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Protein

Bifunctional epoxide hydrolase 2

Gene

EPHX2

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Bifunctional enzyme. The C-terminal domain has epoxide hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and arene oxides. Plays a role in xenobiotic metabolism by degrading potentially toxic epoxides. Also determines steady-state levels of physiological mediators. The N-terminal domain has lipid phosphatase activity, with the highest activity towards threo-9,10-phosphonooxy-hydroxy-octadecanoic acid, followed by erythro-9,10-phosphonooxy-hydroxy-octadecanoic acid, 12-phosphonooxy-octadec-9Z-enoic acid, 12-phosphonooxy-octadec-9E-enoic acid, and p-nitrophenyl phosphate (By similarity).By similarity1 Publication

Catalytic activityi

An epoxide + H2O = a glycol.
(9S,10S)-10-hydroxy-9-(phosphonooxy)octadecanoate + H2O = (9S,10S)-9,10-dihydroxyoctadecanoate + phosphate.

Cofactori

Mg2+By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi9MagnesiumBy similarity1
Metal bindingi11MagnesiumBy similarity1
Metal bindingi185MagnesiumBy similarity1
Active sitei335NucleophileBy similarity1
Binding sitei383SubstrateBy similarity1
Active sitei466Proton donorBy similarity1
Active sitei524Proton acceptorBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Aromatic hydrocarbons catabolism, Detoxification, Lipid metabolism

Keywords - Ligandi

Magnesium, Metal-binding

Protein family/group databases

ESTHERisussc-q6q2c2. Epoxide_hydrolase.
MEROPSiS33.973.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional epoxide hydrolase 2
Including the following 2 domains:
Cytosolic epoxide hydrolase 2 (EC:3.3.2.10)
Short name:
CEH
Alternative name(s):
Epoxide hydratase
Soluble epoxide hydrolase
Short name:
SEH
Lipid-phosphate phosphatase (EC:3.1.3.76)
Gene namesi
Name:EPHX2
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000841131 – 555Bifunctional epoxide hydrolase 2Add BLAST555

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei43N6-acetyllysineBy similarity1
Modified residuei191N6-acetyllysineBy similarity1
Modified residuei215N6-acetyllysineBy similarity1
Modified residuei370PhosphoserineBy similarity1
Modified residuei455N6-succinyllysineBy similarity1
Modified residuei505N6-succinyllysineBy similarity1
Lipidationi522S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteineBy similarity1
Modified residuei554N6-succinyllysineBy similarity1

Post-translational modificationi

The covalent modification of cysteine by 15-deoxy-Delta12,14-prostaglandin-J2 is autocatalytic and reversible. It may occur as an alternative to other cysteine modifications, such as S-nitrosylation and S-palmitoylation (By similarity).By similarity

Keywords - PTMi

Acetylation, Lipoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ6Q2C2.
PeptideAtlasiQ6Q2C2.
PRIDEiQ6Q2C2.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000010323.

Structurei

3D structure databases

ProteinModelPortaliQ6Q2C2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini259 – 531AB hydrolase-1Sequence analysisAdd BLAST273

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 224PhosphataseAdd BLAST224
Regioni123 – 124Phosphate bindingBy similarity2
Regioni235 – 555Epoxide hydrolaseAdd BLAST321

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi553 – 555Microbody targeting signalSequence analysis3

Domaini

The N-terminal domain has phosphatase activity. The C-terminal domain has epoxide hydrolase activity.

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3085. Eukaryota.
KOG4178. Eukaryota.
COG1011. LUCA.
HOGENOMiHOG000028073.
HOVERGENiHBG006095.
InParanoidiQ6Q2C2.
KOiK08726.

