v5.1.0.3
Cicer data from the Legume Information System
| Type | Family |
| Description | These proteins are members of the wider radical SAM superfamily of enzymes that enzymes utilise an iron-sulphur redox cluster and S-adenosylmethionine to carry out diverse radical mediated reactions [ ]. The Acidithiobacillus ferrooxidans ATCC 23270 protein (AFE_0975) is encoded in the same locus as the genes for squalene-hopene cyclase (SHC, ) and other proteins associated with the biosynthesis of hopanoid natural products. Similarly, in Ralstonia eutropha (strain JMP134) (Alcaligenes eutrophus) (Reut_B4901) this protein is encoded adjacent to the genes for HpnAB, IspH and HpnH ( ), although SHC itself is elsewhere in the genome. Notably, this protein (here named HpnJ) and three others form a conserved set (HpnIJKL) which occur in a subset of all genomes containing the SHC enzyme. This relationship was discerned using the method of partial phylogenetic profiling []. This group includes Zymomonas mobilis the organism where the initial hopanoid biosynthesis locus was described consisting of the genes HpnA-E and SHC (HpnF) []. Continuing past SHC are genes encoding a phosphorylase enzyme (ZMO0873, i.e. HpnG, ) and another radical SAM enzyme (ZMO0874), HpnH. Although discontinuous in Z. mobilis, we continue the gene symbol sequence with HpnIJKL. One of the well-described hopanoid intermediates is bacteriohopanetetrol. In the conversion from hopene several reactions must occur in the side chain for which a radical mechanism might be reasonable. These include the four (presumably anaerobic) hydroxylations and a methyl shift. |
| Short Name | Hopanoid_synth-assoc_rSAM_HpnJ |