| Type |
Details |
Score |
| Protein Domain |
| Type: |
Family |
| Description: |
Iron-sulphur (FeS) clusters are important cofactors for numerous proteins involved in electron transfer, in redox and non-redox catalysis, in gene regulation, and as sensors of oxygen and iron. These functions depend on the various FeS cluster prosthetic groups, the most common being [2Fe-2S]and [4Fe-4S][]. FeS cluster assembly is a complex process involving the mobilisation of Fe and S atoms from storage sources, their assembly into [Fe-S]form, their transport to specific cellular locations, and their transfer to recipient apoproteins. So far, three FeS assembly machineries have been identified, which are capable of synthesising all types of [Fe-S]clusters: ISC (iron-sulphur cluster), SUF (sulphur assimilation), and NIF (nitrogen fixation) systems.The ISC system is conserved in eubacteria and eukaryotes (mitochondria), and has broad specificity, targeting general FeS proteins [, ]. It is encoded by the isc operon (iscRSUA-hscBA-fdx-iscX). IscS is a cysteine desulphurase, which obtains S from cysteine (converting it to alanine) and serves as a S donor for FeS cluster assembly. IscU and IscA act as scaffolds to accept S and Fe atoms, assembling clusters and transfering them to recipient apoproteins. HscA is a molecular chaperone and HscB is a co-chaperone. Fdx is a [2Fe-2S]-type ferredoxin. IscR is a transcription factor that regulates expression of the isc operon. IscX (also known as YfhJ) appears to interact with IscS and may function as an Fe donor during cluster assembly [].The SUF system is an alternative pathway to the ISC system that operates under iron starvation and oxidative stress. It is found in eubacteria, archaea and eukaryotes (plastids). The SUF system is encoded by the suf operon (sufABCDSE), and the six encoded proteins are arranged into two complexes (SufSE and SufBCD) and one protein (SufA). SufS is a pyridoxal-phosphate (PLP) protein displaying cysteine desulphurase activity. SufE acts as a scaffold protein that accepts S from SufS and donates it to SufA []. SufC is an ATPase with an unorthodox ATP-binding cassette (ABC)-like component. SufA is homologous to IscA [], acting 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.In the NIF system, NifS and NifU are required for the formation of metalloclusters of nitrogenase in Azotobacter vinelandii, and other organisms, as well as in the maturation of other FeS proteins. Nitrogenase catalyses the fixation of nitrogen. It contains a complex cluster, the FeMo cofactor, which contains molybdenum, Fe and S. NifS is a cysteine desulphurase. NifU binds one Fe atom at its N-terminal, assembling an FeS cluster that is transferred to nitrogenase apoproteins []. Nif proteins involved in the formation of FeS clusters can also be found in organisms that do not fix nitrogen [].This entry represents SufD proteins that form part of the SufBCD complex in the SUF system. No specific functions have been assigned to these proteins. |
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| Protein Domain |
| Type: |
Family |
| Description: |
Iron-sulphur (FeS) clusters are important cofactors for numerous proteins involved in electron transfer, in redox and non-redox catalysis, in gene regulation, and as sensors of oxygen and iron. These functions depend on the various FeS cluster prosthetic groups, the most common being [2Fe-2S]and [4Fe-4S][]. FeS cluster assembly is a complex process involving the mobilisation of Fe and S atoms from storage sources, their assembly into [Fe-S]form, their transport to specific cellular locations, and their transfer to recipient apoproteins. So far, three FeS assembly machineries have been identified, which are capable of synthesising all types of [Fe-S]clusters: ISC (iron-sulphur cluster), SUF (sulphur assimilation), and NIF (nitrogen fixation) systems.The ISC system is conserved in eubacteria and eukaryotes (mitochondria), and has broad specificity, targeting general FeS proteins [, ]. It is encoded by the isc operon (iscRSUA-hscBA-fdx-iscX). IscS is a cysteine desulphurase, which obtains S from cysteine (converting it to alanine) and serves as a S donor for FeS cluster assembly. IscU and IscA act as scaffolds to accept S and Fe atoms, assembling clusters and transfering them to recipient apoproteins. HscA is a molecular chaperone and HscB is a co-chaperone. Fdx is a [2Fe-2S]-type ferredoxin. IscR is a transcription factor that regulates expression of the isc operon. IscX (also known as YfhJ) appears to interact with IscS and may function as an Fe donor during cluster assembly [].The SUF system is an alternative pathway to the ISC system that operates under iron starvation and oxidative stress. It is found in eubacteria, archaea and eukaryotes (plastids). The SUF system is encoded by the suf operon (sufABCDSE), and the six encoded proteins are arranged into two complexes (SufSE and SufBCD) and one protein (SufA). SufS is a pyridoxal-phosphate (PLP) protein displaying cysteine desulphurase activity. SufE acts as a scaffold protein that accepts S from SufS and donates it to SufA []. SufC is an ATPase with an unorthodox ATP-binding cassette (ABC)-like component. SufA is homologous to IscA [], acting 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.In the NIF system, NifS and NifU are required for the formation of metalloclusters of nitrogenase in Azotobacter vinelandii, and other organisms, as well as in the maturation of other FeS proteins. Nitrogenase catalyses the fixation of nitrogen. It contains a complex cluster, the FeMo cofactor, which contains molybdenum, Fe and S. NifS is a cysteine desulphurase. NifU binds one Fe atom at its N-terminal, assembling an FeS cluster that is transferred to nitrogenase apoproteins []. Nif proteins involved in the formation of FeS clusters can also be found in organisms that do not fix nitrogen [].This entry represents the HscA chaperone protein from the SUF system. HscA (or Hsc66) is a specialised bacterial Hsp70-class molecular chaperone that participates in the assembly of iron-sulphur cluster proteins. HscA resembles DnaK, but belongs to a separate clade. HscA interacts with IscU, which is believed to serve as a template for Fe-S cluster formation. The HscA-IscU interaction is facilitated by the J-type co-chaperone protein HscB (or Hsc20), which binds to both HscA and IscU, bringing them into contact with each other. HscA recognises a conserved LPPVK sequence motif at positions 99-103 of IscU []. |
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| Protein Domain |
| Type: |
Family |
| Description: |
Iron-sulphur (FeS) clusters are important cofactors for numerous proteins involved in electron transfer, in redox and non-redox catalysis, in gene regulation, and as sensors of oxygen and iron. These functions depend on the various FeS cluster prosthetic groups, the most common being [2Fe-2S]and [4Fe-4S][]. FeS cluster assembly is a complex process involving the mobilisation of Fe and S atoms from storage sources, their assembly into [Fe-S]form, their transport to specific cellular locations, and their transfer to recipient apoproteins. So far, three FeS assembly machineries have been identified, which are capable of synthesising all types of [Fe-S]clusters: ISC (iron-sulphur cluster), SUF (sulphur assimilation), and NIF (nitrogen fixation) systems.The ISC system is conserved in eubacteria and eukaryotes (mitochondria), and has broad specificity, targeting general FeS proteins [, ]. It is encoded by the isc operon (iscRSUA-hscBA-fdx-iscX). IscS is a cysteine desulphurase, which obtains S from cysteine (converting it to alanine) and serves as a S donor for FeS cluster assembly. IscU and IscA act as scaffolds to accept S and Fe atoms, assembling clusters and transfering them to recipient apoproteins. HscA is a molecular chaperone and HscB is a co-chaperone. Fdx is a [2Fe-2S]-type ferredoxin. IscR is a transcription factor that regulates expression of the isc operon. IscX (also known as YfhJ) appears to interact with IscS and may function as an Fe donor during cluster assembly [].The SUF system is an alternative pathway to the ISC system that operates under iron starvation and oxidative stress. It is found in eubacteria, archaea and eukaryotes (plastids). The SUF system is encoded by the suf operon (sufABCDSE), and the six encoded proteins are arranged into two complexes (SufSE and SufBCD) and one protein (SufA). SufS is a pyridoxal-phosphate (PLP) protein displaying cysteine desulphurase activity. SufE acts as a scaffold protein that accepts S from SufS and donates it to SufA []. SufC is an ATPase with an unorthodox ATP-binding cassette (ABC)-like component. SufA is homologous to IscA [], acting 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.In the NIF system, NifS and NifU are required for the formation of metalloclusters of nitrogenase in Azotobacter vinelandii, and other organisms, as well as in the maturation of other FeS proteins. Nitrogenase catalyses the fixation of nitrogen. It contains a complex cluster, the FeMo cofactor, which contains molybdenum, Fe and S. NifS is a cysteine desulphurase. NifU binds one Fe atom at its N-terminal, assembling an FeS cluster that is transferred to nitrogenase apoproteins []. Nif proteins involved in the formation of FeS clusters can also be found in organisms that do not fix nitrogen [].This entry represents SufC, which acts as an ATPase in the SUF system. SufC belongs to the ATP-binding cassette transporter family () but is no longer thought to be part of a transporter.The complex is reported as cytosolic or associated with the membrane []. |
