EC Number | Cloned (Comment) | Organism |
---|---|---|
1.15.1.2 | cloning of the desulfoferrodoxin, encoded adjacent to a gene encoding a type I rubredoxin forming a single transcriptional unit | Desulfovibrio vulgaris |
1.15.1.2 | DNA and amino acid sequence analysis, phylogenetic tree | Archaeoglobus fulgidus |
1.15.1.2 | DNA and amino acid sequence analysis, phylogenetic tree | Treponema pallidum |
1.15.1.2 | DNA and amino acid sequence analysis, phylogenetic tree | Desulfarculus baarsii |
1.15.1.2 | DNA and amino acid sequence analysis, phylogenetic tree | Nanoarchaeum equitans |
1.15.1.2 | DNA and amino acid sequence analysis, phylogenetic tree | Pyrococcus furiosus |
1.15.1.2 | DNA and amino acid sequence analysis, phylogenetic tree | Desulfovibrio desulfuricans |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.15.1.2 | crystal structure analysis of the native and ferricyanide bound wild-type enzyme, PDB ID 1DFX | Desulfovibrio desulfuricans |
1.15.1.2 | crystal structure analysis of the native and Glu unbound wild-type enzyme, PDB ID 1Y07 | Treponema pallidum |
1.15.1.2 | crystal structure analysis of the oxidized and Glu bound wild-type enzyme, PDB ID 2HVB | Pyrococcus horikoshii |
1.15.1.2 | crystal structure analysis of the reduced or the oxidized and Glu bound wild-type enzyme, PDB IDs 1DQI, 1DO6, and 1DQK | Pyrococcus furiosus |
1.15.1.2 | crystal structure analysis of the reduced wild-type enzyme, PDB ID 2AMU | Thermotoga maritima |
1.15.1.2 | crystal structure analysis of the wild-type and E114A mutant enzymes in different oxidation states, PDB IDs 2JI3, 2JI2, 2JI1, and 1VZI | Desulfarculus baarsii |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.15.1.2 | E114A | crystal structure | Desulfarculus baarsii |
1.15.1.2 | E12V | redox properties of the mutant compared to the wild-type enzyme | Archaeoglobus fulgidus |
1.15.1.2 | E47A | redox properties of the mutant compared to the wild-type enzyme | Desulfovibrio vulgaris |
1.15.1.2 | E47A | redox properties of the mutant compared to the wild-type enzyme | Desulfarculus baarsii |
1.15.1.2 | K48A | redox properties of the mutant compared to the wild-type enzyme | Desulfovibrio vulgaris |
1.15.1.2 | K48A | redox properties of the mutant compared to the wild-type enzyme | Treponema pallidum |
1.15.1.2 | K48A | redox properties of the mutant compared to the wild-type enzyme | Desulfarculus baarsii |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.15.1.2 | additional information | - |
additional information | steady-state kinetics | Megalodesulfovibrio gigas |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.15.1.2 | Iron | 1Fe-SOR and 2Fe-SOR, an iron ion is bound at the catalytic site to four histidines and a cysteine that, in its reduced form, reacts with superoxide anion with a diffusion-limited second order rate constant, metal site structure and mechanism, overview | Archaeoglobus fulgidus | |
1.15.1.2 | Iron | 1Fe-SOR, an iron ion is bound at the catalytic site to four histidines and a cysteine that, in its reduced form, reacts with superoxide anion with a diffusion-limited second order rate constant, metal site structure and mechanism, overview | Treponema pallidum | |
1.15.1.2 | Iron | 1Fe-SOR, an iron ion is bound at the catalytic site to four histidines and a cysteine that, in its reduced form, reacts with superoxide anion with a diffusion-limited second order rate constant, metal site structure and mechanism, overview | Thermotoga maritima | |
1.15.1.2 | Iron | 1Fe-SOR, an iron ion is bound at the catalytic site to four histidines and a cysteine that, in its reduced form, reacts with superoxide anion with a diffusion-limited second order rate constant, metal site structure and mechanism, overview | Pyrococcus horikoshii | |
1.15.1.2 | Iron | 1Fe-SOR, an iron ion is bound at the catalytic site to four histidines and a cysteine that, in its reduced form, reacts with superoxide anion with a diffusion-limited second order rate constant. The electrostatic surface close to center II has a positive character, mainly due to the metal ion and to residue Lys 15 of 1Fe-SOR, metal site structure and mechanism, overview | Pyrococcus furiosus | |
