ID A0A1R3K3C8_9ROSI Unreviewed; 847 AA.
AC A0A1R3K3C8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=COLO4_11759 {ECO:0000313|EMBL:OMP01599.1};
OS Corchorus olitorius.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX NCBI_TaxID=93759 {ECO:0000313|EMBL:OMP01599.1, ECO:0000313|Proteomes:UP000187203};
RN [1] {ECO:0000313|Proteomes:UP000187203}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. O-4 {ECO:0000313|Proteomes:UP000187203};
RA Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA Rashid M.M., Khan S.A., Rahman M.S., Alam M., Yahiya A.S., Khan M.S.,
RA Azam M.S., Haque T., Lashkar M.Z.H., Akhand A.I., Morshed G., Roy S.,
RA Uddin K.S., Rabeya T., Hossain A.S., Chowdhury A., Snigdha A.R.,
RA Mortoza M.S., Matin S.A., Hoque S.M.E., Islam M.K., Roy D.K., Haider R.,
RA Moosa M.M., Elias S.M., Hasan A.M., Jahan S., Shafiuddin M., Mahmood N.,
RA Shommy N.S.;
RT "Corchorus olitorius genome sequencing.";
RL Submitted (SEP-2013) 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:OMP01599.1}.
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DR EMBL; AWUE01014740; OMP01599.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R3K3C8; -.
DR STRING; 93759.A0A1R3K3C8; -.
DR OrthoDB; 3014064at2759; -.
DR Proteomes; UP000187203; 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; IPR025202; PLD-like_dom.
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; PF13091; PLDc_2; 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:UP000187203}.
FT DOMAIN 1..150
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 355..390
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 693..720
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 847 AA; 95826 MW; 969DBCA12DF9BA99 CRC64;
MGRDSTESSG SDGEAFFLHG ELDLWIIEAK SLPNMDLASE RLRRIFTMFG TCDTHFCKKS
KKAASGRKSI ITSDPYVSVC LAGATVAQTR IITNCENPSW DEHFIVPVAH PVAKVEFLVK
DNDVLGAQLI GVVDIAVEKV LSGQEINDWF PIVGQFGNCL KPYPELHISI QFRSVRDNPL
YQHGVGTGPD YIGVPNTYFP LRIGGSVTLY QDAHVKNSLL PEISLDGGKV YQQGKCWEDI
CHAILEAHHL IYIVGWSVYH PIKLVREPTK PLPDGGQLSL GDLLKYKSEE GVRVMMLIWD
DKTSHDKGLL KTAGVMQTHD EETKNFFKHS SVRCVLAPRY ASNKLSFFKQ QVVGTLFTHH
QKCVLLDTQA SGNNRKITAF IGGLDLCDGR YDTPEHRIFR DLDTVFKDDF HNPTFPSSAQ
SPRQPWHDLH CKIEGPAAYD ILTNFEQRWR KAAKWRNFKL KSVNPWHEEA LLRVDRISWI
ISPSSGPDGD KIVRVCDEDD PENWHVQVFR SIDSGSVKGF PKDVKQASNQ SLICGKNLKV
DRSIHTAYVK AIRSAQRFIY IENQYFLGSS YFWPSYKDAG ADNLIPIELA LKIANKISAN
ERFSVYIVIP MWPEGVPTSN AVQEILFWQT QTMGMMYSII AQELEKAGLS EQYHPQDYLN
FYCLGKRDPP SSECSSQETD NRALALAQQF RRFMIYVHAK GMIVDDEFVL MGSANINQRS
LEGSRDTEIA MGAYQPNYTW ARNQSHPHGQ VYGYRMSLWA EHLGKLEDTF QEPQSLECVK
RVNKIAKRNW KSFVDDDYSE MSGHLMMYPI KIRKNGMVGP LPGYETFPDV GGKILGASTN
LPDVLTT
//
