Aconitate hydratase 1; Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. The apo form of AcnA functions as a RNA- binding regulatory protein which plays a role as a maintenance or survival enzyme during nutritional or oxidative stress. During oxidative stress inactive AcnA apo-enzyme without iron sulfur clusters binds the acnA mRNA 3' UTRs (untranslated regions), stabilizes acnA mRNA and increases AcnA synthesis, thus mediating a post- transcriptional positive autoregulatory switch. AcnA also enhances the stability of the sodA transcript.

Aconitate hydratase 2; Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and the 2- methylcitrate cycle I (propionate degradation route). Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. Also catalyzes the hydration of 2-methyl-cis-aconitate to yield (2R,3S)-2-methylisocitrate. The apo form of AcnB functions as a RNA- binding regulatory protein. During oxidative stress inactive AcnB apo- enzyme without iron sulfur clusters binds the acnB mRNA 3' UTRs (untranslated regions), stabilize [...]

Aconitate hydratase 1; Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. The apo form of AcnA functions as a RNA- binding regulatory protein which plays a role as a maintenance or survival enzyme during nutritional or oxidative stress. During oxidative stress inactive AcnA apo-enzyme without iron sulfur clusters binds the acnA mRNA 3' UTRs (untranslated regions), stabilizes acnA mRNA and increases AcnA synthesis, thus mediating a post- transcriptional positive autoregulatory switch. AcnA also enhances the stability of the sodA transcript.

Fe/S biogenesis protein, putative scaffold/chaperone protein; Involved in iron-sulfur cluster biogenesis under severe conditions such as iron starvation or oxidative stress. Binds a 4Fe-4S cluster, can transfer this cluster to apoproteins, and thereby intervenes in the maturation of Fe/S proteins. Could also act as a scaffold/chaperone for damaged Fe/S proteins. Required for E.coli to sustain oxidative stress and iron starvation. Also necessary for the use of extracellular DNA as the sole source of carbon and energy. Belongs to the NfuA family.

Aconitate hydratase 1; Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. The apo form of AcnA functions as a RNA- binding regulatory protein which plays a role as a maintenance or survival enzyme during nutritional or oxidative stress. During oxidative stress inactive AcnA apo-enzyme without iron sulfur clusters binds the acnA mRNA 3' UTRs (untranslated regions), stabilizes acnA mRNA and increases AcnA synthesis, thus mediating a post- transcriptional positive autoregulatory switch. AcnA also enhances the stability of the sodA transcript.

SufBCD Fe-S cluster assembly scaffold protein, ATP-binding protein; Has low ATPase activity. The SufBCD complex acts synergistically with SufE to stimulate the cysteine desulfurase activity of SufS. The SufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation.

Aconitate hydratase 2; Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and the 2- methylcitrate cycle I (propionate degradation route). Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. Also catalyzes the hydration of 2-methyl-cis-aconitate to yield (2R,3S)-2-methylisocitrate. The apo form of AcnB functions as a RNA- binding regulatory protein. During oxidative stress inactive AcnB apo- enzyme without iron sulfur clusters binds the acnB mRNA 3' UTRs (untranslated regions), stabilize [...]

Aconitate hydratase 1; Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. The apo form of AcnA functions as a RNA- binding regulatory protein which plays a role as a maintenance or survival enzyme during nutritional or oxidative stress. During oxidative stress inactive AcnA apo-enzyme without iron sulfur clusters binds the acnA mRNA 3' UTRs (untranslated regions), stabilizes acnA mRNA and increases AcnA synthesis, thus mediating a post- transcriptional positive autoregulatory switch. AcnA also enhances the stability of the sodA transcript.

Iron-sulfur cluster insertion protein; Probably involved in the insertion of Fe-S clusters into apoproteins in vivo including IspG and/or IspH. Essential for growth under aerobic conditions and for anaerobic respiration but not for fermentation. In vitro it binds Fe-S clusters and transfers them to apo-IspG, which is involved in quinone biosynthesis among many other cell components. Experiments indicate that it is probably also involved in the insertion of other Fe-S clusters than IspG/IspH; Belongs to the HesB/IscA family.

[2Fe-2S] ferredoxin; Ferredoxin are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. Although the function of this ferredoxin is unknown it is probable that it has a role as a cellular electron transfer protein. Involved in the in vivo assembly of the Fe-S clusters in a wide variety of iron-sulfur proteins.

Iron-sulfur cluster insertion protein; Probably involved in the insertion of Fe-S clusters into apoproteins in vivo including IspG and/or IspH. Essential for growth under aerobic conditions and for anaerobic respiration but not for fermentation. In vitro it binds Fe-S clusters and transfers them to apo-IspG, which is involved in quinone biosynthesis among many other cell components. Experiments indicate that it is probably also involved in the insertion of other Fe-S clusters than IspG/IspH; Belongs to the HesB/IscA family.

