Top Level Name

  ⌊ Superfamily (core) Haloacid Dehalogenase

    ⌊ Subgroup C1.5: HAD, Beta-PGM, Phosphatase Like

  ⌊ C1.5.1: Epoxide Hydrolase Phosphatase Like

     ⌊ Family epoxide hydrolase n-terminal phosphatase

  ⌊ FunctionalDomain epoxide hydrolase n-terminal phosphatase (ID 2236)

Superfamily Assignment Evidence Code(s) ISS
Family Assignment Evidence Code CFM PubMed:12574508
This entry was last updated onNov. 22, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Mus musculus Taxon ID: 10090 31982393 NP_031966.2 (RefSeq) PRP URP
n/a 532876228 AGU04326.1 (Genbank)
n/a 510973649 AGN61909.1 (Genbank)
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Uniprot

Protein NameAccessionEC Number Identifier
Bifunctional epoxide hydrolase 2 P34914 HYES_MOUSE (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 554 | Length of Functional Domain: 227

1       10        20        30        40        50        60

MALRVAAFDLDGVLALPSIAGAFRRSEEALALPRDFLLGAYQTEFPEGPTEQLMKGKITF
SQWVPLMDESYRKSSKACGANLPENFSISQIFSQAMAARSINRPMLQAAIALKKKGFTTC
IVTNNWLDDGDKRDSLAQMMCELSQHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPNEV
VFLDDFGSNLKPARDMGMVTILVHNTASALRELEKVTGTQFPEAPLPVPCNPNDVSHGYV
TVKPGIRLHFVEMGSGPALCLCHGFPESWFSWRYQIPALAQAGFRVLAIDMKGYGDSSSP
PEIEEYAMELLCKEMVTFLDKLGIPQAVFIGHDWAGVMVWNMALFYPERVRAVASLNTPF
MPPDPDVSPMKVIRSIPVFNYQLYFQEPGVAEAELEKNMSRTFKSFFRASDETGFIAVHK
ATEIGGILVNTPEDPNLSKITTEEEIEFYIQQFKKTGFRGPLNWYRNTERNWKWSCKGLG
RKILVPALMVTAEKDIVLRPEMSKNMEKWIPFLKRGHIEDCGHWTQIEKPTEVNQILIKW
LQTEVQNPSVTSKI
This shows the full-length sequence of the enzyme. The region of the functional domain is highlighted in black letters, while the residual residues are shown in grey. The Superfamily domain, when present, is shown using underlining. In many cases the functional domain is the full-length sequence.
Conserved catalytic residues (as determined by automated alignment to family, subgroup, or superfamily HMMs) are shown with teal highlighting . Conserved catalytic residues which do not matched the Conserved Alignment Residue are shown with maroon highlighting . Information regarding their function can be found in the Conserved Residues section below.
FASTA formatted full-length sequence.
BLAST this sequence against SFLD.
Scan SFLD-HMMs with this sequence.

Conserved Residues
Superfamily CAR This EFD conserves 2/2 Superfamily-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
9 Asp (D) side chain nucleophile: forms covalent intermediate covalent catalysis -- reactant ISS
123 Thr (T) side chain interacts with substrate/intermediate substrate binding -- binding ISS
Subgroup CAR This EFD conserves 5/5 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
9 Asp (D) side chain nucleophile: attacks phosphate moiety of substrate to form covalent intermediate; Mg2+ ligand covalent catalysis -- reactant,
metal ligand -- binding 		IDA PubMed:12574508
124 Asn (N) side chain binds phosphate moiety of substrate substrate binding -- binding ICS PubMed:15096040
160 Lys (K) side chain stabilizes negatively charged intermediate electrostatic stabiliser -- spectator ISS PubMed:12574508
184 Asp (D) side chain Mg2+ ligand (via water) metal ligand -- binding ICS PubMed:15096040
185 Asp (D) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:15096040
Family CAR This EFD conserves 6/6 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
9 Asp (D) side chain nucleophile: attacks phosphate moiety of substrate to form covalent intermediate covalent catalysis -- reactant IDA PubMed:12574508
11 Asp (D) side chain Mg2+ ligand, binds phosphate moiety of substrate electrostatic stabiliser -- spectator,
metal ligand -- binding 		ISS PubMed:12574508
123 Thr (T) side chain binds phosphate moiety of substrate substrate binding -- binding ISS PubMed:12574508
160 Lys (K) side chain stabilizes negatively charged intermediate electrostatic stabiliser -- spectator ISS PubMed:12574508
184 Asp (D) side chain Mg2+ ligand metal ligand -- binding ISS PubMed:12574508
185 Asp (D) side chain Mg2+ ligand metal ligand -- binding ISS PubMed:12574508

Catalyzed Reaction

lipid-phosphate phosphatase

+ +
(9S,10S)-10-hydroxy-9-(phosphonatooxy)octadecanoate
58796		 water
15377		 (9S,10S)-9,10-dihydroxyoctadecanoate
58797		 hydrogenphosphate
43474

EC: | IntEnz: | Kegg: | BioCyc: | BRENDA: |

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
1CR6 Crystal Structure Of Murine Soluble Epoxide Hydrolase Complexed With Cpu Inhibitor Epoxide Hydrolase 5 2.8 N-Cyclohexyl-N'-(Propyl)Phenyl Urea CSA • PDB • PDBSum
1CQZ Crystal Structure Of Murine Soluble Epoxide Hydrolase. Epoxide Hydrolase 5 2.8 CSA • PDB • PDBSum
1EK1 Crystal Structure Of Murine Soluble Epoxide Hydrolase Complexed With Ciu Inhibitor Epoxide Hydrolase 5 3.1 N-Cyclohexyl-N'-(4-Iodophenyl)Urea CSA • PDB • PDBSum
1EK2 Crystal Structure Of Murine Soluble Epoxide Hydrolase Complexed With Cdu Inhibitor Epoxide Hydrolase 5 3.0 N-Cyclohexyl-N'-Decylurea CSA • PDB • PDBSum
Percent identity and alignment length from the BLAST match of the Functional Domain sequence to the PDB sequence.
"Yes" indicates that a GI associated with this Functional Domain was mapped to the PDB ID via UniProtKB.

Curation History
Time Change Annotation Old Value New Value
Nov. 3, 2014, 9:26 a.m. update curation agent sbrown setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.