EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.15.1.2 | crystal structure determination at 1.55 A resolution, PDB ID 1Y07 | Treponema pallidum |
1.15.1.2 | crystal structure determination at 1.9 A resolution, PDB ID 1DFX | Desulfovibrio desulfuricans |
1.15.1.2 | crystal structure determination at 2.0 A and 1.1 A resolution, respectively, PDB IDs 2AMU and 3QZB | Thermotoga maritima |
1.15.1.2 | crystal structure determination at 2.0 A and 1.7 A resolution, respectively, PDB IDs 1DO6 and 1DQI | Pyrococcus furiosus |
1.15.1.2 | crystal structure determination at 2.5 A resolution, PDB ID 2HVB | Pyrococcus horikoshii |
1.15.1.2 | crystal structures determination of wild/tzp and mutant enzymes at 1.15-1.95 A resolution, PDB IDs 1VZI, 1VZG, 1VZH, 2JI1, 2JI2, and 2JI3 | Desulfarculus baarsii |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.15.1.2 | E114A | site-directed mutagenesis, crystal structure determination | Desulfarculus baarsii |
1.15.1.2 | E12Q | site-directed mutagenesis | Archaeoglobus fulgidus |
1.15.1.2 | E12V | site-directed mutagenesis | Archaeoglobus fulgidus |
1.15.1.2 | E23A | site-directed mutagenesis | Ignicoccus hospitalis |
1.15.1.2 | E46A | site-directed mutagenesis, crystal structure determination | Desulfarculus baarsii |
1.15.1.2 | E47A | site-directed mutagenesis | Desulfovibrio desulfuricans |
1.15.1.2 | E47A | site-directed mutagenesis | Desulfovibrio vulgaris |
1.15.1.2 | E47A | site-directed mutagenesis, crystal structure determination | Desulfarculus baarsii |
1.15.1.2 | E48A | site-directed mutagenesis | Desulfovibrio desulfuricans |
1.15.1.2 | E48A | site-directed mutagenesis | Desulfovibrio vulgaris |
1.15.1.2 | E48A | site-directed mutagenesis | Treponema pallidum |
1.15.1.2 | K48I | site-directed mutagenesis | Desulfarculus baarsii |
1.15.1.2 | T24K | site-directed mutagenesis | Ignicoccus hospitalis |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.15.1.2 | Fe2+ | catalytic Fe2+ binding residues are H10, H35, H41, C97, and H100. With the exception of the class IV (methanoferrodoxins) and the atypical SORs, they all appear to contain one or two iron centers: the catalytic center plus the desulforedoxin-like and rubredoxin-like, Dx/Rb-like, center | Nanoarchaeum equitans | |
1.15.1.2 | Fe2+ | catalytic Fe2+ binding residues are H14, H40, H46, C110, and H113. With the exception of the class IV (methanoferrodoxins) and the atypical SORs, they all appear to contain one or two iron centers: the catalytic center plus the desulforedoxin-like and rubredoxin-like, Dx/Rb-like, center | Archaeoglobus fulgidus | |
1.15.1.2 | Fe2+ | catalytic Fe2+ binding residues are H16, H41, H47, C111, and H114. With the exception of the class IV (methanoferrodoxins) and the atypical SORs, they all appear to contain one or two iron centers: the catalytic center plus the desulforedoxin-like and rubredoxin-like, Dx/Rb-like, center | Pyrococcus furiosus | |
1.15.1.2 | Fe2+ | catalytic Fe2+ binding residues are H16, H41, H47, C111, and H114. With the exception of the class IV (methanoferrodoxins) and the atypical SORs, they all appear to contain one or two iron centers: the catalytic center plus the desulforedoxin-like and rubredoxin-like, Dx/Rb-like, center | Archaeoglobus fulgidus | |
1.15.1.2 | Fe2+ | catalytic Fe2+ binding residues are H17, H45, H51, C115, and H118. With the exception of the class IV (methanoferrodoxins) and the atypical SORs, they all appear to contain one or two iron centers: the catalytic center plus the desulforedoxin-like and rubredoxin-like, Dx/Rb-like, center | Dosidicus gigas | |
1.15.1.2 | Fe2+ | catalytic Fe2+ binding residues are H17, H45, H51, C115, and H118. With the exception of the class IV (methanoferrodoxins) and the atypical SORs, they all appear to contain one or two iron centers: the catalytic center plus the desulforedoxin-like and rubredoxin-like, Dx/Rb-like, center | Thermotoga maritima | |
1.15.1.2 | Fe2+ | catalytic Fe2+ binding residues are H25, H50, H56, C109, and H112. With the exception of the class IV (methanoferrodoxins) and the atypical SORs, they all appear to contain one or two iron centers: the catalytic center plus the desulforedoxin-like and rubredoxin-like, Dx/Rb-like, center | Ignicoccus hospitalis | |
1.15.1.2 | Fe2+ | catalytic Fe2+ binding residues are H25, H50, H56, C111, and H114. With the exception of the class IV (methanoferrodoxins) and the atypical SORs, they all appear to contain one or two iron centers: the catalytic center plus the desulforedoxin-like and rubredoxin-like, Dx/Rb-like, center | Pyrococcus horikoshii | |
