HYEP_BOMMO
ID HYEP_BOMMO Reviewed; 461 AA.
AC Q6U6J0; A8CGI8;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Juvenile hormone epoxide hydrolase {ECO:0000303|PubMed:15681225, ECO:0000312|EMBL:AAQ87024.1};
DE Short=bommo-JHEH {ECO:0000303|PubMed:15681225};
DE EC=3.3.2.9 {ECO:0000269|PubMed:15681225};
GN Name=JHEH {ECO:0000312|EMBL:BAF81491.1};
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAQ87024.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RC STRAIN=Jingsong X Haoyue {ECO:0000269|PubMed:15681225};
RC TISSUE=Larval fat body {ECO:0000269|PubMed:15681225};
RX PubMed=15681225; DOI=10.1016/j.ibmb.2004.10.010;
RA Zhang Q.R., Xu W.H., Chen F.S., Li S.;
RT "Molecular and biochemical characterization of juvenile hormone epoxide
RT hydrolase from the silkworm, Bombyx mori.";
RL Insect Biochem. Mol. Biol. 35:153-164(2005).
RN [2] {ECO:0000312|EMBL:BAF81491.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Seino A., Ogura T., Tsubota T., Shimomura M., Tan A., Mita K., Shinoda T.,
RA Nakagawa Y., Shiotsuki T.;
RT "Characterization of juvenile hormone epoxide hydrolase and its related
RT genes in larval development of silkworm, Bombyx mori.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 23-461, AND SUBUNIT.
RX PubMed=25143157; DOI=10.1002/prot.24676;
RA Zhou K., Jia N., Hu C., Jiang Y.L., Yang J.P., Chen Y., Li S., Li W.F.,
RA Zhou C.Z.;
RT "Crystal structure of juvenile hormone epoxide hydrolase from the silkworm
RT Bombyx mori.";
RL Proteins 82:3224-3229(2014).
CC -!- FUNCTION: Catalyzes juvenile hormone hydrolysis. Degrades juvenile
CC hormone III (JH III) about 3 times and 5 times slower than juvenile
CC hormone I (JH I) and II (JH II), respectively. Degrades cis-stilbene
CC oxide and trans-stilbene oxide about 18 and 43 times slower than JH
CC III, respectively. {ECO:0000269|PubMed:15681225}.
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:15681225};
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:15681225};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.52 uM for juvenile hormone III {ECO:0000269|PubMed:15681225};
CC Vmax=122 nmol/min/mg enzyme with juvenile hormone I as substrate
CC {ECO:0000269|PubMed:15681225};
CC Vmax=223 nmol/min/mg enzyme with juvenile hormone II as substrate
CC {ECO:0000269|PubMed:15681225};
CC Vmax=46 nmol/min/mg enzyme with juvenile hormone III as substrate
CC {ECO:0000269|PubMed:15681225};
CC pH dependence:
CC Optimum pH is 7.5-8.0. Activity decreases rapidly below pH 7.0 and
CC above pH 9.0. {ECO:0000269|PubMed:15681225};
CC Temperature dependence:
CC Activity increases as temperature increases from 0 to 37 degrees
CC Celsius. {ECO:0000269|PubMed:15681225};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:25143157}.
CC -!- SUBCELLULAR LOCATION: Microsome membrane {ECO:0000269|PubMed:15681225};
CC Single-pass membrane protein {ECO:0000250|UniProtKB:P07687}.
CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:15681225}; Single-
CC pass membrane protein {ECO:0000250|UniProtKB:P07687}.
CC -!- TISSUE SPECIFICITY: Expressed in fat body, foregut and midgut but not
CC in brain, subesophageal ganglia or silk gland of larvae on day 1 of
CC fifth instar. {ECO:0000269|PubMed:15681225}.
CC -!- DEVELOPMENTAL STAGE: Expressed in fourth and fifth instar larvae.
CC Initial levels decline until day 2 of fourth instar but increase
CC sharply on day 3. Levels do not significantly change on days 0 and 1 of
CC fifth instar, increase on day 2 before falling again on days 3-4 to the
CC level seen at day 2 of the fourth instar. Expression then remains low
CC until the end of the instar. {ECO:0000269|PubMed:15681225}.
CC -!- SIMILARITY: Belongs to the peptidase S33 family. {ECO:0000255}.
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DR EMBL; AY377854; AAQ87024.1; -; mRNA.
DR EMBL; AB362775; BAF81491.1; -; mRNA.
DR RefSeq; NP_001037201.1; NM_001043736.1.
DR PDB; 4QLA; X-ray; 2.30 A; A/B=23-461.
DR PDBsum; 4QLA; -.
DR AlphaFoldDB; Q6U6J0; -.
DR SMR; Q6U6J0; -.
DR STRING; 7091.BGIBMGA013930-TA; -.
DR ESTHER; bommo-q6u6j0; Epoxide_hydrolase.
DR MEROPS; S33.971; -.
DR GeneID; 692686; -.
DR KEGG; bmor:692686; -.
DR CTD; 37181; -.
DR eggNOG; KOG2565; Eukaryota.
DR HOGENOM; CLU_019414_3_0_1; -.
