PLDA1_VIGUN
ID PLDA1_VIGUN Reviewed; 809 AA.
AC O04865;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Phospholipase D alpha 1;
DE Short=PLD alpha 1;
DE EC=3.1.4.4;
DE AltName: Full=Choline phosphatase 1;
DE AltName: Full=Phosphatidylcholine-hydrolyzing phospholipase D 1;
GN Name=PLD1;
OS Vigna unguiculata (Cowpea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3917;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Epace-1; TISSUE=Leaf;
RA el Maarouf H., Pham Thi A.T., Gareil M., D'Arcy-Lameta A., Zuily-Fodil Y.;
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal
CC phosphodiesteric bond. Plays an important role in various cellular
CC processes.
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC -!- DOMAIN: C2 domain is a calcium-binding fold, and the binding promotes
CC the protein association with membranes. A lower affinity toward calcium
CC can be anticipated for PLD alpha due to the absence of two potential
CC calcium ligands.
CC -!- SIMILARITY: Belongs to the phospholipase D family. C2-PLD subfamily.
CC {ECO:0000305}.
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DR EMBL; U92656; AAB51392.1; -; mRNA.
DR PIR; T11695; T11695.
DR AlphaFoldDB; O04865; -.
DR SMR; O04865; -.
DR PRIDE; O04865; -.
DR BRENDA; 3.1.4.4; 6657.
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 Gene3D; 2.60.40.150; -; 1.
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; PTHR18896; 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; SSF49562; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50035; PLD; 2.
PE 2: Evidence at transcript level;
KW Calcium; Hydrolase; Lipid degradation; Lipid metabolism; Metal-binding;
KW Repeat.
FT CHAIN 1..809
FT /note="Phospholipase D alpha 1"
FT /id="PRO_0000218824"
FT DOMAIN 1..125
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 326..365
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT DOMAIN 655..682
FT /note="PLD phosphodiesterase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 331
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 333
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 338
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 660
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 662
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 667
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT BINDING 186
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 331
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58608"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 371
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 405
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 521
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58608"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 660
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58608"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 721
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
SQ SEQUENCE 809 AA; 91565 MW; 4EFE00B634DDD946 CRC64;
MAQILLHGTL HATIYEVDEL HGGGGGNFFS KLKQNIEETV GIGKGVTKLY ATIDLEKARV
GRTRIIENET TNPKWNESFH IYCGHLASNI IFTVKDDNPI GATLIGRAYV PVSEVLDGHE
IDKWVEILDT EKNPIEGGSK IHVRLQYFDV LKDRNWARGI RSPKYPGVPY TFFSQRQGCK
VFLYQDAHVP DNFVPKIPLA GGKNYEAHRC WEDIFDAITN AKHLIYITGW SVYTEISLIR
DSRRPKAGGD QTIGELLKKK ASEGVRVLML VWDDRTSVGL LKKDGLMATH DEETEQFFRD
TDVHCVLCPR NPDDGGSIVQ DLQISTMFTH HQKIVVVDSA LPGGGGSDKR RIVSFVGGLD
LCDGRYDTAF HSLFRTLDTA HHDDFHQPNF PGAAITKGGP REPWHDIHSR VEGPIAWDVL
FNFEQRWRKQ GGKDILAPLR ELEDVIIPPS PVTFPDDHET WNVQLFRSID GGAAFGFPDT
PEDAAKAGLV SGKDNIIDRS IQDAYIHAIR RAKNFIYIEN QYFLGSSFSW NNDDIKREEI
GALHLIPKEL SLKIVSKIEA GERFAVYVVV PMWPEGIPES SSVQAILDWQ KRTIEMMYKD
VVQALRAKGS DEDPRNYLTF FCLGNREVKK SGEYEPAEQP EPDSDYQRAQ EARRFMIYVH
TKMMIVDDEY IIIGSANINQ RSMDGARDSE IAMGGYQPYH LANTQPARGQ VYGFRMSLWY
EHLGMLHDTF QRPESEECIN KVNQIADKYW DLYSSESLER DLPGHLLRYP IGVASEGEVT
ELPGFEFFPD TKARILGAKA DYLPPILTT
