Catechol dioxygenase, N-terminal (IPR007535)

Short name: Catechol_dOase_N

Overlapping homologous superfamilies

Domain relationships



This domain is the N-terminal region of catechol, chlorocatechol or hydroxyquinol 1,2-dioxygenase proteins. This region is always found adjacent to the dioxygenase domain (IPR000627).

Dioxygenases catalyse the incorporation of both atoms of molecular oxygen into substrates using a variety of reaction mechanisms. Cleavage of aromatic rings is one of the most important functions of dioxygenases, which play key roles in the degradation of aromatic compounds. The substrates of ring-cleavage dioxygenases can be classified into two groups according to the mode of scission of the aromatic ring. Intradiol enzymes use a non-haem Fe(III) to cleave the aromatic ring between two hydroxyl groups (ortho-cleavage), whereas extradiol enzymes (IPR000486) use a non-haem Fe(II) to cleave the aromatic ring between a hydroxylated carbon and an adjacent non-hydroxylated carbon (meta-cleavage) [PMID: 10730195]. These two subfamilies differ in sequence, structural fold, iron ligands, and the orientation of second sphere active site amino acid residues.

Enzymes that belong to the intradiol family include catechol 1,2-dioxygenase (1,2-CTD) (EC:; protocatechuate 3,4-dioxygenase (3,4-PCD) (EC:; and chlorocatechol 1,2-dioxygenase (EC: [PMID: 15060064].

GO terms

Biological Process

GO:0009712 catechol-containing compound metabolic process
GO:0055114 oxidation-reduction process

Molecular Function

GO:0018576 catechol 1,2-dioxygenase activity
GO:0005506 iron ion binding

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.