Total 100% <100%
Functional domains 7 0 7
UniProtKB 5 0 5
GI 63 0 63
Structures 27
Reactions 1
Functional domains of this family were last updated on Nov. 22, 2017

Enzymes in the epoxide hydrolase n-terminal phosphatase family contain two structural domains, each with a seperate and independent active site. Only the N-terminal domain is part of the haloacid dehalogenase superfamily. This domain has lipid phosphatase activity, but the biologically relevant substrate has not yet been identified. Mg2+ is required for optimal activity. The C-terminal domain has epoxide hydrolase activity, but is not a part of the haloacid dehalogenase superfamily.

Cronin, A., et al.

The N-terminal domain of mammalian soluble epoxide hydrolase is a phosphatase

▸ Abstract

Proc Natl Acad Sci U S A 2003;100(4):1552-1557 | PubMed ID: 12574508

Newman JW, Morisseau C, Harris TR, Hammock BD

The soluble epoxide hydrolase encoded by EPXH2 is a bifunctional enzyme with novel lipid phosphate phosphatase activity

▸ Abstract

Proc Natl Acad Sci U S A 2003;100(4):1558-1563 | PubMed ID: 12574510

No notes.

Static File Downloads

File Name Description Parameters Stats
sfld_alignment_fam40.msa Annotated Sequence Alignment, Stockholm format 2 sequences
size: 1.7K

Total number of functional domains in this group.
Number of Functional Domains that have been manually or automatically been assigned to a family.
Number of Functional Domains that have not been assigned to a family.
Number of structures available from the PDB for members of this group.
Number of Functional Domains with 100% of Conserved Residues
Number of Functional Domains with less than 100% Conserved Residues

Active Site

Catalyzed Reaction(s)

lipid-phosphate phosphatase

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

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