Protein Family Models

This domain is found in various molybdopterin - containing oxidoreductases and tungsten formylmethanofuran dehydrogenase subunit d (FwdD) and molybdenum formylmethanofuran dehydrogenase subunit (FmdD); where the domain constitutes almost the entire subunit. The formylmethanofuran dehydrogenase catalyses the first step in methane formation from CO2 in methanogenic archaea and has a molybdopterin dinucleotide cofactor [1]. This domain corresponds to the C-terminal domain IV in dimethyl sulfoxide (DMSO)reductase which interacts with the 2-amino pyrimidone ring of both molybdopterin guanine dinucleotide molecules [2]. [1]. 9818358. The formylmethanofuran dehydrogenase isoenzymes in. Methanobacterium wolfei and Methanobacterium. thermoautotrophicum: induction of the molybdenum isoenzyme by. molybdate and constitutive synthesis of the tungsten isoenzyme.. Hochheimer A, Hedderich R, Thauer RK;. Arch Microbiol 1998;170:389-393.. [2]. 8890912. Crystal structure of dimethyl sulfoxide reductase from. Rhodobacter capsulatus at 1.88 A resolution.. Schneider F, Lowe J, Huber R, Schindelin H, Kisker C, Knablein. J;. J Mol Biol 1996;263:53-69. (from Pfam)

Date:

2024-08-14

Date:

2024-08-14

This model represents a well-defined clade of oxidoreductase alpha subunits most closely related to a group of formate dehydrogenases including the E. coli FdhH protein (TIGR01591). These alpha subunits contain a molybdopterin cofactor and generally associate with two other subunits which contain iron-sulfur clusters and cytochromes. The particular subunits with which this enzyme interacts and the substrate which is reduced is unknown at this time. In Ralstonia, the gene is associated with the cbb operon [1], but is not essential for CO2 fixation.

Date:

2024-06-04