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| Protein Domain |
| Type: |
Family |
| Description: |
Iron-sulphur (FeS) clusters are important cofactors for numerous proteins involved in electron transfer, in redox and non-redox catalysis, in gene regulation, and as sensors of oxygen and iron. These functions depend on thevarious FeS cluster prosthetic groups, the most common being [2Fe-2S]and [4Fe-4S][]. FeS cluster assembly is a complex process involving the mobilisation of Fe and S atoms from storage sources, their assembly into [Fe-S]form, their transport to specific cellular locations, and their transfer to recipient apoproteins. So far, three FeS assembly machineries have been identified, which are capable of synthesising all types of [Fe-S]clusters: ISC (iron-sulphur cluster), SUF (sulphur assimilation), and NIF (nitrogen fixation) systems.The ISC system is conserved in eubacteria and eukaryotes (mitochondria), and has broad specificity, targeting general FeS proteins [, ]. It is encoded by the isc operon (iscRSUA-hscBA-fdx-iscX). IscS is a cysteine desulphurase, which obtains S from cysteine (converting it to alanine) and serves as a S donor for FeS cluster assembly. IscU and IscA act as scaffolds to accept S and Fe atoms, assembling clusters and transfering them to recipient apoproteins. HscA is a molecular chaperone and HscB is a co-chaperone. Fdx is a [2Fe-2S]-type ferredoxin. IscR is a transcription factor that regulates expression of the isc operon. IscX (also known as YfhJ) appears to interact with IscS and may function as an Fe donor during cluster assembly [].The SUF system is an alternative pathway to the ISC system that operates under iron starvation and oxidative stress. It is found in eubacteria, archaea and eukaryotes (plastids). The SUF system is encoded by the suf operon (sufABCDSE), and the six encoded proteins are arranged into two complexes (SufSE and SufBCD) and one protein (SufA). SufS is a pyridoxal-phosphate (PLP) protein displaying cysteine desulphurase activity. SufE acts as a scaffold protein that accepts S from SufS and donates it to SufA []. SufC is an ATPase with an unorthodox ATP-binding cassette (ABC)-like component. SufA is homologous to IscA [], acting 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.In the NIF system, NifS and NifU are required for the formation of metalloclusters of nitrogenase in Azotobacter vinelandii, and other organisms, as well as in the maturation of other FeS proteins. Nitrogenase catalyses the fixation of nitrogen. It contains a complex cluster, the FeMo cofactor, which contains molybdenum, Fe and S. NifS is a cysteine desulphurase. NifU binds one Fe atom at its N-terminal, assembling an FeS cluster that is transferred to nitrogenase apoproteins []. Nif proteins involved in the formation of FeS clusters can also be found in organisms that do not fix nitrogen [].This entry represents a distinct group of NifU-like proteins, always found with a NifS-like protein and restricted to species that lack a SUF system. Typically, NIF systems service a smaller number of FeS-containing proteins than do ISC or SUF. These proteins are often encoded near the mnmA gene, involved in the carboxymethylaminomethyl modification of U34 in some tRNAs (see ). While other NifU proteins are associated with nitrogen fixation, this family is not. |
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| Protein Domain |
| Type: |
Domain |
| Description: |
Iron-sulphur (FeS) clusters are important cofactors for numerous proteins involved in electron transfer, in redox and non-redox catalysis, in gene regulation, and as sensors of oxygen and iron. These functions depend on the various FeS cluster prosthetic groups, the most common being [2Fe-2S]and [4Fe-4S][]. FeS cluster assembly is a complex process involving the mobilisation of Fe and S atoms from storage sources, their assembly into [Fe-S]form, their transport to specific cellular locations, and their transfer to recipient apoproteins. So far, three FeS assembly machineries have been identified, which are capable of synthesising all types of [Fe-S]clusters: ISC (iron-sulphur cluster), SUF (sulphur assimilation), and NIF (nitrogen fixation) systems.The ISC system is conserved in eubacteria and eukaryotes (mitochondria), and has broad specificity, targeting general FeS proteins [, ]. It is encoded by the isc operon (iscRSUA-hscBA-fdx-iscX). IscS is a cysteine desulphurase, which obtains S from cysteine (converting it to alanine) and serves as a S donor for FeS cluster assembly. IscU and IscA act as scaffolds to accept S and Fe atoms, assembling clusters and transfering them to recipient apoproteins. HscA is a molecular chaperone and HscB is a co-chaperone. Fdx is a [2Fe-2S]-type ferredoxin. IscR is a transcription factor that regulates expression of the isc operon. IscX (also known as YfhJ) appears to interact with IscS and may function as an Fe donor during cluster assembly [].The SUF system is an alternative pathway to the ISC system that operates under iron starvation and oxidative stress. It is found in eubacteria, archaea and eukaryotes (plastids). The SUF system is encoded by the suf operon (sufABCDSE), and the six encoded proteins are arranged into two complexes (SufSE and SufBCD) and one protein (SufA). SufS is a pyridoxal-phosphate (PLP) protein displaying cysteine desulphurase activity. SufE acts as a scaffold protein that accepts S from SufS and donates it to SufA []. SufC is an ATPase with an unorthodox ATP-binding cassette (ABC)-like component. SufA is homologous to IscA [], acting 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.In the NIF system, NifS and NifU are required for the formation of metalloclusters of nitrogenase in Azotobacter vinelandii, and other organisms, as well as in the maturation of other FeS proteins. Nitrogenase catalyses the fixation of nitrogen. It contains a complex cluster, the FeMo cofactor, which contains molybdenum, Fe and S. NifS is a cysteine desulphurase. NifU binds one Fe atom at its N-terminal, assembling an FeS cluster that is transferred to nitrogenase apoproteins []. Nif proteins involved in the formation of FeS clusters can also be found in organisms that do not fix nitrogen [].This entry represents the C-terminal of NifU and homologous proteins. NifU contains two domains: an N-terminal () and a C-terminal domain []. These domains exist either together or on different polypeptides, both domains being found in organisms that do not fix nitrogen (e.g. yeast), so they have a broader significance in the cell than nitrogen fixation. |
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| Protein Domain |
| Type: |
Homologous_superfamily |
| Description: |
