ID A0A2I0JKG6_PUNGR Unreviewed; 1095 AA.
AC A0A2I0JKG6;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN ORFNames=CRG98_022887 {ECO:0000313|EMBL:PKI56727.1};
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:PKI56727.1, ECO:0000313|Proteomes:UP000233551};
RN [1] {ECO:0000313|EMBL:PKI56727.1, 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:PKI56727.1};
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 -!- 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:PIRNR009376};
CC -!- SIMILARITY: Belongs to the phospholipase D family.
CC {ECO:0000256|PIRNR:PIRNR009376}.
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:PKI56727.1}.
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DR EMBL; PGOL01001578; PKI56727.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I0JKG6; -.
DR STRING; 22663.A0A2I0JKG6; -.
DR Proteomes; UP000233551; Unassembled WGS sequence.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-UniRule.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IEA:InterPro.
DR CDD; cd01254; PH_PLD; 1.
DR CDD; cd09138; PLDc_vPLD1_2_yPLD_like_1; 1.
DR CDD; cd09141; PLDc_vPLD1_2_yPLD_like_2; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR InterPro; IPR016555; PLipase_D_euk.
DR InterPro; IPR015679; PLipase_D_fam.
DR PANTHER; PTHR18896:SF76; PHOSPHOLIPASE; 1.
DR PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR Pfam; PF00614; PLDc; 1.
DR Pfam; PF13091; PLDc_2; 1.
DR PIRSF; PIRSF009376; Phospholipase_D_euk; 3.
DR SMART; SM00233; PH; 1.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50035; PLD; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR009376};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR009376};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR009376};
KW Reference proteome {ECO:0000313|Proteomes:UP000233551}.
FT DOMAIN 246..350
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 485..512
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 913..940
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 1095 AA; 124326 MW; 37829079957176A9 CRC64;
MASEQLMQGG SGPRYFQMQS EPSVSAMSSL WPGSGEPARM FDELPKATIV SVSRPDASDI
SPMLLSYTIE CQYKQAHLSY TMPLLFKWRL LKKASQVLYL HFALKKRAFI EEIHEKQEQV
KEWLQNLGIG DHAPMVQDDD DADDEAVLLH HDESVKNRDV PSIAALPVIR PALGRQHSIS
DRAKNAMQEY LNHFLGNMDI VNSREVCKFL EVSKLSFSPE YGPKLKEDYV MVKHLPKIPR
PDDSRKCCSC GWFSCCNDNW QKVWAVLKPG FLALLADPFD TKPLDIVVFD VLPPSDGNGE
GRVSLAKEIK DPNPLRHAFR VTCGNRSIRV RAKSSAKVKD WVAAINDAGL RPPEGWCHPH
RFGSFAPPRG LTEDGSQAQW FVDGQAAFDA IASSLDNAKS EIFICGWWLC PELYLRRPFH
SHASSRLDAL LEAKARQGVQ IYILLYKEVA LALKINSMYS KRKLLNIHEN VRVLRYPDHF
SSGVYLWSHH EKLVIVDNEI CFIGGLDLCF GRYDNSEHKV GDNPPTIWPG KDYYNPRESE
PNSWEDAMTD ELDRKKYPRM PWHDVHCALW GPPCRDIARH FVQRWNYAKR NKAPNEEAIP
LLMPQQHMVI PHYMGSKGIE IERKNVEDSN KILQRQDSFT SRSSLQDIPL LLPQEPGSMD
TPLTGSPKPN GFSSTGHVTD HQSRIIRNQP FSFRKSKAEA LVPDMPMKGF VDDRELELHR
KVPSTSGKNL DSEWWETQER GDQMVSLDET GQVGPRTSCR CQVIRSVSQW SSGTSQTEES
IHNAYCSLIE KAEHFIYIEN QFFISGLSGD MIIRNRVLEA LYRRILRAHN DKKHFRVIIV
IPLLPGFQGG LDDGGAASVR AIMHWQYRTI YRGSNSILHN LYNLLGSKAH DFISFYGLRA
YGKLSDDGPI ASSQIYVHSK IMIVDDCMTL IGSANINDRS LLGSRDSEIG ILIEDTEFVD
SAMGGMPWSA GRFSLSLRLS LWSEHLGLRP GEMNTAIYQD VFACLPNDLI HSRLALRESA
AGWKEKLGYT TIDLGIAPDK LESYHNGELR RINPMDRLES VRGHLVSFPL DFMCKEDLRP
VFNESEYYAS PQVFH
//