1.15.1.2 | Iron | 2Fe-SOR, an iron ion is bound at the catalytic site to four histidines and a cysteine that, in its reduced form, reacts with superoxide anion with a diffusion-limited second order rate constant, metal site structure and mechanism, overview | Desulfarculus baarsii | |
1.15.1.2 | Iron | 2Fe-SOR, an iron ion is bound at the catalytic site to four histidines and a cysteine that, in its reduced form, reacts with superoxide anion with a diffusion-limited second order rate constant, metal site structure and mechanism, overview | Desulfovibrio desulfuricans | |
1.15.1.2 | Iron | an iron ion is bound at the catalytic site to four histidines and a cysteine that, in its reduced form, reacts with superoxide anion with a diffusion-limited second order rate constant, metal site structure and mechanism, overview | Desulfovibrio vulgaris | |
1.15.1.2 | Iron | an iron ion is bound at the catalytic site to four histidines and a cysteine that, in its reduced form, reacts with superoxide anion with a diffusion-limited second order rate constant, metal site structure and mechanism, overview | Megalodesulfovibrio gigas | |
1.15.1.2 | Iron | an iron ion is bound at the catalytic site to four histidines and a cysteine that, in its reduced form, reacts with superoxide anion with a diffusion-limited second order rate constant, metal site structure and mechanism, overview | Nanoarchaeum equitans |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.15.1.2 | reduced rubredoxin + superoxide + 2 H+ | Desulfovibrio vulgaris | - |
rubredoxin + H2O2 | - |
? | |
1.15.1.2 | reduced rubredoxin + superoxide + 2 H+ | Archaeoglobus fulgidus | - |
rubredoxin + H2O2 | - |
? | |
1.15.1.2 | reduced rubredoxin + superoxide + 2 H+ | Megalodesulfovibrio gigas | - |
rubredoxin + H2O2 | - |
? | |
1.15.1.2 | reduced rubredoxin + superoxide + 2 H+ | Treponema pallidum | - |
rubredoxin + H2O2 | - |
? | |
1.15.1.2 | reduced rubredoxin + superoxide + 2 H+ | Desulfarculus baarsii | - |
rubredoxin + H2O2 | - |
? | |
1.15.1.2 | reduced rubredoxin + superoxide + 2 H+ | Nanoarchaeum equitans | - |
rubredoxin + H2O2 | - |
? | |
1.15.1.2 | reduced rubredoxin + superoxide + 2 H+ | Pyrococcus furiosus | - |
rubredoxin + H2O2 | - |
? | |
1.15.1.2 | reduced rubredoxin + superoxide + 2 H+ | Thermotoga maritima | - |
rubredoxin + H2O2 | - |
? | |
1.15.1.2 | reduced rubredoxin + superoxide + 2 H+ | Pyrococcus horikoshii | - |
rubredoxin + H2O2 | - |
? | |
1.15.1.2 | reduced rubredoxin + superoxide + 2 H+ | Desulfovibrio desulfuricans | - |
rubredoxin + H2O2 | - |
? | |
1.15.1.2 | reduced rubredoxin + superoxide + 2 H+ | Pyrococcus horikoshii OT-3 | - |
rubredoxin + H2O2 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.15.1.2 | Archaeoglobus fulgidus | - |
- |
- |
1.15.1.2 | Desulfarculus baarsii | - |
- |
- |
1.15.1.2 | Desulfovibrio desulfuricans | P22076 | - |
- |
1.15.1.2 | Desulfovibrio vulgaris | - |
- |
- |
1.15.1.2 | Megalodesulfovibrio gigas | - |
- |
- |
1.15.1.2 | Nanoarchaeum equitans | - |
- |
- |
1.15.1.2 | Pyrococcus furiosus | P82385 | - |
- |
1.15.1.2 | Pyrococcus horikoshii | O58810 | - |
- |
1.15.1.2 | Pyrococcus horikoshii OT-3 | O58810 | - |
- |
1.15.1.2 | Thermotoga maritima | Q9WZC6 | - |
- |
1.15.1.2 | Treponema pallidum | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.15.1.2 | isolation of center I and II | Megalodesulfovibrio gigas |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
1.15.1.2 | superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin | reaction mechanism, geometry of the catalytic center, oxidative cycle/reductive pathway, overview | Pyrococcus furiosus | |
1.15.1.2 | superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin | reaction mechanism, geometry of the catalytic center, oxidative cycle/reductive pathway, overview | Desulfovibrio desulfuricans | |
