NifU family protein; Conserved protein displaying similarity with the C-terminal domain of the Nitrogen fixation protein nifU. This latter protein is involved in the formation or repair of [Fe-S] clusters present in iron-sulfur proteins. Localized in the cytoplasm; Family membership.

Cysteine desulfurases mobilize the sulfur from L-cysteine to yield L-alanine, an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules as thio-nucleosides in tRNA, thiamine, biotin, lipoate, molybdopterin and Fe-S cluster; Uses the Pyridoxal phosphate as prosthetic group linked to a lysine residue; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; High confidence in function and specificity.

NifU family protein; Conserved protein displaying similarity with the C-terminal domain of the Nitrogen fixation protein nifU. This latter protein is involved in the formation or repair of [Fe-S] clusters present in iron-sulfur proteins. Localized in the cytoplasm; Family membership.

Some of the Nif proteins are specifically involved in the formation of the Fe-S cluster of nitrogenase and these are found in organisms that do not fix nitrogen; C-terminal domain; Family membership.

NifU family protein; Conserved protein displaying similarity with the C-terminal domain of the Nitrogen fixation protein nifU. This latter protein is involved in the formation or repair of [Fe-S] clusters present in iron-sulfur proteins. Localized in the cytoplasm; Family membership.

Protein SufA is a part of the suf operon (sufABCDSE). The six encoded proteins are arranged into two complexes (SufSE and SufBCD) and one protein. SufA acts as a scaffold protein in which Fe and S atoms are assembled into [FeS] cluster forms, which can then easily be transferred to apoproteins targets; The SUF system 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; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the H [...]

Protoheme IX farnesyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.

The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3); High confidence in function and specificity.

Protoheme IX farnesyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.

Protein SufA is a part of the suf operon (sufABCDSE). The six encoded proteins are arranged into two complexes (SufSE and SufBCD) and one protein. SufA acts as a scaffold protein in which Fe and S atoms are assembled into [FeS] cluster forms, which can then easily be transferred to apoproteins targets; The SUF system 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; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the H [...]

Cysteine desulfurases mobilize the sulfur from L-cysteine to yield L-alanine, an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules as thio-nucleosides in tRNA, thiamine, biotin, lipoate, molybdopterin and Fe-S cluster; Uses the Pyridoxal phosphate as prosthetic group linked to a lysine residue; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; High confidence in function and specificity.

NifU family protein; Conserved protein displaying similarity with the C-terminal domain of the Nitrogen fixation protein nifU. This latter protein is involved in the formation or repair of [Fe-S] clusters present in iron-sulfur proteins. Localized in the cytoplasm; Family membership.

Cysteine desulfurases mobilize the sulfur from L-cysteine to yield L-alanine, an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules as thio-nucleosides in tRNA, thiamine, biotin, lipoate, molybdopterin and Fe-S cluster; Uses the Pyridoxal phosphate as prosthetic group linked to a lysine residue; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; High confidence in function and specificity.

Some of the Nif proteins are specifically involved in the formation of the Fe-S cluster of nitrogenase and these are found in organisms that do not fix nitrogen; C-terminal domain; Family membership.

Cysteine desulfurases mobilize the sulfur from L-cysteine to yield L-alanine, an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules as thio-nucleosides in tRNA, thiamine, biotin, lipoate, molybdopterin and Fe-S cluster; Uses the Pyridoxal phosphate as prosthetic group linked to a lysine residue; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; High confidence in function and specificity.

Protein SufA is a part of the suf operon (sufABCDSE). The six encoded proteins are arranged into two complexes (SufSE and SufBCD) and one protein. SufA acts as a scaffold protein in which Fe and S atoms are assembled into [FeS] cluster forms, which can then easily be transferred to apoproteins targets; The SUF system 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; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the H [...]

Cysteine desulfurases mobilize the sulfur from L-cysteine to yield L-alanine, an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules as thio-nucleosides in tRNA, thiamine, biotin, lipoate, molybdopterin and Fe-S cluster; Uses the Pyridoxal phosphate as prosthetic group linked to a lysine residue; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; High confidence in function and specificity.

Cysteine desulfurase; Catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine.

Some of the Nif proteins are specifically involved in the formation of the Fe-S cluster of nitrogenase and these are found in organisms that do not fix nitrogen; C-terminal domain; Family membership.

