ID A0A0N4U644_DRAME Unreviewed; 341 AA.
AC A0A0N4U644;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=N-acetylphosphatidylethanolamine-hydrolyzing phospholipase D {ECO:0000256|ARBA:ARBA00012279};
DE EC=3.1.4.54 {ECO:0000256|ARBA:ARBA00012279};
GN ORFNames=DME_LOCUS6729 {ECO:0000313|EMBL:VDN56756.1};
OS Dracunculus medinensis (Guinea worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Dracunculoidea; Dracunculidae; Dracunculus.
OX NCBI_TaxID=318479 {ECO:0000313|Proteomes:UP000038040, ECO:0000313|WBParaSite:DME_0000236901-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:DME_0000236901-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDN56756.1, ECO:0000313|Proteomes:UP000274756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-1,2-di-(9Z-
CC octadecenoyl)-sn-glycero-3-phosphoethanolamine = 1,2-di-(9Z-
CC octadecenoyl)-sn-glycero-3-phosphate + H(+) + N-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-ethanolamine; Xref=Rhea:RHEA:45528,
CC ChEBI:CHEBI:2700, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:74546, ChEBI:CHEBI:85277;
CC Evidence={ECO:0000256|ARBA:ARBA00023540};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45529;
CC Evidence={ECO:0000256|ARBA:ARBA00023540};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR038896-51};
CC Note=Binds 2 zinc divalent cations per subunit.
CC {ECO:0000256|PIRSR:PIRSR038896-51};
CC -!- SIMILARITY: Belongs to the NAPE-PLD family.
CC {ECO:0000256|ARBA:ARBA00010127}.
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DR EMBL; UYYG01001157; VDN56756.1; -; Genomic_DNA.
DR STRING; 318479.A0A0N4U644; -.
DR WBParaSite; DME_0000236901-mRNA-1; DME_0000236901-mRNA-1; DME_0000236901.
DR Proteomes; UP000038040; Unplaced.
DR Proteomes; UP000274756; Unassembled WGS sequence.
DR GO; GO:0102200; F:N-acetylphosphatidylethanolamine-hydrolysing phospholipase activity; IEA:UniProtKB-EC.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009395; P:phospholipid catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR024884; NAPE-PLD.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR PANTHER; PTHR15032; N-ACYL-PHOSPHATIDYLETHANOLAMINE-HYDROLYZING PHOSPHOLIPASE D; 1.
DR PANTHER; PTHR15032:SF4; N-ACYL-PHOSPHATIDYLETHANOLAMINE-HYDROLYZING PHOSPHOLIPASE D; 1.
DR Pfam; PF12706; Lactamase_B_2; 1.
DR PIRSF; PIRSF038896; NAPE-PLD; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
PE 3: Inferred from homology;
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022668};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022668};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR038896-51};
KW Phospholipid degradation {ECO:0000256|ARBA:ARBA00022668};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00022668};
KW Reference proteome {ECO:0000313|Proteomes:UP000274756};
KW Zinc {ECO:0000256|PIRSR:PIRSR038896-51}.
FT DOMAIN 90..292
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|Pfam:PF12706"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR038896-51"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR038896-51"
FT BINDING 135
FT /ligand="N-acyl-1,2-diacyl-sn-glycero-3-
FT phosphoethanolamine"
FT /ligand_id="ChEBI:CHEBI:62537"
FT /evidence="ECO:0000256|PIRSR:PIRSR038896-50"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR038896-51"
FT BINDING 137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR038896-51"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR038896-51"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR038896-51"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR038896-51"
FT BINDING 269
FT /ligand="N-acyl-1,2-diacyl-sn-glycero-3-
FT phosphoethanolamine"
FT /ligand_id="ChEBI:CHEBI:62537"
FT /evidence="ECO:0000256|PIRSR:PIRSR038896-50"
FT BINDING 291
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR038896-51"
SQ SEQUENCE 341 AA; 39184 MW; FE55A0622E1CB0F1 CRC64;
MEMEENLFVK PEYNGNYFKN PSSFVGWTGL PNVLAILGWM MGPNSGRPPS KQVLDETLPV
YKPSFDVNNS SLQCTWLGHA TVLVHLDGIN FITDPVWSDT ASPFRTFGPK RYRQPPCSID
DLPDLDFAVI SHNHYDHFDA EAIQSLNKRF KRMQWYVPSG LKTYMHKYVP VENVHELSWG
ESKNLVIGDR EYYIHCVPAQ HWSQRGLFDR YKTLWSGWVV VGPTKRFYFA GDTGYCDEFR
KIKKIFGQID LATLPIGCYS PRWFMKPQHI DPAEAVQIHK DIGSKKSIGI HWGTYAMGST
EAYLEPADLL RDEVKKAGLN VNDFIVLHHG QTWTEVNCDE K
//
