Cloned (Comment) | Organism |
---|---|
expression of class I Dfx, phylogenetic analysis | Methanothermobacter thermautotrophicus |
expression of class I Dfx, phylogenetic analysis | Desulfarculus baarsii |
expression of class II Nlr and of class I Dfx, phylogenetic analysis | Archaeoglobus fulgidus |
expression of class II Nlr, phylogenetic analysis | Pyrococcus furiosus |
expression of class II Nlr, phylogenetic analysis | Thermotoga maritima |
expression of class III enzyme in Escherichia coli, phylogenetic analysis | Treponema pallidum |
gene dsr, expression of class II Nlr in Escherichia coli, phylogenetic analysis | Megalodesulfovibrio gigas |
gene rbo, expression of class I Dfx, phylogenetic analysis | Desulfovibrio vulgaris |
phylogenetic analysis | Desulfovibrio desulfuricans |
Crystallization (Comment) | Organism |
---|---|
crystallization of the native enzyme, X-ray diffraction structure determination and analysis at 1.9 A resolution, modelling | Desulfovibrio desulfuricans |
crystallization of the recombinant and the native enzyme | Pyrococcus furiosus |
crystallization of the recombinant enzyme | Treponema pallidum |
crystallization of the recombinant enzyme | Desulfarculus baarsii |
crystallization of the recombinant enzyme | Thermotoga maritima |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | at the dimer interface coordinated by eight oxygen atoms, Ser87, Thr89 from both monomers, and two water molecules | Desulfovibrio desulfuricans | |
Fe2+ | the class I enzyme contains two iron-centers, binding structure, overview | Methanothermobacter thermautotrophicus | |
Fe2+ | the class I enzyme contains two iron-centers, binding structure, overview | Desulfarculus baarsii | |
Fe2+ | the class I enzyme contains two iron-centers, binding structure, overview | Desulfovibrio vulgaris | |
Fe2+ | the class I enzyme contains two iron-centers, i.e. two iron atoms per subunit, binding structure, overview | Desulfovibrio desulfuricans | |
Fe2+ | the class I enzyme contains two iron-centers, while the class II enzyme contains one iron-center, binding structure, overview | Archaeoglobus fulgidus | |
Fe2+ | the class II enzyme contains one iron-center, binding structure, overview | Megalodesulfovibrio gigas | |
Fe2+ | the class II enzyme contains one iron-center, binding structure, overview | Thermotoga maritima | |
Fe2+ | the class II enzyme contains one iron-center, iron ligands Glu14, His47 and His114 in addition to adjacent residues Trp11, Ile39, Pro40, Pro42, Thr44 and Ile113, binding structure, overview | Pyrococcus furiosus | |
Fe2+ | the class III enzyme contains one iron-center, a homodimer containing a sole iron site per monomer, binding structure, overview | Treponema pallidum |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
14000 | - |
2 * 14000 | Desulfovibrio desulfuricans |
14000 | - |
2 * 14000, a homodimer | Treponema pallidum |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
reduced rubredoxin + superoxide + H+ | Methanothermobacter thermautotrophicus | - |
rubredoxin + H2O2 | - |
? | |
reduced rubredoxin + superoxide + H+ | Desulfovibrio desulfuricans | - |
rubredoxin + H2O2 | - |
? | |
reduced rubredoxin + superoxide + H+ | Megalodesulfovibrio gigas | - |
rubredoxin + H2O2 | - |
? | |
reduced rubredoxin + superoxide + H+ | Treponema pallidum | - |
rubredoxin + H2O2 | - |
? | |
reduced rubredoxin + superoxide + H+ | Pyrococcus furiosus | - |
rubredoxin + H2O2 | - |
? | |
reduced rubredoxin + superoxide + H+ | Archaeoglobus fulgidus | - |
rubredoxin + H2O2 | - |
? | |
reduced rubredoxin + superoxide + H+ | Desulfarculus baarsii | - |
rubredoxin + H2O2 | - |
? | |
reduced rubredoxin + superoxide + H+ | Desulfovibrio vulgaris | - |
rubredoxin + H2O2 | - |
? | |
reduced rubredoxin + superoxide + H+ | Thermotoga maritima | - |
rubredoxin + H2O2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Archaeoglobus fulgidus | O29903 | - |
- |
Desulfarculus baarsii | Q46495 | - |
- |
Desulfovibrio desulfuricans | - |
strain ATCC 27774 | - |
Desulfovibrio vulgaris | P20418 | var. Hildenborough, gene rbo | - |
Megalodesulfovibrio gigas | - |
gene dsr | - |
Methanothermobacter thermautotrophicus | - |
- |
- |
Pyrococcus furiosus | P82385 | - |
- |
Thermotoga maritima | Q9WZC6 | - |
- |
Treponema pallidum | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin | enzyme active site structure and mechanism | Methanothermobacter thermautotrophicus | |
superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin | enzyme active site structure and mechanism | Desulfovibrio desulfuricans | |
superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin | enzyme active site structure and mechanism | Megalodesulfovibrio gigas | |
superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin | enzyme active site structure and mechanism | Treponema pallidum | |
superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin | enzyme active site structure and mechanism | Pyrococcus furiosus | |
superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin | enzyme active site structure and mechanism | Archaeoglobus fulgidus | |
superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin | enzyme active site structure and mechanism | Desulfarculus baarsii | |
superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin | enzyme active site structure and mechanism | Desulfovibrio vulgaris | |
superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin | enzyme active site structure and mechanism | Thermotoga maritima |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | structure-function relationship, overview | Methanothermobacter thermautotrophicus | ? | - |
? | |
additional information | structure-function relationship, overview | Desulfovibrio desulfuricans | ? | - |
? | |
additional information | structure-function relationship, overview | Megalodesulfovibrio gigas | ? | - |
? | |
additional information | structure-function relationship, overview | Treponema pallidum | ? | - |
? | |
additional information | structure-function relationship, overview | Pyrococcus furiosus | ? | - |
? | |
additional information | structure-function relationship, overview | Archaeoglobus fulgidus | ? | - |
? | |
additional information | structure-function relationship, overview | Desulfarculus baarsii | ? | - |
? | |
additional information | structure-function relationship, overview | Desulfovibrio vulgaris | ? | - |
? | |
additional information | structure-function relationship, overview | Thermotoga maritima | ? | - |
? | |
reduced rubredoxin + superoxide + H+ | - |
Methanothermobacter thermautotrophicus | rubredoxin + H2O2 | - |
? | |
reduced rubredoxin + superoxide + H+ | - |
Desulfovibrio desulfuricans | rubredoxin + H2O2 | - |
? | |
reduced rubredoxin + superoxide + H+ | - |
Megalodesulfovibrio gigas | rubredoxin + H2O2 | - |
? | |
reduced rubredoxin + superoxide + H+ | - |
Treponema pallidum | rubredoxin + H2O2 | - |
? | |
reduced rubredoxin + superoxide + H+ | - |
Pyrococcus furiosus | rubredoxin + H2O2 | - |
? | |
reduced rubredoxin + superoxide + H+ | - |
Archaeoglobus fulgidus | rubredoxin + H2O2 | - |
? | |
reduced rubredoxin + superoxide + H+ | - |
Desulfarculus baarsii | rubredoxin + H2O2 | - |
? | |
reduced rubredoxin + superoxide + H+ | - |
Desulfovibrio vulgaris | rubredoxin + H2O2 | - |
? | |
reduced rubredoxin + superoxide + H+ | - |
Thermotoga maritima | rubredoxin + H2O2 | - |
? | |
reduced rubredoxin + superoxide + H+ | functionally important residues are Glu14, Lys15, His16, His41, His51, His118, Ile49, and Cys111, mechanistic aspects of biological superoxide anion reduction, overview | Pyrococcus furiosus | rubredoxin + H2O2 | - |
? | |
reduced rubredoxin + superoxide + H+ | functionally important residues are Glu15, Lys16, His17, His45, His51, His118, Ile53, and Cys115, mechanistic aspects of biological superoxide anion reduction, overview | Thermotoga maritima | rubredoxin + H2O2 | - |
? | |
reduced rubredoxin + superoxide + H+ | functionally important residues are Glu46, Lys47, His48, His68, His74, His118, Ile76, and Cys115, mechanistic aspects of biological superoxide anion reduction, overview | Desulfovibrio desulfuricans | rubredoxin + H2O2 | - |
? | |
reduced rubredoxin + superoxide + H+ | functionally important residues are Glu47, Lys48, His49, His69, His75, His119, Ile77, and Cys116, mechanistic aspects of biological superoxide anion reduction, overview | Desulfarculus baarsii | rubredoxin + H2O2 | - |
? | |
reduced rubredoxin + superoxide + H+ | functionally important residues are Glu47, Lys48, His49, His69, His75, His119, Ile77, and Cys116, mechanistic aspects of biological superoxide anion reduction, overview | Desulfovibrio vulgaris | rubredoxin + H2O2 | - |
? | |
reduced rubredoxin + superoxide + H+ | functionally important residues are Glu48, Lys49, His50, His70, His76, His122, Ile78, and Cys119, mechanistic aspects of biological superoxide anion reduction, overview | Treponema pallidum | rubredoxin + H2O2 | - |
? | |
reduced rubredoxin + superoxide + H+ | mechanistic aspects of biological superoxide anion reduction, overview | Methanothermobacter thermautotrophicus | rubredoxin + H2O2 | - |