1.15.1.2 | Fe2+ | catalytic Fe2+ binding residues are H49, H69, H74, C115, and H118. With the exception of the class IV (methanoferrodoxins) and the atypical SORs, they all appear to contain one or two iron centers: the catalytic center plus the desulforedoxin-like and rubredoxin-like, Dx/Rb-like, center | Desulfovibrio desulfuricans | |
1.15.1.2 | Fe2+ | catalytic Fe2+ binding residues are H49, H69, H74, C115, and H118. With the exception of the class IV (methanoferrodoxins) and the atypical SORs, they all appear to contain one or two iron centers: the catalytic center plus the desulforedoxin-like and rubredoxin-like, Dx/Rb-like, center | Desulfovibrio vulgaris | |
1.15.1.2 | Fe2+ | catalytic Fe2+ binding residues are H49, H69, H74, C115, and H118. With the exception of the class IV (methanoferrodoxins) and the atypical SORs, they all appear to contain one or two iron centers: the catalytic center plus the desulforedoxin-like and rubredoxin-like, Dx/Rb-like, center | Desulfarculus baarsii | |
1.15.1.2 | Fe2+ | catalytic Fe2+ binding residues are H50, H70, H76, C119, and H122. With the exception of the class IV (methanoferrodoxins) and the atypical SORs, they all appear to contain one or two iron centers: the catalytic center plus the desulforedoxin-like and rubredoxin-like, Dx/Rb-like, center | Treponema pallidum |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.15.1.2 | superoxide + reduced acceptor + 2 H+ | Desulfovibrio desulfuricans | - |
H2O2 + oxidized acceptor | - |
? | |
1.15.1.2 | superoxide + reduced acceptor + 2 H+ | Desulfovibrio vulgaris | - |
H2O2 + oxidized acceptor | - |
? | |
1.15.1.2 | superoxide + reduced acceptor + 2 H+ | Archaeoglobus fulgidus | - |
H2O2 + oxidized acceptor | - |
? | |
1.15.1.2 | superoxide + reduced acceptor + 2 H+ | Dosidicus gigas | - |
H2O2 + oxidized acceptor | - |
? | |
1.15.1.2 | superoxide + reduced acceptor + 2 H+ | Pyrococcus furiosus | - |
H2O2 + oxidized acceptor | - |
? | |
1.15.1.2 | superoxide + reduced acceptor + 2 H+ | Desulfarculus baarsii | - |
H2O2 + oxidized acceptor | - |
? | |
1.15.1.2 | superoxide + reduced acceptor + 2 H+ | Thermotoga maritima | - |
H2O2 + oxidized acceptor | - |
? | |
1.15.1.2 | superoxide + reduced acceptor + 2 H+ | Pyrococcus horikoshii | - |
H2O2 + oxidized acceptor | - |
? | |
1.15.1.2 | superoxide + reduced acceptor + 2 H+ | Nanoarchaeum equitans | - |
H2O2 + oxidized acceptor | - |
? | |
1.15.1.2 | superoxide + reduced acceptor + 2 H+ | Ignicoccus hospitalis | - |
H2O2 + oxidized acceptor | - |
? | |
1.15.1.2 | superoxide + reduced acceptor + 2 H+ | Treponema pallidum | - |
H2O2 + oxidized acceptor | - |
? | |
1.15.1.2 | superoxide + reduced acceptor + 2 H+ | Archaeoglobus fulgidus ATCC 49558 | - |
H2O2 + oxidized acceptor | - |
? | |
1.15.1.2 | superoxide + reduced acceptor + 2 H+ | Ignicoccus hospitalis KIN4/I / DSM 18386 / JCM 14125 | - |
H2O2 + oxidized acceptor | - |
? | |
1.15.1.2 | superoxide + reduced acceptor + 2 H+ | Pyrococcus furiosus ATCC 43587 | - |
H2O2 + oxidized acceptor | - |
? | |
1.15.1.2 | superoxide + reduced acceptor + 2 H+ | Desulfarculus baarsii ATCC 33931 | - |
H2O2 + oxidized acceptor | - |
? | |
1.15.1.2 | superoxide + reduced acceptor + 2 H+ | Thermotoga maritima ATCC 43589 | - |
H2O2 + oxidized acceptor | - |
? | |
1.15.1.2 | superoxide + reduced acceptor + 2 H+ | Treponema pallidum Nichols | - |
H2O2 + oxidized acceptor | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.15.1.2 | Archaeoglobus fulgidus | - |
- |
- |
1.15.1.2 | Archaeoglobus fulgidus | O29903 | - |
- |
1.15.1.2 | Archaeoglobus fulgidus ATCC 49558 | O29903 | - |
- |
1.15.1.2 | Desulfarculus baarsii | Q46495 | - |
- |
1.15.1.2 | Desulfarculus baarsii ATCC 33931 | Q46495 | - |
- |
1.15.1.2 | Desulfovibrio desulfuricans | - |
- |
- |
1.15.1.2 | Desulfovibrio vulgaris | - |
- |
- |
1.15.1.2 | Dosidicus gigas | - |
- |
- |
1.15.1.2 | Ignicoccus hospitalis | A8AC72 | - |
- |
1.15.1.2 | Ignicoccus hospitalis KIN4/I / DSM 18386 / JCM 14125 | A8AC72 | - |
- |
1.15.1.2 | Nanoarchaeum equitans | Q74MF3 | - |
- |
1.15.1.2 | Pyrococcus furiosus | P82385 | - |
- |
1.15.1.2 | Pyrococcus furiosus ATCC 43587 | P82385 | - |
- |
1.15.1.2 | Pyrococcus horikoshii | O58810 | - |
- |
1.15.1.2 | Thermotoga maritima | Q9WZC6 | - |
- |
1.15.1.2 | Thermotoga maritima ATCC 43589 | Q9WZC6 | - |
- |
1.15.1.2 | Treponema pallidum | O82795 | - |
- |