NifU family protein; Conserved protein displaying similarity with the C-terminal domain of the Nitrogen fixation protein nifU. This latter protein is involved in the formation or repair of [Fe-S] clusters present in iron-sulfur proteins. Localized in the cytoplasm; Family membership.

Some of the Nif proteins are specifically involved in the formation of the Fe-S cluster of nitrogenase and these are found in organisms that do not fix nitrogen; C-terminal domain; Family membership.

Cysteine desulfurases mobilize the sulfur from L-cysteine to yield L-alanine, an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules as thio-nucleosides in tRNA, thiamine, biotin, lipoate, molybdopterin and Fe-S cluster; Uses the Pyridoxal phosphate as prosthetic group linked to a lysine residue; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; High confidence in function and specificity.

Some of the Nif proteins are specifically involved in the formation of the Fe-S cluster of nitrogenase and these are found in organisms that do not fix nitrogen; C-terminal domain; Family membership.

Protein SufA is a part of the suf operon (sufABCDSE). The six encoded proteins are arranged into two complexes (SufSE and SufBCD) and one protein. SufA acts as a scaffold protein in which Fe and S atoms are assembled into [FeS] cluster forms, which can then easily be transferred to apoproteins targets; The SUF system 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; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the H [...]

Peptide chain release factor 1; Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.

Protein SufA is a part of the suf operon (sufABCDSE). The six encoded proteins are arranged into two complexes (SufSE and SufBCD) and one protein. SufA acts as a scaffold protein in which Fe and S atoms are assembled into [FeS] cluster forms, which can then easily be transferred to apoproteins targets; The SUF system 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; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the H [...]

The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3); High confidence in function and specificity.

Protoheme IX farnesyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.

The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3); High confidence in function and specificity.

Protein SufA is a part of the suf operon (sufABCDSE). The six encoded proteins are arranged into two complexes (SufSE and SufBCD) and one protein. SufA acts as a scaffold protein in which Fe and S atoms are assembled into [FeS] cluster forms, which can then easily be transferred to apoproteins targets; The SUF system 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; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the H [...]

Protein SufA is a part of the suf operon (sufABCDSE). The six encoded proteins are arranged into two complexes (SufSE and SufBCD) and one protein. SufA acts as a scaffold protein in which Fe and S atoms are assembled into [FeS] cluster forms, which can then easily be transferred to apoproteins targets; The SUF system 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; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the H [...]

NifU family protein; Conserved protein displaying similarity with the C-terminal domain of the Nitrogen fixation protein nifU. This latter protein is involved in the formation or repair of [Fe-S] clusters present in iron-sulfur proteins. Localized in the cytoplasm; Family membership.

Protein SufA is a part of the suf operon (sufABCDSE). The six encoded proteins are arranged into two complexes (SufSE and SufBCD) and one protein. SufA acts as a scaffold protein in which Fe and S atoms are assembled into [FeS] cluster forms, which can then easily be transferred to apoproteins targets; The SUF system 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; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the H [...]

Protoheme IX farnesyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.

Protein SufA is a part of the suf operon (sufABCDSE). The six encoded proteins are arranged into two complexes (SufSE and SufBCD) and one protein. SufA acts as a scaffold protein in which Fe and S atoms are assembled into [FeS] cluster forms, which can then easily be transferred to apoproteins targets; The SUF system 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; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the H [...]

Cysteine desulfurases mobilize the sulfur from L-cysteine to yield L-alanine, an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules as thio-nucleosides in tRNA, thiamine, biotin, lipoate, molybdopterin and Fe-S cluster; Uses the Pyridoxal phosphate as prosthetic group linked to a lysine residue; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; High confidence in function and specificity.

Protein SufA is a part of the suf operon (sufABCDSE). The six encoded proteins are arranged into two complexes (SufSE and SufBCD) and one protein. SufA acts as a scaffold protein in which Fe and S atoms are assembled into [FeS] cluster forms, which can then easily be transferred to apoproteins targets; The SUF system 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; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the H [...]

Some of the Nif proteins are specifically involved in the formation of the Fe-S cluster of nitrogenase and these are found in organisms that do not fix nitrogen; C-terminal domain; Family membership.

Protein SufA is a part of the suf operon (sufABCDSE). The six encoded proteins are arranged into two complexes (SufSE and SufBCD) and one protein. SufA acts as a scaffold protein in which Fe and S atoms are assembled into [FeS] cluster forms, which can then easily be transferred to apoproteins targets; The SUF system 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; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the H [...]

Peptide chain release factor 1; Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.