ID   PYRHY_SPHWJ             Reviewed;         280 AA.
AC   C0LA90;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 31.
DE   RecName: Full=Pyrethroid hydrolase;
DE            EC=3.1.1.88;
GN   Name=pytH;
OS   Sphingobium wenxiniae (strain DSM 21828 / JZ-1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=595605;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX   PubMed=19581484; DOI=10.1128/aem.01298-09;
RA   Wang B.Z., Guo P., Hang B.J., Li L., He J., Li S.P.;
RT   "Cloning of a novel pyrethroid-hydrolyzing carboxylesterase gene from
RT   Sphingobium sp. strain JZ-1 and characterization of the gene product.";
RL   Appl. Environ. Microbiol. 75:5496-5500(2009).
CC   -!- FUNCTION: Catalyzes the hydrolysis of pyrethroids pesticides. Catalyzes
CC       the hydrolysis of cypermethrin to equimolar amounts of cyano-3-
CC       phenoxybenzyl alcohol and 2,2-dimethyl-3-(2,2-dichlorovinyl)-
CC       cyclopropanecarboxylic acid. Hydrolyzes cis-permethrin at approximately
CC       equal rate to trans-permethrin. {ECO:0000269|PubMed:19581484}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(-)-trans-permethrin + H2O = (1S,3R)-3-(2,2-dichlorovinyl)-
CC         2,2-dimethylcyclopropanecarboxylate + (3-phenoxyphenyl)methanol +
CC         H(+); Xref=Rhea:RHEA:30283, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:62523, ChEBI:CHEBI:62527, ChEBI:CHEBI:62531; EC=3.1.1.88;
CC         Evidence={ECO:0000269|PubMed:19581484};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.062 uM for trans-Permethrin {ECO:0000269|PubMed:19581484};
CC         KM=0.065 uM for cis-Permethrin {ECO:0000269|PubMed:19581484};
CC         KM=0.106 uM for Fenpropathrin {ECO:0000269|PubMed:19581484};
CC         KM=0.110 uM for trans-Cypermethrin {ECO:0000269|PubMed:19581484};
CC         KM=0.108 uM for cis-Cypermethrin {ECO:0000269|PubMed:19581484};
CC         KM=0.348 uM for Cyhalothrin {ECO:0000269|PubMed:19581484};
CC         KM=0.585 uM for Fenvalerate {ECO:0000269|PubMed:19581484};
CC         KM=0.788 uM for Deltamethrin {ECO:0000269|PubMed:19581484};
CC         KM=1.586 uM for Bifenthrin {ECO:0000269|PubMed:19581484};
CC         KM=124 uM for p-Nitrophenyl acetate {ECO:0000269|PubMed:19581484};
CC         KM=176 uM for p-Nitrophenyl butyrate {ECO:0000269|PubMed:19581484};
CC         KM=325 uM for p-Nitrophenyl caproate {ECO:0000269|PubMed:19581484};
CC         Note=kcat is 3.03 sec(-1) with trans-Permethrin acetate as substrate.
CC         kcat is 3.00 sec(-1) with cis-Permethrin acetate as substrate. kcat
CC         is 2.61 sec(-1) with Fenpropathrin acetate as substrate. kcat is 2.53
CC         sec(-1) with trans-Cypermethrin acetate as substrate. kcat is 2.57
CC         sec(-1) with cis-Cypermethrin acetate as substrate. kcat is 1.28
CC         sec(-1) with Cyhalothrin acetate as substrate. kcat is 0.91 sec(-1)
CC         with Fenvalerate acetate as substrate. kcat is 0.79 sec(-1) with
CC         Deltamethrin acetate as substrate. kcat is 0.44 sec(-1) with
CC         Bifenthrin acetate as substrate. kcat is 183 sec(-1) with p-
CC         Nitrophenyl acetate as substrate. kcat is 118 sec(-1) with p-
CC         Nitrophenyl butyrate acetate as substrate. kcat is 49 sec(-1) with p-
CC         Nitrophenyl caproate acetate as substrate.;
CC       pH dependence:
CC         Optimum pH is 7.5. {ECO:0000269|PubMed:19581484};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:19581484}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
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DR   EMBL; FJ688006; ACM79141.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0LA90; -.
DR   SMR; C0LA90; -.
DR   ESTHER; sphwj-c0la90; HNLyase_Bact.
DR   KEGG; ag:ACM79141; -.
DR   BRENDA; 3.1.1.88; 7695.
DR   SABIO-RK; C0LA90; -.
DR   GO; GO:0102209; F:trans-permethrin hydrolase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR045889; MES/HNL.
DR   PANTHER; PTHR10992; PTHR10992; 1.
DR   Pfam; PF12697; Abhydrolase_6; 1.
DR   PRINTS; PR00111; ABHYDROLASE.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Serine esterase.
FT   CHAIN           1..280
FT                   /note="Pyrethroid hydrolase"
FT                   /id="PRO_0000424212"
FT   REGION          254..280
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        202
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        230
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   280 AA;  30012 MW;  C7ABD56FDF3BE7AC CRC64;
     MTVTDIILIH GALNRGACYD AVVPLLEARG YRVHAPDLTG HTPGDGGHLS VVDMEHYTRP
     VADILARAEG QSILLGHSLG GASISWLAQH HPDKVAGLIY LTAVLTAPGI TPETFVLPGE
     PNRGTPHALD LIQPVDEGRG LQADFSRLER LREVFMGDYP GEGMPPAEQF IQTQSTVPFG
     TPNPMEGRAL EIPRLYIEAL DDVVIPIAVQ RQMQKEFPGP VAVVSLPASH APYYSMPERL
     AEAIADFADA PAEYRQTATK AGPDRPAGAD GGRADRADLP