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Database: UniProt
Entry: A0A3P8T5U0_AMPPE
LinkDB: A0A3P8T5U0_AMPPE
Original site: A0A3P8T5U0_AMPPE 
ID   A0A3P8T5U0_AMPPE        Unreviewed;       337 AA.
AC   A0A3P8T5U0;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Paraoxonase {ECO:0000256|RuleBase:RU368025};
DE            EC=3.1.1.2 {ECO:0000256|RuleBase:RU368025};
OS   Amphiprion percula (Orange clownfish) (Lutjanus percula).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Amphiprion.
OX   NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000019548.1, ECO:0000313|Proteomes:UP000265080};
RN   [1] {ECO:0000313|Ensembl:ENSAPEP00000019548.1, ECO:0000313|Proteomes:UP000265080}
RP   NUCLEOTIDE SEQUENCE.
RA   Lehmann R.;
RT   "Finding Nemo's genes: A chromosome-scale reference assembly of the genome
RT   of the orange clownfish Amphiprion percula.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSAPEP00000019548.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a phenyl acetate + H2O = a phenol + acetate + H(+);
CC         Xref=Rhea:RHEA:17309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30089, ChEBI:CHEBI:33853, ChEBI:CHEBI:140310; EC=3.1.1.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00000368,
CC         ECO:0000256|RuleBase:RU368025};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602640-2,
CC         ECO:0000256|RuleBase:RU368025};
CC       Note=Binds 2 calcium ions per subunit. {ECO:0000256|PIRSR:PIRSR602640-
CC       2, ECO:0000256|RuleBase:RU368025};
CC   -!- SIMILARITY: Belongs to the paraoxonase family.
CC       {ECO:0000256|ARBA:ARBA00008595, ECO:0000256|RuleBase:RU368025}.
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DR   AlphaFoldDB; A0A3P8T5U0; -.
DR   Ensembl; ENSAPET00000020076.1; ENSAPEP00000019548.1; ENSAPEG00000013924.1.
DR   GeneTree; ENSGT00390000008932; -.
DR   Proteomes; UP000265080; Chromosome 7.
DR   GO; GO:0004064; F:arylesterase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR002640; Arylesterase.
DR   PANTHER; PTHR11799; PARAOXONASE; 1.
DR   PANTHER; PTHR11799:SF12; PARAOXONASE-RELATED; 1.
DR   Pfam; PF01731; Arylesterase; 1.
DR   PRINTS; PR01785; PARAOXONASE.
DR   SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|PIRSR:PIRSR602640-2, ECO:0000256|RuleBase:RU368025};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR602640-3,
KW   ECO:0000256|RuleBase:RU368025};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180,
KW   ECO:0000256|RuleBase:RU368025};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368025};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR602640-2,
KW   ECO:0000256|RuleBase:RU368025};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265080}.
FT   ACT_SITE        94
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602640-1"
FT   BINDING         35
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT   BINDING         36
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT   BINDING         96
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT   BINDING         148
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT   BINDING         149
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT   BINDING         205
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT   BINDING         250
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT   BINDING         251
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT   DISULFID        24..334
FT                   /note="In form B"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602640-3"
SQ   SEQUENCE   337 AA;  38176 MW;  81A90FD0B3F5674F CRC64;
     MTFTHCRKRF LATREPAKNH LPNCVLLKNL EHGTEDIMIL GDGLAFISAG LKYPGIPSSD
     EPGKIFVLDL KDSRMKPMEL RMPRNFDLET FNPHGISLYT DPSDDAVYLF VVNHPHHKSQ
     IEVFKFVEEE LSLVHLKTIK HELLHSVNDI VAVGVDSFYA TNDHYFENQF LKSYVEMLLC
     QPWGNVVYYS PTEVKEVSQG YYFANGINMS PDKRHIYVAD VFDHTVHVFE RKEDNALTRV
     KTVAVGSLVD NIEVDPETGD LWVGCHPNAW KLFFFDPNDP AGSEVIRIQN IHSDKPQVTQ
     VYEDDGHVLI GSSVAATYGG KLLIGTVFHK ALVCDLK
//
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