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InterPro: IPR012801 Catechol 1,2-dioxygenase, proteobacteria

Protein matchesHelp
UniProtKB
Matches:
148 proteins
AccessionHelp IPR012801 Cchol_dOase_prob
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Contains IPR000627 Intradiol ring-cleavage dioxygenase, C-terminal
IPR007535 Catechol dioxygenase, N-terminal
IPR015889 Intradiol ring-cleavage dioxygenase, core
GO Term annotationHelp
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
BioMart Logo Entry Details in BioMart
AbstractHelp

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 linksHelp
SCOP: b.3.6.1
CATH: 2.60.130.10
Database linksHelp
Enzyme: EC:1.13.11.1

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR012801 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P07773 Catechol 1,2-dioxygenase

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR000627 Intradiol ring-cleavage dioxygenase, C-terminal
IPR015889 Intradiol ring-cleavage dioxygenase, core
IPR007535 Catechol dioxygenase, N-terminal
IPR012801 Catechol 1,2-dioxygenase, proteobacteria
PDB Chain
ModBase
CATH Domain
SCOP Domain

PublicationsHelp

Additional ReadingHelp
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
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InterPro 23.1