ID A0A2I0L2D0_PUNGR Unreviewed; 860 AA.
AC A0A2I0L2D0;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=CRG98_004633 {ECO:0000313|EMBL:PKI74861.1};
OS Punica granatum (Pomegranate).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Lythraceae; Punica.
OX NCBI_TaxID=22663 {ECO:0000313|EMBL:PKI74861.1, ECO:0000313|Proteomes:UP000233551};
RN [1] {ECO:0000313|EMBL:PKI74861.1, ECO:0000313|Proteomes:UP000233551}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AG2017 {ECO:0000313|Proteomes:UP000233551};
RC TISSUE=Leaf {ECO:0000313|EMBL:PKI74861.1};
RA Akparov Z., Amiraslanov A., Hajiyeva S., Abbasov M., Kaur K., Hamwieh A.,
RA Solovyev V., Salamov A., Braich B., Kosarev P., Mahmoud A., Hajiyev E.,
RA Babayeva S., Izzatullayeva V., Mammadov A., Mammadov A., Sharifova S.,
RA Ojaghi J., Eynullazada K., Bayramov B., Abdulazimova A., Shahmuradov I.;
RT "De-novo sequencing of pomegranate (Punica granatum L.) genome.";
RL Submitted (NOV-2017) 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:PKI74861.1}.
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DR EMBL; PGOL01000189; PKI74861.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I0L2D0; -.
DR STRING; 22663.A0A2I0L2D0; -.
DR Proteomes; UP000233551; 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: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:UP000233551}.
FT DOMAIN 9..162
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 367..402
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 706..733
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 860 AA; 97323 MW; F3549B8821AC0F48 CRC64;
MSHEGKANPP DNKTVPCNGN GTAATGKLVF LHGELDMYIV EAKSLPNMDL ASERMRQCCT
MFGPCSSPFN KRFLGRSGKH SIITSDPYVS VCLAGATVAR TRVINNCENP LWDEHFCVPV
AHPVVKVEFH VKDNDVFGAE LIGVVEIPVT KLLSGNVIND WFPIISHYGS PLKPYPELHI
SVQFKPVGEN RLYLDGIGAG PDCKGVPNTY FPLRKGGNVT LYQDAHVPDG MLPEIPLDDG
KVFQQGKCWE DICHAILEAH HLIYVIGWSV YHPVKLVREP TRPLPSGGEL ALGELLKYKS
QEGVRVVMLI WDDKTSHDKF LIKTEGVMQT HDEETKKFFR HSSVHCALSP RYASNKLSIF
KQQVVGTLYT HHQKCVLVDT QASGNNRKIT AFIGGLDLCD GRYDTPEHRL FRDLDTIFKN
DFHNPTFTTT NNVPRQPWHD LHCKIEGPAA YDILTNFEQR WRKATKWRDF KLNRVTHWHD
DALIRLERIS WIVSPYSNEE AVHVRDENDP ENWHVQIFRS IDSGSVKGFP KSVQEAETQN
LICGKNLKVD KSIHTAYVKA IRSAQHFIYI ENQYFLGSSY YWPSYKNAGA NNLIPMELAL
KIASKISANE RFSVYVVMPM WPEGVPNSAP VQEILFWQGQ TMSMMYQIIA QALEKAGLSG
QYHPQDYLNF FCLGKREPPF SSEGHAPINS SSENNPAVLA QKFRRFMIYV HAKGMIVDDE
YVIIGSANIN QRSLDGSRDT EIAMGSYQPK YTWAEKQRHP RGQVYGYRMS LWAEHLGMLE
DEFQEPQSLE CVKRVNEIAK QNWMAYVSED SQEMRGHLMQ YPVKVSREGK VGPLPGLETF
PDVGGKVLGA PTTLPDALTT
//