Family and domain databases

Gene3Di1.10.150.240. 1 hit.
3.40.50.1000. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000639. Epox_hydrolase-like.
IPR023214. HAD-like_dom.
IPR006439. HAD-SF_hydro_IA.
IPR011945. HAD-SF_ppase_IA/epoxid_hydro_N.
IPR023198. PGP_dom2.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PRINTSiPR00111. ABHYDROLASE.
PR00412. EPOXHYDRLASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
SSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR02247. HAD-1A3-hyp. 1 hit.
TIGR01509. HAD-SF-IA-v3. 1 hit.

Sequencei

Sequence statusi: Complete.

Q6Q2C2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALRAAVFDL DGVLALPSIT TSWARAEEKL ALPRGFLNEA FKKGGQDGSV
60 70 80 90 100
ARVMTGEITF SQWVPFMEED CRKCAEDSGI RLPENFSVKH IFDKALSEKK
110 120 130 140 150
INYPMLQAAL TLKKKGFSTC ILTNNWLDDS AQRGSRAQLM CELRPHFDFL
160 170 180 190 200
IESCRVGMAK PDPQIYKLML DTLKAEPNEV VFLDDVGTHL KPVRDLGMAT
210 220 230 240 250
ILVRDTDTAL RELEKVTGVQ LLQTPALPPT SCDPSALSHG YVLIKPGVRL
260 270 280 290 300
HFVEMGSGPA VCLCHGFPES WFSWRYQIPA LAQAGFRVLA VDMKGYGESS
310 320 330 340 350
APPEIEEYSL EVLCKDMVTF LNKLGLSQAV FIGHDWGGVL VWNMALFYPE
360 370 380 390 400
RVRAVASLNT PFMPSNPNVS PMEIIKANPV FDYQLYFQEP GVAEAELEQN
410 420 430 440 450
LDRTFKNFFR AHDETFLTTN RVRELGGLFV GTPEEPSLSR LVTEEDIQFY
460 470 480 490 500
VQQFKKSGFR GPLNWYRNME RNWQWGCKGS GRKILIPALM VTAENDLVLH
510 520 530 540 550
PKMSKHMENW IPHLKRGHIK DCGHWTQIDK PAELNRILIE WLETDARNPL

VDSKL
Length:555
Mass (Da):62,767
Last modified:July 5, 2004 - v1
Checksum:i996EF83CBF82FBEF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY566232 mRNA. Translation: AAS68016.1.
RefSeqiNP_001001641.1. NM_001001641.1.
UniGeneiSsc.8278.

Genome annotation databases

GeneIDi414425.
KEGGissc:414425.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY566232 mRNA. Translation: AAS68016.1.
RefSeqiNP_001001641.1. NM_001001641.1.
UniGeneiSsc.8278.

3D structure databases

ProteinModelPortaliQ6Q2C2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000010323.

Protein family/group databases

ESTHERisussc-q6q2c2. Epoxide_hydrolase.
MEROPSiS33.973.

Proteomic databases

PaxDbiQ6Q2C2.
PeptideAtlasiQ6Q2C2.
PRIDEiQ6Q2C2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi414425.
KEGGissc:414425.

Organism-specific databases

CTDi2053.

Phylogenomic databases

eggNOGiKOG3085. Eukaryota.
KOG4178. Eukaryota.
COG1011. LUCA.
HOGENOMiHOG000028073.
HOVERGENiHBG006095.
InParanoidiQ6Q2C2.
KOiK08726.

Family and domain databases

Gene3Di1.10.150.240. 1 hit.
3.40.50.1000. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000639. Epox_hydrolase-like.
IPR023214. HAD-like_dom.
IPR006439. HAD-SF_hydro_IA.
IPR011945. HAD-SF_ppase_IA/epoxid_hydro_N.
IPR023198. PGP_dom2.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PRINTSiPR00111. ABHYDROLASE.
PR00412. EPOXHYDRLASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
SSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR02247. HAD-1A3-hyp. 1 hit.
TIGR01509. HAD-SF-IA-v3. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiHYES_PIG
AccessioniPrimary (citable) accession number: Q6Q2C2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: July 5, 2004
Last modified: November 2, 2016
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.