Alkyl hydroperoxide reductase, C22 subunit; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. Is the primary scavenger for endogenously generated hydrogen peroxides; Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.

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.

Alkyl hydroperoxide reductase, C22 subunit; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. Is the primary scavenger for endogenously generated hydrogen peroxides; Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.

Catalase-peroxidase HPI, heme b-containing; Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Displays also NADH oxidase, INH lyase and isonicotinoyl-NAD synthase activity; Belongs to the peroxidase family. Peroxidase/catalase subfamily.

Alkyl hydroperoxide reductase, C22 subunit; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. Is the primary scavenger for endogenously generated hydrogen peroxides; Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.

Oxidative and nitrosative stress transcriptional regulator; Hydrogen peroxide sensor. Activates the expression of a regulon of hydrogen peroxide-inducible genes such as katG, gor, ahpC, ahpF, oxyS (a regulatory RNA), dps, fur and grxA. OxyR expression is negatively autoregulated by binding to a 43 bp region upstream of its own coding sequence. OxyR is inactivated by reduction of its essential disulfide bond by the product of GrxA, itself positively regulated by OxyR. Has also a positive regulatory effect on the production of surface proteins that control the colony morphology and auto- [...]

[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.

Isc operon transcriptional repressor; Regulates the transcription of several operons and genes involved in the biogenesis of Fe-S clusters and Fe-S-containing proteins. Transcriptional repressor of the iscRSUA operon, which is involved in the assembly of Fe-S clusters into Fe-S proteins. In its apoform, under conditions of oxidative stress or iron deprivation, it activates the suf operon, which is a second operon involved in the assembly of Fe-S clusters. Represses its own transcription as well as that of toxin rnlA.

[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 [...]

[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 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.

Fumarate hydratase (fumarase A), aerobic Class I; Catalyzes the reversible hydration of fumarate to (S)-malate. Functions as an aerobic enzyme in the direction of malate formation as part of the citric acid cycle. Accounts for about 80% of the fumarase activity when the bacteria grow aerobically. To a lesser extent, also displays D-tartrate dehydratase activity in vitro, but is not able to convert (R)-malate, L-tartrate or meso-tartrate. Can also catalyze the isomerization of enol- to keto-oxaloacetate.

Anaerobic class I fumarate hydratase (fumarase B); Catalyzes the reversible hydration of fumarate to (S)-malate. Functions in the generation of fumarate for use as an anaerobic electron acceptor. To a lesser extent, also displays D-tartrate dehydratase activity, but is not able to convert (R)-malate, L-tartrate or meso-tartrate. Is required for anaerobic growth on D-tartrate. Belongs to the class-I fumarase family.

Anaerobic class I fumarate hydratase (fumarase B); Catalyzes the reversible hydration of fumarate to (S)-malate. Functions in the generation of fumarate for use as an anaerobic electron acceptor. To a lesser extent, also displays D-tartrate dehydratase activity, but is not able to convert (R)-malate, L-tartrate or meso-tartrate. Is required for anaerobic growth on D-tartrate. Belongs to the class-I fumarase family.

Fumarate hydratase (fumarase A), aerobic Class I; Catalyzes the reversible hydration of fumarate to (S)-malate. Functions as an aerobic enzyme in the direction of malate formation as part of the citric acid cycle. Accounts for about 80% of the fumarase activity when the bacteria grow aerobically. To a lesser extent, also displays D-tartrate dehydratase activity in vitro, but is not able to convert (R)-malate, L-tartrate or meso-tartrate. Can also catalyze the isomerization of enol- to keto-oxaloacetate.

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.

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.

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.

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.

Isc operon transcriptional repressor; Regulates the transcription of several operons and genes involved in the biogenesis of Fe-S clusters and Fe-S-containing proteins. Transcriptional repressor of the iscRSUA operon, which is involved in the assembly of Fe-S clusters into Fe-S proteins. In its apoform, under conditions of oxidative stress or iron deprivation, it activates the suf operon, which is a second operon involved in the assembly of Fe-S clusters. Represses its own transcription as well as that of toxin rnlA.

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.

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 [...]

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 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.

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.

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.

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.

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.

Isc operon transcriptional repressor; Regulates the transcription of several operons and genes involved in the biogenesis of Fe-S clusters and Fe-S-containing proteins. Transcriptional repressor of the iscRSUA operon, which is involved in the assembly of Fe-S clusters into Fe-S proteins. In its apoform, under conditions of oxidative stress or iron deprivation, it activates the suf operon, which is a second operon involved in the assembly of Fe-S clusters. Represses its own transcription as well as that of toxin rnlA.

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.

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 [...]

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 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.