Protein Domain : IPR002355

Type:  Binding_site Name:  Multicopper oxidase, copper-binding site
Description:  Copper is one of the most prevalent transition metals in living organisms and its biological function is intimately related to its redox properties. Since free copper is toxic, even at very low concentrations, its homeostasis in living organisms is tightly controlled by subtle molecular mechanisms. In eukaryotes, before being transported inside the cell via the high-affinity copper transporters of the CTR family, the copper (II) ion is reduced to copper (I). In blue copper proteins such as cupredoxin, the copper (I) ion form is stabilised by a constrained His2Cys coordination environment.Multicopper oxidases oxidise their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre; dioxygen binds to the trinuclear centre and, following the transfer of four electrons, is reduced to two molecules of water []. There are three spectroscopically different copper centres found in multicopper oxidases: type 1 (or blue), type 2 (or normal) and type 3 (or coupled binuclear) [, ]. Multicopper oxidases consist of 2, 3 or 6 of these homologous domains, which also share homology to the cupredoxins azurin and plastocyanin. Structurally, these domains consist of a cupredoxin-like fold, a beta-sandwich consisting of 7 strands in 2 beta-sheets, arranged in a Greek-key beta-barrel []. Multicopper oxidases include:Ceruloplasmin () (ferroxidase), a 6-domain enzyme found in the serum of mammals and birds that oxidizes different inorganic and organic substances; exhibits internal sequence homology that appears to have evolved from the triplication of a Cu-binding domain similar to that of laccase and ascorbate oxidase. Laccase () (urishiol oxidase), a 3-domain enzyme found in fungi and plants, which oxidizes different phenols and diamines. CueO is a laccase found in Escherichia colithat is involved in copper-resistance [].Ascorbate oxidase (), a 3-domain enzyme found in higher plants.Nitrite reductase (), a 2-domain enzyme containing type-1 and type-2 copper centres [, ].In addition to the above enzymes there are a number of other proteins that are similar to the multi-copper oxidases in terms of structure and sequence, some of which have lost the ability to bind copper. These include: copper resistance protein A (copA) from a plasmid in Pseudomonas syringae; domain A of (non-copper binding) blood coagulation factors V (Fa V) and VIII (Fa VIII) []; yeast FET3 required for ferrous iron uptake []; yeast hypothetical protein YFL041w; and the fission yeast homologue SpAC1F7.08.The pattern of this signature is specific to sites that are Cu-binding. A related pattern can detect sites that have lost the ability to bind copper, such as those in Fa V and Fa VIII, . Short Name:  Cu_oxidase_Cu_BS

0 Child Features

0 Contains

2 Cross Referencess

Identifier
PS00079
PS00080

9 Found Ins

DB identifier Type Name
IPR008972 Domain Cupredoxin
IPR011707 Domain Multicopper oxidase, type 3
IPR011706 Domain Multicopper oxidase, type 2
IPR017761 Family Laccase
IPR017760 Family L-ascorbate oxidase, plants
IPR006376 Family Copper-resistance protein CopA
IPR010532 Family Sulfocyanin
IPR001243 Family Rusticyanin
IPR017762 Family L-ascorbate oxidase, fungi

1 GO Annotation

GO Term Gene Name
GO:0005507 IPR002355

1 Ontology Annotations

GO Term Gene Name
GO:0005507 IPR002355

0 Parent Features

0 Proteins

8 Publications

First Author Title Year Journal Volume Pages PubMed ID
            1995346
            3052293
            8293473
            2404764
            11867755
            14572631
            11041837
            16234932