1.15.1.2 | Treponema pallidum Nichols | O82795 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.15.1.2 | superoxide + reduced acceptor + 2 H+ | - |
Desulfovibrio desulfuricans | H2O2 + oxidized acceptor | - |
? | |
1.15.1.2 | superoxide + reduced acceptor + 2 H+ | - |
Desulfovibrio vulgaris | H2O2 + oxidized acceptor | - |
? | |
1.15.1.2 | superoxide + reduced acceptor + 2 H+ | - |
Archaeoglobus fulgidus | H2O2 + oxidized acceptor | - |
? | |
1.15.1.2 | superoxide + reduced acceptor + 2 H+ | - |
Dosidicus gigas | H2O2 + oxidized acceptor | - |
? | |
1.15.1.2 | superoxide + reduced acceptor + 2 H+ | - |
Pyrococcus furiosus | H2O2 + oxidized acceptor | - |
? | |
1.15.1.2 | superoxide + reduced acceptor + 2 H+ | - |
Desulfarculus baarsii | H2O2 + oxidized acceptor | - |
? | |
1.15.1.2 | superoxide + reduced acceptor + 2 H+ | - |
Thermotoga maritima | H2O2 + oxidized acceptor | - |
? | |
1.15.1.2 | superoxide + reduced acceptor + 2 H+ | - |
Pyrococcus horikoshii | H2O2 + oxidized acceptor | - |
? | |
1.15.1.2 | superoxide + reduced acceptor + 2 H+ | - |
Nanoarchaeum equitans | H2O2 + oxidized acceptor | - |
? | |
1.15.1.2 | superoxide + reduced acceptor + 2 H+ | - |
Ignicoccus hospitalis | H2O2 + oxidized acceptor | - |
? | |
1.15.1.2 | superoxide + reduced acceptor + 2 H+ | - |
Treponema pallidum | H2O2 + oxidized acceptor | - |
? | |
1.15.1.2 | superoxide + reduced acceptor + 2 H+ | - |
Archaeoglobus fulgidus ATCC 49558 | H2O2 + oxidized acceptor | - |
? | |
1.15.1.2 | superoxide + reduced acceptor + 2 H+ | - |
Ignicoccus hospitalis KIN4/I / DSM 18386 / JCM 14125 | H2O2 + oxidized acceptor | - |
? | |
1.15.1.2 | superoxide + reduced acceptor + 2 H+ | - |
Pyrococcus furiosus ATCC 43587 | H2O2 + oxidized acceptor | - |
? | |
1.15.1.2 | superoxide + reduced acceptor + 2 H+ | - |
Desulfarculus baarsii ATCC 33931 | H2O2 + oxidized acceptor | - |
? | |
1.15.1.2 | superoxide + reduced acceptor + 2 H+ | - |
Thermotoga maritima ATCC 43589 | H2O2 + oxidized acceptor | - |
? | |
1.15.1.2 | superoxide + reduced acceptor + 2 H+ | - |
Treponema pallidum Nichols | H2O2 + oxidized acceptor | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.15.1.2 | dimer | - |
Desulfovibrio desulfuricans |
1.15.1.2 | dimer | - |
Desulfarculus baarsii |
1.15.1.2 | dimer | - |
Treponema pallidum |
1.15.1.2 | tetramer | - |
Pyrococcus furiosus |
1.15.1.2 | tetramer | - |
Thermotoga maritima |
1.15.1.2 | tetramer | - |
Pyrococcus horikoshii |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.15.1.2 | 1Fe-SOR | - |
Archaeoglobus fulgidus |
1.15.1.2 | 1Fe-SOR | - |
Dosidicus gigas |
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 | 1Fe-SOR | - |
Nanoarchaeum equitans |
1.15.1.2 | 1Fe-SOR | - |
Ignicoccus hospitalis |
1.15.1.2 | 1Fe-SOR | - |
Treponema pallidum |
1.15.1.2 | 2Fe-SOR | - |
Desulfovibrio desulfuricans |
1.15.1.2 | 2Fe-SOR | - |
Desulfovibrio vulgaris |
1.15.1.2 | 2Fe-SOR | - |
Archaeoglobus fulgidus |
1.15.1.2 | 2Fe-SOR | - |
Desulfarculus baarsii |
1.15.1.2 | class I SOR | - |
Desulfovibrio desulfuricans |
1.15.1.2 | class I SOR | - |
Desulfovibrio vulgaris |
1.15.1.2 | class I SOR | - |
Archaeoglobus fulgidus |
1.15.1.2 | class I SOR | - |
Desulfarculus baarsii |
1.15.1.2 | class II SOR | - |
Archaeoglobus fulgidus |
1.15.1.2 | class II SOR | - |
Dosidicus gigas |
1.15.1.2 | class II SOR | - |
Pyrococcus furiosus |
1.15.1.2 | class II SOR | - |
Thermotoga maritima |
1.15.1.2 | class II SOR | - |
Pyrococcus horikoshii |
1.15.1.2 | class II SOR | - |
Nanoarchaeum equitans |
1.15.1.2 | class II SOR | - |
Ignicoccus hospitalis |
1.15.1.2 | class II SOR | - |
Treponema pallidum |
1.15.1.2 | SOR | - |
Desulfovibrio desulfuricans |
1.15.1.2 | SOR | - |
Desulfovibrio vulgaris |
1.15.1.2 | SOR | - |
Archaeoglobus fulgidus |
1.15.1.2 | SOR | - |
Dosidicus gigas |
1.15.1.2 | SOR | - |
Pyrococcus furiosus |
1.15.1.2 | SOR | - |
Desulfarculus baarsii |
1.15.1.2 | SOR | - |
Thermotoga maritima |
1.15.1.2 | SOR | - |
Pyrococcus horikoshii |
1.15.1.2 | SOR | - |
Nanoarchaeum equitans |
1.15.1.2 | SOR | - |
Ignicoccus hospitalis |
1.15.1.2 | SOR | - |
