node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
MCBB_1184 | MCBB_1263 | MCBB_1184 | MCBB_1263 | Rubredoxin; Rubredoxin is a small nonheme, iron protein lacking acid- labile sulfide. Its single Fe, chelated to 4 Cys, functions as an electron acceptor and may also stabilize the conformation of the molecule. | Putative rubrerythrin; May provide oxidative stress protection via catalytic reduction of intracellular hydrogen peroxide. Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence=; Note=Binds 3 Fe(3+) ions per subunit; non-sulfur oxo-bridged di-iron centers per dimer (By similarity); sp|Q58144|RUBY_METJA;evalue=7e-076; PctID=67.18; score=283. | 0.619 |
MCBB_1184 | MCBB_1754 | MCBB_1184 | MCBB_1754 | Rubredoxin; Rubredoxin is a small nonheme, iron protein lacking acid- labile sulfide. Its single Fe, chelated to 4 Cys, functions as an electron acceptor and may also stabilize the conformation of the molecule. | Digeranylgeranylglyceryl phosphate synthase; Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids. | 0.555 |
MCBB_1184 | dfx | MCBB_1184 | MCBB_1262 | Rubredoxin; Rubredoxin is a small nonheme, iron protein lacking acid- labile sulfide. Its single Fe, chelated to 4 Cys, functions as an electron acceptor and may also stabilize the conformation of the molecule. | Desulfoferrodoxin; Catalyzes the one-electron reduction of superoxide anion radical to hydrogen peroxide at a nonheme ferrous iron center. Plays a fundamental role in case of oxidative stress via its superoxide detoxification activity (By similarity). oxidized rubredoxin + H(2)O(2). Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence=; Note=Binds 1 Fe(3+) ion per subunit. The iron ion 1 is coordinated via 4 cysteine residues; Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence=; Note=Binds 1 Fe(2+) ion per subunit. The iron ion 2 is coordinated via four histidines and one cysteine residue.; has a [...] | 0.576 |
MCBB_1184 | ftnA | MCBB_1184 | MCBB_1187 | Rubredoxin; Rubredoxin is a small nonheme, iron protein lacking acid- labile sulfide. Its single Fe, chelated to 4 Cys, functions as an electron acceptor and may also stabilize the conformation of the molecule. | Bacterial non-heme ferritin; May alleviate iron toxicity in the presence of oxygen. H(+). spherical protein shell (12 +/-1 nM diameter) that can sequester at least 2000 iron atoms. an oxidative environment but not in reduced anaerobic conditions. Is also regulated by oxyR; sp|E1WS50|FTN_BACF6,sp|P0CJ83|FTN_BACFR;evalue=2e-029; PctID=41.25; score=128. | 0.425 |
MCBB_1184 | nifH2 | MCBB_1184 | MCBB_0533 | Rubredoxin; Rubredoxin is a small nonheme, iron protein lacking acid- labile sulfide. Its single Fe, chelated to 4 Cys, functions as an electron acceptor and may also stabilize the conformation of the molecule. | Nitrogenase iron protein 2; The key enzymatic reactions in nitrogen fixation are catalyzed by the nitrogenase complex, which has 2 components: the iron protein and the molybdenum-iron protein; Belongs to the NifH/BchL/ChlL family. | 0.551 |
MCBB_1184 | paaK1 | MCBB_1184 | MCBB_1183 | Rubredoxin; Rubredoxin is a small nonheme, iron protein lacking acid- labile sulfide. Its single Fe, chelated to 4 Cys, functions as an electron acceptor and may also stabilize the conformation of the molecule. | Phenylacetate-coenzyme A ligase; Catalyzes the activation of phenylacetic acid (PA) to phenylacetyl-CoA (PA-CoA). Involved in the phenylalanine metabolism. Can also use CTP and UTP as substrate. + phenylacetyl-CoA. mercury) and by the sulfhydryl reagents 5,5-dithiobis(2-nitrobenzoic acid), N-ethylmaleimide and p-chloromercuribenzoate. Kinetic parameters: KM=9.7 mM for ATP (at 30 degrees Celsius and pH 8.2); KM=1 mM for CoA (at 30 degrees Celsius and pH 8.2); KM=16.5 mM for PA (at 30 degrees Celsius and pH 8.2); pH dependence: Optimum pH is 8.2; Temperature dependence: Optimum temperatu [...] | 0.437 |
MCBB_1184 | rdxA | MCBB_1184 | MCBB_2277 | Rubredoxin; Rubredoxin is a small nonheme, iron protein lacking acid- labile sulfide. Its single Fe, chelated to 4 Cys, functions as an electron acceptor and may also stabilize the conformation of the molecule. | Putative rubredoxin; sp|Q50533|RUBH_METTH;evalue=2e-017; PctID=45.74; score=89.0; Belongs to the rubredoxin family. | 0.515 |
