 |
InterPro: IPR012801 Catechol 1,2-dioxygenase, proteobacteria
Protein matches
|
UniProtKB Matches: 148 proteins |
|
Accession
|
IPR012801 Cchol_dOase_prob |
Type
|
Family |
Signatures
|
|
InterPro Relationships
|
|
Contains
|
IPR000627 Intradiol ring-cleavage dioxygenase, C-terminal
IPR007535 Catechol dioxygenase, N-terminal
IPR015889 Intradiol ring-cleavage dioxygenase, core
|
GO Term annotation
|
|
Process
|
GO:0019614 catechol catabolic process
GO:0055114 oxidation reduction
|
|
Function
|
GO:0005506 iron ion binding
GO:0018576 catechol 1,2-dioxygenase activity
|
|
InterPro annotation
|
|
Entry Details in BioMart
|
Abstract
|
Members of this family known so far are catechol 1,2-dioxygenases of the proteobacteria. They are distinct from catechol 1,2-dioxygenases and chlorocatechol 1,2-dioxygenases of the actinobacteria, which are quite similar to each other and resolved by separate entries. This enzyme catalyses intradiol cleavage in which catechol + O2 becomes cis,cis-muconate. Catechol is an intermediate in the catabolism of many different aromatic compounds, as is the alternative intermediate protocatechuate. In Acinetobacter lwoffii, two isozymes are present with abilities, differing somewhat, to act on catechol analogues 3-methylcatechol, 4-methylcatechol, 4-methoxycatechol, and 4-chlorocatechol.
|
Structural links
|
|
Database links
|
|
Additional Reading
|
|
Vetting MW, Ohlendorf DH.
The 1.8 A crystal structure of catechol 1,2-dioxygenase reveals a novel hydrophobic helical zipper as a subunit linker.
Structure 8 2000 429-40
[PubMed: 10801478]
http://dx.doi.org/10.1016/S0969-2126(00)00122-2
|
|
Kim SI, Leem SH, Choi JS, Chung YH, Kim S, Park YM, Park YK, Lee YN, Ha KS.
Cloning and characterization of two catA genes in Acinetobacter lwoffii K24.
J. Bacteriol. 179 1997 5226-31
[PubMed: 9260969]
http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=9260969
|
|
|
InterPro 23.1
|