Treponema pallidum |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.15.1.2 | evolution | Fe-SOR classification, detailed overview. One classification takes into consideration the primary and tertiary structures of SORs some enzymes contain only one Fe ion, but have a longer N-terminus with amino acid sequence and structural similarities with those of the respective domain of desulfoferrodoxins, but lacking the cysteine ligands to the desulforedoxin (Dfxs)-like center. According to the authors, SORs fall into three classes: classes I (Dfxs), II (neelaredoxins), and III (neelaredoxins structurally homologous to desulfoferrodoxins, with only one Fe center). In dendograms constructed from available amino acid sequences, class III enzymes cluster within the class I enzymes, it is plausible that class III SORs evolved from class I proteins by loss of the cysteine residues binding the desulforedoxin-like center, an event that may have occurred more than once because the Dfxs are not monophyletic. This classification misses the family of methanoferrodoxins. Another classification is based on the variability of N-terminal domains classifying SORs into seven classes. Class I or Dx-SOR includes the 2Fe-SORs, where the N-terminal is a desulforedoxin-like (Dx) domain. Class II includes the 1Fe-SORs that have no extra N-terminal domain. Class III SORs are analogous to Dx-SORs but lacking some or all of the Fe cysteine ligands (FeCys4) for the desulforedoxin-like Fe center and therefore lacking the FeCy4 site. Class IV includes SORs with an extra C-terminal domain containing an iron-sulfur center. The fifth class, termed HTH-Dx-SOR, includes Dx-SORs (2Fe-SOR) with an extended N-terminal helix-turn-helix domain present in transcription regulators. The sixth class, termed TAT-SOR, includes SORs from only a few organisms and the sequences are preceded by a putative twin-arginine signal peptide that suggests their periplasmic localization | Desulfovibrio desulfuricans |
1.15.1.2 | evolution | Fe-SOR classification, detailed overview. One classification takes into consideration the primary and tertiary structures of SORs some enzymes contain only one Fe ion, but have a longer N-terminus with amino acid sequence and structural similarities with those of the respective domain of desulfoferrodoxins, but lacking the cysteine ligands to the desulforedoxin (Dfxs)-like center. According to the authors, SORs fall into three classes: classes I (Dfxs), II (neelaredoxins), and III (neelaredoxins structurally homologous to desulfoferrodoxins, with only one Fe center). In dendograms constructed from available amino acid sequences, class III enzymes cluster within the class I enzymes, it is plausible that class III SORs evolved from class I proteins by loss of the cysteine residues binding the desulforedoxin-like center, an event that may have occurred more than once because the Dfxs are not monophyletic. This classification misses the family of methanoferrodoxins. Another classification is based on the variability of N-terminal domains classifying SORs into seven classes. Class I or Dx-SOR includes the 2Fe-SORs, where the N-terminal is a desulforedoxin-like (Dx) domain. Class II includes the 1Fe-SORs that have no extra N-terminal domain. Class III SORs are analogous to Dx-SORs but lacking some or all of the Fe cysteine ligands (FeCys4) for the desulforedoxin-like Fe center and therefore lacking the FeCy4 site. Class IV includes SORs with an extra C-terminal domain containing an iron-sulfur center. The fifth class, termed HTH-Dx-SOR, includes Dx-SORs (2Fe-SOR) with an extended N-terminal helix-turn-helix domain present in transcription regulators. The sixth class, termed TAT-SOR, includes SORs from only a few organisms and the sequences are preceded by a putative twin-arginine signal peptide that suggests their periplasmic localization | Desulfovibrio vulgaris |
1.15.1.2 | evolution | Fe-SOR classification, detailed overview. One classification takes into consideration the primary and tertiary structures of SORs some enzymes contain only one Fe ion, but have a longer N-terminus with amino acid sequence and structural similarities with those of the respective domain of desulfoferrodoxins, but lacking the cysteine ligands to the desulforedoxin (Dfxs)-like center. According to the authors, SORs fall into three classes: classes I (Dfxs), II (neelaredoxins), and III (neelaredoxins structurally homologous to desulfoferrodoxins, with only one Fe center). In dendograms constructed from available amino acid sequences, class III enzymes cluster within the class I enzymes, it is plausible that class III SORs evolved from class I proteins by loss of the cysteine residues binding the desulforedoxin-like center, an event that may have occurred more than once because the Dfxs are not monophyletic. This classification misses the family of methanoferrodoxins. Another classification is based on the variability of N-terminal