CATH Classification

Domain Context

CATH Clusters

Superfamily Fumarylacetoacetase-like, C-terminal domain
Functional Family 2-oxo-hepta-3-ene-1,7-dioic acid hydratase

Enzyme Information

4.2.1.163
2-oxo-hept-4-ene-1,7-dioate hydratase.
based on mapping to UniProt Q46982
(4Z)-2-oxohept-4-enedioate + H(2)O = (4S)-4-hydroxy-2-oxoheptanedioate.
-!- Part of a 4-hydroxyphenylacetate degradation pathway in Escherichia coli C.
4.1.1.77
2-oxo-3-hexenedioate decarboxylase.
based on mapping to UniProt Q46982
(3E)-2-oxohex-3-enedioate = 2-oxopent-4-enoate + CO(2).
-!- Involved in the meta-cleavage pathway for the degradation of phenols, modified phenols and catechols. -!- The enzyme has been reported to accept multiple tautomeric forms. -!- However, careful analysis of the stability of the different tautomers, as well as characterization of the enzyme that produces its substrate, EC 5.3.2.6, showed that the actual substrate for the enzyme is (3E)-2-oxohex-3-enedioate.
4.2.1.-
Hydro-lyases.
based on mapping to UniProt Q46982
4.2.-.-
Carbon-oxygen lyases.
based on mapping to UniProt Q46982
4.2.1.80
2-oxopent-4-enoate hydratase.
based on mapping to UniProt Q46982
4-hydroxy-2-oxopentanoate = 2-oxopent-4-enoate + H(2)O.
-!- Also acts, more slowly, on cis-2-oxohex-4-enoate, but not on the trans-isomer.

UniProtKB Entries (1)

Q46982
Q46982_ECOLX
Escherichia coli
2-hydroxyhexa-2,4-dienoate hydratase

PDB Structure

PDB 2EB4
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Structure and Mechanism of HpcG, a Hydratase in the Homoprotocatechuate Degradation Pathway of Escherichia coli
Izumi, A., Rea, D., Adachi, T., Unzai, S., Park, S.Y., Roper, D.I., Tame, J.R.H.
J.Mol.Biol.