ID   HYEP1_CTEFE             Reviewed;         464 AA.
AC   Q8MZR6;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Juvenile hormone epoxide hydrolase 1;
DE            EC=3.3.2.9 {ECO:0000269|PubMed:12125060};
DE   AltName: Full=CfEH1;
DE   AltName: Full=Juvenile hormone epoxide hydrolase I;
DE            Short=JHEH I;
DE   AltName: Full=Juvenile hormone-specific epoxide hydrolase I;
GN   Name=EH1 {ECO:0000303|PubMed:12125060};
OS   Ctenocephalides felis (Cat flea).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Siphonaptera; Pulicidae; Archaeopsyllinae;
OC   Ctenocephalides.
OX   NCBI_TaxID=7515;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAM22694.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-26, FUNCTION, CATALYTIC
RP   ACTIVITY, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Larva {ECO:0000269|PubMed:12125060};
RX   PubMed=12125060; DOI=10.1002/arch.10044;
RA   Keiser K.C.L., Brandt K.S., Silver G.M., Wisnewski N.;
RT   "Cloning, partial purification and in vivo developmental profile of
RT   expression of the juvenile hormone epoxide hydrolase of Ctenocephalides
RT   felis.";
RL   Arch. Insect Biochem. Physiol. 50:191-206(2002).
CC   -!- FUNCTION: Catalyzes juvenile hormone hydrolysis.
CC       {ECO:0000269|PubMed:12125060}.
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:0000269|PubMed:12125060};
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:0000269|PubMed:12125060};
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   -!- TISSUE SPECIFICITY: Developing oocytes, fat body and midgut epithelium
CC       of adults. {ECO:0000269|PubMed:12125060}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in all stages examined from first instar
CC       larva to adult. Expression remains relatively constant throughout the
CC       larval stages and elevates slightly in adults.
CC       {ECO:0000269|PubMed:12125060}.
CC   -!- SIMILARITY: Belongs to the peptidase S33 family. {ECO:0000255}.
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DR   EMBL; AF503908; AAM22694.1; -; mRNA.
DR   AlphaFoldDB; Q8MZR6; -.
DR   SMR; Q8MZR6; -.
DR   ESTHER; ctefe-Q8MZR6; 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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:12125060"
FT   CHAIN           2..464
FT                   /note="Juvenile hormone epoxide hydrolase 1"
FT                   /id="PRO_0000080860"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        224
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P07687"
FT   ACT_SITE        370
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P34913"
FT   ACT_SITE        427
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P07687"
SQ   SEQUENCE   464 AA;  52614 MW;  A3DA8725F7DCD9BC CRC64;
     MGKCCRMLIF AAIAGIAVLY YQITKELPKP NIPLDTWWGP GKPQNVDISI RPFKININNK
     VIENLKLKLN DVQYTLPLEG INFEYGFNTD SLKKIVDFWR TQYNWREREA LLNKYPHFKT
     NIQGLDIHYV HIKPQVSKNI EVLPLVMIHG WPGSFVEFYK IIPMLTTPRA GYNFVFELIL
     PSIPGYGFSQ AAAKPGLGST QVAVIMRNLM ERIGFKKYYV QGGDWGSMII SAMSTLFPEN
     VLGQHSNMCF VNTPSSNIKA IIGSFFPESF AGTGNAHKMY PMSEHFFTLL EEMGYLHLQA
     TKPDTVGVAL RDSPAGLAAY ILEKFSTWTN RSWRSVKDGN LLLKYNIPEL LDNVMIYYVT
     DSITTSMRLY AESFTKAHLA LNLDRVRNHV PAACAKFPNE LAYVTDCQLA EKYKTLLQSN
     DMPSGGHFAA FEEPGLLAED IFTAVKKFKE FYSKKAESQK KADL