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MetaCyc Polypeptide: dimethylsulfide dehydrogenase α subunit

Gene: ddhA Accession Number: G-10873 (MetaCyc)

Species: Rhodovulum sulfidophilum

Component of: dimethylsulfide dehydrogenase (extended summary available)

Gene Citations: [McDevitt02]

Molecular Weight of Polypeptide: 102.31 kD (from nucleotide sequence), 94.0 kD (experimental)

Unification Links: Protein Model Portal:Q8GPG4, UniProt:Q8GPG4

Relationship Links: Entrez-Nucleotide:RELATED-TO:AF453479, InterPro:IN-FAMILY:IPR006311, InterPro:IN-FAMILY:IPR006655, InterPro:IN-FAMILY:IPR006656, InterPro:IN-FAMILY:IPR006657, InterPro:IN-FAMILY:IPR006963, InterPro:IN-FAMILY:IPR009010, InterPro:IN-FAMILY:IPR017840, Pfam:IN-FAMILY:PF00384, Pfam:IN-FAMILY:PF01568, Prosite:IN-FAMILY:PS00932, Prosite:IN-FAMILY:PS51318, Prosite:IN-FAMILY:PS51669

Gene-Reaction Schematic

Gene-Reaction Schematic

Subunit of: dimethylsulfide dehydrogenase

Species: Rhodovulum sulfidophilum

Subunit composition of dimethylsulfide dehydrogenase = [DdhA][DdhB][DdhC]
         dimethylsulfide dehydrogenase α subunit = DdhA
         dimethylsulfide dehydrogenase β subunit = DdhB (summary available)
         dimethylsulfide dehydrogenase γ subunit = DdhC

Dimethylsulfide dehydrogenase catalyzes the oxidation of dimethyl sulfide to dimethyl sulfoxide (DMSO) during photoautotrophic growth of the purple non-sulfur phototrophic bacterium Rhodovulum sulfidophilum.

The enzyme was purified to homogeneity and found to be a complex of 152 kDa, composed of three distinct subunits [Hanlon96]. The enzyme can reduce a variety of N-oxides using reduced methylviologen as electron donor but dimethyl sulfoxide is reduced at a very low rate. The enzyme contains a cytochrome with a b-type heme and a guanylyl molybdenum cofactor cofactor, as well as multiple iron-sulfur clusters [McDevitt02]. The heme and pterin molybdenum cofactor are associated with the 94-kDa subunit.

Analysis of a ddhA mutant showed that dimethylsulfide dehydrogenase was essential for photolithotrophic growth of the organism on dimethyl sulfide but not for chemotrophic growth on the same substrate. Mutational analysis showed that cytochrome c2 mediated photosynthetic electron transfer from the enzyme to the photochemical reaction centre, although this cytochrome was not essential for photoheterotrophic growth of the bacterium [McDevitt02].

Molecular Weight: 152.0 kD (experimental) [Hanlon96]

Created 24-Oct-2008 by Caspi R, SRI International

Enzymatic reaction of: dimethylsulfide dehydrogenase

Inferred from experiment

Synonyms: dimethylsulfide:receptor oxidoreductase

EC Number:

dimethyl sulfide + 2 an oxidized cytochrome c2 + H2O → dimethyl sulfoxide + 2 a reduced cytochrome c2 + 2 H+

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

In Pathways: dimethyl sulfide degradation III (oxidation)

Cofactors or Prosthetic Groups: a [4Fe-4S] iron-sulfur cluster [Hanlon96], guanylyl molybdenum cofactor [McDevitt02]


Hanlon96: Hanlon SP, Toh TH, Solomon PS, Holt RA, McEwan AG (1996). "Dimethylsulfide:acceptor oxidoreductase from Rhodobacter sulfidophilus. The purified enzyme contains b-type haem and a pterin molybdenum cofactor." Eur J Biochem 239(2);391-6. PMID: 8706745

McDevitt02: McDevitt CA, Hugenholtz P, Hanson GR, McEwan AG (2002). "Molecular analysis of dimethyl sulphide dehydrogenase from Rhodovulum sulfidophilum: its place in the dimethyl sulphoxide reductase family of microbial molybdopterin-containing enzymes." Mol Microbiol 44(6);1575-87. PMID: 12067345

Park06a: Park YJ, Yoo CB, Choi SY, Lee HB (2006). "Purifications and characterizations of a ferredoxin and its related 2-oxoacid:ferredoxin oxidoreductase from the hyperthermophilic archaeon, Sulfolobus solfataricus P1." J Biochem Mol Biol 39(1);46-54. PMID: 16466637

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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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