PTER_DROER
ID PTER_DROER Reviewed; 350 AA.
AC B3P1R1;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Phosphotriesterase-related protein;
DE EC=3.1.-.-;
DE AltName: Full=Parathion hydrolase-related protein;
GN ORFNames=GG16392;
OS Drosophila erecta (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7220;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14021-0224.01;
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:P45548};
CC Note=Binds 2 divalent metal cations per subunit.
CC {ECO:0000250|UniProtKB:P45548};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Phosphotriesterase family. {ECO:0000255|PROSITE-ProRule:PRU00679}.
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DR EMBL; CH954181; EDV49799.1; -; Genomic_DNA.
DR RefSeq; XP_001980841.1; XM_001980805.2.
DR AlphaFoldDB; B3P1R1; -.
DR SMR; B3P1R1; -.
DR STRING; 7220.FBpp0134938; -.
DR EnsemblMetazoa; FBtr0136446; FBpp0134938; FBgn0108624.
DR GeneID; 6552545; -.
DR KEGG; der:6552545; -.
DR eggNOG; ENOG502QQQR; Eukaryota.
DR HOGENOM; CLU_054760_0_1_1; -.
DR OMA; MVKCGFI; -.
DR OrthoDB; 972282at2759; -.
DR PhylomeDB; B3P1R1; -.
DR Proteomes; UP000008711; 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.
FT CHAIN 1..350
FT /note="Phosphotriesterase-related protein"
FT /id="PRO_0000388674"
FT BINDING 22
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P45548"
FT BINDING 24
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 350 AA; 39317 MW; 2B6E101672F5AAB0 CRC64;
MSTVQTVLGT ITPNLLGRTL THEHVALDFE HFYRPPPPDF ECELKAKISM STLGYVRLYP
YSSKENVRFY DGEALEAAKK DVLLYKKHGG GSIVENSSYG LKRNLEFIVE LAKSTGVHFI
AGTGHYIHAM QDASHASLSV EQMSDLYSKD IITGLQVNGK MVKCGFIGEV ASVYPIHDFE
KNAIKAAGEI QEVLGCGVSM HPHRVTKAPF EIMRLYLEAG GRADKCVMSH LDRTIFDIDE
LLEFAKLGCY IQYDLFGTEC SFYQLNTSVD MISDGQRIDN LIKLIKEGLV DKLLMSHDIH
TKHRLTSYGG HGYHHIHTNI LPRMFDRGVT LEQVEQMTVT NPANWLAFDP
