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InterPro: IPR016457 Formylmethanofuran dehydrogenase, subunit B

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84 proteins
AccessionHelp IPR016457 Formylmethanofuran_DH_bsu
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Contains IPR006656 Molybdopterin oxidoreductase
GO Term annotationHelp
Process GO:0015948 methanogenesis
Function GO:0018493 formylmethanofuran dehydrogenase activity
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Formylmethanofuran dehydrogenases (EC:1.2.99.5) is found in methanogenic and sulphate-reducing archaea. The enzyme contains molybdenum or tungsten, a molybdopterin guanine dinuceotide cofactor (MGD) and iron-sulphur clusters [1]. It catalyses the reversible reduction of CO2 and methanofuran via N-carboxymethanofuran (carbamate) to N-formylmethanofuran, the first and second steps in methanogenesis from CO2 [2, 3]. This reaction is important for the reduction of CO2 to methane, in autotrophic CO2 fixation, and in CO2 formation from reduced C1 units [4]. The synthesis of formylmethanofuran is crucial for the energy metabolism of archaea. Methanogenic archaea derives the energy for autrophic growth from the reduction of CO2 with molecular hydrogen as the electron donor [5]. The process of methanogenesis consists of a series of reduction reactions at which the one-carbon unit derived from CO2 is bound to C1 carriers.

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 [6]. The archaea Methanobacterium thermoautotrophicum contains a 4-subunit (FwdA, FwdB, FwdC, FwdD) tungsten formylmethanofuran dehydrogenase and a 3-subunit (FmdA, FmdB, FmdC) molybdenum formylmethanofuran dehydrogenase [4].

This entry represents subunit B (FmdB and FwdB) of formylmethanofuran dehydrogenases. The other subunits are subunit A (IPR012027), subunit C (IPR012023), subunit D (IPR012040), subunit E (IPR012204) and subunit F (IPR016459). Some organisms also encode a fusion of the C and D subunits(IPR012048).

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P61154 Tungsten-containing formylmethanofuran dehydrogenase 2 subunit B

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InterPro entry accession number/name and structure databases Colour code
IPR006656 Molybdopterin oxidoreductase
IPR016457 Formylmethanofuran dehydrogenase, subunit B

PublicationsHelp
1. Bertram PA, Karrasch M, Schmitz RA, Bocher R, Albracht SP, Thauer RK.
Formylmethanofuran dehydrogenases from methanogenic Archaea. Substrate specificity, EPR properties and reversible inactivation by cyanide of the molybdenum or tungsten iron-sulfur proteins.
Eur. J. Biochem. 220 477-84 1994 [PubMed: 8125106]
http://dx.doi.org/10.1111/j.1432-1033.1994.tb18646.x
2. Hochheimer A, Schmitz RA, Thauer RK, Hedderich R.
The tungsten formylmethanofuran dehydrogenase from Methanobacterium thermoautotrophicum contains sequence motifs characteristic for enzymes containing molybdopterin dinucleotide.
Eur. J. Biochem. 234 910-20 1995 [PubMed: 8575452]
http://dx.doi.org/10.1111/j.1432-1033.1995.910_a.x
3. Vorholt JA, Thauer RK.
The active species of 'CO2' utilized by formylmethanofuran dehydrogenase from methanogenic Archaea.
Eur. J. Biochem. 248 919-24 1997 [PubMed: 9342247]
http://dx.doi.org/10.1111/j.1432-1033.1997.00919.x
4. Hochheimer A, Linder D, Thauer RK, Hedderich R.
The molybdenum formylmethanofuran dehydrogenase operon and the tungsten formylmethanofuran dehydrogenase operon from Methanobacterium thermoautotrophicum. Structures and transcriptional regulation.
Eur. J. Biochem. 242 156-62 1996 [PubMed: 8954165]
http://dx.doi.org/10.1111/j.1432-1033.1996.0156r.x
5. de Poorter LM, Geerts WG, Theuvenet AP, Keltjens JT.
Bioenergetics of the formyl-methanofuran dehydrogenase and heterodisulfide reductase reactions in Methanothermobacter thermautotrophicus.
Eur. J. Biochem. 270 66-75 2003 [PubMed: 12492476]
http://dx.doi.org/10.1046/j.1432-1033.2003.03362.x
6. Hochheimer A, Hedderich R, Thauer RK.
The formylmethanofuran dehydrogenase isoenzymes in Methanobacterium wolfei and Methanobacterium thermoautotrophicum: induction of the molybdenum isoenzyme by molybdate and constitutive synthesis of the tungsten isoenzyme.
Arch. Microbiol. 170 389-93 1998 [PubMed: 9818358]
http://dx.doi.org/10.1007/s002030050658

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InterPro 23.1