Fungal multicopper oxidase, cupredoxin domain 3 (IPR035666)

Short name: MCO_CuRO_3

Overlapping homologous superfamilies


Domain relationships


This domain is found in fungal proteins with similarity to ascorbate oxidase [PMID: 9858779]. Ascorbate oxidase catalyzes the oxidation of ascorbic acid to dehydroascorbic acid. It can detect levels of ascorbic acid and eliminate it. The biological function of ascorbate oxidase is still not clear.

Ascorbate oxidase belongs to multicopper oxidase (MCO) family which couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper centre and transferring them to the active site trinuclear copper centre. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3 [PMID: 16234932, PMID: 17639274, PMID: 19816718, PMID: 2404764].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.