Iron-sulphur (FeS) clusters are important cofactors for numerous proteins involved in electron transfer, in redox and non-redox catalysis, in gene regulation, and as sensors of oxygen and iron. These functions depend on the various FeS cluster prosthetic groups, the most common being [2Fe-2S]and [4Fe-4S][]. FeS cluster assembly is a complex process involving the mobilisation of Fe and S atoms from storage sources, their assembly into [Fe-S]form, their transport to specific cellular locations, and their transfer to recipient apoproteins. So far, three FeS assembly machineries have been identified, which are capable of synthesising all types of [Fe-S]clusters: ISC (iron-sulphur cluster), SUF (sulphur assimilation), and NIF (nitrogen fixation) systems.The ISC system is conserved in eubacteria and eukaryotes (mitochondria), and has broad specificity, targeting general FeS proteins [, ]. It is encoded by the isc operon (iscRSUA-hscBA-fdx-iscX). IscS is a cysteine desulphurase, which obtains S from cysteine (converting it to alanine) and serves as a S donor for FeS cluster assembly. IscU and IscA act as scaffolds to accept S and Fe atoms, assembling clusters and transfering them to recipient apoproteins. HscA is a molecular chaperone and HscB is a co-chaperone. Fdx is a [2Fe-2S]-type ferredoxin. IscR is a transcription factor that regulates expression of the isc operon. IscX (also known as YfhJ) appears to interact with IscS and may function as an Fe donor during cluster assembly [].The SUF system is an alternative pathway to the ISC system that operates under iron starvation and oxidative stress. It is found in eubacteria, archaea and eukaryotes (plastids). The SUF system is encoded by the suf operon (sufABCDSE), and the six encoded proteins are arranged into two complexes (SufSE and SufBCD) and one protein (SufA). SufS is a pyridoxal-phosphate (PLP) protein displaying cysteine desulphurase activity. SufE acts as a scaffold protein that accepts S from SufS and donates it to SufA []. SufC is an ATPase with an unorthodox ATP-binding cassette (ABC)-like component. SufA is homologous to IscA [], acting 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.In the NIF system, NifS and NifU are required for the formation of metalloclusters of nitrogenase in Azotobacter vinelandii, and other organisms, as well as in the maturation of other FeS proteins. Nitrogenase catalyses the fixation of nitrogen. It contains a complex cluster, the FeMo cofactor, which contains molybdenum, Fe and S. NifS is a cysteine desulphurase. NifU binds one Fe atom at its N-terminal, assembling an FeS cluster that is transferred to nitrogenase apoproteins []. Nif proteins involved in the formation of FeS clusters can also be found in organisms that do not fix nitrogen [].This entry represents SufB and SufD proteins, which are homologous, and form part of the SufBCD complex in the SUF system []. SufB accepts sulfur transferred from SufE [], whereas SufD may play a role in iron acquisition []. |
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| Protein Domain |
| Type: |
Family |
| Description: |
Iron-sulphur(FeS) clusters are important cofactors for numerous proteins involved in electron transfer, in redox and non-redox catalysis, in gene regulation, and as sensors of oxygen and iron. These functions depend on the various FeS cluster prosthetic groups, the most common being [2Fe-2S]and [4Fe-4S][]. FeS cluster assembly is a complex process involving the mobilisation of Fe and S atoms from storage sources, their assembly into [Fe-S]form, their transport to specific cellular locations, and their transfer to recipient apoproteins. So far, three FeS assembly machineries have been identified, which are capable of synthesising all types of [Fe-S]clusters: ISC (iron-sulphur cluster), SUF (sulphur assimilation), and NIF (nitrogen fixation) systems.The ISC system is conserved in eubacteria and eukaryotes (mitochondria), and has broad specificity, targeting general FeS proteins [, ]. It is encoded by the isc operon (iscRSUA-hscBA-fdx-iscX). IscS is a cysteine desulphurase, which obtains S from cysteine (converting it to alanine) and serves as a S donor for FeS cluster assembly. IscU and IscA act as scaffolds to accept S and Fe atoms, assembling clusters and transfering them to recipient apoproteins. HscA is a molecular chaperone and HscB is a co-chaperone. Fdx is a [2Fe-2S]-type ferredoxin. IscR is a transcription factor that regulates expression of the isc operon. IscX (also known as YfhJ) appears to interact with IscS and may function as an Fe donor during cluster assembly [].The SUF system is an alternative pathway to the ISC system that operates under iron starvation and oxidative stress. It is found in eubacteria, archaea and eukaryotes (plastids). The SUF system is encoded by the suf operon (sufABCDSE), and the six encoded proteins are arranged into two complexes (SufSE and SufBCD) and one protein (SufA). SufS is a pyridoxal-phosphate (PLP) protein displaying cysteine desulphurase activity. SufE acts as a scaffold protein that accepts S from SufS and donates it to SufA []. SufC is an ATPase with an unorthodox ATP-binding cassette (ABC)-like component. SufA is homologous to IscA [], acting 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.In the NIF system, NifS and NifU are required for the formation of metalloclusters of nitrogenase in Azotobacter vinelandii, and other organisms, as well as in the maturation of other FeS proteins. Nitrogenase catalyses the fixation of nitrogen. It contains a complex cluster, the FeMo cofactor, which contains molybdenum, Fe and S. NifS is a cysteine desulphurase. NifU binds one Fe atom at its N-terminal, assembling an FeS cluster that is transferred to nitrogenase apoproteins []. Nif proteins involved in the formation of FeS clusters can also be found in organisms that do not fix nitrogen [].This entry represents IscU from the ISC system, a homologue of the N-terminal region of NifU (NIF system), an Fe-S cluster assembly protein found mostly in nitrogen-fixing bacteria. IscU is a scaffold protein on which Fe-S clusters are assembled before transfer to apoproteins []. This family includes largely proteobacterial and eukaryotic forms and excludes the true NifU proteins from Klebsiella sp. and Anabaena sp. as well as the archaeal homologues. |
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| Protein Domain |
| Type: |
Domain |
| Description: |
Iron-sulphur (FeS) clusters are important cofactors for numerous proteins involved in electron transfer, in redox and non-redox catalysis, in gene regulation, and as sensors of oxygen and iron. These functions depend on the various FeS cluster prosthetic groups, the most common being [2Fe-2S]and [4Fe-4S][]. FeS cluster assembly is a complex process involving the mobilisation of Fe and S atoms from storage sources, their assembly into [Fe-S]form, their transport to specific cellular locations, and their transfer to recipient apoproteins. So far, three FeS assembly machineries have been identified, which are capable of synthesising all types of [Fe-S]clusters: ISC (iron-sulphur cluster), SUF (sulphur assimilation), and NIF (nitrogen fixation) systems.The ISC system is conserved in eubacteria and eukaryotes (mitochondria), and has broad specificity, targeting general FeS proteins [, ]. It is encoded by the isc operon (iscRSUA-hscBA-fdx-iscX). IscS is a cysteine desulphurase, which obtains S from cysteine (converting it to alanine) and serves as a S donor for FeS cluster assembly. IscU and IscA act as scaffolds to accept S and Fe atoms, assembling clusters and transfering them to recipient apoproteins. HscA is a molecular chaperone and HscB is a co-chaperone. Fdx is a [2Fe-2S]-type ferredoxin. IscR is a transcription factor that regulates expression of the isc operon. IscX (also known as YfhJ) appears to interact with IscS and may function as an Fe donor during cluster assembly [].The SUF system is an alternative pathway to the ISC system that operates under iron starvation and oxidative stress. It is found in eubacteria, archaea and eukaryotes (plastids). The SUF system is encoded by the suf operon (sufABCDSE), and the six encoded proteins are arranged into two complexes (SufSE and SufBCD) and one protein (SufA). SufS is a pyridoxal-phosphate (PLP) protein displaying cysteine desulphurase activity. SufE acts as a scaffold protein that accepts S from SufS and donates it to SufA []. SufC is an ATPase with an unorthodox ATP-binding cassette (ABC)-like component. SufA is homologous to IscA [], acting 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.In the NIF system, NifS and NifU are required for the formation of metalloclusters of nitrogenase in Azotobacter vinelandii, and other organisms, as well as in the maturation of other FeS proteins. Nitrogenase catalyses the fixation of nitrogen. It contains a complex cluster, the FeMo cofactor, which contains molybdenum, Fe and S. NifS is a cysteine desulphurase. NifU binds one Fe atom at its N-terminal, assembling an FeS cluster that is transferred to nitrogenase apoproteins []. Nif proteins involved in the formation of FeS clusters can also be found in organisms that do not fix nitrogen [].This entry represents SufB and SufD proteins, which are homologous, and form part of the SufBCD complex in the SUF system []. SufB accepts sulfur transferred from SufE [], whereas SufD mayplay a role in iron acquisition [].This domain is found at the N-terminal part of the SufB and SufD proteins, which has a right-handed parallel beta helix structure []. |
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| Publication |
