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Protein

Juvenile hormone epoxide hydrolase

Gene

JHEH

Organism
Bombyx mori (Silk moth)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes juvenile hormone hydrolysis. Degrades juvenile hormone III (JH III) about 3 times and 5 times slower than juvenile hormone I (JH I) and II (JH II), respectively. Degrades cis-stilbene oxide and trans-stilbene oxide about 18 and 43 times slower than JH III, respectively.1 Publication

Catalytic activityi

Cis-stilbene oxide + H2O = (+)-(1R,2R)-1,2-diphenylethane-1,2-diol.1 Publication

Kineticsi

  1. KM=0.52 µM for juvenile hormone III1 Publication

Vmax=122 nmol/min/mg enzyme with juvenile hormone I as substrate1 Publication

Vmax=223 nmol/min/mg enzyme with juvenile hormone II as substrate1 Publication

Vmax=46 nmol/min/mg enzyme with juvenile hormone III as substrate1 Publication

pH dependencei

Optimum pH is 7.5-8.0. Activity decreases rapidly below pH 7.0 and above pH 9.0.1 Publication

Temperature dependencei

Activity increases as temperature increases from 0 to 37 degrees Celsius.1 Publication

GO - Molecular functioni

  1. cis-stilbene-oxide hydrolase activity Source: UniProtKB-EC

GO - Biological processi

  1. aromatic compound catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Aromatic hydrocarbons catabolism

Protein family/group databases

MEROPSiS33.971.

Names & Taxonomyi

Protein namesi
Recommended name:
Juvenile hormone epoxide hydrolase1 PublicationImported (EC:3.3.2.9)
Short name:
bommo-JHEH1 Publication
Gene namesi
Name:JHEHImported
OrganismiBombyx mori (Silk moth)
Taxonomic identifieri7091 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaLepidopteraGlossataDitrysiaBombycoideaBombycidaeBombycinaeBombyx
ProteomesiUP000005204 Componenti: Unplaced

Subcellular locationi

  1. Microsome membrane Curated1 Publication; Single-pass type II membrane protein 1 Publication
  2. Endoplasmic reticulum membrane Curated1 Publication; Single-pass type II membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei4 – 2421Helical; Signal-anchorSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 461461Juvenile hormone epoxide hydrolasePRO_0000389521Add
BLAST

Expressioni

Tissue specificityi

Expressed in fat body, foregut and midgut but not in brain, subesophageal ganglia or silk gland of larvae on day 1 of fifth instar.1 Publication

Developmental stagei

Expressed in fourth and fifth instar larvae. Initial levels decline until day 2 of fourth instar but increase sharply on day 3. Levels do not significantly change on days 0 and 1 of fifth instar, increase on day 2 before falling again on days 3-4 to the level seen at day 2 of the fourth instar. Expression then remains low until the end of the instar.1 Publication

Structurei

Secondary structure

1
461
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi42 – 465Combined sources
Beta strandi53 – 553Combined sources
Helixi61 – 7212Combined sources
Turni85 – 884Combined sources
Helixi92 – 943Combined sources
Helixi95 – 10410Combined sources
Helixi108 – 1158Combined sources
Beta strandi120 – 1256Combined sources
Beta strandi128 – 1358Combined sources
Beta strandi144 – 1518Combined sources
Helixi158 – 1647Combined sources
Helixi165 – 1684Combined sources
Beta strandi176 – 1849Combined sources
Beta strandi196 – 1983Combined sources
Helixi202 – 21615Combined sources
Beta strandi219 – 2268Combined sources
Helixi228 – 23912Combined sources
Turni241 – 2433Combined sources
Beta strandi244 – 2518Combined sources
Helixi257 – 26812Combined sources
Helixi270 – 2723Combined sources
Turni276 – 2783Combined sources
Helixi279 – 2813Combined sources
Helixi285 – 29511Combined sources
Helixi297 – 3048Combined sources
Helixi306 – 31510Combined sources
Helixi317 – 33014Combined sources
Helixi334 – 3385Combined sources
Beta strandi339 – 3413Combined sources
Turni342 – 3454Combined sources
Helixi350 – 36112Combined sources
Turni362 – 3643Combined sources
Helixi366 – 37611Combined sources
Helixi379 – 3824Combined sources
Turni386 – 3883Combined sources
Beta strandi395 – 3995Combined sources
Helixi409 – 4157Combined sources
Beta strandi419 – 4246Combined sources
Helixi432 – 4354Combined sources
Helixi437 – 45418Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4QLAX-ray2.30A/B23-461[»]
ProteinModelPortaliQ6U6J0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S33 family.Sequence Analysis

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

InParanoidiQ6U6J0.
KOiK10719.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000639. Epox_hydrolase-like.
IPR010497. Epoxide_hydro_N.
IPR016292. Epoxide_hydrolase.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
PF06441. EHN. 1 hit.
[Graphical view]
PIRSFiPIRSF001112. Epoxide_hydrolase. 1 hit.
PRINTSiPR00412. EPOXHYDRLASE.
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequencei

Sequence statusi: Complete.

