1.8.5.6: sulfite dehydrogenase (quinone)
This is an abbreviated version!
For detailed information about sulfite dehydrogenase (quinone), go to the full flat file.
Word Map on EC 1.8.5.6
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1.8.5.6
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sulfur
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sulfur-oxidizing
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phototrophic
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sulfide
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arsenite
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chlorobaculum
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polysulfide
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tepidum
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lake
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dissimilatory
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soxcd
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sulfite-oxidizing
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chlorobium
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thiosulfate
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heterodisulfide
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chemolithoautotrophic
- 1.8.5.6
- sulfur
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sulfur-oxidizing
-
phototrophic
- sulfide
- arsenite
- chlorobaculum
- polysulfide
- tepidum
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lake
-
dissimilatory
- soxcd
-
sulfite-oxidizing
- chlorobium
- thiosulfate
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heterodisulfide
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chemolithoautotrophic
Reaction
Synonyms
Alvin_2489, Alvin_2490, Alvin_2491, CT0876, quinone-reducing molybdenum sulfite dehydrogenase, soeAB, SoeABC, SreABC, sulfur reductase
ECTree
1.8.5.6 sulfite dehydrogenase (quinone)Advanced search results
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General Information on EC 1.8.5.6 - sulfite dehydrogenase (quinone)
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
O67280; O67279; O67278
phylogenetic tree of Mo-bisPGD enzymes involved in sulfur compounds conversion, phylogenetic analysis, overview
metabolism
O67280; O67279; O67278
SoeABC is involved in the sulfite oxidation in the marine hyperthermophilic bacterium Aquifex aeolicus
physiological function
additional information
physiological function
a mutant in which the region between genes CT0868 and CT0876 is replaced by a transposon insertion resulting in the truncation or deletion of nine genes including a quinone-interacting membrane-bound oxidoreductase (Qmo) complex (CT0866-0868), hypothetical proteins (CT0869-0875) and sulfide:quinone oxidoreductase is completely defective for growth on thiosulfate as the sole electron donor, but only slightly defective for growth on sulfide or thiosulfate plus sulfide. The strain does not oxidize thiosulfate and also displayes a defect in acetate assimilation under all growth conditions
physiological function
D3RNN8; D3RNN7; D3RNN6
SoeABC is the major sulfite-oxidizing enzyme in Allochromatium vinosum. The periplasmic sulfur substrate-binding protein SoxYZ is needed in parallel to the cytoplasmic enzymes for effective sulfite oxidation. A SoeABC-deficient mutant displays about 17% of wild-type sulifte oxidation. A knockout of both adenosine-5'-phosphosulfate reductase gene aprB and soeA leads to an additive effect with a residual specific rate of sulfite oxidation for whole cells of only 7%
physiological function
O67280; O67279; O67278
electrons generated by sulfite oxidation in the cytoplasm enter the respiratory chain at the level of quinones
physiological function
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SoeABC is the major sulfite-oxidizing enzyme in Allochromatium vinosum. The periplasmic sulfur substrate-binding protein SoxYZ is needed in parallel to the cytoplasmic enzymes for effective sulfite oxidation. A SoeABC-deficient mutant displays about 17% of wild-type sulifte oxidation. A knockout of both adenosine-5'-phosphosulfate reductase gene aprB and soeA leads to an additive effect with a residual specific rate of sulfite oxidation for whole cells of only 7%
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physiological function
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a mutant in which the region between genes CT0868 and CT0876 is replaced by a transposon insertion resulting in the truncation or deletion of nine genes including a quinone-interacting membrane-bound oxidoreductase (Qmo) complex (CT0866-0868), hypothetical proteins (CT0869-0875) and sulfide:quinone oxidoreductase is completely defective for growth on thiosulfate as the sole electron donor, but only slightly defective for growth on sulfide or thiosulfate plus sulfide. The strain does not oxidize thiosulfate and also displayes a defect in acetate assimilation under all growth conditions
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additional information
O67280; O67279; O67278
the SoeABC enzyme is a member of the DMSO-reductase family of molybdenum enzymes, or complex iron-sulfur molybdoenzymes (CISM) family
additional information
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the SoeABC enzyme is a member of the DMSO-reductase family of molybdenum enzymes, or complex iron-sulfur molybdoenzymes (CISM) family
