Tetrahaem cytochrome domain (IPR012286)

Short name: Tetrahaem_cytochrome

Overlapping homologous superfamilies

Domain relationships


Flavocytochrome C3 (Fcc3) enzymes from a number of Shewanella species, including Shewanella frigidimarina (strain NCIMB 400), have respiratory fumarate reductase activity, which enables the bacteria to respire anaerobically with fumarate as a terminal electron acceptor. Flavocytochrome C3 in S. frigidimarina is a soluble, single chain tetrahaem enzyme found in the periplasm, making it distinct from other bacterial fumarate reductases (IPR010960), which are membrane-bound, multi-subunit enzymes, even though their function is analogous.

Shewanella Fcc3 is composed of three domains: an N-terminal tetrahaem cytochrome domain, a flavin domain and a clamp domain. The cytochrome domain can also occur on its own in some tetrahaem cytochromes implicated in iron oxidation. This entry represents the cytochrome domain, which has a different arrangement of the polypeptide chain in comparison to classical tetra-haem cytochrome C3 [PMID: 12080059, PMID: 15581639].

Contributing signatures

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