| First Author: |
Dombrecht B |
| Year: |
2002 |
| Journal: |
Mol Genet Genomics |
| Title: |
The Rhizobium etli gene iscN is highly expressed in bacteroids and required for nitrogen fixation. |
| Volume: |
267 |
| Issue: |
6 |
| Pages: |
820-8 |
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| Protein Domain |
| Type: |
Conserved_site |
| Description: |
These proteins in this entry are small (106 to 135 amino-acid residues in bacteria, about 200 residues in fungi) that contain a number of conserved regions. They appear to be associated with the process of FeS-cluster assembly. The HesB proteins are associated with the nif gene cluster and the Rhizobium gene IscN has been shown to be required for nitrogen fixation []. Nitrogenase includes multiple FeS clusters and many genes for their assembly. The Escherichia coli SufA protein is associated with SufS, a NifS homologue and SufD which are involved in the FeS cluster assembly of the FhnF protein []. The Azotobacter protein IscA (homologues of which are also found in E. coli) is associated which IscS, another NifS homologue and IscU, a nifU homologue as well as other factors consistent with a role in FeS cluster chemistry []. A homologue from Geobacter contains a selenocysteine in place of an otherwise invariant cysteine, further suggesting a role in redox chemistry.This entry represents a conserved site in the C-terminal extremity, it contains two conserved cysteines. |
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| Publication |
| First Author: |
Nicolet Y |
| Year: |
2000 |
| Journal: |
Trends Biochem Sci |
| Title: |
A novel FeS cluster in Fe-only hydrogenases. |
| Volume: |
25 |
| Issue: |
3 |
| Pages: |
138-43 |
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| Protein Domain |
| Type: |
Family |
| Description: |
Iron-sulphur (FeS) clusters are important cofactors for numerous proteins involved in electron transfer, in redox and non-redox catalysis, in gene regulation, and as sensors of oxygen and iron. These functions depend on the various FeS cluster prosthetic groups, the most common being [2Fe-2S]and [4Fe-4S][]. FeS cluster assembly is a complex process involving the mobilisation of Fe and S atoms from storage sources, their assembly into [Fe-S]form, their transport to specific cellular locations, and their transfer to recipient apoproteins. So far, three FeS assembly machineries have been identified, which are capable of synthesising all types of [Fe-S]clusters: ISC (iron-sulphur cluster), SUF (sulphur assimilation), and NIF (nitrogen fixation) systems.The SUF system is an alternative pathway to the ISC system that operates under iron starvation and oxidative stress. It is found in eubacteria, archaea and eukaryotes (plastids). The SUF system is encoded by the suf operon (sufABCDSE), and the six encoded proteins are arranged into two complexes (SufSE and SufBCD) and one protein (SufA). SufS is a pyridoxal-phosphate (PLP) protein displaying cysteine desulphurase activity. SufE acts as a scaffold protein that accepts S from SufS and donates it to SufA []. SufC is an ATPase with an unorthodox ATP-binding cassette (ABC)-like component. SufA is homologous to IscA [], acting 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.This entry represents SufB and SufD proteins, which are homologous, and form part of the SufBCD complex in the SUF system []. SufB accepts sulfur transferred from SufE [], whereas SufD may play a role in iron acquisition []. |
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| Protein Domain |
| Type: |
Family |
| Description: |
This entry represents iron-sulphur cluster insertion proteins ErpA. It is an A-type Fe-S protein with an essential role in cellular metabolism []and is required in Escherichia coli for the delivery of iron-sulphur clusters to the hydrogen-oxidizing [NiFe]-hydrogenases []. |
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| Publication |
| First Author: |
Zheng L |
| Year: |
1998 |
| Journal: |
J Biol Chem |
| Title: |
Assembly of iron-sulfur clusters. Identification of an iscSUA-hscBA-fdx gene cluster from Azotobacter vinelandii. |
| Volume: |
273 |
| Issue: |
21 |
| Pages: |
13264-72 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Pastore C |
| Year: |
2006 |
| Journal: |
Structure |
| Title: |
YfhJ, a molecular adaptor in iron-sulfur cluster formation or a frataxin-like protein? |
| Volume: |
14 |
| Issue: |
5 |
| Pages: |
857-67 |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Iron-sulphur (FeS) clusters are important cofactors for numerous proteins involved in electron transfer, in redox and non-redox catalysis, in gene regulation, and as sensors of oxygen and iron. These functions depend on the various FeS cluster prosthetic groups, the most common being [2Fe-2S]and [4Fe-4S][]. FeS cluster assembly is a complex process involving the mobilisation of Fe and S atoms from storage sources, their assembly into [Fe-S]form, their transport to specific cellular locations, and their transfer to recipient apoproteins. So far, three FeS assembly machineries have been identified, which are capable of synthesising all types of [Fe-S]clusters: ISC (iron-sulphur cluster), SUF (sulphur assimilation), and NIF (nitrogen fixation) systems.The ISC system is conserved in eubacteria and eukaryotes (mitochondria), and has broad specificity, targeting general FeS proteins [, ]. It is encoded by the isc operon (iscRSUA-hscBA-fdx-iscX). IscS is a cysteine desulphurase, which obtains S from cysteine (converting it to alanine) and serves as a S donor for FeS cluster assembly. IscU and IscA act as scaffolds to accept S and Fe atoms, assembling clusters and transfering them to recipient apoproteins. HscA is a molecular chaperone and HscB is a co-chaperone. Fdx is a [2Fe-2S]-type ferredoxin. IscR is a transcription factor that regulates expression of the isc operon. IscX (also known as YfhJ) appears to interact with IscS and may function as an Fe donor during cluster assembly [].The SUF system is an alternative pathway to the ISC system that operates under iron starvation and oxidative stress. It is found in eubacteria, archaea and eukaryotes (plastids). The SUF system is encoded by the suf operon (sufABCDSE), and the six encoded proteins are arranged into two complexes (SufSE and SufBCD) and one protein (SufA). SufS is a pyridoxal-phosphate (PLP) protein displaying cysteine desulphurase activity. SufE acts as a scaffold protein that accepts S from SufS and donates it to SufA []. SufC is an ATPase with an unorthodox ATP-binding cassette (ABC)-like component. SufA is homologous to IscA [], acting 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.In the NIF system, NifS and NifU are required for the formation of metalloclusters of nitrogenase in Azotobacter vinelandii, and other organisms, as well as in the maturation of other FeS proteins. Nitrogenase catalyses the fixation of nitrogen. It contains a complex cluster, the FeMo cofactor, which contains molybdenum, Fe and S. NifS is a cysteine desulphurase. NifU binds one Fe atom at its N-terminal, assembling an FeS cluster that is transferred to nitrogenase apoproteins []. Nif proteins involved in the formation of FeS clusters can also be found in organisms that do not fix nitrogen [].This entry represents members of the SufR cyanobacterial protein family of transcriptional regulators that control the SUF system. In all cases, the sufR gene is encoded near SUF system genes but in the opposite direction. This DNA-binding protein belongs to the DeoR family of helix-loop-helix proteins. All members also have a probable metal-binding motif C-X(12)-C-X(13)-C-X(14)-C near the C terminus. |
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•
•
•
•
•
|
| Publication |
| First Author: |
Liu H |
| Year: |
2008 |
| Journal: |
Cell |
| Title: |
Structure of the DNA repair helicase XPD. |
| Volume: |
133 |
| Issue: |
5 |
| Pages: |
801-12 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Fan L |
| Year: |
2008 |
| Journal: |
Cell |
| Title: |
XPD helicase structures and activities: insights into the cancer and aging phenotypes from XPD mutations. |
| Volume: |
133 |
| Issue: |
5 |
| Pages: |
789-800 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Rudolf J |
| Year: |
2006 |
| Journal: |
Mol Cell |
| Title: |
The DNA repair helicases XPD and FancJ have essential iron-sulfur domains. |
| Volume: |
23 |
| Issue: |
6 |
| Pages: |
801-8 |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Homologous_superfamily |
| Description: |
