RRRIVSFVGG
IDLCDGRYDT AFHSLFRTLD TVHHDDFHQP NFPGADITKG GPREPWHDIH SRLEGPIAWD
VLFNFEQRWR KQGGKDLLVS LRELEDVFIP PSAVTFPEDH ETWNVQLFRS IDGGAAFGFP
DTPEEAARAG LISGKDNIID RSIQDAYINA IRRAKNFIYI ENQYFLGSSF AWAPEDIKPE
DIGALHLIPK ELSLKIVSKI EAGERFTVYV VVPMWPEGVP ESASVQAILD WQRRTLEMMY
KDVVQALRAK GSDEDPRNYL TFFCLGNREV KKQGEYEPSE KPEEDSDYQR AQEARRFMIY
VHTKMMIVDD EYIIVGSANI NQRSMDGARD SEIAMGAYQP YHLATRQPAR GQIHGFRMSL
WYEHLGMLHE SFDNPENEEC IRKVNQIADK YWDLYSNESL ERDLPGHLLR YPIGVASEGD
ITELPGFEFF PDTKARILGG KVDYMPPILT T
//
