Top Level Name

  ⌊ Superfamily (core) Haloacid Dehalogenase

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

  ⌊ C1.5.1: Epoxide Hydrolase Phosphatase Like

  ⌊ FunctionalDomain C1.5.1: Epoxide Hydrolase Phosphatase Like (ID 37154)

Superfamily Assignment Evidence Code(s) IEA
This entry was last updated onFeb. 13, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Mus musculus Taxon ID: 10090 406647884 NP_001258350.1 (RefSeq) PRP URP
Mus musculus Taxon ID: 10090 156766670 ABU95055.1 (Genbank) PRP URP

Uniprot

Protein NameAccessionEC Number Identifier
n/a A8JYK8 A8JYK8_MOUSE (TrEMBL)

Sequence

Length of Enzyme (full-length): 488 | Length of Functional Domain: 161

1       10        20        30        40        50        60

MDESYRKSSKACGANLPENFSISQIFSQAMAARSINRPMLQAAIALKKKGFTTCIVTNNW
LDDGDKRDSLAQMMCELSQHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPNEVVFLDDF
GSNLKPARDMGMVTILVHNTASALRELEKVTGTQFPEAPLPVPCNPNDVSHGYVTVKPGI
RLHFVEMGSGPALCLCHGFPESWFSWRYQIPALAQAGFRVLAIDMKGYGDSSSPPEIEEY
AMELLCKEMVTFLDKLGIPQAVFIGHDWAGVMVWNMALFYPERVRAVASLNTPFMPPDPD
VSPMKVIRSIPVFNYQLYFQEPGVAEAELEKNMSRTFKSFFRASDETGFIAVHKATEIGG
ILVNTPEDPNLSKITTEEEIEFYIQQFKKTGFRGPLNWYRNTERNWKWSCKGLGRKILVP
ALMVTAEKDIVLRPEMSKNMEKWIPFLKRGHIEDCGHWTQIEKPTEVNQILIKWLQTEVQ
NPSVTSKI
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 1/2 Superfamily-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
57 Thr (T) side chain interacts with substrate/intermediate substrate binding -- binding ISS
Subgroup CAR This EFD conserves 4/5 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
58 Asn (N) side chain binds phosphate moiety of substrate substrate binding -- binding ICS PubMed:15096040
94 Lys (K) side chain stabilizes negatively charged intermediate electrostatic stabiliser -- spectator ISS PubMed:12574508
118 Asp (D) side chain Mg2+ ligand (via water) metal ligand -- binding ICS PubMed:15096040
119 Asp (D) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:15096040

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
April 30, 2014, 6:07 a.m. update curation agent sbrown setDomainBoundaries.py
update domain end position 157 161
EC number assigned by UniProtKB accession ID.