|PROSITE documentation PDOC00079
Intradiol ring-cleavage dioxygenases signature
Dioxygenases catalyze the incorporation of both atoms of molecular oxygen into
substrates. Cleavage of aromatic rings is one of the most important function
of dioxygenases. The substrates of ring-cleavage dioxygenases can be
classified into two groups according to the mode of scission of the aromatic
ring. Intradiol enzymes cleave the aromatic ring between two hydroxyl groups,
whereas extradiol enzymes cleave the aromatic ring between a hydroxylated
carbon and another adjacent nonhydroxylated carbon . Intradiol dioxygenases
require a nonheme ferric ion as a cofactor. The enzymes that belong to this
- Protocatechuate 3,4-dioxygenase (EC 220.127.116.11) (3,4-PCD), an oligomeric
enzyme complex which consists of 12 copies each of an α and a β
subunits. Both subunits are evolutionary related.
- Catechol 1,2-dioxygenase (EC 18.104.22.168) (gene catA or clcA).
- Chlorocatechol 1,2-dioxygenase (EC 22.214.171.124) (gene tfdC).
As a signature pattern for these enzymes we selected a region that includes
a tyrosine residue which, in 3,4-PCD, has been shown , to be implicated in
the binding of the ferric iron atom.
December 2004 / Pattern and text revised.
PROSITE method (with tools and information) covered by this documentation:
|INTRADIOL_DIOXYGENAS, PS00083; Intradiol ring-cleavage dioxygenases signature (PATTERN)
Y is an iron ligand
|Sequences in UniProtKB/Swiss-Prot known to belong to this class detected by PS00083:
||20 true positives with 4 partials.
|Other sequence(s) in UniProtKB/Swiss-Prot detected by PS00083:
|Matching PDB structures:
1DLM 1DLQ 1DLT 1DMH ... [ALL]
||Harayama S., Rekik M.
||Bacterial aromatic ring-cleavage enzymes are classified into two different gene families.
||J. Biol. Chem. 264:15328-15333(1989).
||Ohlendorf D.H., Lipscomb J.D., Weber P.C.
||Structure and assembly of protocatechuate 3,4-dioxygenase.
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