v5.1.0.3
Cicer data from the Legume Information System
| Type | Family |
| Description | MauD appears critical to proper formation of the small subunit of methylamine dehydrogenase, which has both an unusual tryptophan tryptophylquinone cofactor and multiple disulphide bonds. MauD shares sequence similarity, including a CPxC motif, with a number of thiol:disulphide interchange proteins. In MauD mutants, the small subunit apparently does not form properly and is rapidly degraded [ ]. |
| Short Name | MeN_DH_accessory |