Q6U6J0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRLLFIALP LLVLASIPLY LLVLKSPPPM PKLDLEEWWG PPELKQKQDT
60 70 80 90 100
SIKPFEITFS ETMVKELKER IKKRRPFAPP LEGVGFKYGF NSKQLDSWLK
110 120 130 140 150
YWAEEYPFAE RQKFLNQYPH FKTNIQGLNI HFMRITPKVP KDVEIVPLLL
160 170 180 190 200
LHGWPGSVRE FYEAIPHLTA VSRDRNFALE IIAPSLPGYG FSDAAVRPGL
210 220 230 240 250
AAAEVAVIFK NLMARLGYKQ YYVQGGDWGA LIGSAMATSF PKEIIGFHSY
260 270 280 290 300
MALTLSPAAT FLEFVGALFP SLIVEPELAN RLYPLSEKYS TLLEELGYMH
310 320 330 340 350
IQATKPDTVG IGLTDSPAGL LAYILEKFST WTNPDLRSKE DGGLSYRWTK
360 370 380 390 400
DQLIDNLMLY WSTKSIVTSM RLYAESFSSR HFDLKLDEIQ VQVPTWVLQA
410 420 430 440 450
KHELAYQPPC ILKLKYTKLV NASVIEDGGH FLAFELPEIF AKDVLKAIGE
460
FRKLKNVKTE L
Length:461
Mass (Da):52,441
Last modified:July 5, 2004 - v1
Checksum:i21A6EE19AD54CA57
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 83FIA → LIV in BAF81491 (Ref. 2) Curated
Sequence conflicti173 – 1731R → K in BAF81491 (Ref. 2) Curated
Sequence conflicti239 – 2391S → F in BAF81491 (Ref. 2) Curated
Sequence conflicti250 – 2501Y → N in BAF81491 (Ref. 2) Curated
Sequence conflicti417 – 4171T → P in BAF81491 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY377854 mRNA. Translation: AAQ87024.1.
AB362775 mRNA. Translation: BAF81491.1.
RefSeqiNP_001037201.1. NM_001043736.1.
UniGeneiBmo.321.

Genome annotation databases

GeneIDi692686.
KEGGibmor:692686.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY377854 mRNA. Translation: AAQ87024.1.
AB362775 mRNA. Translation: BAF81491.1.
RefSeqiNP_001037201.1. NM_001043736.1.
UniGeneiBmo.321.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4QLAX-ray2.30A/B23-461[»]
ProteinModelPortaliQ6U6J0.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS33.971.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi692686.
KEGGibmor:692686.

Organism-specific databases

CTDi37181.

Phylogenomic databases

InParanoidiQ6U6J0.
KOiK10719.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000639. Epox_hydrolase-like.
IPR010497. Epoxide_hydro_N.
IPR016292. Epoxide_hydrolase.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
PF06441. EHN. 1 hit.
[Graphical view]
PIRSFiPIRSF001112. Epoxide_hydrolase. 1 hit.
PRINTSiPR00412. EPOXHYDRLASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Molecular and biochemical characterization of juvenile hormone epoxide hydrolase from the silkworm, Bombyx mori."
    Zhang Q.R., Xu W.H., Chen F.S., Li S.
    Insect Biochem. Mol. Biol. 35:153-164(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: Jingsong X Haoyue1 Publication.
    Tissue: Larval fat body1 Publication.
  2. "Characterization of juvenile hormone epoxide hydrolase and its related genes in larval development of silkworm, Bombyx mori."
    Seino A., Ogura T., Tsubota T., Shimomura M., Tan A., Mita K., Shinoda T., Nakagawa Y., Shiotsuki T.
    Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiHYEP_BOMMO
AccessioniPrimary (citable) accession number: Q6U6J0
Secondary accession number(s): A8CGI8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 24, 2009
Last sequence update: July 5, 2004
Last modified: March 4, 2015
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.