1.8.99.B2: tetrathionate reductase
This is an abbreviated version!
For detailed information about tetrathionate reductase, go to the full flat file.
Word Map on EC 1.8.99.B2
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1.8.99.B2
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campylobacter
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thiosulfate-oxidizing
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tsdas
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microaerophilic
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octaheme
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oneidensis
- 1.8.99.B2
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campylobacter
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thiosulfate-oxidizing
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tsdas
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microaerophilic
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octaheme
- oneidensis
Reaction
Synonyms
AFE_0042, C8J_0815, CjTsdA, di-heme TsdA, tetrathionate-forming thiosulfate dehydrogenase, tetrathionate-forming TSD, thiosulfate dehydrogenase, thiosulfate:quinone reductase, TQO, TSD, TsdA, ttrA, WsTsdA
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General Information
General Information on EC 1.8.99.B2 - tetrathionate reductase
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evolution
physiological function
additional information
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strain SH might have acquired a unique gene encoding the 44 kDa protein by horizontal transfer, as the protein with a high score and coverage is not found in other Acidithiobacillus thiooxidans genomes
evolution
the enzyme encoded by gene PSR1_00330 belongs to the tetrathionate reductase (TtrA) clade in the DMSO reductase family, phylogenetic analysis. Phylogenetic analysis of gene PSR1_00329 suggested that the encoded TtrB-related proteins does not form a single clade but consists of three distinct clades within the small electron transfer subunits of the DMSO reductase family. The putative psr1_00329-psr1_00330 operon lacked a gene encoding a membrane anchor subunit of tetrathionate reductase (TtrC), but a gene encoding a c-type cytochrome (cyt c) is adjacent to these two genes
evolution
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strain SH might have acquired a unique gene encoding the 44 kDa protein by horizontal transfer, as the protein with a high score and coverage is not found in other Acidithiobacillus thiooxidans genomes
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a thiosulfate metabolizing enzyme is required for the sulfur-grown cells to metabolize the resulting thiosulfate
physiological function
thiosulfate dehydrogenase plays a significant role in thiosulfate oxidation in the acidophilic, obligately chemolithoautotroph, Acidithiobacillus ferrooxidans
physiological function
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thiosulfate dehydrogenases (TsdAs) are bidirectional bacterial di-heme enzymes that catalyze the interconversion of tetrathionate and thiosulfate at measurable rates in both directions, cf. EC 1.8.2.2, thiosulfate dehydrogenase. The active site heme 1 in the enzyme has His/Cys ligation in the ferric and ferrous states. In Campylobacter jejuni, TsdA heme 2 has His/Met ligation. Enzyme CjTsdA allows use of tetrathionate as a terminal respiratory electron sink
physiological function
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a thiosulfate metabolizing enzyme is required for the sulfur-grown cells to metabolize the resulting thiosulfate
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the dissimilatory As(V) reductase of strain PSR-1 shows no tetrathionate reductase activity
additional information
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the tetrathionate reductase of Salmonella enterica strain 1651 shows no dissimilatory As(V) reductase activity
additional information
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TsdA is closely associated with the unprecedented lipoprotein TsdC encoded immediately downstream of tsdA in the same direction of transcription. TsdA from Wolinella succinogenes is a periplasmic diheme cytochrome c with hemes, lacking the 21-aa signal peptide. Two Cys-X-X-Cys-His heme c binding motifs are present in the sequence. The active site heme (heme 1) is characterized by an unusual His/Cys axial ligation in TsdA enzymes
additional information
Salmonella enterica JM1651
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the tetrathionate reductase of Salmonella enterica strain 1651 shows no dissimilatory As(V) reductase activity
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