PTER_PONAB
ID PTER_PONAB Reviewed; 349 AA.
AC Q5R5E9;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Phosphotriesterase-related protein;
DE EC=3.1.-.-;
DE AltName: Full=Parathion hydrolase-related protein;
GN Name=PTER;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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; CR860912; CAH93017.1; -; mRNA.
DR RefSeq; NP_001126783.1; NM_001133311.1.
DR AlphaFoldDB; Q5R5E9; -.
DR SMR; Q5R5E9; -.
DR STRING; 9601.ENSPPYP00000002456; -.
DR GeneID; 100173787; -.
DR KEGG; pon:100173787; -.
DR CTD; 9317; -.
DR eggNOG; ENOG502QQQR; Eukaryota.
DR InParanoid; Q5R5E9; -.
DR OrthoDB; 972282at2759; -.
DR Proteomes; UP000001595; Unplaced.
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 2: Evidence at transcript level;
KW Hydrolase; Metal-binding; Reference proteome.
FT CHAIN 1..349
FT /note="Phosphotriesterase-related protein"
FT /id="PRO_0000388666"
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; 38966 MW; 02F5A54248B620B6 CRC64;
MSSLSGKVQT VLGLVEPSKL GRTLTHEHLA MTFDCCYCPP PPCQEAISKE PIVMKNLYWI
QKNAYSHKEN LQLNQETEAI KEELLYFKAN GGGALVENTT TGISRDTQTL KRLAEETGVH
IISGAGFYVD ATHSSETRAM SVEQLTDVLM NGILHGADGT SIKCGVIGEI GCSWPLTESE
RKVLQATAHA QAQLGCPVII HPGRSSRAPF QIIRILQEAG ADISKTVMSH LDRTILDKKE
LLEFAQLGCY SEYDLFGTEL LHYQLGPDID MPDDNKRIRR VRLLVEEGYE DRILVAHDIH
TKTRLMKYGG HGYSHILTNV VPKMLLRGIT ENVLDKILIE NPKQWLTFK
