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Database: UniProt
Entry: A0A093F3E3_GAVST
LinkDB: A0A093F3E3_GAVST
Original site: A0A093F3E3_GAVST 
ID   A0A093F3E3_GAVST        Unreviewed;       400 AA.
AC   A0A093F3E3;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D {ECO:0000256|ARBA:ARBA00016017};
DE            EC=3.1.4.54 {ECO:0000256|ARBA:ARBA00012279};
DE   Flags: Fragment;
GN   ORFNames=N328_10357 {ECO:0000313|EMBL:KFV52137.1};
OS   Gavia stellata (Red-throated diver) (Colymbus stellatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Gaviiformes; Gaviidae; Gavia.
OX   NCBI_TaxID=37040 {ECO:0000313|EMBL:KFV52137.1, ECO:0000313|Proteomes:UP000054313};
RN   [1] {ECO:0000313|EMBL:KFV52137.1, ECO:0000313|Proteomes:UP000054313}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N328 {ECO:0000313|EMBL:KFV52137.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-O-(1Z-octadecenoyl)-2-(9Z-octadecenoyl)-sn-glycero-3-
CC         phospho-N-hexadecanoyl-ethanolamine + H2O = 1-O-(1Z-octadecenoyl)-2-
CC         (9Z-octadecenoyl)-sn-glycero-3-phosphate + H(+) + N-
CC         hexadecanoylethanolamine; Xref=Rhea:RHEA:56464, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:71464, ChEBI:CHEBI:138663,
CC         ChEBI:CHEBI:140452; Evidence={ECO:0000256|ARBA:ARBA00024142};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56465;
CC         Evidence={ECO:0000256|ARBA:ARBA00024142};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N,1,2-tri-(9Z-octadecenoyl)-sn-glycero-3-
CC         phosphoethanolamine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate
CC         + H(+) + N-(9Z-octadecenoyl) ethanolamine; Xref=Rhea:RHEA:45532,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:71466,
CC         ChEBI:CHEBI:74546, ChEBI:CHEBI:85291;
CC         Evidence={ECO:0000256|ARBA:ARBA00023539};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45533;
CC         Evidence={ECO:0000256|ARBA:ARBA00023539};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N,1-diacyl-sn-glycero-3-phosphoethanolamine = a 1-acyl-
CC         sn-glycero-3-phosphate + an N-acylethanolamine + H(+);
CC         Xref=Rhea:RHEA:53164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:52640, ChEBI:CHEBI:57970, ChEBI:CHEBI:85216;
CC         Evidence={ECO:0000256|ARBA:ARBA00023521};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53165;
CC         Evidence={ECO:0000256|ARBA:ARBA00023521};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N,1-dihexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-
CC         glycero-3-phosphoethanolamine = 1-hexadecanoyl-2-(9Z,12Z-
CC         octadecadienoyl)-sn-glycero-3-phosphate + H(+) + N-
CC         hexadecanoylethanolamine; Xref=Rhea:RHEA:45596, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:71464, ChEBI:CHEBI:72860,
CC         ChEBI:CHEBI:85334; Evidence={ECO:0000256|ARBA:ARBA00023516};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45597;
CC         Evidence={ECO:0000256|ARBA:ARBA00023516};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N,1-dihexadecanoyl-sn-glycero-3-phosphoethanolamine = 1-
CC         hexadecanoyl-sn-glycero-3-phosphate + H(+) + N-
CC         hexadecanoylethanolamine; Xref=Rhea:RHEA:45592, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57518, ChEBI:CHEBI:71464,
CC         ChEBI:CHEBI:85335; Evidence={ECO:0000256|ARBA:ARBA00023492};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45593;
CC         Evidence={ECO:0000256|ARBA:ARBA00023492};
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-1,2-diacyl-sn-
CC         glycero-3-phosphoethanolamine = a 1,2-diacyl-sn-glycero-3-phosphate +
CC         H(+) + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine;
CC         Xref=Rhea:RHEA:56548, ChEBI:CHEBI:2700, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:58608, ChEBI:CHEBI:140532;
CC         Evidence={ECO:0000256|ARBA:ARBA00023542};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56549;
CC         Evidence={ECO:0000256|ARBA:ARBA00023542};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-1-(9Z-octadecenoyl)-
CC         sn-glycero-3-phosphoethanolamine = 1-(9Z-octadecenoyl)-sn-glycero-3-
CC         phosphate + H(+) + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine;
CC         Xref=Rhea:RHEA:45544, ChEBI:CHEBI:2700, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:74544, ChEBI:CHEBI:85223;
CC         Evidence={ECO:0000256|ARBA:ARBA00023561};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45545;
CC         Evidence={ECO:0000256|ARBA:ARBA00023561};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-butanoyl-1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-