XPD belongs to a family of ATP-dependent helicases that are characterised by a 'D-E-A-H' motif []. This resembles the 'D-E-A-D-box' of other known helicases, which represents a special version of the B motif of ATP-binding proteins. In XPD, His replaces the second Asp.XPD is divided into four domains. The first three domains together with α-helix 22 from domain 4 form a donut-shaped structure containing a hole []. Domains 1 and 4 represent the RecA-like fold that is present in all helicases of superfamilies 1 and 2 (SF1 and SF2) []. Domains 2 and 3 are insertions, which emerge from domain 1. Domain 2 displays an exclusively α-helical architecture consisting of six α-helices and one 3-10 helix that surround the central 4Fe4S cluster. The FeS cluster is coordinated by four cysteines, consistent with the coordination typically observed in 4Fe4S clusters []. The FeS domain is vital for its helicase activity and might be involved in the damage recognition process [, , , ].This entry represents the FeS cluster domain found in XPD family members that are mostly from bacteria and archaea. |
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•
•
•
•
•
|
| Publication |
| First Author: |
Loiseau L |
| Year: |
2007 |
| Journal: |
Proc Natl Acad Sci U S A |
| Title: |
ErpA, an iron sulfur (Fe S) protein of the A-type essential for respiratory metabolism in Escherichia coli. |
| Volume: |
104 |
| Issue: |
34 |
| Pages: |
13626-31 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Pinske C |
| Year: |
2012 |
| Journal: |
PLoS One |
| Title: |
Delivery of iron-sulfur clusters to the hydrogen-oxidizing [NiFe]-hydrogenases in Escherichia coli requires the A-type carrier proteins ErpA and IscA. |
| Volume: |
7 |
| Issue: |
2 |
| Pages: |
e31755 |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
The function of these proteins is unknown but they are almost always encoded in operons for the SUF system of iron-sulphur cluster biosynthesis. In a few species the SUF system is present elsewhere on the chromosome. This group shares this property of association with the SUF system with a related group, . These groups of proteins both share a domain of unknown function which covers the whole protein in but only the C-terminal portion of proteins in this entry, which have an additional unique uncharacterised N-terminal domain. As these proteins are encoded immediately downstream of the cysteine desulphurase gene sufS in many contexts, they have been deignated SufT. Homologous proteins not covered by this entry or are found in operons associated with phenylacetic acid (or other ring-hydroxylating) degradation pathways. |
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•
•
•
•
•
|
| Interaction Experiment |
| Description: |
The Fes protein-tyrosine kinase phosphorylates a subset of macrophage proteins that are involved in cell adhesion and cell-cell signaling. |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
168
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
136
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Ouzounis C |
| Year: |
1994 |
| Journal: |
Trends Biochem Sci |
| Title: |
The modular structure of NifU proteins. |
| Volume: |
19 |
| Issue: |
5 |
| Pages: |
199-200 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Chandramouli K |
| Year: |
2006 |
| Journal: |
Biochemistry |
| Title: |
HscA and HscB stimulate [2Fe-2S] cluster transfer from IscU to apoferredoxin in an ATP-dependent reaction. |
| Volume: |
45 |
| Issue: |
37 |
| Pages: |
11087-95 |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
129
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
154
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
146
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
129
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Patzer SI |
| Year: |
1999 |
| Journal: |
J Bacteriol |
| Title: |
SufS is a NifS-like protein, and SufD is necessary for stability of the [2Fe-2S] FhuF protein in Escherichia coli. |
| Volume: |
181 |
| Issue: |
10 |
| Pages: |
3307-9 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Layer G |
| Year: |
2007 |
| Journal: |
J Biol Chem |
| Title: |
SufE transfers sulfur from SufS to SufB for iron-sulfur cluster assembly. |
| Volume: |
282 |
| Issue: |
18 |
| Pages: |
13342-50 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Saini A |
| Year: |
2010 |
| Journal: |
Biochemistry |
| Title: |
SufD and SufC ATPase activity are required for iron acquisition during in vivo Fe-S cluster formation on SufB. |
| Volume: |
49 |
| Issue: |
43 |
| Pages: |
9402-12 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Hirabayashi K |
| Year: |
2015 |
| Journal: |
J Biol Chem |
| Title: |
Functional Dynamics Revealed by the Structure of the SufBCD Complex, a Novel ATP-binding Cassette (ABC) Protein That Serves as a Scaffold for Iron-Sulfur Cluster Biogenesis. |
| Volume: |
290 |
| Issue: |
50 |
| Pages: |
29717-31 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Voisset E |
| Year: |
2007 |
| Journal: |
Blood |
| Title: |
The tyrosine kinase FES is an essential effector of KITD816V proliferation signal. |
| Volume: |
110 |
| Issue: |
7 |
| Pages: |
2593-9 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Madueño F |
| Year: |
1992 |
| Journal: |
Plant Mol Biol |
| Title: |
Import and processing of the precursor of the Rieske FeS protein of tobacco chloroplasts. |
| Volume: |
20 |
| Issue: |
2 |
| Pages: |
289-99 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Mashruwala AA |
| Year: |
2016 |
| Journal: |
PLoS Genet |
| Title: |
The DUF59 Containing Protein SufT Is Involved in the Maturation of Iron-Sulfur (FeS) Proteins during Conditions of High FeS Cofactor Demand in Staphylococcus aureus. |
| Volume: |
12 |
| Issue: |
8 |
| Pages: |
e1006233 |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
255
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
256
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Matos CF |
| Year: |
2009 |
| Journal: |
EMBO Rep |
| Title: |
TatD is a central component of a Tat translocon-initiated quality control system for exported FeS proteins in Escherichia coli. |
| Volume: |
10 |
| Issue: |
5 |
| Pages: |
474-9 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Hänzelmann P |
| Year: |
2006 |
| Journal: |
Proc Natl Acad Sci U S A |
| Title: |
Binding of 5'-GTP to the C-terminal FeS cluster of the radical S-adenosylmethionine enzyme MoaA provides insights into its mechanism. |
| Volume: |
103 |
| Issue: |
18 |
| Pages: |
6829-34 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Harosh I |
| Year: |
1991 |
| Journal: |
Nucleic Acids Res |
| Title: |
The RAD3 gene is a member of the DEAH family RNA helicase-like protein. |
| Volume: |
19 |
| Issue: |
22 |
| Pages: |
6331 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Gabellini N |
| Year: |
1986 |
| Journal: |
Eur J Biochem |
| Title: |
Nucleotide sequence and transcription of the fbc operon from Rhodopseudomonas sphaeroides. Evaluation of the deduced amino acid sequences of the FeS protein, cytochrome b and cytochrome c1. |
| Volume: |
154 |
| Issue: |
3 |
| Pages: |
569-79 |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Singleton MR |
| Year: |
2007 |
| Journal: |
Annu Rev Biochem |
| Title: |
Structure and mechanism of helicases and nucleic acid translocases. |
| Volume: |
76 |
|
| Pages: |
23-50 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Barras F |
| Year: |
2005 |
| Journal: |
Adv Microb Physiol |
| Title: |
How Escherichia coli and Saccharomyces cerevisiae build Fe/S proteins. |
| Volume: |
50 |
|
| Pages: |
41-101 |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Hwang DM |
| Year: |
1996 |
| Journal: |
J Mol Evol |
| Title: |
A modular domain of NifU, a nitrogen fixation cluster protein, is highly conserved in evolution. |
| Volume: |
43 |
| Issue: |
5 |
| Pages: |
536-40 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Seidler A |
| Year: |
2001 |
| Journal: |
Biochem Soc Trans |
| Title: |
Incorporation of iron-sulphur clusters in membrane-bound proteins. |
| Volume: |
29 |
| Issue: |
Pt 4 |
| Pages: |
418-21 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Fontecave M |
| Year: |
2005 |
| Journal: |
J Biol Inorg Chem |
| Title: |
Mechanisms of iron-sulfur cluster assembly: the SUF machinery. |
| Volume: |
10 |
| Issue: |
7 |
| Pages: |
713-21 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Lill R |
| Year: |
2006 |
| Journal: |
Biochim Biophys Acta |
| Title: |
Mechanisms of iron-sulfur protein maturation in mitochondria, cytosol and nucleus of eukaryotes. |
| Volume: |
1763 |
| Issue: |
7 |
| Pages: |
652-67 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Shimomura Y |
| Year: |
2005 |
| Journal: |
Proteins |
| Title: |
