Rusticyanin (IPR001243)

Short name: Rusticyanin

Overlapping homologous superfamilies

Family relationships



Rusticyanin is a blue copper protein, described in an obligate acidophilic chemolithoautroph, Acidithiobacillus ferrooxidans, as an electron transfer protein. It can constitute up to 5 percent of protein in cells grown on Fe(II) and is thought to be part of an electron chain for Fe(II) oxidation, with two c-type cytochromes, an aa3-type cytochrome oxidase, and 02 as terminal electron acceptor [PMID: 15256554, PMID: 15357880]. It is rather closely related to sulfocyanin (IPR010532).

The NMR structure indicates the fold to be a compact beta-barrel or beta-sandwich, which contains a hydrophobic core rich in aromatic residues [PMID: 7990128]. Its sequence is highly diverged from related copper-blue proteins, but it has a similar active site, containing conserved His and Cys residues responsible for binding copper.

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0005507 copper ion binding
GO:0009055 electron transfer activity

Cellular Component

No terms assigned in this category.

Contributing signatures

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