CC         glycero-3-phosphoethanolamine = 1-hexadecanoyl-2-(9Z,12Z-
CC         octadecadienoyl)-sn-glycero-3-phosphate + H(+) + N-butanoyl
CC         ethanolamine; Xref=Rhea:RHEA:45620, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:72860, ChEBI:CHEBI:85298,
CC         ChEBI:CHEBI:85304; Evidence={ECO:0000256|ARBA:ARBA00023528};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45621;
CC         Evidence={ECO:0000256|ARBA:ARBA00023528};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-decanoyl-1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-
CC         glycero-3-phosphoethanolamine = 1-hexadecanoyl-2-(9Z,12Z-
CC         octadecadienoyl)-sn-glycero-3-phosphate + H(+) + N-decanoyl
CC         ethanolamine; Xref=Rhea:RHEA:45608, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:72860, ChEBI:CHEBI:85295,
CC         ChEBI:CHEBI:85301; Evidence={ECO:0000256|ARBA:ARBA00023560};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45609;
CC         Evidence={ECO:0000256|ARBA:ARBA00023560};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-dodecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-
CC         phosphoethanolamine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate
CC         + H(+) + N-dodecanoylethanolamine; Xref=Rhea:RHEA:45556,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:74546,
CC         ChEBI:CHEBI:85263, ChEBI:CHEBI:85294;
CC         Evidence={ECO:0000256|ARBA:ARBA00023499};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45557;
CC         Evidence={ECO:0000256|ARBA:ARBA00023499};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-hexadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-
CC         phosphoethanolamine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate
CC         + H(+) + N-hexadecanoylethanolamine; Xref=Rhea:RHEA:45540,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:71464,
CC         ChEBI:CHEBI:74546, ChEBI:CHEBI:78097;
CC         Evidence={ECO:0000256|ARBA:ARBA00023534};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45541;
CC         Evidence={ECO:0000256|ARBA:ARBA00023534};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-hexanoyl-1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-
CC         glycero-3-phosphoethanolamine = 1-hexadecanoyl-2-(9Z,12Z-
CC         octadecadienoyl)-sn-glycero-3-phosphate + H(+) + N-hexanoyl
CC         ethanolamine; Xref=Rhea:RHEA:45616, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:72860, ChEBI:CHEBI:85297,
CC         ChEBI:CHEBI:85303; Evidence={ECO:0000256|ARBA:ARBA00023523};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45617;
CC         Evidence={ECO:0000256|ARBA:ARBA00023523};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-octadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-
CC         phosphoethanolamine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate
CC         + H(+) + N-octadecanoyl ethanolamine; Xref=Rhea:RHEA:45536,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:74546,
CC         ChEBI:CHEBI:85292, ChEBI:CHEBI:85299;
CC         Evidence={ECO:0000256|ARBA:ARBA00023524};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45537;
CC         Evidence={ECO:0000256|ARBA:ARBA00023524};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-octanoyl-1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-
CC         glycero-3-phosphoethanolamine = 1-hexadecanoyl-2-(9Z,12Z-
CC         octadecadienoyl)-sn-glycero-3-phosphate + H(+) + N-octanoyl
CC         ethanolamine; Xref=Rhea:RHEA:45612, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:72860, ChEBI:CHEBI:85296,
CC         ChEBI:CHEBI:85302; Evidence={ECO:0000256|ARBA:ARBA00023500};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45613;
CC         Evidence={ECO:0000256|ARBA:ARBA00023500};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-tetradecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-
CC         phosphoethanolamine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate
CC         + H(+) + N-tetradecanoylethanolamine; Xref=Rhea:RHEA:45552,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:74546,
CC         ChEBI:CHEBI:85262, ChEBI:CHEBI:85293;
CC         Evidence={ECO:0000256|ARBA:ARBA00023547};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45553;
CC         Evidence={ECO:0000256|ARBA:ARBA00023547};
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   -!- SUBUNIT: Homodimer. Bile acids promote the assembly of inactive
CC       monomers into an active dimer and enable catalysis.