? | |
reduced rubredoxin + superoxide + H+ | mechanistic aspects of biological superoxide anion reduction, overview | Megalodesulfovibrio gigas | rubredoxin + H2O2 | - |
? | |
reduced rubredoxin + superoxide + H+ | mechanistic aspects of biological superoxide anion reduction, overview | Archaeoglobus fulgidus | rubredoxin + H2O2 | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | 2 * 14000 | Desulfovibrio desulfuricans |
dimer | 2 * 14000, a homodimer | Treponema pallidum |
More | structure-function relationship, overview | Methanothermobacter thermautotrophicus |
More | structure-function relationship, overview | Desulfovibrio desulfuricans |
More | structure-function relationship, overview | Treponema pallidum |
More | structure-function relationship, overview | Archaeoglobus fulgidus |
More | structure-function relationship, overview | Desulfarculus baarsii |
More | structure-function relationship, overview | Desulfovibrio vulgaris |
More | structure-function relationship, overview | Thermotoga maritima |
More | primary structure, structure-function relationship, overview | Megalodesulfovibrio gigas |
More | primary structure, structure-function relationship, overview | Pyrococcus furiosus |
Synonyms | Comment | Organism |
---|---|---|
desulfoferrodoxin | - |
Desulfovibrio desulfuricans |
desulfoferrodoxin | - |
Archaeoglobus fulgidus |
desulfoferrodoxin | - |
Desulfarculus baarsii |
desulfoferrodoxin | - |
Desulfovibrio vulgaris |
Dfx | - |
Desulfovibrio desulfuricans |
Dfx | - |
Archaeoglobus fulgidus |
Dfx | - |
Desulfarculus baarsii |
Dfx | - |
Desulfovibrio vulgaris |
More | Dfx belongs to the class I of superoxide reductases, while Nlr belongs to the class II superoxide reductases | Archaeoglobus fulgidus |
More | the enzyme belongs to the class I of superoxide reductases | Desulfovibrio desulfuricans |
More | the enzyme belongs to the class I of superoxide reductases | Desulfarculus baarsii |
More | the enzyme belongs to the class I of superoxide reductases | Desulfovibrio vulgaris |
More | the enzyme belongs to the class II of superoxide reductases | Methanothermobacter thermautotrophicus |
More | the enzyme belongs to the class II of superoxide reductases | Megalodesulfovibrio gigas |
More | the enzyme belongs to the class II of superoxide reductases | Pyrococcus furiosus |
More | the enzyme belongs to the class II of superoxide reductases | Thermotoga maritima |
More | the enzyme belongs to the class III of superoxide reductases | Treponema pallidum |
neelaredoxin | - |
Methanothermobacter thermautotrophicus |
neelaredoxin | - |
Megalodesulfovibrio gigas |
neelaredoxin | - |
Treponema pallidum |
neelaredoxin | - |
Pyrococcus furiosus |
neelaredoxin | - |
Archaeoglobus fulgidus |
neelaredoxin | - |
Thermotoga maritima |
Nlr | - |
Methanothermobacter thermautotrophicus |
Nlr | - |
Megalodesulfovibrio gigas |
Nlr | - |
Treponema pallidum |
Nlr | - |
Pyrococcus furiosus |
Nlr | - |
Archaeoglobus fulgidus |
Nlr | - |
Thermotoga maritima |
rubredoxin oxidoreductase | - |
Methanothermobacter thermautotrophicus |
rubredoxin oxidoreductase | - |
Desulfovibrio desulfuricans |
rubredoxin oxidoreductase | - |
Megalodesulfovibrio gigas |
rubredoxin oxidoreductase | - |
Treponema pallidum |
rubredoxin oxidoreductase | - |
Pyrococcus furiosus |
rubredoxin oxidoreductase | - |
Archaeoglobus fulgidus |
rubredoxin oxidoreductase | - |
Desulfarculus baarsii |
rubredoxin oxidoreductase | - |
Desulfovibrio vulgaris |
rubredoxin oxidoreductase | - |
Thermotoga maritima |
SOR | - |
Methanothermobacter thermautotrophicus |
SOR | - |
Desulfovibrio desulfuricans |
SOR | - |
Megalodesulfovibrio gigas |
SOR | - |
Treponema pallidum |
SOR | - |
Pyrococcus furiosus |
SOR | - |
Archaeoglobus fulgidus |
SOR | - |
Desulfarculus baarsii |
SOR | - |
Desulfovibrio vulgaris |
SOR | - |
Thermotoga maritima |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
reduced rubredoxin | - |
Methanothermobacter thermautotrophicus | |
reduced rubredoxin | - |
Desulfovibrio desulfuricans | |
reduced rubredoxin | - |
Megalodesulfovibrio gigas | |
reduced rubredoxin | - |
Treponema pallidum | |
reduced rubredoxin | - |
Archaeoglobus fulgidus | |
reduced rubredoxin | - |
Desulfarculus baarsii | |
reduced rubredoxin | - |
Thermotoga maritima | |
reduced rubredoxin | a potential Rd binding site is located in the vicinity of the solvent-exposed residues that are close to the iron centre | Pyrococcus furiosus | |
reduced rubredoxin | encoded by gene rub | Desulfovibrio vulgaris |