PYRHY_KLESP
ID PYRHY_KLESP Reviewed; 637 AA.
AC Q52NW7;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Pyrethroid hydrolase;
DE EC=3.1.1.88;
GN Name=estP;
OS Klebsiella sp.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=576;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-18, FUNCTION,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND CATALYTIC ACTIVITY.
RC STRAIN=ZD112;
RX PubMed=16448191; DOI=10.1021/jf052691u;
RA Wu P.C., Liu Y.H., Wang Z.Y., Zhang X.Y., Li H., Liang W.Q., Luo N.,
RA Hu J.M., Lu J.Q., Luan T.G., Cao L.X.;
RT "Molecular cloning, purification, and biochemical characterization of a
RT novel pyrethroid-hydrolyzing esterase from Klebsiella sp. strain ZD112.";
RL J. Agric. Food Chem. 54:836-842(2006).
CC -!- FUNCTION: Catalyzes the hydrolysis of pyrethroids pesticides.
CC Hydrolyzes cis-permethrin at approximately equal rate to trans-
CC permethrin. {ECO:0000269|PubMed:16448191}.
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:16448191};
CC -!- ACTIVITY REGULATION: Inhibited by Hg(2+), Ag(+) and rho-
CC chloromercuribenzoate. {ECO:0000269|PubMed:16448191}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.16 uM for cis-permethrin {ECO:0000269|PubMed:16448191};
CC KM=0.11 uM for trans-permethrin {ECO:0000269|PubMed:16448191};
CC KM=0.21 uM for cypermethrin {ECO:0000269|PubMed:16448191};
CC KM=0.91 uM for fenvalerate {ECO:0000269|PubMed:16448191};
CC KM=1.23 uM for deltamethrin {ECO:0000269|PubMed:16448191};
CC KM=0.87 uM for malathion {ECO:0000269|PubMed:16448191};
CC Note=kcat is 1.05 sec(-1) with cis-permethrin as substrate. kcat is
CC 1.14 sec(-1) with trans-permethrin as substrate. kcat is 0.288 sec(-
CC 1) with cypermethrin as substrate. kcat is 0.103 sec(-1) with
CC fenvalerate as substrate. kcat is 0.016 sec(-1) with deltamethrin as
CC substrate. kcat is 0.07 sec(-1) with malathion as substrate.;
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:16448191};
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DR EMBL; AY995176; AAX93318.1; -; Genomic_DNA.
DR AlphaFoldDB; Q52NW7; -.
DR SMR; Q52NW7; -.
DR KEGG; ag:AAX93318; -.
DR BioCyc; MetaCyc:MON-16247; -.
DR BRENDA; 3.1.1.1; 2818.
DR GO; GO:0102209; F:trans-permethrin hydrolase activity; IEA:UniProtKB-EC.
DR InterPro; IPR007505; PDDEXK_7.
DR Pfam; PF04411; PDDEXK_7; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase; Serine esterase.
FT CHAIN 1..637
FT /note="Pyrethroid hydrolase"
FT /id="PRO_0000424209"
SQ SEQUENCE 637 AA; 73427 MW; 002CB509CD802DD9 CRC64;
MEICTKGSRK HLTSRASEPS YNVPENQYVL YVVSSTLSIV KQLVKVAESK KSRFSGAIEK
LNERLDSLKD YRIINRDLVV KDLERLKKRF DTEVINAELS EQLAKINVNL SRSYSEKGYL
RLEKATGSEN EWWAKIKPSQ NDDWQQFEPD GYTIFSSRDH YASLFKSYSD YEIEAKIPLP
LRRGKAVVLY PEYISRICVL PESRSIQREQ ENFTKLRDKG IALSKKDWQA KLTTDELAEQ
EKERATINKR LGYFATEHEK VGIVHKALEP KLKPFQQIEK EWRQCKVKSK STFPNSMTFV
QNPAYQAVHS GFKKLKEQIG LADEDILLSL EKIEAIGLVN MPLLYERWCL LQIIKVLTQA
FRYQPEDNWK RKLIANIQGN EEQISIQFFN PSVSRAITLQ YEPFLANGKR PDFVLDVEAI
TKSGNQISKR LVVDAKYYSA AYLKQRGGIG GVIHELYNGK DYSECQENSV FVLHPVLDAV
EKVVSPQEWA KDSYLGELSM FDWEPAHHQR QATNYGAVCA NPMKSQRYLD EIQRMLGMFL
QYGIEDNTSF RGASDDTHAV NFCVSCGSEK VVDVTKSMSS NNQKRWYRCN ECTHFTVYTH
CGTCNTRLIK NGEYWTYLSL MPMSSINIKC PNCESPV
