PLD_PHYIN
ID PLD_PHYIN Reviewed; 1807 AA.
AC Q5BMR2;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 58.
DE RecName: Full=Phospholipase D;
DE EC=3.1.4.4;
DE AltName: Full=PiPLD1;
GN Name=PLD {ECO:0000303|PubMed:15826868};
OS Phytophthora infestans (Potato late blight agent) (Botrytis infestans).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4787;
RN [1] {ECO:0000312|EMBL:AAX28839.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15826868; DOI=10.1016/j.gene.2005.02.012;
RA Meijer H.J.G., Latijnhouwers M., Ligterink W., Govers F.;
RT "A transmembrane phospholipase D in Phytophthora; a novel PLD subfamily.";
RL Gene 350:173-182(2005).
CC -!- FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal
CC phosphodiesteric bond. {ECO:0000305}.
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:0000305};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the phospholipase D family. TM-PLD subfamily.
CC {ECO:0000255, ECO:0000305}.
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DR EMBL; AY929154; AAX28839.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5BMR2; -.
DR SMR; Q5BMR2; -.
DR VEuPathDB; FungiDB:PITG_00284; -.
DR BRENDA; 3.1.4.4; 4811.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-EC.
DR GO; GO:0004630; F:phospholipase D activity; NAS:UniProtKB.
DR GO; GO:0046475; P:glycerophospholipid catabolic process; NAS:UniProtKB.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR InterPro; IPR015679; PLipase_D_fam.
DR PANTHER; PTHR18896; PTHR18896; 1.
DR Pfam; PF00614; PLDc; 1.
DR SMART; SM00155; PLDc; 2.
DR PROSITE; PS50035; PLD; 2.
PE 3: Inferred from homology;
KW Hydrolase; Lipid degradation; Lipid metabolism; Membrane; Repeat;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..1807
FT /note="Phospholipase D"
FT /id="PRO_0000239465"
FT TRANSMEM 257..277
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 587..607
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 853..880
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT DOMAIN 1249..1276
FT /note="PLD phosphodiesterase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1531..1621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..725
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1531..1583
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1598..1621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 858
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 860
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 865
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 1254
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 1256
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 1261
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
SQ SEQUENCE 1807 AA; 203320 MW; A3F18D62F52E0A56 CRC64;
MPGPDDDVRE PTAAARTNNS GYGLRAAPSS ITSGLDSVVS VNSYRSSELN AEEVNVDDQE
CADSDILESP NDGMTIMNDD DADLSEEEEE VMENSIDFSV NRATVTKAGV IPCCVFVGRV
RWGTTDWEIY FGQKQLLRLH FNLHLYSLFN RHKLLRGVHL PCTIWREKRA EKRVMDVYVV
QDYIRQLLKD RDLRNSEPLL SFLEVSPSRA MLRLGPSLKE GYVHMRINGP FQLPLYTCFN
RTIEALYRHL YRAWMRIAFV SAIVGFIFPI CLVIVTSLPT FFSPQKELVN SDSGTKEVST
KLNTAGVFLG LAVLGGILFF AVFVYKFFQH RLGVIRRWVV LKPSCFAAYR NRNDREPSEV
FLFDKNFTAR KGSYRQGVSW MPSGLVVGSK AGDIEIDTGH YYTRLTAFVA LMGVCYGIMR
LSNSIYDFEY LSLDKSMGVP ITNASGYENW TESRDAEYCG YYFIVPKGTT VYVESKDDSA
VISQLQMPSS NSMTANLGFF WQSDSMGYSL NVITNAVGAG TMVSVVKPID AKNDRFFESG
TNYSMPTVGN LTLEGVKTDI DVQSFSNVES FCAITVRIAP LTWRSYVYYI LFLFAGGIIA
PVVGFLANYF VTYLGIWHPH VRRDHWFRCV RRLQKLKRQE TSTRFNSFAP QHISTIDDDE
SATITAKAKA AKLAIGNTPT SNINQVVDSV VKQEAETASR MGTGNLAPAS SRVDSSTQSE
DSFEAPKPPP SSVSWHVDAE DTYAAMYKAI SNAKYEILIA GWWVCPDLFL LRPGRKLPPR
EADEDPDGQQ VNKTMLRQVL MKKAEAGVKI YVLIYREVKL ALTLNSAYTK RSLMVHPNIR
VLRDPIFQIQ SLGFWSHHEK IVCIDQSLAF VGGLDLCFGR YDHHGHPISD PSDDPVWTGK
DYSNPIIKDF VRVNKPFEDL IDRASQPRMP WHDVHCSISG PPVQDVAYHL IQRWNFVCSK
NDYQLRTGWC ICFRSRRFKF LPKCLVPMDF NGWTLQYPSS DPEPMRDGST RTTIPLVRED
SLSMVEPFQV VQSVNPMYPC TATGPQWPPT SSLHPINPMR PPLTSASTTT GPLDDGEVLR
AQRGESILQV FHPSANICNI QVCRSVSMWS AGVPTEASIQ AAYMDVIANS KHFLYIENQF
FVSGMDGNGI VRNRILQALV DRIERAVQRD EKFRVYVVMP LLPAFEGNIR SHELTNLHAV
MHWQFATICR GRYSLFEALK GVTNHPENYV AFFGLRKYGI MPNGCAATEQ IYIHSKLMIA
DDRCAILGSA NINDRSMNGD RDSEIALVIE DMQYEDGVMN EKPYRRGVAA SKLRLQLFRE
HLGLADDDLS VADPTSDHTW QAIKSTASSN TKIFEAVFDC APSNRMRAFV NFQSIEVTQI
FENQRMNVLK VPGRSHVWDA QNLKDGDYAP WTDVNGVPIA ADRVDLRDFE VDNYRDKKKK
LFSMDHDGWC YARNFSIFQE VRTMKTDYKK REKLQHLVAD RLMAQVRRRR WVKKGLLPPR
DPRESSFSLA SDDEEHGRFY SLWRRLQQGD FSRSNSVSTP TNFSQLDTDG GISGSVSVGG
TNHGRRLYNS NSMPSNASIL GDNPTTRPPV LGDAPSYPNS PSVASFQHTP QSPAIATGAR
SVRSARTSSL LCTGAGVRTR GNTRSARGSF YGMFSVTGNR NLDTDDESSD AGSEYGGGHG
IRASLKRWYS TMDVLDFGRR SKFNAEYFDT DEDHLHSDDP LLEDGRGSYH AATREGLLTE
EAVEGSDDED AECQIGHVQT AATVRKEDET RARAQLSEIR GHLVEFPLDF LVEEILKPSV
LPADIHI