1.15.1.2 | superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin | reaction mechanism, oxidative cycle/reductive pathway, overview | Desulfovibrio vulgaris | |
1.15.1.2 | superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin | reaction mechanism, oxidative cycle/reductive pathway, overview | Archaeoglobus fulgidus | |
1.15.1.2 | superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin | reaction mechanism, oxidative cycle/reductive pathway, overview | Megalodesulfovibrio gigas | |
1.15.1.2 | superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin | reaction mechanism, oxidative cycle/reductive pathway, overview | Treponema pallidum | |
1.15.1.2 | superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin | reaction mechanism, oxidative cycle/reductive pathway, overview | Desulfarculus baarsii | |
1.15.1.2 | superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin | reaction mechanism, oxidative cycle/reductive pathway, overview | Nanoarchaeum equitans | |
1.15.1.2 | superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin | reaction mechanism, oxidative cycle/reductive pathway, overview | Thermotoga maritima | |
1.15.1.2 | superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin | reaction mechanism, oxidative cycle/reductive pathway, overview | Pyrococcus horikoshii |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.15.1.2 | additional information | redox properties of SOR's catalytic center, overview | Archaeoglobus fulgidus | ? | - |
? | |
1.15.1.2 | additional information | redox properties of SOR's catalytic center, overview | Megalodesulfovibrio gigas | ? | - |
? | |
1.15.1.2 | additional information | redox properties of SOR's catalytic center, overview | Treponema pallidum | ? | - |
? | |
1.15.1.2 | additional information | redox properties of SOR's catalytic center, overview | Desulfarculus baarsii | ? | - |
? | |
1.15.1.2 | additional information | redox properties of SOR's catalytic center, overview | Nanoarchaeum equitans | ? | - |
? | |
1.15.1.2 | additional information | redox properties of SOR's catalytic center, overview | Desulfovibrio desulfuricans | ? | - |
? | |
1.15.1.2 | reduced rubredoxin + superoxide + 2 H+ | - |
Desulfovibrio vulgaris | rubredoxin + H2O2 | - |
? | |
1.15.1.2 | reduced rubredoxin + superoxide + 2 H+ | - |
Archaeoglobus fulgidus | rubredoxin + H2O2 | - |
? | |
1.15.1.2 | reduced rubredoxin + superoxide + 2 H+ | - |
Megalodesulfovibrio gigas | rubredoxin + H2O2 | - |
? | |
1.15.1.2 | reduced rubredoxin + superoxide + 2 H+ | - |
Treponema pallidum | rubredoxin + H2O2 | - |
? | |
1.15.1.2 | reduced rubredoxin + superoxide + 2 H+ | - |
Desulfarculus baarsii | rubredoxin + H2O2 | - |
? | |
1.15.1.2 | reduced rubredoxin + superoxide + 2 H+ | - |
Nanoarchaeum equitans | rubredoxin + H2O2 | - |
? | |
1.15.1.2 | reduced rubredoxin + superoxide + 2 H+ | - |
Pyrococcus furiosus | rubredoxin + H2O2 | - |
? | |
1.15.1.2 | reduced rubredoxin + superoxide + 2 H+ | - |
Thermotoga maritima | rubredoxin + H2O2 | - |
? | |
1.15.1.2 | reduced rubredoxin + superoxide + 2 H+ | - |
Pyrococcus horikoshii | rubredoxin + H2O2 | - |
? | |
1.15.1.2 | reduced rubredoxin + superoxide + 2 H+ | - |
Desulfovibrio desulfuricans | rubredoxin + H2O2 | - |
? | |
1.15.1.2 | reduced rubredoxin + superoxide + 2 H+ | - |
Pyrococcus horikoshii OT-3 | rubredoxin + H2O2 | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.15.1.2 | homodimer | - |
Desulfarculus baarsii |
1.15.1.2 | homodimer | the 1Fe-SOR from Treponema pallidum, which has an extra N-terminal domain reminiscent of those from 2Fe-SORs, is a homodimer | Treponema pallidum |
1.15.1.2 | homodimer | three-dimensional structure of SOR, overview | Desulfovibrio desulfuricans |
1.15.1.2 | homotetramer | - |
Archaeoglobus fulgidus |
1.15.1.2 | homotetramer | - |
Nanoarchaeum equitans |
1.15.1.2 | homotetramer | - |
Thermotoga maritima |
1.15.1.2 | homotetramer | - |
Pyrococcus horikoshii |
1.15.1.2 | homotetramer | 1Fe-SOR | Pyrococcus furiosus |