Crystal structure of Escherichia coli YfhJ protein, a member of the ISC machinery involved in assembly of iron-sulfur clusters. |
| Volume: |
60 |
| Issue: |
3 |
| Pages: |
566-9 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Sendra M |
| Year: |
2007 |
| Journal: |
FEBS Lett |
| Title: |
The SUF iron-sulfur cluster biosynthetic machinery: sulfur transfer from the SUFS-SUFE complex to SUFA. |
| Volume: |
581 |
| Issue: |
7 |
| Pages: |
1362-8 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Ollagnier-de-Choudens S |
| Year: |
2004 |
| Journal: |
J Biol Inorg Chem |
| Title: |
SufA/IscA: reactivity studies of a class of scaffold proteins involved in [Fe-S] cluster assembly. |
| Volume: |
9 |
| Issue: |
7 |
| Pages: |
828-38 |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
This entry represents the C-terminal domain of Hydrogen maturase F (HydF) from Thermotoga neapolitana. HydF is a GTPase that contains an FeS cluster-binding motif and is able to activate HydA production. This domain is known as domain III and is primarily responsible for homotetramer formation. Interactions between the two FeS cluster-binding domains are the interactions between the beta-2 strands, the initial part of the long loop that connects strand beta-2 to strand beta-3, and the loop that connects strand beta-1 to helix alpha-3. There are three highly conserved cysteine residues (Cys-302, Cys-353, and Cys-356) that represent the FeS cluster-binding site which form a superficial pocket []. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
Iron-sulphur (FeS) clusters are important cofactors for numerous proteins involved in electron transfer, in redox and non-redox catalysis, in gene regulation, and as sensors of oxygen and iron. These functions depend on the various FeS cluster prosthetic groups, the most common being [2Fe-2S]and [4Fe-4S][]. FeS cluster assembly is a complex process involving the mobilisation of Fe and S atoms from storage sources, their assembly into [Fe-S]form, their transport to specific cellular locations, and their transfer to recipient apoproteins. So far, three FeS assembly machineries have been identified, which are capable of synthesising all types of [Fe-S]clusters: ISC (iron-sulphur cluster), SUF (sulphur assimilation), and NIF (nitrogen fixation) systems.In the NIF system, NifS and NifU are required for the formation of metalloclusters of nitrogenase in Azotobacter vinelandii, and other organisms, as well as in the maturation of other FeS proteins. Nitrogenase catalyses the fixation of nitrogen. It contains a complex cluster, the FeMo cofactor, which contains molybdenum, Fe and S. NifS is a cysteine desulphurase. NifU binds one Fe atom at its N-terminal, assembling an FeS cluster that is transferred to nitrogenase apoproteins []. Nif proteins involved in the formation of FeS clusters can also be found in organisms that do not fix nitrogen [].This domain is found at the N terminus of NifU (from NIF system) and NifU related proteins, and in the human Nfu protein. Both of these proteins are thought to be involved in the assembly of iron-sulphur clusters, functioning as scaffolds [, ]. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Homologous_superfamily |
| Description: |
Iron-sulphur (FeS) clusters are important cofactors for numerous proteins involved in electron transfer, in redox and non-redox catalysis, in gene regulation, and as sensors of oxygen and iron. These functions depend on the various FeS cluster prosthetic groups, the most common being [2Fe-2S]and [4Fe-4S][]. FeS cluster assembly is a complex process involving the mobilisation of Fe and S atoms from storage sources, their assembly into [Fe-S]form, their transport to specific cellular locations, and their transfer to recipient apoproteins. So far, three FeS assembly machineries have been identified, which are capable of synthesising all types of [Fe-S]clusters: ISC (iron-sulphur cluster), SUF (sulphur assimilation), and NIF (nitrogen fixation) systems.In the NIF system, NifS and NifU are required for the formation of metalloclusters of nitrogenase in Azotobacter vinelandii, and other organisms, as well as in the maturation of other FeS proteins. Nitrogenase catalyses the fixation of nitrogen. It contains a complex cluster, the FeMo cofactor, which contains molybdenum, Fe and S. NifS is a cysteine desulphurase. NifU binds one Fe atom at its N-terminal, assembling an FeS cluster that is transferred to nitrogenase apoproteins []. Nif proteins involved in the formation of FeS clusters can also be found in organisms that do not fix nitrogen [].This domain is found at the N terminus of NifU (from NIF system) and NifU related proteins, and in the human Nfu protein. Both of these proteins are thought to be involved in the assembly of iron-sulphur clusters, functioning as scaffolds [, ]. |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
255
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Tong WH |
| Year: |
2003 |
| Journal: |
Proc Natl Acad Sci U S A |
| Title: |
Subcellular compartmentalization of human Nfu, an iron-sulfur cluster scaffold protein, and its ability to assemble a [4Fe-4S] cluster. |
| Volume: |
100 |
| Issue: |
17 |
| Pages: |
9762-7 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Dos Santos PC |
| Year: |
2004 |
| Journal: |
J Biol Chem |
| Title: |
Iron-sulfur cluster assembly: NifU-directed activation of the nitrogenase Fe protein. |
| Volume: |
279 |
| Issue: |
19 |
| Pages: |
19705-11 |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Homologous_superfamily |
| Description: |
Iron-sulphur (FeS) clusters are important cofactors for numerous proteins involved in electron transfer, in redox and non-redox catalysis, in gene regulation, and as sensors of oxygen and iron. These functions depend on the various FeS cluster prosthetic groups, the most common being [2Fe-2S]and [4Fe-4S][]. FeS cluster assembly is a complex process involving the mobilisation of Fe and S atoms from storage sources, their assembly into [Fe-S]form, their transport to specific cellular locations, and their transfer to recipient apoproteins. So far, three FeS assembly machineries have been identified, which are capable of synthesising all types of [Fe-S]clusters: ISC (iron-sulphur cluster), SUF (sulphur assimilation), and NIF (nitrogen fixation) systems.The ISC system is conserved in eubacteria and eukaryotes (mitochondria), and has broad specificity, targeting general FeS proteins [, ]. It is encoded by the isc operon (iscRSUA-hscBA-fdx-iscX). IscS is a cysteine desulphurase, which obtains S from cysteine (converting it to alanine) and serves as a S donor for FeS cluster assembly. IscU and IscA act as scaffolds to accept S and Fe atoms, assembling clusters and transfering them to recipient apoproteins. HscA is a molecular chaperone and HscB is a co-chaperone. Fdx is a [2Fe-2S]-type ferredoxin. IscR is a transcription factor that regulates expression of the isc operon. IscX (also known as YfhJ) appears to interact with IscS and may function as an Fe donor during cluster assembly [].The SUF system is an alternative pathway to the ISC system that operates under iron starvation and oxidative stress. It is found in eubacteria, archaea and eukaryotes (plastids). The SUF system is encoded by the suf operon (sufABCDSE), and the six encoded proteins are arranged into two complexes (SufSE and SufBCD) and oneprotein (SufA). SufS is a pyridoxal-phosphate (PLP) protein displaying cysteine desulphurase activity. SufE acts as a scaffold protein that accepts S from SufS and donates it to SufA []. SufC is an ATPase with an unorthodox ATP-binding cassette (ABC)-like component. SufA is homologous to IscA [], acting 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.In the NIF system, NifS and NifU are required for the formation of metalloclusters of nitrogenase in Azotobacter vinelandii, and other organisms, as well as in the maturation of other FeS proteins. Nitrogenase catalyses the fixation of nitrogen. It contains a complex cluster, the FeMo cofactor, which contains molybdenum, Fe and S. NifS is a cysteine desulphurase. NifU binds one Fe atom at its N-terminal, assembling an FeS cluster that is transferred to nitrogenase apoproteins []. Nif proteins involved in the formation of FeS clusters can also be found in organisms that do not fix nitrogen []. |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Bange G |
| Year: |
2011 |
| Journal: |
Nat Struct Mol Biol |
| Title: |
Structural basis for the molecular evolution of SRP-GTPase activation by protein. |
| Volume: |
18 |
| Issue: |
12 |
| Pages: |
1376-80 |
|
•
•
•
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•
|
| Publication |
