| Description | Formylmethanofuran dehydrogenases ( ), found in methanogenic archaea, are molybdenum or tungsten iron-sulphur proteins containing a pterin dinucleotide cofactor. Formylmethanofuran dehydrogenase catalyses the reversible reduction of CO 2and methanofuran via N-carboxymethanofuran (carbamate) to N-formylmethanofuran, the first and second steps in methanogenesis from CO 2[ ]. There are two isoenzymes of formylmethanofuran dehydrogenase: a tungsten-containing isoenzyme (Fwd) and a molybdenum-containing isoenzyme (Fmd). The tungsten isoenzyme is constitutively transcribed, whereas transcription of the molybdenum operon is induced by molybdate [].This entry represents a domain found in subunit E of formylmethanofuran dehydrogenase (FmdE). It appears to be related to the Tubulin/FtsZ 2-layer sandwich domain. | Name | Formylmethanofuran dehydrogenase, subunit E domain |
| Short Name | FmdEsu_dom | Type | Domain |
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