MCBB_1263 | MCBB_1184 | MCBB_1263 | MCBB_1184 | Putative rubrerythrin; May provide oxidative stress protection via catalytic reduction of intracellular hydrogen peroxide. Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence=; Note=Binds 3 Fe(3+) ions per subunit; non-sulfur oxo-bridged di-iron centers per dimer (By similarity); sp|Q58144|RUBY_METJA;evalue=7e-076; PctID=67.18; score=283. | Rubredoxin; Rubredoxin is a small nonheme, iron protein lacking acid- labile sulfide. Its single Fe, chelated to 4 Cys, functions as an electron acceptor and may also stabilize the conformation of the molecule. | 0.619 |
MCBB_1263 | MCBB_1754 | MCBB_1263 | MCBB_1754 | Putative rubrerythrin; May provide oxidative stress protection via catalytic reduction of intracellular hydrogen peroxide. Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence=; Note=Binds 3 Fe(3+) ions per subunit; non-sulfur oxo-bridged di-iron centers per dimer (By similarity); sp|Q58144|RUBY_METJA;evalue=7e-076; PctID=67.18; score=283. | Digeranylgeranylglyceryl phosphate synthase; Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids. | 0.481 |
MCBB_1263 | dfx | MCBB_1263 | MCBB_1262 | Putative rubrerythrin; May provide oxidative stress protection via catalytic reduction of intracellular hydrogen peroxide. Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence=; Note=Binds 3 Fe(3+) ions per subunit; non-sulfur oxo-bridged di-iron centers per dimer (By similarity); sp|Q58144|RUBY_METJA;evalue=7e-076; PctID=67.18; score=283. | Desulfoferrodoxin; Catalyzes the one-electron reduction of superoxide anion radical to hydrogen peroxide at a nonheme ferrous iron center. Plays a fundamental role in case of oxidative stress via its superoxide detoxification activity (By similarity). oxidized rubredoxin + H(2)O(2). Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence=; Note=Binds 1 Fe(3+) ion per subunit. The iron ion 1 is coordinated via 4 cysteine residues; Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence=; Note=Binds 1 Fe(2+) ion per subunit. The iron ion 2 is coordinated via four histidines and one cysteine residue.; has a [...] | 0.885 |
MCBB_1263 | nifH2 | MCBB_1263 | MCBB_0533 | Putative rubrerythrin; May provide oxidative stress protection via catalytic reduction of intracellular hydrogen peroxide. Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence=; Note=Binds 3 Fe(3+) ions per subunit; non-sulfur oxo-bridged di-iron centers per dimer (By similarity); sp|Q58144|RUBY_METJA;evalue=7e-076; PctID=67.18; score=283. | Nitrogenase iron protein 2; The key enzymatic reactions in nitrogen fixation are catalyzed by the nitrogenase complex, which has 2 components: the iron protein and the molybdenum-iron protein; Belongs to the NifH/BchL/ChlL family. | 0.476 |
MCBB_1754 | MCBB_1184 | MCBB_1754 | MCBB_1184 | Digeranylgeranylglyceryl phosphate synthase; Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids. | Rubredoxin; Rubredoxin is a small nonheme, iron protein lacking acid- labile sulfide. Its single Fe, chelated to 4 Cys, functions as an electron acceptor and may also stabilize the conformation of the molecule. | 0.555 |
MCBB_1754 | MCBB_1263 | MCBB_1754 | MCBB_1263 | Digeranylgeranylglyceryl phosphate synthase; Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids. | Putative rubrerythrin; May provide oxidative stress protection via catalytic reduction of intracellular hydrogen peroxide. Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence=; Note=Binds 3 Fe(3+) ions per subunit; non-sulfur oxo-bridged di-iron centers per dimer (By similarity); sp|Q58144|RUBY_METJA;evalue=7e-076; PctID=67.18; score=283. | 0.481 |
MCBB_1754 | nifH2 | MCBB_1754 | MCBB_0533 | Digeranylgeranylglyceryl phosphate synthase; Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids. | Nitrogenase iron protein 2; The key enzymatic reactions in nitrogen fixation are catalyzed by the nitrogenase complex, which has 2 components: the iron protein and the molybdenum-iron protein; Belongs to the NifH/BchL/ChlL family. | 0.787 |
dfx | MCBB_1184 | MCBB_1262 | MCBB_1184 | Desulfoferrodoxin; Catalyzes the one-electron reduction of superoxide anion radical to hydrogen peroxide at a nonheme ferrous iron center. Plays a fundamental role in case of oxidative stress via its superoxide detoxification activity (By similarity). oxidized rubredoxin + H(2)O(2). Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence=; Note=Binds 1 Fe(3+) ion per subunit. The iron ion 1 is coordinated via 4 cysteine residues; Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence=; Note=Binds 1 Fe(2+) ion per subunit. The iron ion 2 is coordinated via four histidines and one cysteine residue.; has a [...] | Rubredoxin; Rubredoxin is a small nonheme, iron protein lacking acid- labile sulfide. Its single Fe, chelated to 4 Cys, functions as an electron acceptor and may also stabilize the conformation of the molecule. | 0.576 |
