LIS - Legume Information System
Information about legume traits for crop improvement
GlycineMine
v5.1.0.3
Glycine data from LIS
v5.1.0.3
Glycine data from LIS
| Type | Conserved_site |
| Description | A number of proteins involved in the biosynthesis of metallo cofactors have been shown [, ] to be evolutionary related. These include:Bacterial and archebacterial protein moaA, which is involved in the biosynthesis of the molybdenum cofactor (molybdopterin; MPT).Arabidopsis thaliana (Mouse-ear cress) cnx2, a protein involved in molybdopterin biosynthesis and which is highly similar to moaA.Bacillus subtilis narA, which seems to be the moaA ortholog in that bacteria.Bacterial protein nifB (or fixZ) which is involved in the biosynthesis of the nitrogenase iron-molybdenum cofactor.Bacterial protein pqqE which is involved in the biosynthesis of the cofactor pyrrolo-quinoline-quinone (PQQ).Pyrococcus furiosus cmo, a protein involved in the synthesis of a molybdopterin-based tungsten cofactor.Caenorhabditis elegans hypothetical protein F49E2.1.These proteins share, in their N-terminal region, a conserved domain thatcontains three cysteines. In moaA, these cysteines have been shown to be important for biological activity by binding a [4Fe-4S] cluster []. The three cysteines each coordinate one Fe, while S-adenosylmethionine is the fourth ligand to the cluster and binds to its unique Fe as an N/O chelate. |
| Short Name | MoaA_NifB_PqqE_Fe-S-bd_CS |
