ID A0A2G9GUW0_9LAMI Unreviewed; 851 AA.
AC A0A2G9GUW0;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=CDL12_18420 {ECO:0000313|EMBL:PIN08995.1};
OS Handroanthus impetiginosus.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Bignoniaceae; Crescentiina; Tabebuia alliance;
OC Handroanthus.
OX NCBI_TaxID=429701 {ECO:0000313|EMBL:PIN08995.1, ECO:0000313|Proteomes:UP000231279};
RN [1] {ECO:0000313|Proteomes:UP000231279}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. UFG-1 {ECO:0000313|Proteomes:UP000231279};
RX PubMed=29253216; DOI=10.1093/gigascience/gix125;
RA Silva-Junior O.B., Grattapaglia D., Novaes E., Collevatti R.G.;
RT "Genome assembly of the Pink Ipe (Handroanthus impetiginosus,
RT Bignoniaceae), a highly valued, ecologically keystone Neotropical timber
RT forest tree.";
RL Gigascience 7:1-16(2018).
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:PIN08995.1}.
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DR EMBL; NKXS01003645; PIN08995.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G9GUW0; -.
DR STRING; 429701.A0A2G9GUW0; -.
DR OrthoDB; 3014064at2759; -.
DR Proteomes; UP000231279; Unassembled WGS sequence.
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:SF130; PHOSPHOLIPASE D GAMMA 1-RELATED; 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:UP000231279}.
FT DOMAIN 24..163
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 363..398
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 697..724
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 851 AA; 95989 MW; 0BA4B87B2AC9B185 CRC64;
MAHLTYSDSM SGGSQHGQGV QFVPFKTSAG SLRVLLLHGN LDIWVKEARN LPNMDLFHKN
LGDMFGRLSG KFISKIEGST PTKITSDPYV TIAVSDAVIG RTFVISNSEN PVWNQHFHVP
VAHYGAEVHF VVKDSDVVGS QMIGAVGVPV EQIISGARIE GTYPIFGPKK KHCNPGAVLS
LSIQYIPMEM VPLYHGGVGA DLSYQGVPGT YFPLRRGGTV TLYQDAHTHD GLLPKLWLAN
GRLYQHGQCW RDIYDAIFQA RRLIYITGWS VYHLVQLVRD DPNVKNSTLG ELLKAKSQEG
VRVLLLVWDD PSSTSILGYK TEGVMNTSDE ETRRYFKHSS VQVLLCPRTA GKGSWAKKSE
TGTIYTHHQK SVIVDADAGN YRRKIVAFVG GLDLCKGRYD TQKHPVFSTL QTVHKDDYHN
PNFTGPAAGC PREPWHDLHC KIDGPAAYDV LTNFEERWLK ASKRNKLQKM KASYDDSLLK
LDRIPDVLAI AEAGSQREGD PEGWHVQVFR SIDSNSVKGF PKDPKEAPNR NLVCGKNILI
DMSIHTAYVK AIRAAQHFIY IENQYFLGSS YNWANYNKDL GANNLIPMEI ALKVANKIRA
RERFAVYIII PMWPEGVPTS TPTQRILFWQ YNTMQMMYET IYKALEEMGL EKEYEPQDYL
NFFCLGNREV EDSRSKPDTK SSNGNTPQAL TRKNRRFMIY VHSKGMIVDD EYVILGSANI
NQRSLEGTRD TEIAMGAYQP HYTWASKRAN PHGQIYGYRM ALWAEHTGAL EQCFEQPQSL
ECIRRVRWMG EQNWQRFAAS EVSEMRGHLL KYPVQVDRMG KVTPLPGCET FPDMGGKIIG
TFSGIQENLT I
//
