ID   HYEP_MANSE              Reviewed;         462 AA.
AC   Q25489;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Juvenile hormone epoxide hydrolase;
DE            Short=JHEH;
DE            EC=3.3.2.9 {ECO:0000250|UniProtKB:Q6U6J0};
DE   AltName: Full=Juvenile hormone-specific epoxide hydrolase;
OS   Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Sphingidae; Sphinginae; Sphingini; Manduca.
OX   NCBI_TaxID=7130;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 91-110 AND 237-250.
RC   TISSUE=Egg;
RX   PubMed=8645304; DOI=10.1006/bbrc.1996.0404;
RA   Wojtasek H., Prestwich G.D.;
RT   "An insect juvenile hormone-specific epoxide hydrolase is related to
RT   vertebrate microsomal epoxide hydrolases.";
RL   Biochem. Biophys. Res. Commun. 220:323-329(1996).
CC   -!- FUNCTION: Catalyzes juvenile hormone hydrolysis.
CC       {ECO:0000250|UniProtKB:Q6U6J0}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cis-stilbene oxide + H2O = (1R,2R)-hydrobenzoin;
CC         Xref=Rhea:RHEA:23900, ChEBI:CHEBI:15377, ChEBI:CHEBI:50004,
CC         ChEBI:CHEBI:50014; EC=3.3.2.9;
CC         Evidence={ECO:0000250|UniProtKB:Q6U6J0};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(4-methoxyphenyl)-N-methyl-N-[(3-methyloxetan-3-
CC         yl)methyl]methanamine + H2O = 2-{[(4-
CC         methoxybenzyl)(methyl)amino]methyl}-2-methylpropane-1,3-diol;
CC         Xref=Rhea:RHEA:55764, ChEBI:CHEBI:15377, ChEBI:CHEBI:139161,
CC         ChEBI:CHEBI:139164; EC=3.3.2.9;
CC         Evidence={ECO:0000250|UniProtKB:Q6U6J0};
CC   -!- SUBCELLULAR LOCATION: Microsome membrane
CC       {ECO:0000250|UniProtKB:Q6U6J0}; Single-pass membrane protein
CC       {ECO:0000250|UniProtKB:P07687}. Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q6U6J0}; Single-pass membrane protein
CC       {ECO:0000250|UniProtKB:P07687}.
CC   -!- SIMILARITY: Belongs to the peptidase S33 family. {ECO:0000305}.
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DR   EMBL; U46682; AAC47018.1; -; mRNA.
DR   PIR; JC4686; JC4686.
DR   AlphaFoldDB; Q25489; -.
DR   SMR; Q25489; -.
DR   BindingDB; Q25489; -.
DR   ESTHER; manse-hyep; Epoxide_hydrolase.
DR   MEROPS; S33.971; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0033961; F:cis-stilbene-oxide hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000639; Epox_hydrolase-like.
DR   InterPro; IPR010497; Epoxide_hydro_N.
DR   InterPro; IPR016292; Epoxide_hydrolase.
DR   Pfam; PF06441; EHN; 1.
DR   PIRSF; PIRSF001112; Epoxide_hydrolase; 1.
DR   PRINTS; PR00412; EPOXHYDRLASE.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; Direct protein sequencing;
KW   Endoplasmic reticulum; Hydrolase; Membrane; Microsome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..462
FT                   /note="Juvenile hormone epoxide hydrolase"
FT                   /id="PRO_0000080862"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        227
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P07687"
FT   ACT_SITE        372
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P34913"
FT   ACT_SITE        428
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P07687"
SQ   SEQUENCE   462 AA;  52612 MW;  667D1A66C2EE430B CRC64;
     MYKILSSFVA GVAIGSGLVI TYVLYNVPEP PELDLQRWWG IGTRPTEEDK SIRPFSIDFN
     DTVILDLKER LKNRRPFTKP LEGINSEYGM NTEYLETVLE YWLNEYNFKK RAELLNKFPH
     YKTRIQGLDL HFIRVKPEIK EGVQVLPLLM MHGWPSSSKE FDKVIPILTT PKHEYNIVFE
     VVAVDLPGYG FSEGTNKPGL NPVQIGVMMR NLMLRLGFEK FYIQAGDWGS QCATHMATLF
     PDQVLGLHTN MPLSSRPLST VKLFIGALFP SLIVDAKYMD RIYPLKNLFS YILRETGYFH
     IQATKPDTIG VALTDSPAGL AGYLIEKMAI CSNRDQLDTP HGGLENLNLD DVLDTVTINW
     INNCIVTSTR LYAEGFSWPE VLIVHRIPSM VPTAGINFKY EVLYQPDWIL RDKFPNLVRS
     TVLDFGGHFA ALHTPQALAD DIFASAVQFL KFHDRKRNQK SS