Glutaredoxin-4; Monothiol glutaredoxin involved in the biogenesis of iron- sulfur clusters; Belongs to the glutaredoxin family. Monothiol subfamily.

Iron-sulfur cluster insertion protein; Probably involved in the insertion of Fe-S clusters into apoproteins in vivo including IspG and/or IspH. Essential for growth under aerobic conditions and for anaerobic respiration but not for fermentation. In vitro it binds Fe-S clusters and transfers them to apo-IspG, which is involved in quinone biosynthesis among many other cell components. Experiments indicate that it is probably also involved in the insertion of other Fe-S clusters than IspG/IspH; Belongs to the HesB/IscA family.

DnaK-like molecular chaperone specific for IscU; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. Involved in the maturation of IscU; Belongs to the heat shock protein 70 family.

Iron-sulfur cluster insertion protein; Probably involved in the insertion of Fe-S clusters into apoproteins in vivo including IspG and/or IspH. Essential for growth under aerobic conditions and for anaerobic respiration but not for fermentation. In vitro it binds Fe-S clusters and transfers them to apo-IspG, which is involved in quinone biosynthesis among many other cell components. Experiments indicate that it is probably also involved in the insertion of other Fe-S clusters than IspG/IspH; Belongs to the HesB/IscA family.

HscA co-chaperone, J domain-containing protein Hsc56; Co-chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Seems to help targeting proteins to be folded toward HscA; Belongs to the HscB family.

Iron-sulfur cluster insertion protein; Probably involved in the insertion of Fe-S clusters into apoproteins in vivo including IspG and/or IspH. Essential for growth under aerobic conditions and for anaerobic respiration but not for fermentation. In vitro it binds Fe-S clusters and transfers them to apo-IspG, which is involved in quinone biosynthesis among many other cell components. Experiments indicate that it is probably also involved in the insertion of other Fe-S clusters than IspG/IspH; Belongs to the HesB/IscA family.

Cysteine desulfurase (tRNA sulfurtransferase), PLP-dependent; Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins. Preferentially binds to disordered IscU on which the Fe-S is assembled, IscU converts to the structured state and then dissociates from IscS to transfer the Fe-S to a [...]

Iron-sulfur cluster insertion protein; Probably involved in the insertion of Fe-S clusters into apoproteins in vivo including IspG and/or IspH. Essential for growth under aerobic conditions and for anaerobic respiration but not for fermentation. In vitro it binds Fe-S clusters and transfers them to apo-IspG, which is involved in quinone biosynthesis among many other cell components. Experiments indicate that it is probably also involved in the insertion of other Fe-S clusters than IspG/IspH; Belongs to the HesB/IscA family.

Iron-sulfur cluster assembly scaffold protein; A scaffold on which IscS assembles Fe-S clusters. Exists as 2 interconverting forms, a structured (S) and disordered (D) form. The D- state is the preferred substrate for IscS. Converts to the S-state when an Fe-S cluster is assembled, which helps it dissociate from IscS to transfer the Fe-S to an acceptor. It is likely that Fe-S cluster coordination is flexible as the role of this complex is to build and then hand off Fe-S clusters; Belongs to the NifU family.

Iron-sulfur cluster insertion protein; Probably involved in the insertion of Fe-S clusters into apoproteins in vivo including IspG and/or IspH. Essential for growth under aerobic conditions and for anaerobic respiration but not for fermentation. In vitro it binds Fe-S clusters and transfers them to apo-IspG, which is involved in quinone biosynthesis among many other cell components. Experiments indicate that it is probably also involved in the insertion of other Fe-S clusters than IspG/IspH; Belongs to the HesB/IscA family.

Fe/S biogenesis protein, putative scaffold/chaperone protein; Involved in iron-sulfur cluster biogenesis under severe conditions such as iron starvation or oxidative stress. Binds a 4Fe-4S cluster, can transfer this cluster to apoproteins, and thereby intervenes in the maturation of Fe/S proteins. Could also act as a scaffold/chaperone for damaged Fe/S proteins. Required for E.coli to sustain oxidative stress and iron starvation. Also necessary for the use of extracellular DNA as the sole source of carbon and energy. Belongs to the NfuA family.

Iron-sulfur cluster insertion protein; Probably involved in the insertion of Fe-S clusters into apoproteins in vivo including IspG and/or IspH. Essential for growth under aerobic conditions and for anaerobic respiration but not for fermentation. In vitro it binds Fe-S clusters and transfers them to apo-IspG, which is involved in quinone biosynthesis among many other cell components. Experiments indicate that it is probably also involved in the insertion of other Fe-S clusters than IspG/IspH; Belongs to the HesB/IscA family.