| First Author: |
Camire EJ |
| Year: |
2015 |
| Journal: |
J Biol Chem |
| Title: |
The Yeast Nbp35-Cfd1 Cytosolic Iron-Sulfur Cluster Scaffold Is an ATPase. |
| Volume: |
290 |
| Issue: |
39 |
| Pages: |
23793-802 |
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•
•
|
| Publication |
| First Author: |
Cendron L |
| Year: |
2011 |
| Journal: |
J Biol Chem |
| Title: |
Crystal structure of HydF scaffold protein provides insights into [FeFe]-hydrogenase maturation. |
| Volume: |
286 |
| Issue: |
51 |
| Pages: |
43944-50 |
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•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
This family contains YlxH (also annotated FleN/FlhG), which regules aspects of flagellar assembly, placement and number [, ]. YlxH/FlhG activates the SRP-GTPase FlhF []. This family also contains members of the MRP/Nbp35 class of iron-sulfur (FeS) cluster scaffolds, such as Nbp35 and Cfd1, that function to assemble nascent FeS clusters for transfer to FeS-requiring enzymes. They have been identified as ATPases []. |
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•
•
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| Protein Domain |
| Type: |
Family |
| Description: |
Members of this protein family, to date, are found in a completed prokaryotic genome if and only if the species is one of the archaeal methanogens. The exact function is unknown, but likely is linked to methanogenesis or a process closely connected to it. This protein is a predicted to bind FeS clusters, based on the presence of a 4Fe-4S domain (). |
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| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
163
|
| Fragment?: |
false |
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•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
160
|
| Fragment?: |
false |
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•
•
•
•
•
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| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
136
|
| Fragment?: |
false |
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•
•
•
•
|
| Publication |
| First Author: |
Yeo WS |
| Year: |
2006 |
| Journal: |
Mol Microbiol |
| Title: |
IscR acts as an activator in response to oxidative stress for the suf operon encoding Fe-S assembly proteins. |
| Volume: |
61 |
| Issue: |
1 |
| Pages: |
206-18 |
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•
•
•
•
•
|
| Publication |
| First Author: |
Giel JL |
| Year: |
2006 |
| Journal: |
Mol Microbiol |
| Title: |
IscR-dependent gene expression links iron-sulphur cluster assembly to the control of O2-regulated genes in Escherichia coli. |
| Volume: |
60 |
| Issue: |
4 |
| Pages: |
1058-75 |
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•
•
•
•
•
|
| Publication |
| First Author: |
Ollagnier-de-Choudens S |
| Year: |
2001 |
| Journal: |
J Biol Chem |
| Title: |
Iron-sulfur cluster assembly: characterization of IscA and evidence for a specific and functional complex with ferredoxin. |
| Volume: |
276 |
| Issue: |
25 |
| Pages: |
22604-7 |
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•
•
•
•
•
|
| Publication |
| First Author: |
Tokumoto U |
| Year: |
2001 |
| Journal: |
J Biochem |
| Title: |
Genetic analysis of the isc operon in Escherichia coli involved in the biogenesis of cellular iron-sulfur proteins. |
| Volume: |
130 |
| Issue: |
1 |
| Pages: |
63-71 |
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•
•
•
•
•
|
| Publication |
| First Author: |
Morimoto K |
| Year: |
2006 |
| Journal: |
J Mol Biol |
| Title: |
The asymmetric IscA homodimer with an exposed [2Fe-2S] cluster suggests the structural basis of the Fe-S cluster biosynthetic scaffold. |
| Volume: |
360 |
| Issue: |
1 |
| Pages: |
117-32 |
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•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Iron-sulphur (FeS) clusters are important cofactors for numerous proteins involved in electron transfer, in redox and non-redox catalysis, in gene regulation, and as sensors of oxygen and iron. These functions depend on the various FeS cluster prosthetic groups, the most common being [2Fe-2S]and [4Fe-4S][]. FeS cluster assembly is a complex process involving the mobilisation of Fe and S atoms from storage sources, their assembly into [Fe-S]form, their transport to specific cellular locations, and their transfer to recipient apoproteins. So far, three FeS assembly machineries have been identified, which are capable of synthesising all types of [Fe-S]clusters: ISC (iron-sulphur cluster), SUF (sulphur assimilation), and NIF (nitrogen fixation) systems.The ISC system is conserved in eubacteria and eukaryotes (mitochondria), and has broad specificity, targeting general FeS proteins [, ]. It is encoded by the isc operon (iscRSUA-hscBA-fdx-iscX). IscS is a cysteine desulphurase, which obtains S from cysteine (converting it to alanine) and serves as a S donor for FeS cluster assembly. IscU and IscA act as scaffolds to accept S and Fe atoms, assembling clusters and transfering them to recipient apoproteins. HscA is a molecular chaperone and HscB is a co-chaperone. Fdx is a [2Fe-2S]-type ferredoxin. IscR is a transcription factor that regulates expression of the isc operon. IscX (also known as YfhJ) appears to interact with IscS and may function as an Fe donor during cluster assembly [].The SUF system is an alternative pathway to the ISC system that operates under iron starvation and oxidative stress. It is found in eubacteria, archaea and eukaryotes (plastids). The SUF system is encoded by the suf operon (sufABCDSE), and the six encoded proteins are arranged into two complexes (SufSE and SufBCD) and one protein (SufA). SufS is a pyridoxal-phosphate (PLP) protein displaying cysteine desulphurase activity. SufE acts as a scaffold protein that accepts S from SufS and donates it to SufA []. SufC is an ATPase with an unorthodox ATP-binding cassette (ABC)-like component. SufA is homologous to IscA [], acting 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.In the NIF system, NifS and NifU are required for the formation of metalloclusters of nitrogenase in Azotobacter vinelandii, and other organisms, as well as in the maturation of other FeS proteins. Nitrogenase catalyses the fixation of nitrogen. It contains a complex cluster, the FeMo cofactor, which contains molybdenum, Fe and S. NifS is a cysteine desulphurase. NifU binds one Fe atom at its N-terminal, assembling an FeS cluster that is transferred to nitrogenase apoproteins []. Nif proteins involved in the formation of FeS clusters can also be found in organisms that do not fix nitrogen [].This entry represents the IscA component of the ISC system for iron-sulphur cluster assembly. IscA is believed to act as a scaffold upon which 2Fe-2S clusters are assembled and subsequently transferred to ferredoxin [, , ]. This clade is limited to the proteobacteria. |
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•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Iron-sulphur (FeS) clusters are important cofactors for numerous proteins involved in electron transfer, in redox and non-redox catalysis, in gene regulation, and as sensors of oxygen and iron. These functions depend on the various FeS cluster prosthetic groups, the most common being [2Fe-2S]and [4Fe-4S][]. FeS cluster assembly is a complex process involving the mobilisation of Fe and S atoms from storage sources, their assembly into [Fe-S]form, their transport to specific cellular locations, and their transfer to recipient apoproteins. So far, three FeS assembly machineries have been identified, which are capable of synthesising all types of [Fe-S]clusters: ISC (iron-sulphur cluster), SUF (sulphur assimilation), and NIF (nitrogen fixation) systems.The ISC system is conserved in eubacteria and eukaryotes (mitochondria), and has broad specificity, targeting general FeS proteins [, ]. It is encoded by the isc operon (iscRSUA-hscBA-fdx-iscX). IscS is a cysteine desulphurase, which obtains S from cysteine (converting it to alanine) and serves as a S donor for FeS cluster assembly. IscU and IscA act as scaffolds to accept S and Fe atoms, assembling clusters and transfering them to recipient apoproteins. HscA is a molecular chaperone and HscB is a co-chaperone. Fdx is a [2Fe-2S]-type ferredoxin. IscR is a transcription factor that regulates expression of the isc operon. IscX (also known as YfhJ) appears to interact with IscS and may function as an Fe donor during cluster assembly [].The SUF system is an alternative pathway to the ISC system that operates under iron starvation and oxidative stress. It is found in