ID A0A067FJJ9_CITSI Unreviewed; 852 AA.
AC A0A067FJJ9;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=CISIN_1g003057mg {ECO:0000313|EMBL:KDO63612.1};
OS Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=2711 {ECO:0000313|EMBL:KDO63612.1, ECO:0000313|Proteomes:UP000027120};
RN [1] {ECO:0000313|EMBL:KDO63612.1, ECO:0000313|Proteomes:UP000027120}
RP NUCLEOTIDE SEQUENCE.
RG International Citrus Genome Consortium;
RA Gmitter F., Chen C., Farmerie W., Harkins T., Desany B., Mohiuddin M.,
RA Kodira C., Borodovsky M., Lomsadze A., Burns P., Jenkins J., Prochnik S.,
RA Shu S., Chapman J., Pitluck S., Schmutz J., Rokhsar D.;
RL Submitted (APR-2014) 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}.
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DR EMBL; KK784912; KDO63612.1; -; Genomic_DNA.
DR EMBL; KK784912; KDO63613.1; -; Genomic_DNA.
DR STRING; 2711.A0A067FJJ9; -.
DR PaxDb; 2711-XP_006477359-1; -.
DR eggNOG; KOG1329; Eukaryota.
DR Proteomes; UP000027120; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:InterPro.
DR GO; GO:0009395; P:phospholipid catabolic process; IBA:GO_Central.
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:UP000027120}.
FT DOMAIN 26..165
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 364..399
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 698..725
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 852 AA; 95139 MW; E8ADEB4401BC2E7A CRC64;
MAAHPAYAET MSFGGSNHGQ GQEAVPFETH QGSLKVLLLH GNLDIWVKEA KNLPNMDMFH
KKIGDVFGKL NVKVTSKIES HLSDKITSDP YVTVSICGAV IGRTFVISNS ESPVWMQHFN
VPVAHSAAEV HFVVKDNDFV GSQIMGAVGI PVEKLCSGDK IEGAFPILNS SRKPCKAGAV
LSLSIQYTPV ENMSLYYRGV GSGPDYIGVP GTYFPLRRGG KVTLYQDAHA HDGCLADLKL
DGGVQFNHES CWQDVYDAIN QARRLIYITG WSVYHTVRLV RDGSNTLMLG DLLKIKSQEG
VRVLILAWDD PTSRSILGYK TDGIMSTNDE ETRRFFKHSS VQVLLCPRSA GKGHSFVKKQ
EVGTIYTHHQ KTVVVDADAG QFKRKIIAFV GGLDLCKGRY DTPAHPLFKT LETVHKDDYY
NPSLLEPIAG GPREPWHDLH CRIDGPAAYD ILTNFEERWL KASKPHGLQK LKSSNDDSLL
KLERIPEIVG MTEASYLSEN DPEAWHAQVF RSIDSNSVKG FPVEPRDATS MNLVCGKNVL
IDMSIHTAYV KAIRAAQHFI YIENQYFLGS SFNWDSHRDL GANNLIPMEI ALKIANKIRA
NERFAAYILI PMWPEGITTS PQIQRILYWQ HKTMQMMYET IYKALVESGL QNKYVPQDYL
NFFCLGNREA LDGVDSSNAK DSTAANTPQA LAKKNRRFQI YIHSKGMIVD DEYVIIGSAN
INQRSLEGTR DTEIAMGAYQ PRHTWASKLS NPYGQVYGYR MSLWAEHIGA IEECFNRPES
LGCVRRVRSL SEQNWKQYAA DEVTQLKGHL LKYPVDVDPT GKVNALPGCA QFPDVGGNIL
GSFIAIQENL TI
//
