ID   PTER_TETNG              Reviewed;         349 AA.
AC   Q4RWX9;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Phosphotriesterase-related protein;
DE            EC=3.1.-.-;
DE   AltName: Full=Parathion hydrolase-related protein;
GN   Name=pter; ORFNames=GSTENG00027649001;
OS   Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS   nigroviridis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX   NCBI_TaxID=99883;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15496914; DOI=10.1038/nature03025;
RA   Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA   Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA   Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA   Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA   Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA   Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA   Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA   McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA   Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA   Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA   Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT   "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT   early vertebrate proto-karyotype.";
RL   Nature 431:946-957(2004).
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250};
CC       Note=Binds 2 divalent metal cations per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Phosphotriesterase family. {ECO:0000255|PROSITE-ProRule:PRU00679}.
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DR   EMBL; CAAE01014981; CAG07103.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4RWX9; -.
DR   SMR; Q4RWX9; -.
DR   STRING; 99883.ENSTNIP00000017883; -.
DR   Ensembl; ENSTNIT00000018107; ENSTNIP00000017883; ENSTNIG00000014842.
DR   KEGG; tng:GSTEN00027649G001; -.
DR   GeneTree; ENSGT00390000006960; -.
DR   HOGENOM; CLU_054760_0_1_1; -.
DR   InParanoid; Q4RWX9; -.
DR   OMA; MVKCGFI; -.
DR   TreeFam; TF323205; -.
DR   Proteomes; UP000007303; Unassembled WGS sequence.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0009056; P:catabolic process; IEA:InterPro.
DR   CDD; cd00530; PTE; 1.
DR   InterPro; IPR017947; AryldialkylPase_Zn-BS.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR001559; Phosphotriesterase.
DR   PANTHER; PTHR10819; PTHR10819; 1.
DR   Pfam; PF02126; PTE; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   PROSITE; PS01322; PHOSPHOTRIESTERASE_1; 1.
DR   PROSITE; PS51347; PHOSPHOTRIESTERASE_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Reference proteome.
FT   CHAIN           1..349
FT                   /note="Phosphotriesterase-related protein"
FT                   /id="PRO_0000388669"
FT   BINDING         26
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P45548"
FT   BINDING         28
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P45548"
FT   BINDING         169
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P45548"
FT   BINDING         169
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P45548"
FT   BINDING         201
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P45548"
FT   BINDING         230
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P45548"
FT   BINDING         298
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P45548"
SQ   SEQUENCE   349 AA;  38894 MW;  4C45BBBA781B9B27 CRC64;
     MSNLSGKVQT VLGPVDPEQL GKTLTHEHLT MSFECCYHPP PAGDEAVAES PFQMQHMYWL
     RQNPYSCHEN LLLLQETLAV REELLAYRKA GGGAVVENTT TGIQRDLPTL RQLSKDTGVH
     IIAGAGYYVD CTHTEDTRRM SVEKLSDVIV SEVLHGADGT DIRCGVIGEI GTCWPITDSE
     RKVLKATAHA QSQLGCPVII HPGRNPAAPA EVVRILQEAG GDISKTVMSH LDRTIFDEGE
     LLEFAKLGSY LEYDLFGMEM LNYPYNSEVD MPSDSQRVKA LAFLVKEGYE DKIVVAHDIH
     TKNRLTKFGG HGYSHILKNI VPKMLRRGIS QRQVDKILVD NPKEWLTFK