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Database: UniProt
Entry: A0A445KPK1_GLYSO
LinkDB: A0A445KPK1_GLYSO
Original site: A0A445KPK1_GLYSO 
ID   A0A445KPK1_GLYSO        Unreviewed;       879 AA.
AC   A0A445KPK1;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   08-NOV-2023, entry version 20.
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=D0Y65_012535 {ECO:0000313|EMBL:RZC12826.1};
OS   Glycine soja (Wild soybean).
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=3848 {ECO:0000313|EMBL:RZC12826.1, ECO:0000313|Proteomes:UP000289340};
RN   [1] {ECO:0000313|EMBL:RZC12826.1, ECO:0000313|Proteomes:UP000289340}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. W05 {ECO:0000313|Proteomes:UP000289340};
RC   TISSUE=Hypocotyl of etiolated seedlings {ECO:0000313|EMBL:RZC12826.1};
RA   Xie M., Chung C.Y.L., Li M.-W., Wong F.-L., Chan T.-F., Lam H.-M.;
RT   "A high-quality reference genome of wild soybean provides a powerful tool
RT   to mine soybean genomes.";
RL   Submitted (SEP-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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RZC12826.1}.
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DR   EMBL; QZWG01000005; RZC12826.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A445KPK1; -.
DR   Proteomes; UP000289340; 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; 3.
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; 3.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00155; PLDc; 1.
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; 1.
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:UP000289340}.
FT   DOMAIN          6..156
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          725..752
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
SQ   SEQUENCE   879 AA;  98707 MW;  6D965987DFE13752 CRC64;
     MDCHGGISQS SPNREYEGLN GPVFLHGDLD LLIIEAKSLP NLDLSSETIR KCITMGNMCH
     PPFIKGLKTH SGKDKMITSD PYVSVCIAGA TIAQTRVIAN CENPLWDEQF IVPVAHPAQK
     LEFLVKDNDI LGAELIGVVE IPVQKIIAGN TVNDWFPIIG QYGNCLKPYP ELHISVQYRQ
     IGVNRSESIS SGDGKALGVP KTYFPLRKGG SVTLYQDAHL PDGMLPEITL EGGKVFQHNK
     CWEDICHAIL EAHHLIYIIG WSVYHPVRLV REATKPLPSG GELSLGELLK YKSQEGLRVV
     MLIWDDRTSH DKFLLKTDGV MQTHDEETKK FFKHSTVHCV LSPRYASNKL SIFKQQLHSN
     SCAPRQPWHD LHCKIEGPAA YDILTNFEQR WRKAKKWRDF RLKKVTNWHD DALLRLDRIS
     WIVKPSPSSN GDKSVHVTDE NDPESWNVQI FRSIDSGSVK GFPKDVDKAK AQNLFCGKNL
     KVDQSIHTAY VRAIRSAEHF VYIENQYFLG SSYHWPSYKN NAGANHLVPM ELALKIAGKI
     GANERFCVYI VIPMWPEGVP TSAAVQEILF WQGQTMSMMY KIVADALEKA GLSYQYHPQD
     YLNFYCLGKR EPQSTNISPT PNPSENRALI WEKECSDLNK KNLDPVRLVA LLLHPAAEDV
     LQLFTVALVV GDEQAAENGS NDGTIVVEHG FASGLGILVG DEGEVVVAGA GGRRRCVSVK
     KFRRFMIYVH AKGMVVDDEY VIIGSANINQ RSLDGSRDTE IAMGAYQPKY TWTEKNAHPR
     GQVYGYRMSL WAEHLGSLDH CFAEPHNLEC VRHVNKIAKR NWDIYVSEEE NRMRGHLMQY
     PVKISRDGKV SALDDYESFP DVGGKILGSP NSLPDALTT
//
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