CC       {ECO:0000256|ARBA:ARBA00011543}.
CC   -!- SUBCELLULAR LOCATION: Early endosome membrane
CC       {ECO:0000256|ARBA:ARBA00004220}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004220}. Golgi apparatus membrane
CC       {ECO:0000256|ARBA:ARBA00004395}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004395}.
CC   -!- SIMILARITY: Belongs to the NAPE-PLD family.
CC       {ECO:0000256|ARBA:ARBA00010127}.
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DR   EMBL; KK623020; KFV52137.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093F3E3; -.
DR   Proteomes; UP000054313; Unassembled WGS sequence.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
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:ARBA00022963};
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:ARBA00023264};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054313};
KW   Zinc {ECO:0000256|PIRSR:PIRSR038896-51}.
FT   DOMAIN          151..351
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|Pfam:PF12706"
FT   REGION          1..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..51
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         192
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038896-51"
FT   BINDING         194
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038896-51"
FT   BINDING         195
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         196
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038896-51"
FT   BINDING         197
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038896-51"
FT   BINDING         260
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038896-51"
FT   BINDING         263
FT                   /ligand="deoxycholate"
FT                   /ligand_id="ChEBI:CHEBI:23614"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038896-52"
FT   BINDING         267
FT                   /ligand="deoxycholate"
FT                   /ligand_id="ChEBI:CHEBI:23614"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038896-52"
FT   BINDING         291
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038896-51"
FT   BINDING         291
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038896-51"
FT   BINDING         328
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         350
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038896-51"
FT   BINDING         355
FT                   /ligand="deoxycholate"
FT                   /ligand_id="ChEBI:CHEBI:23614"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038896-52"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFV52137.1"
FT   NON_TER         400
FT                   /evidence="ECO:0000313|EMBL:KFV52137.1"
SQ   SEQUENCE   400 AA;  46118 MW;  BA4D4973A10A7D70 CRC64;
     SPPQKDMDKK MDEEQTSTAC NQYPKEAVKK RQNSGRGSRG SDSSRTSRKS FRLDYRLEED
     VTKSKRGKDG KFVNPWPTWK SPTLPNVLKW YFMEKNNSNV PCSKQELDKE LPVLKPYFVQ
     KPELAGKTGT GMRVTWLGHA SVMVEMDEII FLTDPIFSQR ASPTQLVGPK RFRGPPCTVE
     QLPKIDAVVI SHTHYDHLDY NTVTSLNERF GSELRWFVPL GLLNWMQRCG CENVIELDWW
     EENCVPGHDA VTFVFTPSQH WCKRTVTDDN KVLWGSWSVL GPWNRFFFSG DTGYCVAFEQ
     IGKRFGPFDL AAIPIGAYEP RWFMKYQHVD PEEAVRIHID VQAKKSVAIH WGTFALANEY
     YLDPPVKLNE ALERYGLKKE DFFLLNHGES RDLSTNDGFE
//
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