domains classifying SORs into seven classes. Class I or Dx-SOR includes the 2Fe-SORs, where the N-terminal is a desulforedoxin-like (Dx) domain. Class II includes the 1Fe-SORs that have no extra N-terminal domain. Class III SORs are analogous to Dx-SORs but lacking some or all of the Fe cysteine ligands (FeCys4) for the desulforedoxin-like Fe center and therefore lacking the FeCy4 site. Class IV includes SORs with an extra C-terminal domain containing an iron-sulfur center. The fifth class, termed HTH-Dx-SOR, includes Dx-SORs (2Fe-SOR) with an extended N-terminal helix-turn-helix domain present in transcription regulators. The sixth class, termed TAT-SOR, includes SORs from only a few organisms and the sequences are preceded by a putative twin-arginine signal peptide that suggests their periplasmic localization | Archaeoglobus fulgidus |
1.15.1.2 | evolution | Fe-SOR classification, detailed overview. One classification takes into consideration the primary and tertiary structures of SORs some enzymes contain only one Fe ion, but have a longer N-terminus with amino acid sequence and structural similarities with those of the respective domain of desulfoferrodoxins, but lacking the cysteine ligands to the desulforedoxin (Dfxs)-like center. According to the authors, SORs fall into three classes: classes I (Dfxs), II (neelaredoxins), and III (neelaredoxins structurally homologous to desulfoferrodoxins, with only one Fe center). In dendograms constructed from available amino acid sequences, class III enzymes cluster within the class I enzymes, it is plausible that class III SORs evolved from class I proteins by loss of the cysteine residues binding the desulforedoxin-like center, an event that may have occurred more than once because the Dfxs are not monophyletic. This classification misses the family of methanoferrodoxins. Another classification is based on the variability of N-terminal domains classifying SORs into seven classes. Class I or Dx-SOR includes the 2Fe-SORs, where the N-terminal is a desulforedoxin-like (Dx) domain. Class II includes the 1Fe-SORs that have no extra N-terminal domain. Class III SORs are analogous to Dx-SORs but lacking some or all of the Fe cysteine ligands (FeCys4) for the desulforedoxin-like Fe center and therefore lacking the FeCy4 site. Class IV includes SORs with an extra C-terminal domain containing an iron-sulfur center. The fifth class, termed HTH-Dx-SOR, includes Dx-SORs (2Fe-SOR) with an extended N-terminal helix-turn-helix domain present in transcription regulators. The sixth class, termed TAT-SOR, includes SORs from only a few organisms and the sequences are preceded by a putative twin-arginine signal peptide that suggests their periplasmic localization | Dosidicus gigas |
1.15.1.2 | evolution | Fe-SOR classification, detailed overview. One classification takes into consideration the primary and tertiary structures of SORs some enzymes contain only one Fe ion, but have a longer N-terminus with amino acid sequence and structural similarities with those of the respective domain of desulfoferrodoxins, but lacking the cysteine ligands to the desulforedoxin (Dfxs)-like center. According to the authors, SORs fall into three classes: classes I (Dfxs), II (neelaredoxins), and III (neelaredoxins structurally homologous to desulfoferrodoxins, with only one Fe center). In dendograms constructed from available amino acid sequences, class III enzymes cluster within the class I enzymes, it is plausible that class III SORs evolved from class I proteins by loss of the cysteine residues binding the desulforedoxin-like center, an event that may have occurred more than once because the Dfxs are not monophyletic. This classification misses the family of methanoferrodoxins. Another classification is based on the variability of N-terminal domains classifying SORs into seven classes. Class I or Dx-SOR includes the 2Fe-SORs, where the N-terminal is a desulforedoxin-like (Dx) domain. Class II includes the 1Fe-SORs that have no extra N-terminal domain. Class III SORs are analogous to Dx-SORs but lacking some or all of the Fe cysteine ligands (FeCys4) for the desulforedoxin-like Fe center and therefore lacking the FeCy4 site. Class IV includes SORs with an extra C-terminal domain containing an iron-sulfur center. The fifth class, termed HTH-Dx-SOR, includes Dx-SORs (2Fe-SOR) with an extended N-terminal helix-turn-helix domain present in transcription regulators. The sixth class, termed TAT-SOR, includes SORs from only a few organisms and the sequences are preceded by a putative twin-arginine signal peptide that suggests their periplasmic localization | Pyrococcus furiosus |
