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IPR004183 is a Extradiol ring-cleavage dioxygenase, class III enzyme, subunit B.
<p>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 ([interpro:IPR000627]) use a non-haem Fe(III) to cleave the aromatic ring between two hydroxyl groups (ortho-cleavage), whereas extradiol enzymes use a non-haem Fe(II) to cleave the aromatic ring between a hydroxylated carbon and an adjacent non-hydroxylated carbon (meta-cleavage) [[cite:PUB00015256], [cite:PUB00015247]]. These two subfamilies differ in sequence, structural fold, iron ligands, and the orientation of second sphere active site amino acid residues. Extradiol dioxygenases are usually homo-multimeric, bind one atom of ferrous ion per subunit and have a subunit size of about 33kDa. Extradiol dioxygenases can be divided into three classes. Class I and II enzymes ([interpro:IPR000486]) show sequence similarity, with the two-domain class II enzymes having evolved from a class I enzyme through gene duplication. Class III enzymes are different in sequence and structure, but they do share several common active-site characteristics with the class II enzymes, in particular the coordination sphere and the disposition of the putative catalytic base are very similar.</p> <p>Class III enzymes usually have two subunits, designated A and B. Enzymes that belong to the extradiol class III family include Protocatechuate 4,5-dioxygenase (4,5-PCD; LigAB) ([ec:1.13.11.8]) [[cite:PUB00011779]]; and 2'-aminobiphenyl-2,3-diol 1,2-dioxygenase (CarBaBb) [[cite:PUB00015248]].</p> <p>The crystal structure of dioxygenase LigAB revealed that the molecule is an alpha2beta2 tetramer. The active site contains a non-heme iron coordinated by His12, His61, Glu242, and a water molecule located in a deep cleft of the beta subunit, which is covered by the alpha subunit [[cite:PUB00011779]].</p> <p>This entry represents the structural domain of subunit B.</p>
This description is obtained from EB-eye REST.
GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .
| GO term | Namespace | Name | Definition | Relationships |
|---|---|---|---|---|
| Biological process | Cellular aromatic compound metabolic process | The chemical reactions and pathways involving aromatic compounds, any organic compound characterized by one or more planar rings, each of which contains conjugated double bonds and delocalized pi electrons, as carried out by individual cells. | ||
| Molecular function | Ferrous iron binding | Interacting selectively and non-covalently with ferrous iron, Fe(II). | ||
| Molecular function | Oxidoreductase activity | Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced. |
| Transcript | Name | Description | Predicted domains | Domain count |
|---|---|---|---|---|
| – | PREDICTED: 4,5-DOPA dioxygenase extradiol-like protein-like [Glycine max] gi|356559959|ref|XP_003548263.1| | 9 | ||
| – | 11 | |||
| – | PREDICTED: 4,5-DOPA dioxygenase extradiol-like protein-like [Glycine max] gi|356559959|ref|XP_003548263.1| | 9 | ||
| – | PREDICTED: 4,5-DOPA dioxygenase extradiol-like protein-like [Glycine max] gi|356559963|ref|XP_003548265.1| | 9 | ||
| – | 4,5-dioxygenase-like protein; TAIR: AT4G15093.1 catalytic LigB subunit of aromatic ring-opening dioxygenase family; Swiss-Prot: sp|Q70FG7|DODA_BETVU 4,5-DOPA dioxygenase extradiol; TrEMBL-Plants: tr|I3SYT8|I3SYT8_LOTJA Uncharacterized protein; Found in the gene: LotjaGi2g1v0166200 | 9 | ||
| – | 4,5-dioxygenase-like protein; TAIR: AT4G15093.1 catalytic LigB subunit of aromatic ring-opening dioxygenase family; Swiss-Prot: sp|Q70FG7|DODA_BETVU 4,5-DOPA dioxygenase extradiol; TrEMBL-Plants: tr|I3SFC8|I3SFC8_LOTJA Uncharacterized protein; Found in the gene: LotjaGi2g1v0166400 | 9 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| cd07363 | CDD | 1 | 16.67 |