MetaCyc Polypeptide: NAD-dependent formate dehydrogenase α subunit

Gene: fdh1A Accession Number: G-3261 (MetaCyc)

Species: Methylobacterium extorquens AM1

Component of: NAD-dependent formate dehydrogenase (summary available)

Molecular Weight of Polypeptide: 107 kD (experimental) [Laukel03 ]

Unification Links: ModBase:Q8KTI7 , Protein Model Portal:Q8KTI7 , Swiss-Model:Q8KTI7 , UniProt:Q8KTI7

Relationship Links: Entrez-Nucleotide:RELATED-TO:AF489516 , InterPro:IN-FAMILY:IPR001041 , InterPro:IN-FAMILY:IPR001450 , InterPro:IN-FAMILY:IPR006478 , InterPro:IN-FAMILY:IPR006655 , InterPro:IN-FAMILY:IPR006656 , InterPro:IN-FAMILY:IPR006657 , InterPro:IN-FAMILY:IPR006963 , InterPro:IN-FAMILY:IPR009010 , InterPro:IN-FAMILY:IPR012675 , InterPro:IN-FAMILY:IPR017896 , InterPro:IN-FAMILY:IPR017900 , Pfam:IN-FAMILY:PF00384 , Pfam:IN-FAMILY:PF01568 , Pfam:IN-FAMILY:PF04879 , Pfam:IN-FAMILY:PF12838 , Prosite:IN-FAMILY:PS00198 , Prosite:IN-FAMILY:PS00490 , Prosite:IN-FAMILY:PS51085 , Prosite:IN-FAMILY:PS51379 , Prosite:IN-FAMILY:PS51669 , Smart:IN-FAMILY:SM00926

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

MultiFun Terms: metabolism carbon utilization carbon compounds

Subunit of: NAD-dependent formate dehydrogenase

Species: Methylobacterium extorquens AM1

Subunit composition of NAD-dependent formate dehydrogenase = [Fdh1A][Fdh1B]
         NAD-dependent formate dehydrogenase α subunit = Fdh1A
         NAD-dependent formate dehydrogenase β subunit = Fdh1B

NAD+-dependent formate dehydrogenases are widely distributed among methanol oxidizing bacteria, as well as certain strains of yeast and some plants [Jollie91]. These enzymes vary considerably in subunit structure and prosthetic group requirement.

The tungsten-containing NAD-dependent formate dehydrogenase from M. extorquens is a heterodimer containing iron-sulfur clusters, FMN and tungsten. It is somewhat unusual to find a tungsten-containing enzyme in aerobic bacteria, although several other examples have been found.

The smaller β subunit appears to be a fusion protein, with its N-terminal domain related to NueE-like subunits, and its C-termonal domain related to NuoF-like subunits of known NADH-ubiquinone oxidoreductases [Laukel03].

Locations: cytosol

Molecular Weight: 168 kD (experimental) [Laukel03]

GO Terms:

Cellular Component: GO:0005829 - cytosol

Enzymatic reaction of: NAD-dependent formate dehydrogenase

EC Number:

formate + NAD+ <=> CO2 + NADH

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

This reaction is reversible.

In Pathways: superpathway of C1 compounds oxidation to CO2 , oxalate degradation III , formate oxidation to CO2

Cofactors or Prosthetic Groups: an iron-sulfur cluster [Laukel03], FMN [Laukel03], W+6 [Laukel03]

Inhibitors (Unknown Mechanism): azide [Laukel03]

Kinetic Parameters:

Km (μM)

pH(opt): 8.3 [Laukel03]


Jollie91: Jollie DR, Lipscomb JD (1991). "Formate dehydrogenase from Methylosinus trichosporium OB3b. Purification and spectroscopic characterization of the cofactors." J Biol Chem 266(32);21853-63. PMID: 1657982

Laukel03: Laukel M, Chistoserdova L, Lidstrom ME, Vorholt JA (2003). "The tungsten-containing formate dehydrogenase from Methylobacterium extorquens AM1: purification and properties." Eur J Biochem 270(2);325-33. PMID: 12605683

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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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