ID HYEP2_CTEFE Reviewed; 465 AA.
AC Q8MZR5;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 22-FEB-2023, entry version 76.
DE RecName: Full=Juvenile hormone epoxide hydrolase 2;
DE EC=3.3.2.9 {ECO:0000250|UniProtKB:Q8MZR6};
DE AltName: Full=CfEH2;
DE AltName: Full=Juvenile hormone epoxide hydrolase II;
DE Short=JHEH II;
DE AltName: Full=Juvenile hormone-specific epoxide hydrolase II;
GN Name=EH2 {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:AAM22695.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
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:0000250|UniProtKB:Q8MZR6}.
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:Q8MZR6};
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:Q8MZR6};
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:0000255}.
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DR EMBL; AF503909; AAM22695.1; -; mRNA.
DR AlphaFoldDB; Q8MZR5; -.
DR SMR; Q8MZR5; -.
DR ESTHER; ctefe-Q8MZR5; Epoxide_hydrolase.
DR MEROPS; S33.971; -.
DR OrthoDB; 5472392at2759; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000639; Epox_hydrolase-like.
DR InterPro; IPR010497; Epoxide_hydro_N.
DR InterPro; IPR016292; Epoxide_hydrolase.
DR PANTHER; PTHR21661:SF35; EPOXIDE HYDROLASE; 1.
DR PANTHER; PTHR21661; EPOXIDE HYDROLASE 1-RELATED; 1.
DR Pfam; PF06441; EHN; 1.
DR PIRSF; PIRSF001112; Epoxide_hydrolase; 1.
DR PRINTS; PR00412; EPOXHYDRLASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 2: Evidence at transcript level;
KW Aromatic hydrocarbons catabolism; Endoplasmic reticulum; Hydrolase;
KW Membrane; Microsome; Transmembrane; Transmembrane helix.
FT CHAIN 1..465
FT /note="Juvenile hormone epoxide hydrolase 2"
FT /id="PRO_0000080861"
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 465 AA; 53025 MW; BB85199CCADA4860 CRC64;
MSNCCRILWI AIVIGLGVLY YEITKEFPKP NIPLDTWWGT GKSQKIDTSM RPFKIAINDE
VLNTLKVKLS DVSFTPPLEG IDFQYGFNTN TLKKLVDFWR TQYNWREREA LLNKYPHFKT
NIQGLDIHYV HIKPQVSKNI HVLPMIMVHG WPGSFVEFYK IIPMLTTPRT DYNFVFELIL
PSIPGYGFSQ AAAKPGLGAT QIAVIMHNLM DRIGFKKYYV QGGDWGSRIV SAMSTLFPEN
VLGHHSNLCF LNTLSSNIKS FVGSLFPEWF AGKQNVHKIY PLSEHFFTLL EESGYFHIQA
TKPDTVGVAL RDSPAGLAAY ILEKFSTGTN KAWRSAKDGN LQSKFTFTEL LDNVMIYYVT
GSITTSMRIY AESYSWDHLS LNMDRVPTIV PTACAKFPHE IAYKTDFQLA EKYKTLLQST
IMPRGGHFAA LEEPLLLAED IFSAVKKFID HHSKKDSKNQ ENRDL
//
