| Description | Proteins containing this domain form structural complexes with other known families, such as and . The carbon monoxide (CO) dehydrogenase of Oligotropha carboxidovorans is a heterotrimeric complex composed of a apoflavoprotein, a molybdoprotein, and an iron-sulphur protein. It can be dissociated with sodium dodecylsulphate [ ]. CO dehydrogenase catalyzes the oxidation of CO according to the following equation []:CO + H2O = CO2 + 2e + 2H+Subunit S represents the iron-sulphur protein of CO dehydrogenase and is clearly divided into a C- and an N-terminal domain, each binding a [2Fe-2S] cluster [].The structure of the C-terminal domain has a β(3,4)-α(3) fold arranged in an α+β sandwich. | Name | CO dehydrogenase flavoprotein, C-terminal domain superfamily |
| Short Name | CO_DH_flav_C_dom_sf | Type | Homologous_superfamily |
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