ID   HYES_CORS2              Reviewed;         286 AA.
AC   O52866;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Soluble epoxide hydrolase;
DE            Short=SEH;
DE            EC=3.3.2.10;
DE   AltName: Full=Cytosolic epoxide hydrolase;
DE            Short=cEH;
DE   AltName: Full=Epoxide hydratase;
OS   Corynebacterium sp. (strain C12).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium; unclassified Corynebacterium.
OX   NCBI_TaxID=268954;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-21 AND
RP   127-134.
RX   PubMed=9578475; DOI=10.1046/j.1432-1327.1998.2530173.x;
RA   Misawa E., Chan Kwo Chion C.K.C., Archer I.V., Woodland M.P., Zhou N.-Y.,
RA   Carter S.F., Widdowson D.A., Leak D.J.;
RT   "Characterisation of a catabolic epoxide hydrolase from a Corynebacterium
RT   sp.";
RL   Eur. J. Biochem. 253:173-183(1998).
CC   -!- FUNCTION: Involved in catabolic degradation of epoxides. Shows highest
CC       activity towards C6 and C7 carbocyclic epoxides. Also active towards
CC       linear 1,2-epoxyalkanes.
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: Homotetramer. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral membrane
CC       protein.
CC   -!- INDUCTION: Expressed constitutively at a low level. Induced by
CC       cyclohexane oxide and (+/-)trans-1,2-dihydroxycyclohexane.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Epoxide hydrolase
CC       family. {ECO:0000305}.
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DR   EMBL; AJ224332; CAA11900.1; -; Genomic_DNA.
DR   PDB; 7AC0; X-ray; 2.18 A; AAA/BBB/CCC/DDD/EEE/FFF/GGG/HHH=1-286.
DR   PDBsum; 7AC0; -.
DR   AlphaFoldDB; O52866; -.
DR   SMR; O52866; -.
DR   ESTHER; corsp-cEH; CFTR-inhibitory-factor_Cif.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0033961; F:cis-stilbene-oxide hydrolase activity; IEA:InterPro.
DR   GO; GO:0004301; F:epoxide 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; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR000639; Epox_hydrolase-like.
DR   InterPro; IPR016292; Epoxide_hydrolase.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   PIRSF; PIRSF001112; Epoxide_hydrolase; 1.
DR   PRINTS; PR00111; ABHYDROLASE.
DR   PRINTS; PR00412; EPOXHYDRLASE.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Aromatic hydrocarbons catabolism; Cell membrane; Cytoplasm;
KW   Direct protein sequencing; Hydrolase; Membrane.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9578475"
FT   CHAIN           2..286
FT                   /note="Soluble epoxide hydrolase"
FT                   /id="PRO_0000084110"
FT   DOMAIN          26..123
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        99
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        209
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        264
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   286 AA;  32142 MW;  520DE66D73DB0A8F CRC64;
     MSTEITHHQA MINGYRMHYV TAGSGYPLVL LHGWPQSWYE WRNVIPALAE QFTVIAPDLR
     GLGDSEKPMT GFDKRTMATD VRELVSHLGY DKVGVIGHDW GGSVAFYFAY DNRDLVERLF
     ILDMIPGLIK AGDSFPIPVA LMINHIFFHG GNPDWATALI SKDVNLYLRR FLTTLDYNYS
     PNVFSEEDIA EYVRVNSLPG SIRSGCQWYA TGLREDTENL AKATDKLTIP VIAWGGSHFL
     GDIRPAWQEV AENVEGGAVE NCGHFVPEEK PQFVIDTALK FFAPLR