ID   HYEP_PSEU1              Reviewed;          77 AA.
AC   P80048;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   29-SEP-2021, entry version 48.
DE   RecName: Full=Epoxide hydrolase;
DE            EC=3.3.2.10;
DE   AltName: Full=Epoxide hydratase;
DE   Flags: Fragments;
OS   Pseudomonas sp. (strain AD1).
OC   Bacteria; Proteobacteria.
OX   NCBI_TaxID=72585;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=1662605; DOI=10.1111/j.1432-1033.1991.tb16493.x;
RA   Jacobs M.H., van der Wijngaard A.J., Pentenga M., Janssen D.B.;
RT   "Characterization of the epoxide hydrolase from an epichlorohydrin-
RT   degrading Pseudomonas sp.";
RL   Eur. J. Biochem. 202:1217-1222(1991).
CC   -!- FUNCTION: This enzyme acts on aliphatic epoxides. Its substrates
CC       include epichlorohydrin, epibromohydrin, epoxyoctane and styrene
CC       epoxide.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an epoxide + H2O = an ethanediol; Xref=Rhea:RHEA:19037,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:32955, ChEBI:CHEBI:140594;
CC         EC=3.3.2.10;
CC   -!- SUBUNIT: Monomer.
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DR   PIR; S19575; S19575.
DR   GO; GO:0004301; F:epoxide hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; Direct protein sequencing; Hydrolase.
FT   CHAIN           1..77
FT                   /note="Epoxide hydrolase"
FT                   /id="PRO_0000084108"
FT   NON_CONS        33..34
FT                   /evidence="ECO:0000305"
FT   NON_CONS        49..50
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   77 AA;  8926 MW;  D9BB66F36ACFF939 CRC64;
     TIDXPEDFKH YEVQLPDVKI HYVREGAGPT LLLVEKPEIA IDRIKTAFRK PDNIHGGFNY
     YRANIRPDAA LWTDLDH