dfx | MCBB_1263 | MCBB_1262 | MCBB_1263 | Desulfoferrodoxin; Catalyzes the one-electron reduction of superoxide anion radical to hydrogen peroxide at a nonheme ferrous iron center. Plays a fundamental role in case of oxidative stress via its superoxide detoxification activity (By similarity). oxidized rubredoxin + H(2)O(2). Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence=; Note=Binds 1 Fe(3+) ion per subunit. The iron ion 1 is coordinated via 4 cysteine residues; Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence=; Note=Binds 1 Fe(2+) ion per subunit. The iron ion 2 is coordinated via four histidines and one cysteine residue.; has a [...] | Putative rubrerythrin; May provide oxidative stress protection via catalytic reduction of intracellular hydrogen peroxide. Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence=; Note=Binds 3 Fe(3+) ions per subunit; non-sulfur oxo-bridged di-iron centers per dimer (By similarity); sp|Q58144|RUBY_METJA;evalue=7e-076; PctID=67.18; score=283. | 0.885 |
dfx | ftnA | MCBB_1262 | MCBB_1187 | Desulfoferrodoxin; Catalyzes the one-electron reduction of superoxide anion radical to hydrogen peroxide at a nonheme ferrous iron center. Plays a fundamental role in case of oxidative stress via its superoxide detoxification activity (By similarity). oxidized rubredoxin + H(2)O(2). Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence=; Note=Binds 1 Fe(3+) ion per subunit. The iron ion 1 is coordinated via 4 cysteine residues; Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence=; Note=Binds 1 Fe(2+) ion per subunit. The iron ion 2 is coordinated via four histidines and one cysteine residue.; has a [...] | Bacterial non-heme ferritin; May alleviate iron toxicity in the presence of oxygen. H(+). spherical protein shell (12 +/-1 nM diameter) that can sequester at least 2000 iron atoms. an oxidative environment but not in reduced anaerobic conditions. Is also regulated by oxyR; sp|E1WS50|FTN_BACF6,sp|P0CJ83|FTN_BACFR;evalue=2e-029; PctID=41.25; score=128. | 0.923 |
dfx | rdxA | MCBB_1262 | MCBB_2277 | Desulfoferrodoxin; Catalyzes the one-electron reduction of superoxide anion radical to hydrogen peroxide at a nonheme ferrous iron center. Plays a fundamental role in case of oxidative stress via its superoxide detoxification activity (By similarity). oxidized rubredoxin + H(2)O(2). Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence=; Note=Binds 1 Fe(3+) ion per subunit. The iron ion 1 is coordinated via 4 cysteine residues; Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence=; Note=Binds 1 Fe(2+) ion per subunit. The iron ion 2 is coordinated via four histidines and one cysteine residue.; has a [...] | Putative rubredoxin; sp|Q50533|RUBH_METTH;evalue=2e-017; PctID=45.74; score=89.0; Belongs to the rubredoxin family. | 0.551 |
ftnA | MCBB_1184 | MCBB_1187 | MCBB_1184 | Bacterial non-heme ferritin; May alleviate iron toxicity in the presence of oxygen. H(+). spherical protein shell (12 +/-1 nM diameter) that can sequester at least 2000 iron atoms. an oxidative environment but not in reduced anaerobic conditions. Is also regulated by oxyR; sp|E1WS50|FTN_BACF6,sp|P0CJ83|FTN_BACFR;evalue=2e-029; PctID=41.25; score=128. | Rubredoxin; Rubredoxin is a small nonheme, iron protein lacking acid- labile sulfide. Its single Fe, chelated to 4 Cys, functions as an electron acceptor and may also stabilize the conformation of the molecule. | 0.425 |
ftnA | dfx | MCBB_1187 | MCBB_1262 | Bacterial non-heme ferritin; May alleviate iron toxicity in the presence of oxygen. H(+). spherical protein shell (12 +/-1 nM diameter) that can sequester at least 2000 iron atoms. an oxidative environment but not in reduced anaerobic conditions. Is also regulated by oxyR; sp|E1WS50|FTN_BACF6,sp|P0CJ83|FTN_BACFR;evalue=2e-029; PctID=41.25; score=128. | Desulfoferrodoxin; Catalyzes the one-electron reduction of superoxide anion radical to hydrogen peroxide at a nonheme ferrous iron center. Plays a fundamental role in case of oxidative stress via its superoxide detoxification activity (By similarity). oxidized rubredoxin + H(2)O(2). Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence=; Note=Binds 1 Fe(3+) ion per subunit. The iron ion 1 is coordinated via 4 cysteine residues; Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence=; Note=Binds 1 Fe(2+) ion per subunit. The iron ion 2 is coordinated via four histidines and one cysteine residue.; has a [...] | 0.923 |