Protein Domain : IPR011707

Type:  Domain Name:  Multicopper oxidase, type 3
Description:  Copper is one of the most prevalent transition metals in living organisms and its biological function is intimately related to its redox properties. Sincefree 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.This entry represents multicopper oxidase type 3 (or coupled binuclear) domains. Short Name:  Cu-oxidase_3

0 Child Features

1 Contains

DB identifier Type Name
IPR002355 Binding_site Multicopper oxidase, copper-binding site

1 Cross References

Identifier
PF07732

7 Found Ins

DB identifier Type Name
IPR008972 Domain Cupredoxin
IPR017761 Family Laccase
IPR017760 Family L-ascorbate oxidase, plants
IPR001287 Family Nitrite reductase, copper-type
IPR017762 Family L-ascorbate oxidase, fungi
IPR014707 Family Coagulation factor 8
IPR006376 Family Copper-resistance protein CopA

1 GO Annotation

GO Term Gene Name Organism
GO:0005507 IPR011707

0 Parent Features

1185 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
105894 D8S0U4 PAC:15418074 Selaginella moellendorffii 566  
418427 D8S5N7 PAC:15406664 Selaginella moellendorffii 588  
95740 D8RKK0 PAC:15407038 Selaginella moellendorffii 562  
229918 D8QML5 PAC:15414478 Selaginella moellendorffii 537  
230356 PAC:15413166 Selaginella moellendorffii 566  
404333 D8QV04 PAC:15409398 Selaginella moellendorffii 589  
438115 D8QU75 PAC:15418798 Selaginella moellendorffii 589  
80214 D8QXR5 PAC:15403685 Selaginella moellendorffii 532  
85188 D8R6A7 PAC:15417788 Selaginella moellendorffii 127  
403803 D8QSK9 PAC:15410275 Selaginella moellendorffii 560  
78002 D8QV03 PAC:15418410 Selaginella moellendorffii 533  
123638 D8SSF3 PAC:15402565 Selaginella moellendorffii 66  
165365 D8QU76 PAC:15412743 Selaginella moellendorffii 578  
231207 D8RC89 PAC:15415185 Selaginella moellendorffii 579  
404075 D8QU74 PAC:15407082 Selaginella moellendorffii 570  
78404 D8QV05 PAC:15421352 Selaginella moellendorffii 582  
80405 D8QXB9 PAC:15405211 Selaginella moellendorffii 52  
410532 D8RF19 PAC:15406387 Selaginella moellendorffii 537  
evm.model.supercontig_3.312 PAC:16416605 Carica papaya 562  
evm.TU.contig_43054.1 PAC:16431821 Carica papaya 351  
evm.model.supercontig_103.59 PAC:16404945 Carica papaya 602  
evm.model.supercontig_119.3 PAC:16406545 Carica papaya 552  
evm.model.supercontig_119.4 PAC:16406556 Carica papaya 280  
evm.model.supercontig_139.14 PAC:16408510 Carica papaya 563  
evm.model.supercontig_139.15 PAC:16408511 Carica papaya 509  
evm.model.supercontig_169.17 PAC:16410537 Carica papaya 524  
evm.model.supercontig_19.119 PAC:16411849 Carica papaya 579  
evm.model.supercontig_19.219 PAC:16411960 Carica papaya 317  
evm.model.supercontig_2.357 PAC:16412738 Carica papaya 431  
evm.model.supercontig_20.137 PAC:16412934 Carica papaya 469  

8 Publications

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