1.15.1.2 | More | three-dimensional structure of the neelaredoxin, overview | Pyrococcus furiosus |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.15.1.2 | 1Fe-SOR | - |
Archaeoglobus fulgidus |
1.15.1.2 | 1Fe-SOR | - |
Treponema pallidum |
1.15.1.2 | 1Fe-SOR | - |
Pyrococcus furiosus |
1.15.1.2 | 1Fe-SOR | - |
Thermotoga maritima |
1.15.1.2 | 1Fe-SOR | - |
Pyrococcus horikoshii |
1.15.1.2 | 2Fe-SOR | - |
Archaeoglobus fulgidus |
1.15.1.2 | 2Fe-SOR | - |
Desulfarculus baarsii |
1.15.1.2 | 2Fe-SOR | - |
Desulfovibrio desulfuricans |
1.15.1.2 | Dfx | - |
Desulfovibrio desulfuricans |
1.15.1.2 | neelaredoxin | - |
Pyrococcus furiosus |
1.15.1.2 | SOR | - |
Desulfovibrio vulgaris |
1.15.1.2 | SOR | - |
Archaeoglobus fulgidus |
1.15.1.2 | SOR | - |
Megalodesulfovibrio gigas |
1.15.1.2 | SOR | - |
Treponema pallidum |
1.15.1.2 | SOR | - |
Desulfarculus baarsii |
1.15.1.2 | SOR | - |
Nanoarchaeum equitans |
1.15.1.2 | SOR | - |
Pyrococcus furiosus |
1.15.1.2 | SOR | - |
Thermotoga maritima |
1.15.1.2 | SOR | - |
Pyrococcus horikoshii |
1.15.1.2 | SOR | - |
Desulfovibrio desulfuricans |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.15.1.2 | additional information | structure of the neelaredoxin center, oxidized and reduced forms, overview | Pyrococcus furiosus | |
1.15.1.2 | additional information | the enzyme contains two iron sites: center I, similar to that of desulforedoxin, a small iron protein having a rubredoxin-like FeCys4 center, and center II, another type of iron site, which is named desulfoferrodoxin, Dfx, or rubredoxin. Structure of the FeCys4 center I, oxidized and reduced forms. overview | Desulfovibrio vulgaris | |
1.15.1.2 | additional information | the enzyme contains two iron sites: center I, similar to that of desulforedoxin, a small iron protein having a rubredoxin-like FeCys4 center, and center II, another type of iron site, which is named desulfoferrodoxin, Dfx, or rubredoxin. Structure of the FeCys4 center I, oxidized and reduced forms. overview | Megalodesulfovibrio gigas | |
1.15.1.2 | additional information | the enzyme contains two iron sites: center I, similar to that of desulforedoxin, a small iron protein having a rubredoxin-like FeCys4 center, and center II, another type of iron site, which is named desulfoferrodoxin, Dfx, or rubredoxin. Structure of the FeCys4 center I, oxidized and reduced forms. overview | Desulfovibrio desulfuricans |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.15.1.2 | physiological function | SOR is responsible for reductive elimination of toxic superoxide as part of the detoxifying system | Desulfovibrio vulgaris |
1.15.1.2 | physiological function | SOR is responsible for reductive elimination of toxic superoxide as part of the detoxifying system | Megalodesulfovibrio gigas |
1.15.1.2 | physiological function | SOR is responsible for reductive elimination of toxic superoxide as part of the detoxifying system | Treponema pallidum |
1.15.1.2 | physiological function | SOR is responsible for reductive elimination of toxic superoxide as part of the detoxifying system | Desulfarculus baarsii |
1.15.1.2 | physiological function | SOR is responsible for reductive elimination of toxic superoxide as part of the detoxifying system | Nanoarchaeum equitans |
1.15.1.2 | physiological function | SOR is responsible for reductive elimination of toxic superoxide as part of the detoxifying system | Pyrococcus furiosus |
1.15.1.2 | physiological function | SOR is responsible for reductive elimination of toxic superoxide as part of the detoxifying system | Thermotoga maritima |
1.15.1.2 | physiological function | SOR is responsible for reductive elimination of toxic superoxide as part of the detoxifying system | Pyrococcus horikoshii |
1.15.1.2 | physiological function | SOR is responsible for reductive elimination of toxic superoxide as part of the detoxifying system | Desulfovibrio desulfuricans |
1.15.1.2 | physiological function | SOR is responsible for reductive eliminatioon of toxic superoxide as part of the detoxifying system | Archaeoglobus fulgidus |