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IPR002227 is a Tyrosinase copper-binding domain.
<p>Tyrosinase ([ec:1.14.18.1]) [[cite:PUB00004934]] is a copper monooxygenases that catalyses the hydroxylation of monophenols and the oxidation of o-diphenols to o-quinols. This enzyme, found in prokaryotes as well as in eukaryotes, is involved in the formation of pigments such as melanins and other polyphenolic compounds. Tyrosinase binds two copper ions (CuA and CuB). Each of the two copper ions has been shown [[cite:PUB00000492]] to be bound by three conserved histidines residues. The regions around these copper-binding ligands are well conserved and also shared by some hemocyanins, which are copper-containing oxygen carriers from the hemolymph of many molluscs and arthropods [[cite:PUB00004295], [cite:PUB00004733]]. At least two proteins related to tyrosinase are known to exist in mammals, and include TRP-1 (TYRP1) [[cite:PUB00001267]], which is responsible for the conversion of 5,6-dihydro-xyindole-2-carboxylic acid (DHICA) to indole-5,6-quinone-2-carboxylic acid; and TRP-2 (TYRP2) [[cite:PUB00001230]], which is the melanogenic enzyme DOPAchrome tautomerase ([ec:5.3.3.12]) that catalyses the conversion of DOPAchrome to DHICA. TRP-2 differs from tyrosinases and TRP-1 in that it binds two zinc ions instead of copper [[cite:PUB00000238]]. Other proteins that belong to this family are plant polyphenol oxidases (PPO) ([ec:1.10.3.1]), which catalyze the oxidation of mono- and o-diphenols to o-diquinones [[cite:PUB00004557]]; and Caenorhabditis elegans hypothetical protein C02C2.1.</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 | 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: polyphenol oxidase A1, chloroplastic-like [Glycine max] gi|356555113|ref|XP_003545882.1| | 13 | ||
| – | PREDICTED: polyphenol oxidase A1, chloroplastic-like [Glycine max] gi|356555113|ref|XP_003545882.1| | 23 | ||
| – | Polyphenol oxidase; Swiss-Prot: sp|P43309|PPO_MALDO Polyphenol oxidase, chloroplastic; TrEMBL-Plants: tr|A0A0B2PGN9|A0A0B2PGN9_GLYSO Polyphenol oxidase A1, chloroplastic; Found in the gene: LotjaGi6g1v0335300 | 14 | ||
| – | Polyphenol oxidase; TAIR: AT1G19230.1 Riboflavin synthase-like superfamily protein; Swiss-Prot: sp|Q06215|PPO_VICFA Polyphenol oxidase A1, chloroplastic; TrEMBL-Plants: tr|A0A0B2PGN9|A0A0B2PGN9_GLYSO Polyphenol oxidase A1, chloroplastic; Found in the gene: LotjaGi6g1v0335400 | 18 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| mobidb-lite | MobiDBLite | 1 | 25.00 |