1.15.1.2 | evolution | Fe-SOR classification, detailed overview. One classification takes into consideration the primary and tertiary structures of SORs some enzymes contain only one Fe ion, but have a longer N-terminus with amino acid sequence and structural similarities with those of the respective domain of desulfoferrodoxins, but lacking the cysteine ligands to the desulforedoxin (Dfxs)-like center. According to the authors, SORs fall into three classes: classes I (Dfxs), II (neelaredoxins), and III (neelaredoxins structurally homologous to desulfoferrodoxins, with only one Fe center). In dendograms constructed from available amino acid sequences, class III enzymes cluster within the class I enzymes, it is plausible that class III SORs evolved from class I proteins by loss of the cysteine residues binding the desulforedoxin-like center, an event that may have occurred more than once because the Dfxs are not monophyletic. This classification misses the family of methanoferrodoxins. Another classification is based on the variability of N-terminal domains classifying SORs into seven classes. Class I or Dx-SOR includes the 2Fe-SORs, where the N-terminal is a desulforedoxin-like (Dx) domain. Class II includes the 1Fe-SORs that have no extra N-terminal domain. Class III SORs are analogous to Dx-SORs but lacking some or all of the Fe cysteine ligands (FeCys4) for the desulforedoxin-like Fe center and therefore lacking the FeCy4 site. Class IV includes SORs with an extra C-terminal domain containing an iron-sulfur center. The fifth class, termed HTH-Dx-SOR, includes Dx-SORs (2Fe-SOR) with an extended N-terminal helix-turn-helix domain present in transcription regulators. The sixth class, termed TAT-SOR, includes SORs from only a few organisms and the sequences are preceded by a putative twin-arginine signal peptide that suggests their periplasmic localization | Desulfarculus baarsii |
1.15.1.2 | evolution | Fe-SOR classification, detailed overview. One classification takes into consideration the primary and tertiary structures of SORs some enzymes contain only one Fe ion, but have a longer N-terminus with amino acid sequence and structural similarities with those of the respective domain of desulfoferrodoxins, but lacking the cysteine ligands to the desulforedoxin (Dfxs)-like center. According to the authors, SORs fall into three classes: classes I (Dfxs), II (neelaredoxins), and III (neelaredoxins structurally homologous to desulfoferrodoxins, with only one Fe center). In dendograms constructed from available amino acid sequences, class III enzymes cluster within the class I enzymes, it is plausible that class III SORs evolved from class I proteins by loss of the cysteine residues binding the desulforedoxin-like center, an event that may have occurred more than once because the Dfxs are not monophyletic. This classification misses the family of methanoferrodoxins. Another classification is based on the variability of N-terminal domains classifying SORs into seven classes. Class I or Dx-SOR includes the 2Fe-SORs, where the N-terminal is a desulforedoxin-like (Dx) domain. Class II includes the 1Fe-SORs that have no extra N-terminal domain. Class III SORs are analogous to Dx-SORs but lacking some or all of the Fe cysteine ligands (FeCys4) for the desulforedoxin-like Fe center and therefore lacking the FeCy4 site. Class IV includes SORs with an extra C-terminal domain containing an iron-sulfur center. The fifth class, termed HTH-Dx-SOR, includes Dx-SORs (2Fe-SOR) with an extended N-terminal helix-turn-helix domain present in transcription regulators. The sixth class, termed TAT-SOR, includes SORs from only a few organisms and the sequences are preceded by a putative twin-arginine signal peptide that suggests their periplasmic localization | Thermotoga maritima |
1.15.1.2 | evolution | Fe-SOR classification, detailed overview. One classification takes into consideration the primary and tertiary structures of SORs some enzymes contain only one Fe ion, but have a longer N-terminus with amino acid sequence and structural similarities with those of the respective domain of desulfoferrodoxins, but lacking the cysteine ligands to the desulforedoxin (Dfxs)-like center. According to the authors, SORs fall into three classes: classes I (Dfxs), II (neelaredoxins), and III (neelaredoxins structurally homologous to desulfoferrodoxins, with only one Fe center). In dendograms constructed from available amino acid sequences, class III enzymes cluster within the class I enzymes, it is plausible that class III SORs evolved from class I proteins by loss of the cysteine residues binding the desulforedoxin-like center, an event that may have occurred more than once because the Dfxs are not monophyletic. This classification misses the family of methanoferrodoxins. Another classification is based on the variability of N-terminal domains classifying SORs into seven classes. Class I or Dx-SOR includes the 2Fe-SORs, where the N-terminal is a desulforedoxin-like (Dx) domain. Class II includes the 1Fe-SORs that have no extra N-terminal domain. Class III SORs are analogous to Dx-SORs but lacking some or all of the Fe cysteine ligands (FeCys4) for the desulforedoxin-like Fe center and therefore lacking the FeCy4 site. Class IV includes SORs with an extra C-terminal domain containing an iron-sulfur center. The fifth class, termed HTH-Dx-SOR, includes Dx-SORs (2Fe-SOR) with an extended N-terminal helix-turn-helix domain present in transcription regulators. The sixth class, termed TAT-SOR, includes SORs from only a few organisms and the sequences are preceded by a putative twin-arginine signal peptide that suggests their periplasmic localization | Pyrococcus horikoshii |
1.15.1.2 | evolution | Fe-SOR classification, detailed overview. One classification takes into consideration the primary and tertiary structures of SORs some enzymes contain only one Fe ion, but have a longer N-terminus with amino acid sequence and structural similarities with those of the respective domain of desulfoferrodoxins, but lacking the cysteine ligands to the desulforedoxin (Dfxs)-like center. According to the authors, SORs fall into three classes: classes I (Dfxs), II (neelaredoxins), and III (neelaredoxins structurally homologous to desulfoferrodoxins, with only one Fe center). In dendograms constructed from available amino acid sequences, class III enzymes cluster within the class I enzymes, it is plausible that class III SORs evolved from class I proteins by loss of the cysteine residues binding the desulforedoxin-like center, an event that may have occurred more than once because the Dfxs are not monophyletic. This classification misses the family of methanoferrodoxins. Another classification is based on the variability of N-terminal domains classifying SORs into seven classes. Class I or Dx-SOR includes the 2Fe-SORs, where the N-terminal is a desulforedoxin-like (Dx) domain. Class II includes the 1Fe-SORs that have no extra N-terminal domain. Class III SORs are analogous to Dx-SORs but lacking some or all of the Fe cysteine ligands (FeCys4) for the desulforedoxin-like Fe center and therefore lacking the FeCy4 site. Class IV includes SORs with an extra C-terminal domain containing an iron-sulfur center. The fifth class, termed HTH-Dx-SOR, includes Dx-SORs (2Fe-SOR) with an extended N-terminal helix-turn-helix domain present in transcription regulators. The sixth class, termed TAT-SOR, includes SORs from only a few organisms and the sequences are preceded by a putative twin-arginine signal peptide that suggests their periplasmic localization | Nanoarchaeum equitans |
1.15.1.2 | evolution | Fe-SOR classification, detailed overview. One classification takes into consideration the primary and tertiary structures of SORs some enzymes contain only one Fe ion, but have a longer N-terminus with amino acid sequence and structural similarities with those of the respective domain of desulfoferrodoxins, but lacking the cysteine ligands to the desulforedoxin (Dfxs)-like center. According to the authors, SORs fall into three classes: classes I (Dfxs), II (neelaredoxins), and III (neelaredoxins structurally homologous to desulfoferrodoxins, with only one Fe center). In dendograms constructed from available amino acid sequences, class III enzymes cluster within the class I enzymes, it is plausible that class III SORs evolved from class I proteins by loss of the cysteine residues binding the desulforedoxin-like center, an event that may have occurred more than once because the Dfxs are not monophyletic. This classification misses the family of methanoferrodoxins. Another classification is based on the variability of N-terminal domains classifying SORs into seven classes. Class I or Dx-SOR includes the 2Fe-SORs, where the N-terminal is a desulforedoxin-like (Dx) domain. Class II