DR InParanoid; Q6U6J0; -.
DR OrthoDB; 898504at2759; -.
DR Proteomes; UP000005204; Unassembled WGS sequence.
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 3D-structure; Aromatic hydrocarbons catabolism; Endoplasmic reticulum;
KW Hydrolase; Membrane; Microsome; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..461
FT /note="Juvenile hormone epoxide hydrolase"
FT /id="PRO_0000389521"
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 373
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P34913"
FT ACT_SITE 430
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P07687"
FT CONFLICT 6..8
FT /note="FIA -> LIV (in Ref. 2; BAF81491)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="R -> K (in Ref. 2; BAF81491)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="S -> F (in Ref. 2; BAF81491)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="Y -> N (in Ref. 2; BAF81491)"
FT /evidence="ECO:0000305"
FT CONFLICT 417
FT /note="T -> P (in Ref. 2; BAF81491)"
FT /evidence="ECO:0000305"
FT HELIX 42..46
FT /evidence="ECO:0007829|PDB:4QLA"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:4QLA"
FT HELIX 61..72
FT /evidence="ECO:0007829|PDB:4QLA"
FT TURN 85..88
FT /evidence="ECO:0007829|PDB:4QLA"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:4QLA"
FT HELIX 95..104
FT /evidence="ECO:0007829|PDB:4QLA"
FT HELIX 108..115
FT /evidence="ECO:0007829|PDB:4QLA"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:4QLA"
FT STRAND 128..135
FT /evidence="ECO:0007829|PDB:4QLA"
FT STRAND 144..151
FT /evidence="ECO:0007829|PDB:4QLA"
FT HELIX 158..164
FT /evidence="ECO:0007829|PDB:4QLA"
FT HELIX 165..168
FT /evidence="ECO:0007829|PDB:4QLA"
FT STRAND 176..184
FT /evidence="ECO:0007829|PDB:4QLA"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:4QLA"
FT HELIX 202..216
FT /evidence="ECO:0007829|PDB:4QLA"
FT STRAND 219..226
FT /evidence="ECO:0007829|PDB:4QLA"
FT HELIX 228..239
FT /evidence="ECO:0007829|PDB:4QLA"
FT TURN 241..243
FT /evidence="ECO:0007829|PDB:4QLA"
FT STRAND 244..251
FT /evidence="ECO:0007829|PDB:4QLA"
FT HELIX 257..268
FT /evidence="ECO:0007829|PDB:4QLA"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:4QLA"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:4QLA"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:4QLA"
FT HELIX 285..295
FT /evidence="ECO:0007829|PDB:4QLA"
FT HELIX 297..304
FT /evidence="ECO:0007829|PDB:4QLA"
FT HELIX 306..315
FT /evidence="ECO:0007829|PDB:4QLA"
FT HELIX 317..330
FT /evidence="ECO:0007829|PDB:4QLA"
FT HELIX 334..338
FT /evidence="ECO:0007829|PDB:4QLA"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:4QLA"
FT TURN 342..345
FT /evidence="ECO:0007829|PDB:4QLA"
FT HELIX 350..361
FT /evidence="ECO:0007829|PDB:4QLA"
FT TURN 362..364
FT /evidence="ECO:0007829|PDB:4QLA"
FT HELIX 366..376
FT /evidence="ECO:0007829|PDB:4QLA"
FT HELIX 379..382
FT /evidence="ECO:0007829|PDB:4QLA"
FT TURN 386..388
FT /evidence="ECO:0007829|PDB:4QLA"
FT STRAND 395..399
FT /evidence="ECO:0007829|PDB:4QLA"
FT HELIX 409..415
FT /evidence="ECO:0007829|PDB:4QLA"
FT STRAND 419..424
FT /evidence="ECO:0007829|PDB:4QLA"
FT HELIX 432..435
FT /evidence="ECO:0007829|PDB:4QLA"
FT HELIX 437..454
FT /evidence="ECO:0007829|PDB:4QLA"
SQ SEQUENCE 461 AA; 52441 MW; 21A6EE19AD54CA57 CRC64;
MSRLLFIALP LLVLASIPLY LLVLKSPPPM PKLDLEEWWG PPELKQKQDT SIKPFEITFS
ETMVKELKER IKKRRPFAPP LEGVGFKYGF NSKQLDSWLK YWAEEYPFAE RQKFLNQYPH
FKTNIQGLNI HFMRITPKVP KDVEIVPLLL LHGWPGSVRE FYEAIPHLTA VSRDRNFALE
IIAPSLPGYG FSDAAVRPGL AAAEVAVIFK NLMARLGYKQ YYVQGGDWGA LIGSAMATSF
PKEIIGFHSY MALTLSPAAT FLEFVGALFP SLIVEPELAN RLYPLSEKYS TLLEELGYMH
IQATKPDTVG IGLTDSPAGL LAYILEKFST WTNPDLRSKE DGGLSYRWTK DQLIDNLMLY
WSTKSIVTSM RLYAESFSSR HFDLKLDEIQ VQVPTWVLQA KHELAYQPPC ILKLKYTKLV
NASVIEDGGH FLAFELPEIF AKDVLKAIGE FRKLKNVKTE L
