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Database: UniProt
Entry: A0A087RKS1_APTFO
LinkDB: A0A087RKS1_APTFO
Original site: A0A087RKS1_APTFO 
ID   A0A087RKS1_APTFO        Unreviewed;       400 AA.
AC   A0A087RKS1;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
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=AS27_01714 {ECO:0000313|EMBL:KFM14075.1};
OS   Aptenodytes forsteri (Emperor penguin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC   Aptenodytes.
OX   NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM14075.1, ECO:0000313|Proteomes:UP000053286};
RN   [1] {ECO:0000313|EMBL:KFM14075.1, ECO:0000313|Proteomes:UP000053286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM14075.1};
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; KL226413; KFM14075.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A087RKS1; -.
DR   STRING; 9233.A0A087RKS1; -.
DR   Proteomes; UP000053286; 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:UP000053286};
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        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:KFM14075.1"
FT   NON_TER         400
FT                   /evidence="ECO:0000313|EMBL:KFM14075.1"
SQ   SEQUENCE   400 AA;  45981 MW;  C9E9BC39686E72D3 CRC64;
     SSPQKDMDKK MGEEQPLTAC NQYPKEAVRK RQNSGRGSRG SDSSRTSRKS FRLDYRLEED
     VTKSKRGKDG KFVNPWPTWK SPTLPNILKW SLMEKNNSNV PCSKQELDKE LPVLKPYFVQ
     KPELAGKTGT GMRVTWLGHA SVMVEMDELV FLTDPIFSQR ASPTQLVGPK RFRGPPCTVE
     QLPKIDAVMI SHTHYDHLDY NTVTSLNERF GSELRWFVPL GLLDWMQRCG CENVIELDWW
     EENCVPGHDA VTFVFTPSQH WCKRTATDDN KVLWGSWSVL GPWNRFFFSG DTGYCVAFEQ
     IGKRFGPFDL AAIPIGAYEP RWFMKYQHVD PEEAVRIHID VQAKKSVAIH WGTFALANEY
     YLDPPVKLNE ALERYGLKKE DFFVLNHGES RDLSTNDGFE
//
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