ID U5DET4_AMBTC Unreviewed; 848 AA.
AC U5DET4;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
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=AMTR_s00071p00126030 {ECO:0000313|EMBL:ERN19957.1};
OS Amborella trichopoda.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX NCBI_TaxID=13333 {ECO:0000313|EMBL:ERN19957.1, ECO:0000313|Proteomes:UP000017836};
RN [1] {ECO:0000313|Proteomes:UP000017836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24357323;
RG Amborella Genome Project;
RT "The Amborella genome and the evolution of flowering plants.";
RL Science 342:1241089-1241089(2013).
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; KI392062; ERN19957.1; -; Genomic_DNA.
DR RefSeq; XP_006858490.1; XM_006858428.2.
DR AlphaFoldDB; U5DET4; -.
DR STRING; 13333.U5DET4; -.
DR EnsemblPlants; ERN19957; ERN19957; AMTR_s00071p00126030.
DR GeneID; 18448359; -.
DR Gramene; ERN19957; ERN19957; AMTR_s00071p00126030.
DR KEGG; atr:18448359; -.
DR eggNOG; KOG1329; Eukaryota.
DR HOGENOM; CLU_004684_0_0_1; -.
DR OMA; MDMMYRI; -.
DR OrthoDB; 3014064at2759; -.
DR Proteomes; UP000017836; 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: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:UP000017836}.
FT DOMAIN 1..147
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 352..387
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 694..721
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 848 AA; 95871 MW; 41C2BB70C05AD7C1 CRC64;
MAESIHGSES EKVIFLHGDL DLSILEAKSL PNMDLVSERM RKCFTMFGTC KIPCKHGEKH
KGSKHKIITS DPYVSVCLAG ATVAQTRIIS NCEDPSWDEQ FHVSIAHPVS KVEFQVKDND
VLGAELIGVV SISAEKIQTG NTITGWFPIL GQYGNPFKPY PELHLSMQFR PVENNPLYKD
GVGAGPDYLG VPNTYFPLRR GGKVTLYQDA HVPDELLPEI QLDGGKLLQH NKCWEDICHA
ILEAHHLIYI IGWSIFHKVK LVREPTRPLP NGGELSLGDL LKFKSQEGVR VVLLIWDDKT
SHDMLLLKTE GVMQTHDEQT LKFFKHSSVH CALSPRYASN KLSIFKQQVV GTLFTHHQKC
VLVDTQASGN NRKITAFIGG LDLCDGRYDT PEHRLFRDLD SVFANDFHNP TFATCTRGPR
QPWHDLHCKI EGPAAYDILT NFEQRWRKAT KWREFKLKKV THWHDDALIK LERISWILSP
STSVPSDDFN LWVSHEDDGE CWHVQVFRSI DSGSVKGFPK VGQEAEAKNL VCGKNLVIDK
SIHAAYVKAI RSAQHFIYIE NQYFLGSSYH WPSYKNAGAD NLIPMELALK IASKIVANER
FAVYIVIPMW PEGVPASASV QEILFWQGQT MDMMYRIIGQ ALQQAGLAGK SHPQDYLNFY
CLGNRERGPR ERLASTSQPS ENSVLGLTQK FRRFMVYVHS KGMIVDDEYV ILGSANINQR
SMDGSRDTEI AMGAYQPHHK WAGSKGPPHG QVYGYRVSLW AEHLGFLEEC FHTPESMECV
TRVNHFAEYN WRTFISEEVK DMKGHLMRYP IKVDSEGRVG PLPGHECFPD VGGRILGSHN
SLPDSLTT
//