Component of SufBCD Fe-S cluster assembly scaffold; The SufBCD complex acts synergistically with SufE to stimulate the cysteine desulfurase activity of SufS. The SufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation.

Iron-sulfur cluster insertion protein; Probably involved in the insertion of Fe-S clusters into apoproteins in vivo including IspG and/or IspH. Essential for growth under aerobic conditions and for anaerobic respiration but not for fermentation. In vitro it binds Fe-S clusters and transfers them to apo-IspG, which is involved in quinone biosynthesis among many other cell components. Experiments indicate that it is probably also involved in the insertion of other Fe-S clusters than IspG/IspH; Belongs to the HesB/IscA family.

SufBCD Fe-S cluster assembly scaffold protein, ATP-binding protein; Has low ATPase activity. The SufBCD complex acts synergistically with SufE to stimulate the cysteine desulfurase activity of SufS. The SufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation.

Iron-sulfur cluster insertion protein; Probably involved in the insertion of Fe-S clusters into apoproteins in vivo including IspG and/or IspH. Essential for growth under aerobic conditions and for anaerobic respiration but not for fermentation. In vitro it binds Fe-S clusters and transfers them to apo-IspG, which is involved in quinone biosynthesis among many other cell components. Experiments indicate that it is probably also involved in the insertion of other Fe-S clusters than IspG/IspH; Belongs to the HesB/IscA family.

Component of SufBCD Fe-S cluster assembly scaffold; The SufBCD complex acts synergistically with SufE to stimulate the cysteine desulfurase activity of SufS. The SufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation. Required for the stability of the FhuF protein.

Iron-sulfur cluster insertion protein; Probably involved in the insertion of Fe-S clusters into apoproteins in vivo including IspG and/or IspH. Essential for growth under aerobic conditions and for anaerobic respiration but not for fermentation. In vitro it binds Fe-S clusters and transfers them to apo-IspG, which is involved in quinone biosynthesis among many other cell components. Experiments indicate that it is probably also involved in the insertion of other Fe-S clusters than IspG/IspH; Belongs to the HesB/IscA family.

Uncharacterized ferredoxin-like protein YfaE; Ferredoxin involved with ribonucleotide reductase diferric-tyrosyl radical (Y*) cofactor maintenance.

[2Fe-2S] ferredoxin; Ferredoxin are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. Although the function of this ferredoxin is unknown it is probable that it has a role as a cellular electron transfer protein. Involved in the in vivo assembly of the Fe-S clusters in a wide variety of iron-sulfur proteins.

Iron-sulfur cluster insertion protein; Probably involved in the insertion of Fe-S clusters into apoproteins in vivo including IspG and/or IspH. Essential for growth under aerobic conditions and for anaerobic respiration but not for fermentation. In vitro it binds Fe-S clusters and transfers them to apo-IspG, which is involved in quinone biosynthesis among many other cell components. Experiments indicate that it is probably also involved in the insertion of other Fe-S clusters than IspG/IspH; Belongs to the HesB/IscA family.

[2Fe-2S] ferredoxin; Ferredoxin are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. Although the function of this ferredoxin is unknown it is probable that it has a role as a cellular electron transfer protein. Involved in the in vivo assembly of the Fe-S clusters in a wide variety of iron-sulfur proteins.

Glutaredoxin-4; Monothiol glutaredoxin involved in the biogenesis of iron- sulfur clusters; Belongs to the glutaredoxin family. Monothiol subfamily.

[2Fe-2S] ferredoxin; Ferredoxin are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. Although the function of this ferredoxin is unknown it is probable that it has a role as a cellular electron transfer protein. Involved in the in vivo assembly of the Fe-S clusters in a wide variety of iron-sulfur proteins.

DnaK-like molecular chaperone specific for IscU; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. Involved in the maturation of IscU; Belongs to the heat shock protein 70 family.

[2Fe-2S] ferredoxin; Ferredoxin are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. Although the function of this ferredoxin is unknown it is probable that it has a role as a cellular electron transfer protein. Involved in the in vivo assembly of the Fe-S clusters in a wide variety of iron-sulfur proteins.

HscA co-chaperone, J domain-containing protein Hsc56; Co-chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Seems to help targeting proteins to be folded toward HscA; Belongs to the HscB family.

[2Fe-2S] ferredoxin; Ferredoxin are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. Although the function of this ferredoxin is unknown it is probable that it has a role as a cellular electron transfer protein. Involved in the in vivo assembly of the Fe-S clusters in a wide variety of iron-sulfur proteins.

Cysteine desulfurase (tRNA sulfurtransferase), PLP-dependent; Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins. Preferentially binds to disordered IscU on which the Fe-S is assembled, IscU converts to the structured state and then dissociates from IscS to transfer the Fe-S to a [...]