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Information on EC 1.8.99.B2 - tetrathionate reductase
for references in articles please use BRENDA:EC1.8.99.B2preliminary BRENDA-supplied EC number
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EC Tree
1.8.99.B2 tetrathionate reductaseSpecify your search results
Word Map
- 1.8.99.B2
-
campylobacter
-
thiosulfate-oxidizing
-
tsdas
-
microaerophilic
-
octaheme
- oneidensis
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
a reduced electron acceptor
=
2
+
an oxidized electron acceptor
Synonyms
tetrathionate reductase, wstsda, thiosulfate:quinone reductase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C8J_0815
tetrathionate-forming TSD
thiosulfate dehydrogenase
thiosulfate:quinone reductase
TQO
TSD
TsdA
ttrA
TsdA
-
bifunctional tetrathionate reductase/thiosulfate dehydrogenase
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
tetrathionate + a reduced electron acceptor = 2 thiosulfate + an oxidized electron acceptor
-
-
-
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 thiosulfate + ferricyanide
tetrathionate + ferrocyanide
-
-
-
?
2 thiosulfate + ferricyanide
tetrathionate + ferrocyanide
-
-
-
-
?
2 thiosulfate + ferricyanide
tetrathionate + ferrocyanide
-
artificial electron acceptor
-
-
?
2 thiosulfate + ferricyanide
tetrathionate + ferrocyanide
-
-
-
-
?
2 thiosulfate + ferricyanide
tetrathionate + ferrocyanide
-
artificial electron acceptor
-
-
?
2 thiosulfate + ubiquinone
tetrathionate + ubiquinol
-
-
-
-
?
tetrathionate + a reduced electron acceptor
2 thiosulfate + an oxidized electron acceptor
-
-
-
-
?
tetrathionate + a reduced electron acceptor
2 thiosulfate + an oxidized electron acceptor
-
bifunctional tetrathionate reductase/thiosulphate dehydrogenase
-
-
?
tetrathionate + a reduced electron acceptor
2 thiosulfate + an oxidized electron acceptor
-
-
-
-
?
tetrathionate + a reduced electron acceptor
2 thiosulfate + an oxidized electron acceptor
-
bifunctional tetrathionate reductase/thiosulphate dehydrogenase
-
-
?
tetrathionate + reduced electron acceptor
2 thiosulfate + oxidized electron acceptor
-
-
-
?
tetrathionate + reduced electron acceptor
2 thiosulfate + oxidized electron acceptor
-
-
-
-
r
tetrathionate + reduced electron acceptor
2 thiosulfate + oxidized electron acceptor
-
for CjTsdA the maximum rate of tetrathionate reduction is approximately twice that of thiosulfate oxidation
-
-
r
tetrathionate + reduced electron acceptor
2 thiosulfate + oxidized electron acceptor
-
-
-
-
?
tetrathionate + reduced electron acceptor
2 thiosulfate + oxidized electron acceptor
Salmonella enterica JM1651
-
-
-
-
?
tetrathionate + reduced electron acceptor
2 thiosulfate + oxidized electron acceptor
-
-
-
-
?
tetrathionate + reduced methyl viologen
2 thiosulfate + oxidized methyl viologen
-
-
-
?
tetrathionate + reduced methyl viologen
2 thiosulfate + oxidized methyl viologen
-
-
-
-
?
tetrathionate + reduced methyl viologen
2 thiosulfate + oxidized methyl viologen
Salmonella enterica JM1651
-
-
-
-
?
tetrathionate + reduced methyl viologen
2 thiosulfate + oxidized methyl viologen
-
-
-
-
r
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
the activity does not couple with mammalian cytochrome c as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
ferricyanide acts as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
the activity does not couple with mammalian cytochrome c as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
ferricyanide acts as electron acceptor
-
?
additional information
?
-
nonenzymatic reduction of ferricyanide is observed with thiosulfate
-
-
?
additional information
?
-
-
no activity with cytochrome c
-
-
?
additional information
?
-
-
tetrathionate is the product of the TSD-oxidized thiosulfate, and ferricyanide or ubiquinone are the electron acceptors
-
-
?
additional information
?
-
-
no activity with cytochrome c
-
-
?
additional information
?
-
-
tetrathionate is the product of the TSD-oxidized thiosulfate, and ferricyanide or ubiquinone are the electron acceptors
-
-
?
additional information
?
-
-
the enzyme functions as a tetrathionate reductase and a thiosulfate oxidase, respectively
-
-
-
additional information
?
