ID A0A077ZF93_TRITR Unreviewed; 346 AA.
AC A0A077ZF93;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 22-FEB-2023, entry version 32.
DE RecName: Full=N-acetylphosphatidylethanolamine-hydrolyzing phospholipase D {ECO:0000256|ARBA:ARBA00012279};
DE EC=3.1.4.54 {ECO:0000256|ARBA:ARBA00012279};
GN ORFNames=TTRE_0000739701 {ECO:0000313|EMBL:CDW59067.1};
OS Trichuris trichiura (Whipworm) (Trichocephalus trichiurus).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichuridae; Trichuris.
OX NCBI_TaxID=36087 {ECO:0000313|EMBL:CDW59067.1};
RN [1] {ECO:0000313|EMBL:CDW59067.1}
RP NUCLEOTIDE SEQUENCE.
RA Aslett M.;
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDW59067.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Foth B.J., Tsai I.J., Reid A.J., Bancroft A.J., Nichol S., Tracey A.,
RA Holroyd N., Cotton J.A., Stanley E.J., Zarowiecki M., Liu J.Z.,
RA Huckvale T., Cooper P.J., Grencis R.K., Berriman M.;
RT "The whipworm genome and dual-species transcriptomics of an intimate host-
RT pathogen interaction.";
RL Submitted (MAR-2014) 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; HG806490; CDW59067.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A077ZF93; -.
DR STRING; 36087.A0A077ZF93; -.
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 Zinc {ECO:0000256|PIRSR:PIRSR038896-51}.
FT DOMAIN 96..298
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|Pfam:PF12706"
FT BINDING 137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR038896-51"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR038896-51"
FT BINDING 140
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 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR038896-51"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR038896-51"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR038896-51"
FT BINDING 238
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR038896-51"
FT BINDING 238
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR038896-51"
FT BINDING 275
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 297
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR038896-51"
SQ SEQUENCE 346 AA; 39230 MW; 12C26545BE1A82A9 CRC64;
MSISESFSFD LLHPITENGK FKNPWPSSHP MPTFMEVLRW KFQSKNRLCS CQLEHSLGPY
LVPDFHEASS LATKHGLSAI WLGHSTVLVN FMKGTFLTDP IFSLSCSPLP FCGPKRISPI
PCKVSELPEI DGVIISHNHY DHLDLPTVRD LISRFGSRLT WFVPSGLKSW FSSLGDVTVN
ELTWNEEISF NSQVGGSFRI VCLPSQHWSM RSVFDRNRSL WCSWAIIGEQ RRFFFAGDTG
YCPAFKVVGT IHGPFDLAAI PIGCYEPRWF MKYQHVGPEE ALQIHKDVRS RTSLGIHWGT
YEMGSYEHAT EPPCKLAATA KAQKLENAFI TLAQGEIWKP FDEIKT
//
