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IPR015881 is a Aromatic-ring-hydroxylating dioxygenase ARHD, Rieske 2Fe-2S-binding site.
<p>This entry represents the Rieske type 2Fe-2S binding site found at the N-terminal in the alpha-subunit of ARHD proteins and related non-heme iron oxygenases. The Rieske-type [2Fe-2S] cluster is coordinated to its protein by two cysteine residues and two histidine residues [[cite:PUB00043836], [cite:PUB00043837]].</p> <p>Aromatic-ring-hydroxylating dioxygenases (ARHD) are multicomponent 1,2-dioxygenase complexes that convert closed-ring structures to non-aromatic cis-diols [[cite:PUB00002151]]. The complex has both hydroxylase and electron transfer components. The hydroxylase component is composed of two subunits: an alpha-subunit of about 50 kDa and a beta-subunit of about 20 kDa. The electron transfer component is either composed of two subunits: a ferredoxin and a ferredoxin reductase or by a single bifunctional ferredoxin/reductase subunit. Sequence analysis of hydroxylase subunits of ring hydroxylating systems (including toluene, benzene, and napthalene 1,2-dioxygenases) suggests they are derived from a common ancestor [[cite:PUB00002151]]. The alpha-subunit binds both a Rieske-like 2Fe-2S cluster and an iron atom: conserved Cys and His residues in the N-terminal region may provide 2Fe-2S ligands, while conserved His and Tyr residues may coordinate the iron. The beta subunit may be responsible for the substrate specificity of the dioxygenase system [[cite:PUB00002151]].</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 |
|---|---|---|---|---|
| Molecular function | Iron ion binding | Interacting selectively and non-covalently with iron (Fe) ions. | ||
| Molecular function | 2 iron, 2 sulfur cluster binding | Interacting selectively and non-covalently with a 2 iron, 2 sulfur (2Fe-2S) cluster; this cluster consists of two iron atoms, with two inorganic sulfur atoms found between the irons and acting as bridging ligands. | ||
| Biological process | Oxidation-reduction process | A metabolic process that results in the removal or addition of one or more electrons to or from a substance, with or without the concomitant removal or addition of a proton or protons. |
| Transcript | Name | Description | Predicted domains | Domain count |
|---|---|---|---|---|
| – | PREDICTED: chlorophyllide a oxygenase, chloroplastic-like [Cicer arietinum] gi|502124009|ref|XP_004498345.1| | 15 | ||
| – | Chlorophyllide A oxygenase; TAIR: AT1G44446.1 Pheophorbide a oxygenase family protein with Rieske 2Fe-2S domain-containing protein; Swiss-Prot: sp|Q9MBA1|CAO_ARATH Chlorophyllide a oxygenase, chloroplastic; TrEMBL-Plants: tr|A0A151RSX8|A0A151RSX8_CAJCA Uncharacterized protein; Found in the gene: LotjaGi1g1v0159200 | 16 | ||
| – | Chlorophyllide A oxygenase; TAIR: AT1G44446.1 Pheophorbide a oxygenase family protein with Rieske 2Fe-2S domain-containing protein; Swiss-Prot: sp|Q8S7E1|CAO_ORYSJ Chlorophyllide a oxygenase, chloroplastic; TrEMBL-Plants: tr|A0A151RSX8|A0A151RSX8_CAJCA Uncharacterized protein; Found in the gene: LotjaGi1g1v0159200 | 16 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| mobidb-lite | MobiDBLite | 1 | 33.33 |