-
-
the TsdAC complex predominantly acts as a tetrathionate reductase in vivo
-
-
-
additional information
?
-
-
recombinant WsTsdA purified from Escherichia coli catalyzes both thiosulfate oxidation and tetrathionate reduction. Activity measurement by performing thiosulfate-dependent ferricyanide reduction
-
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
the TsdAC complex predominantly acts as a tetrathionate reductase in vivo
-
-
-
2 thiosulfate + ubiquinone
tetrathionate + ubiquinol
-
-
-
-
?
tetrathionate + a reduced electron acceptor
2 thiosulfate + an oxidized electron acceptor
-
-
-
-
?
tetrathionate + a reduced electron acceptor
2 thiosulfate + an oxidized electron acceptor
-
-
-
-
?
tetrathionate + reduced electron acceptor
2 thiosulfate + oxidized electron acceptor
-
-
-
?
tetrathionate + reduced electron acceptor
2 thiosulfate + oxidized electron acceptor
-
-
-
-
r
tetrathionate + reduced electron acceptor
2 thiosulfate + oxidized electron acceptor
-
-
-
-
?
tetrathionate + reduced electron acceptor
2 thiosulfate + oxidized electron acceptor
Salmonella enterica JM1651
-
-
-
-
?
tetrathionate + reduced electron acceptor
2 thiosulfate + oxidized electron acceptor
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
heme
-
sequence shows two Cys-X2-Cys-His heme c-binding motifs, bifunctional tetrathionate reductase/thiosulphate dehydrogenase
heme
-
the enzyme TSdA is a periplasmic diheme cytochrome c with hemes. 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
heme
-
two hemes, heme 1 and heme 2. Distal ligation of CjTsdA Heme 2 is provided by Asn254 and Met255
additional information
-
absence of heme groups in the protein
-
additional information
-
no activity with cytochrome c from horse heart
-
additional information
no heme is detected. Ubiquinone and cytochrome C are no cofactors
-
additional information
-
the enzyme contains no c-type heme molecule
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
KCl
MgCl2
Na2SO4
150 mM Na-sulfate is required to generate maximum activity, 60% inhibition at 200 mM
NaCl
sulfite
activates 1.6fold at 2 mM, higher concentration of sulfite ions results in inhibition of the enzyme, and almost complete inhibition at 10 mM sulfite
additional information
-
no stimulation of the enzyme by Na2SO4 at at 100 mM
KCl
-
200 mM, presence of 200 mM NaCl, 86% of the activity in presence of 200 mM NaCl
MgCl2
-
200 mM, presence of 200 mM NaCl, 68% of the activity in presence of 200 mM NaCl
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Na+
-
inhibitory at high concentration above 200 mM; inihibits at high concentrations
Sodium sulfate
-
100 mM, presence of 200 mM NaCl, 57% residual activity
sodium sulfite
-
0.1 mM, presence of 200 mM NaCl, 45% residual activity
2-heptyl-4-hydroxy-quinoline N-oxide
-
1 microM, presence of 200 mM NaCl, 12% residual activity
2-heptyl-4-hydroxyquinoline N-oxide
-
88% inhibition at 0.001 mM
N-ethylmaleimide
-
1 mM, presence of 200 mM NaCl, 84% residual activity
Na2SO4
150 mM Na-sulfate is required to generate maximum activity, 60% inhibition at 200 mM
sulfite
activates 1.6fold at 2 mM, higher concentration of sulfite ions results in inhibition of the enzyme, and almost complete inhibition at 10 mM sulfite
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TsdC
-
a unique membrane-associated lipoprotein from Wolinella succinogenes, enhances tetrathionate reductase activity of enzyme TsdA. This effect is much stronger in the tetrathionate-reducing than in the thiosulfate-oxidizing direction. The TsdAC complex predominantly acts as a tetrathionate reductase in vivo
-
additional information
cofactors might be required for the sulfate-dependent enzyme activation dissociated from the enzyme complex during purification
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Coinfection
Interactions between the tropical sea anemone Aiptasia pallida and Serratia marcescens, an opportunistic pathogen of corals.
Coinfection
The Contribution of Eimeria Coinfection and Intestinal Inflammation to Cecal Colonization and Systemic Spread of Salmonella Typhimurium Deficient in Tetrathionate Reductase or Type III Secretion Systems Salmonella Pathogenicity Island 1 or 2.
