Formylmethanofuran dehydrogenase, subunit E domain (IPR003814)

Short name: FwdEsu_dom

Overlapping homologous superfamilies


Domain relationships


Formylmethanofuran dehydrogenases (EC:, found in methanogenic archaea, are molybdenum or tungsten iron-sulphur proteins containing a pterin dinucleotide cofactor. Formylmethanofuran dehydrogenase catalyses the reversible reduction of CO2 and methanofuran via N-carboxymethanofuran (carbamate) to N-formylmethanofuran, the first and second steps in methanogenesis from CO2 [PMID: 8575452]. 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 [PMID: 9818358].

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.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.