v5.1.0.3
Cicer data from the Legume Information System
| Type | Family |
| Description | Cytochromes c (cytC) can be defined as electron-transfer proteins having one or several haem c groups, bound to the protein by one or, more generally, two thioether bonds involving sulphydryl groups of cysteine residues. The fifth haem iron ligand is always provided by a histidine residue. CytC possess a wide range of properties and function in a large number of different redox processes. Ambler [ ] recognised four classes of cytC.Class I includes the low-spin soluble cytC of mitochondria and bacteria, with the haem-attachment sitetowards the N terminus, and the sixth ligand provided by a methionine residue about 40 residues further on towards the C terminus. On the basisof sequence similarity, class I cytC were further subdivided into five classes, IA to IE. Class IE includes such bacterial proteins as cyt c5, cyt c-555 and Ectothiorhodospira cyt c-551. The 3D structure of cyt c5 from Azotobacter vinelandii has been determined []. The protein consists of 5 α-helices; three 'core' helices form a 'basket' around the haem group, with one haem edge exposed to the solvent. |
| Short Name | Cyt_CIE |