Infections
Interactions between the tropical sea anemone Aiptasia pallida and Serratia marcescens, an opportunistic pathogen of corals.
Typhoid Fever
[On the presence or absence of tetrathionate reductase in a collection of typhoid bacilli of various origins. Possible epidemiological importance of the study of this enzyme]
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
26
-
crude extracts of strain JCM1651 grown on tetrathionate, pH 6.8, 30°C
47
-
recombinant membranes from the Escherichia coli strain producing the WsTsdAC, pH 5.5, 39°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
enzyme activity measured using ferricyanide as the electron acceptor is detected in cell extracts of Astrain ATCC 23270 grown on tetrathionate or sulfur, but no activity is detected in ferrous iron-grown cells
brenda
additional information
-
NaCl at an optimum concentration of 0.35 M stimulates the growth of strain SH on elemental sulfur, while LiCl and KCl cannot sustain the growth of strain SH
brenda
-
NaCl at an optimum concentration of 0.35 M stimulates the growth of strain SH on elemental sulfur, while LiCl and KCl cannot sustain the growth of strain SH
-
brenda
additional information
-
NaCl at an optimum concentration of 0.35 M stimulated the growth of strain SH on elemental sulfur, while LiCl and KCl cannot sustain the growth
brenda
additional information
-
NaCl at an optimum concentration of 0.35 M stimulated the growth of strain SH on elemental sulfur, while LiCl and KCl cannot sustain the growth
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
TsdC from Wolinella succinogenes mediates membrane attachment of TsdA
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
additional information
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
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
-
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
-
physiological function
-
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
-
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
-
a thiosulfate metabolizing enzyme is required for the sulfur-grown cells to metabolize the resulting thiosulfate
-
additional information
the dissimilatory As(V) reductase of strain PSR-1 shows no tetrathionate reductase activity
additional information
-
the tetrathionate reductase of Salmonella enterica strain 1651 shows no dissimilatory As(V) reductase activity
additional information
-
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
-
the tetrathionate reductase of Salmonella enterica strain 1651 shows no dissimilatory As(V) reductase activity
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). B7J3E3_ACIF2
Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455)
270
0
29455
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
monomer
additional information
-
the tsdA-like gene from Wolinella succinogenes encodes 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
?
-
x * 37103, mature protein with two c-hemes, without the signal peptide, and with an N-terminal Strep II-tag preceded by three amino acids and followed by four amino acids, sequence calculation
dimer
-
2 * 40028, TsdA diheme cytochrome c with hemes, lacking the 21-aa signal peptide, sequence calculation
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C138H
-
site-directed mutagenesis, spectroscopic and electrochemical mutant characterization
C138M
-
site-directed mutagenesis, spectroscopic and electrochemical mutant characterization
N254K
-
site-directed mutagenesis, spectroscopic and electrochemical mutant characterization
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
71fold enrichment with a recovery of 4.3% of the total activity
-
native enzyme 71.4fold from the membrane fraction of strain SH by solubilization with n-dodecyl-beta-D-maltopyranoside, ultracentrifugation, anion exchange chromatography, dialysis, ultrafiltration, and gel filtration
-
native enzyme 71.4fold from the solubilized membrane fraction by ultracentrifugation, anion exchange chromatography, dialysis, and ultrafiltration
-
native periplasmic enzyme from strain ATCC 23270 and recombinant enzyme from Escherichia coli strain BL21(DE3) celll extract by ammonium sulfate fractionation, cation exchange chromatography, dialysis, hydrophobic interaction chromatography, ultrafilatration, and gel filtration
recombinant Strep-tagged enzyme TsdA 41fold from Escherichia coli strains BL21(DE3) and C43(DE3) by membrane solubilization, affinity chromatography, desalting gel filtration, and ultrafiltration recombinant Strep-tagged TsdC by two steps of ultracentrifugation at 100000 x g, followed by affinity chromatography
-
using chromatography on Phenyl-Sepharose column, CM-cellulose column and hydroxylapatite column
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene tsdA, recombinant expression of Strep-tagged enzyme in Escherichia coli strains BL21(DE3) and C43(DE3), coexpression with Strep-tagged Wolinella succinogenes TsdC
-
genes PSR1_00330 /ttrA and PSR1_003329/ttrB, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis. The putative psr1_00329-psr1_00330 operon lacks 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. RT-PCR enzyme expression analysis
recombinant enzyme expression in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha
recombinant expression of wild-type and mutant Strep II-tagged enzymes
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information