Description

IPR033138 is a Multicopper oxidases, conserved site.

<p>Multicopper oxidases [[cite:PUB00001382], [cite:PUB00001602]] are enzymes that possess three spectroscopically different copper centres. These centres are called: type 1 (or blue), type 2 (or normal) and type 3 (or coupled binuclear). The enzymes that belong to this family include:</p> <ul> <li>Laccase (EC 1.10.3.2) (urishiol oxidase), an enzyme found in fungi and plants, which oxidizes many different types of phenols and diamines.</li> <li>L-ascorbate oxidase (EC 1.10.3.3), a higher plant enzyme.</li> <li>Ceruloplasmin (EC 1.16.3.1) (ferroxidase), a protein found in the serum of mammals and birds, which oxidizes a great variety of inorganic and organic substances. Structurally ceruloplasmin exhibits internal sequence homology, and seem to have evolved from the triplication of a copper-binding domain similar to that found in laccase and ascorbate oxidase.</li> </ul> <p>In addition to the above enzymes there are a number of proteins which, on the basis of sequence similarities, can be said to belong to this family. These proteins are:</p> <ul> <li>Copper resistance protein A (copA) from a plasmid in Pseudomonas syringae. This protein seems to be involved in the resistance of the microbial host to copper.</li> <li>Blood coagulation factor V (Fa V).</li> <li>Blood coagulation factor VIII (Fa VIII).</li> <li>Yeast FET3 [[cite:PUB00000901]], which is required for ferrous iron uptake.</li> <li>Yeast hypothetical protein YFL041w and SpAC1F7.08, the fission yeast homologue.</li> </ul> <p>Factors V and VIII act as cofactors in blood coagulation and are structurally similar [[cite:PUB00000062]]. Their sequence consists of a triplicated A domain, a B domain and a duplicated C domain; in the following order: A-A-B-A-C-C. The A-type domain is related to the multicopper oxidases.</p> <p>This entry is drawn from a conserved region, which in ascorbate oxidase, laccase, in the third domain of ceruloplasmin, and in copA, contains five residues that are known to be involved in the binding of copper centres. However, it does not make any assumption on the presence of copper-binding residues and thus can detect domains that have lost the ability to bind copper (such as those in Fa V and Fa VIII).</p>

This description is obtained from EB-eye REST.

Associated GO terms

Unable to find any GO terms for the transcript with the identifier.

Associated Lotus transcripts 59

Co-occuring domains 1

A list of co-occurring predicted domains within the L. japonicus gene space: