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Literature summary extracted from

  • Sheng, Y.; Abreu, I.; Cabelli, D.; Maroney, M.; Miller, A.; Teixeira, M.; Valentine, J.
    Superoxide dismutases and superoxide reductases (2014), Chem. Rev., 114, 3854-3918 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

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

Protein Variants

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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

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
-
 ?

Organism

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
-
-

Substrates and Products (Substrate)

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
-
 ?

Subunits

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

Synonyms

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

General Information

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