PLDA1_TOBAC
ID PLDA1_TOBAC Reviewed; 808 AA.
AC P93400; P93399;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 2.
DT 03-AUG-2022, entry version 90.
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 Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. SR1; TISSUE=Leaf;
RA Lein W., Saalbach G.;
RL Submitted (FEB-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; Z84822; CAB06620.1; -; mRNA.
DR PIR; T04092; T04092.
DR RefSeq; NP_001312217.1; NM_001325288.1.
DR STRING; 4097.P93400; -.
DR PRIDE; P93400; -.
DR ProMEX; P93400; -.
DR GeneID; 107779725; -.
DR KEGG; nta:107779725; -.
DR BRENDA; 3.1.4.4; 3645.
DR Proteomes; UP000084051; Unplaced.
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 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 Reference proteome; Repeat.
FT CHAIN 1..808
FT /note="Phospholipase D alpha 1"
FT /id="PRO_0000218823"
FT DOMAIN 1..125
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 326..364
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT DOMAIN 654..681
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 659
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 661
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 666
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 370
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 404
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 520
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58608"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 659
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58608"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 720
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
SQ SEQUENCE 808 AA; 91967 MW; 2937FCA5D5C60B6A CRC64;
MAQILLHGTL HVTIYEVDNL QKEGGGHFFS KIKEHVEETI GFGKGTPAIY ATVDLEKARV
GRTRKIKNEP NNPRWYESFH IYCAHMASNV IFTVKDDNPI GATLIGRAYV PVEELLEGEE
IDKWVEILDR EMNPIAEGSK IHVKLQFFDV SRDPNWERGI RSSKYPGVPY TFFAQRTGCR
VSLYQDAHVP DNFIPKIPLS GGKYYEPHRC WEDIFDAIIN AKHLIYITGW SVYTEITLVR
DSRRQKPGGD ITLGELLKKK ASEGVKVLML VWDDRTSVGL LKKDGLMATH DQETEQFFQG
TEVNCVLCPR NPDDGGSIVQ SLQIGTMFTH HQKIVVVDSE LPSGESEKRR ILSFVGGIDL
CDGRYDTPFH SLFRTLDTAH HDDFHQPNFP DGAITKGGPR EPWHDIHSRL EGPIAWDVLF
NFEQRWRKQG GKDVLVNFRE LDDIIIPPSP VMHLDDSETW NVQLFRSIDE GAAFGFPETP
EDAAKAGLVS GXDNIIDRSI QDAYIHAIRR AKNFIYIENQ YFLGSSYDWQ SDDIKVEDIG
ALHVIPKELA LKIVSKIEAG ERFTVYVVVP MWPEGIPESA SVQAILDWQR RTMEMMYKHI
VQALNAKGIE EDPRNYLTFF CIGNREVKKS GAYEPSETPE PDSDYIRAQE ARRFMIYVHS
KMMIVDDEYI IVGSANINQR SMDGARDSEI AMGAYQPHHL ATREPARGQI HGFRMALWYE
HLGMLDETFL HPESEECVSK VNRMADKYWD LYSSESLERD LPGHLLRYPI GVASEGDVTE
LPGAEHFPDT KARVLGTKSD YLPPILTT