includes the 1Fe-SORs that have no extra N-terminal domain. Class III SORs are analogous to Dx-SORs but lacking some or all of the Fe cysteine ligands (FeCys4) for the desulforedoxin-like Fe center and therefore lacking the FeCy4 site. Class IV includes SORs with an extra C-terminal domain containing an iron-sulfur center. The fifth class, termed HTH-Dx-SOR, includes Dx-SORs (2Fe-SOR) with an extended N-terminal helix-turn-helix domain present in transcription regulators. The sixth class, termed TAT-SOR, includes SORs from only a few organisms and the sequences are preceded by a putative twin-arginine signal peptide that suggests their periplasmic localization | Ignicoccus hospitalis |
1.15.1.2 | evolution | Fe-SOR classification, detailed overview. One classification takes into consideration the primary and tertiary structures of SORs some enzymes contain only one Fe ion, but have a longer N-terminus with amino acid sequence and structural similarities with those of the respective domain of desulfoferrodoxins, but lacking the cysteine ligands to the desulforedoxin (Dfxs)-like center. According to the authors, SORs fall into three classes: classes I (Dfxs), II (neelaredoxins), and III (neelaredoxins structurally homologous to desulfoferrodoxins, with only one Fe center). In dendograms constructed from available amino acid sequences, class III enzymes cluster within the class I enzymes, it is plausible that class III SORs evolved from class I proteins by loss of the cysteine residues binding the desulforedoxin-like center, an event that may have occurred more than once because the Dfxs are not monophyletic. This classification misses the family of methanoferrodoxins. Another classification is based on the variability of N-terminal domains classifying SORs into seven classes. Class I or Dx-SOR includes the 2Fe-SORs, where the N-terminal is a desulforedoxin-like (Dx) domain. Class II includes the 1Fe-SORs that have no extra N-terminal domain. Class III SORs are analogous to Dx-SORs but lacking some or all of the Fe cysteine ligands (FeCys4) for the desulforedoxin-like Fe center and therefore lacking the FeCy4 site. Class IV includes SORs with an extra C-terminal domain containing an iron-sulfur center. The fifth class, termed HTH-Dx-SOR, includes Dx-SORs (2Fe-SOR) with an extended N-terminal helix-turn-helix domain present in transcription regulators. The sixth class, termed TAT-SOR, includes SORs from only a few organisms and the sequences are preceded by a putative twin-arginine signal peptide that suggests their periplasmic localization | Treponema pallidum |
1.15.1.2 | additional information | key catalytic residue is E23, catalytic Fe2+ binding residues are H25, H50, H56, C109, and H112 | Ignicoccus hospitalis |
1.15.1.2 | additional information | key catalytic residue is K9, catalytic Fe2+ binding residues are H10, H35, H41, C97, and H100 | Nanoarchaeum equitans |
1.15.1.2 | additional information | key catalytic residues are E12 and K13, catalytic Fe2+ binding residues are H14, H40, H46, C110, and H113 | Archaeoglobus fulgidus |
1.15.1.2 | additional information | key catalytic residues are E14 and K15, catalytic Fe2+ binding residues are H16, H41, H47, C111, and H114 | Pyrococcus furiosus |
1.15.1.2 | additional information | key catalytic residues are E14 and K15, catalytic Fe2+ binding residues are H16, H41, H47, C111, and H114 | Archaeoglobus fulgidus |
1.15.1.2 | additional information | key catalytic residues are E15 and K16, catalytic Fe2+ binding residues are H17, H45, H51, C115, and H118 | Dosidicus gigas |
1.15.1.2 | additional information | key catalytic residues are E15 and K16, catalytic Fe2+ binding residues are H17, H45, H51, C115, and H118 | Thermotoga maritima |
1.15.1.2 | additional information | key catalytic residues are E23, K24, H25, H50, H56, C111, and H114 | Pyrococcus horikoshii |
1.15.1.2 | additional information | key catalytic residues are E47 and K48, catalytic Fe2+ binding residues are H49, H69, H74, C115, and H118 | Desulfovibrio desulfuricans |
1.15.1.2 | additional information | key catalytic residues are E47 and K48, catalytic Fe2+ binding residues are H49, H69, H74, C115, and H118 | Desulfovibrio vulgaris |
1.15.1.2 | additional information | key catalytic residues are E47 and K48, catalytic Fe2+ binding residues are H49, H69, H74, C115, and H118 | Desulfarculus baarsii |
1.15.1.2 | additional information | key catalytic residues are E48, K40, H50, H70, H76, C119, and H122 | Treponema pallidum |