ID   CEEH2_CAEEL             Reviewed;         355 AA.
AC   G5EDL5; G1K0X1;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Epoxide hydrolase 2 {ECO:0000312|WormBase:K07C5.5};
DE            EC=3.3.2.10 {ECO:0000269|PubMed:18267101};
GN   Name=ceeh-2 {ECO:0000312|WormBase:K07C5.5};
GN   ORFNames=K07C5.5 {ECO:0000312|WormBase:K07C5.5};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN   [1] {ECO:0000312|EMBL:ABV45407.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND DISRUPTION PHENOTYPE.
RX   PubMed=18267101; DOI=10.1016/j.abb.2008.01.016;
RA   Harris T.R., Aronov P.A., Jones P.D., Tanaka H., Arand M., Hammock B.D.;
RT   "Identification of two epoxide hydrolases in Caenorhabditis elegans that
RT   metabolize mammalian lipid signaling molecules.";
RL   Arch. Biochem. Biophys. 472:139-149(2008).
RN   [2] {ECO:0000312|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Catalyzes the hydrolysis of epoxide-containing fatty acids.
CC       Active in vitro against trans-1,3-diphenylpropene oxide (t-DPPO),
CC       epoxyeicosatrienoic acids (EETs) including 8,9-EET, 11,12-EET and
CC       14,15-EET and the linoleic acid metabolites 12,13-epoxy-9-octadecenoate
CC       (12,13-EpOME) and 9,10-epoxy-12-octadecenoate (9,10-EpOME).
CC       {ECO:0000269|PubMed:18267101}.
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; Evidence={ECO:0000269|PubMed:18267101};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.9 uM for 12,13-epoxy-9-octadecenoate
CC         {ECO:0000269|PubMed:18267101};
CC         KM=8.4 uM for 9,10-epoxy-12-octadecenoate
CC         {ECO:0000269|PubMed:18267101};
CC   -!- PATHWAY: Lipid metabolism. {ECO:0000305|PubMed:18267101}.
CC   -!- DISRUPTION PHENOTYPE: RNAi knockdown of both ceeh-1 and ceeh-2 results
CC       in the accumulation of 9,10-EpOME and 12,13-EpOME.
CC       {ECO:0000269|PubMed:18267101}.
CC   -!- MISCELLANEOUS: Less active when compared to ceeh-1.
CC       {ECO:0000269|PubMed:18267101}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Epoxide hydrolase
CC       family. {ECO:0000305}.
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DR   EMBL; EU151492; ABV45407.1; -; mRNA.
DR   EMBL; BX284605; CAA94898.1; -; Genomic_DNA.
DR   PIR; T23406; T23406.
DR   RefSeq; NP_001256211.1; NM_001269282.1.
DR   AlphaFoldDB; G5EDL5; -.
DR   SMR; G5EDL5; -.
DR   STRING; 6239.K07C5.5a; -.
DR   ESTHER; caeel-K07C5.5; Epoxide_hydrolase.
DR   EPD; G5EDL5; -.
DR   PaxDb; G5EDL5; -.
DR   PeptideAtlas; G5EDL5; -.
DR   EnsemblMetazoa; K07C5.5.1; K07C5.5.1; WBGene00010628.
DR   GeneID; 179444; -.
DR   KEGG; cel:CELE_K07C5.5; -.
DR   CTD; 179444; -.
DR   WormBase; K07C5.5; CE06115; WBGene00010628; ceeh-2.
DR   eggNOG; KOG4178; Eukaryota.
DR   GeneTree; ENSGT00940000167498; -.
DR   InParanoid; G5EDL5; -.
DR   OMA; IAMRSNK; -.
DR   OrthoDB; 616687at2759; -.
DR   PhylomeDB; G5EDL5; -.
DR   SABIO-RK; G5EDL5; -.
DR   PRO; PR:G5EDL5; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00010628; Expressed in larva and 2 other tissues.
DR   GO; GO:0004301; F:epoxide hydrolase activity; IDA:WormBase.
DR   GO; GO:0016787; F:hydrolase activity; IBA:GO_Central.
DR   GO; GO:0044255; P:cellular lipid metabolic process; IDA:WormBase.
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   Pfam; PF00561; Abhydrolase_1; 1.
DR   PRINTS; PR00412; EPOXHYDRLASE.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Lipid metabolism; Reference proteome.
FT   CHAIN           1..355
FT                   /note="Epoxide hydrolase 2"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000432073"
FT   DOMAIN          78..323
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        152
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P34914"
FT   ACT_SITE        263
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P34914"
FT   ACT_SITE        319
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P34914"
SQ   SEQUENCE   355 AA;  42116 MW;  67A02F68E71FAE4D CRC64;
     MGFFADLFKV VYSTWRQYIY TTGALLTLTW KWFTEGNEYF VEHVYPEPEC LKNWNHKFVQ
     LKNIRMHYVE EGPADGDVLL MVHGFPEFWY SWRFQLEHFK HTHRCIAIDM RGYNTTDRPS
     GISDYNLTHL VEDIRQFIEI LELKRVTLAA HDWGAIVCWR VAMLHSNLID RLVICNVPHP
     FAFFEVYNMS KEQRNKSWYI YLFQSQYIPE IAMRSNKMKM LEAMFRGSKA GIRNSENFTD
     EDMLAWKHVF SQPGGTTGPL NYYRDLFNAP AIPRKLQIVQ PKVLILWGDE DAFLDKKGAE
     LSVQFCRDCR VQMIRGASHW VQQDQPQLVN VYMEQFMNED SYRPIGEIKT FKSHL