EC Number   |
General Information |
Reference |
|---|
   1.8.99.B2 | evolution |
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 |
-, 742121 |
| 1.8.99.B2 | 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 |
763962 |
| 1.8.99.B2 | more |
the dissimilatory As(V) reductase of strain PSR-1 shows no tetrathionate reductase activity |
763962 |
| 1.8.99.B2 | more |
the tetrathionate reductase of Salmonella enterica strain 1651 shows no dissimilatory As(V) reductase activity |
-, 763962 |
| 1.8.99.B2 | more |
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 |
764683 |
| 1.8.99.B2 | physiological function |
a thiosulfate metabolizing enzyme is required for the sulfur-grown cells to metabolize the resulting thiosulfate |
-, 742121 |
| 1.8.99.B2 | physiological function |
thiosulfate dehydrogenase plays a significant role in thiosulfate oxidation in the acidophilic, obligately chemolithoautotroph, Acidithiobacillus ferrooxidans |
741675 |
| 1.8.99.B2 | physiological function |
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 |
765056 |