eubacteria, archaea and eukaryotes (plastids). TheSUF system is encoded by the suf operon (sufABCDSE), and the six encoded proteins are arranged into two complexes (SufSE and SufBCD) and one protein (SufA). SufS is a pyridoxal-phosphate (PLP) protein displaying cysteine desulphurase activity. SufE acts as a scaffold protein that accepts S from SufS and donates it to SufA []. SufC is an ATPase with an unorthodox ATP-binding cassette (ABC)-like component. SufA is homologous to IscA [], acting 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.In the NIF system, NifS and NifU are required for the formation of metalloclusters of nitrogenase in Azotobacter vinelandii, and other organisms, as well as in the maturation of other FeS proteins. Nitrogenase catalyses the fixation of nitrogen. It contains a complex cluster, the FeMo cofactor, which contains molybdenum, Fe and S. NifS is a cysteine desulphurase. NifU binds one Fe atom at its N-terminal, assembling an FeS cluster that is transferred to nitrogenase apoproteins []. Nif proteins involved in the formation of FeS clusters can also be found in organisms that do not fix nitrogen [].This entry describes IscR, an iron-sulphur binding transcription factor of the ISC iron-sulphur cluster assembly system []. The HTH-type transcriptional regulator IscR (iron-sulphur cluster regulator) regulates the transcription of several operons and genes involved in the biogenesis of Fe-S clusters and Fe-S-containing proteins. It is a 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. It represses its own transcription [, ]. It is induced by oxidative stress conditions and iron starvation []. |
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| Publication |
| First Author: |
Greenwood KT |
| Year: |
1978 |
| Journal: |
Biochim Biophys Acta |
| Title: |
Enzymatic hydrolysis of enterochelin and its iron complex in Escherichia Coli K-12. Properties of enterochelin esterase. |
| Volume: |
525 |
| Issue: |
1 |
| Pages: |
209-18 |
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•
•
•
•
•
|
| Publication |
| First Author: |
Brickman TJ |
| Year: |
1992 |
| Journal: |
J Biol Chem |
| Title: |
Overexpression and purification of ferric enterobactin esterase from Escherichia coli. Demonstration of enzymatic hydrolysis of enterobactin and its iron complex. |
| Volume: |
267 |
| Issue: |
17 |
| Pages: |
12350-5 |
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•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
This domain is found in Hydrogen maturase F (HydF) present in Thermotoga neapolitana. HydF is a GTPase, containing an FeS cluster-binding motif, that is able to are able to activate HydA produced so that HydA can drive the reversible reduction of protons to molecular H2. This domain, referred to as domain II, is responsible for HydF dimerization through the formation of a continuous β-sheet comprising eight β-strands from two monomers []. |
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•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
This entry represents a putative redox-active protein of about 140 residues, with four perfectly conserved Cys residues. It includes a CGAXXG motif. Most members are found within one or two loci of transporter or oxidoreductase genes. A member from Geobacter sulfurreducens, located in a molybdenum transporter operon, has a TAT (twin-arginine translocation) signal sequence for Sec-independent transport across theplasma membrane, a hallmark of bound prosthetic groups such as FeS clusters. |
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•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
This entry describes probable pyridoxal phosphate-dependent enzymes in the aminotransferase class V family. The most closely related characterised proteins are active as cysteine desulfurases, selenocysteine lyases, or both; some are involved in FeS cofactor biosynthesis and are designated NifS. An active site Cys residue present in those sequences, in motifs resembling GHHC or GSAC, is not found in this family. The function ofmembers of this family is unknown. |
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•
•
•
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| Protein Domain |
| Type: |
Domain |
| Description: |
This entry represents the N-terminal domain of enterochelin esterase. The activity of the enzyme has been characterised [, , ]. Fes catalyses the hydrolysis of the 2,3-dihydroxy-N-benzoyl-L-serine trimer, enterochelin, forming 2,3-dihydroxybenzoylserine. It also catalyses hydrolysis of free enterobactin and ferric enterobactin. Upon hydrolysis of ferric enterobactin by Fes, released iron is probably reduced by a second enzyme. Enterochelin esterase represents a family of non-peptidase homologues belonging to the MEROPS peptidase family S9, clan SC. |
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•
•
•
•
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| Protein Domain |
| Type: |
Homologous_superfamily |
| Description: |
The ISC system is conserved in eubacteria and eukaryotes (mitochondria), and has broad specificity, targeting general FeS proteins [, ]. It is encoded by the isc operon (iscRSUA-hscBA-fdx-iscX). IscS is a cysteine desulphurase, which obtains S from cysteine (converting it to alanine) and serves as a S donor for FeS cluster assembly. IscU and IscA act as scaffolds to accept S and Fe atoms, assembling clusters and transfering them to recipient apoproteins. HscA is a molecular chaperone and HscB is a co-chaperone. Fdx is a [2Fe-2S]-type ferredoxin. IscR is a transcription factor that regulates expression of the isc operon. IscX (also known as YfhJ) appears to interact with IscS and may function as an Fe donor during cluster assembly [].This entry represents IscX proteins (also known as hypothetical protein YfhJ) that are part of the ISC system. IscX is active as a monomer. The structure of YfhJ is an orthogonal α-bundle []. YfhJ is a small acidic protein that binds IscS, and contains a modified winged helix motif that is usually found in DNA-binding proteins []. YfhJ/IscX can bind Fe, and may function as an Fe donor in the assembly of FeS clusters |
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| Publication |
| First Author: |
Horton AJ |
| Year: |
2019 |
| Journal: |
Sci Rep |
| Title: |
Nkx2-5 Second Heart Field Target Gene Ccdc117 Regulates DNA Metabolism and Proliferation. |
| Volume: |
9 |
| Issue: |
1 |
| Pages: |
1738 |
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•
•
•
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| Publication |
| First Author: |
Kotarsky H |
| Year: |
2007 |
| Journal: |
Gene Expr Patterns |
| Title: |
BCS1L is expressed in critical regions for neural development during ontogenesis in mice. |
| Volume: |
7 |
| Issue: |
3 |
| Pages: |
266-73 |
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•
•
•
•
|
| Publication |
| First Author: |
Li C |
| Year: |
2009 |
| Journal: |
Hum Mol Genet |
| Title: |
Correlation of expression and methylation of imprinted genes with pluripotency of parthenogenetic embryonic stem cells. |
| Volume: |
18 |
| Issue: |
12 |
| Pages: |
2177-87 |
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•
•
•
|
| Publication |
| First Author: |
Hänzelmann P |
| Year: |
2004 |
| Journal: |
J Biol Chem |
| Title: |
Characterization of MOCS1A, an oxygen-sensitive iron-sulfur protein involved in human molybdenum cofactor biosynthesis. |
| Volume: |
279 |
| Issue: |
33 |
| Pages: |
34721-32 |
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•
•
•
|
| Publication |
| First Author: |
Ronning DR |
| Year: |
2000 |
| Journal: |
Nat Struct Biol |
| Title: |
Crystal structure of the secreted form of antigen 85C reveals potential targets for mycobacterial drugs and vaccines. |
| Volume: |
7 |
| Issue: |
2 |
| Pages: |
141-6 |
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•
•
•
|
| Publication |
| First Author: |
Larsen NA |
| Year: |
2006 |
| Journal: |
Biochemistry |
| Title: |
Structural characterization of enterobactin hydrolase IroE. |
| Volume: |
45 |
| Issue: |
34 |
| Pages: |
10184-90 |
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•
•
•
•
|
| Publication |
| First Author: |
Loiseau L |
| Year: |
2005 |
| Journal: |
J Biol Chem |
| Title: |
Analysis of the heteromeric CsdA-CsdE cysteine desulfurase, assisting Fe-S cluster biogenesis in Escherichia coli. |
| Volume: |
280 |
| Issue: |
29 |
| Pages: |
26760-9 |
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•
•
•
|
| Publication |
| First Author: |
Kim S |
| Year: |
2013 |
| Journal: |
J Biol Chem |
| Title: |
Structural changes during cysteine desulfurase CsdA and sulfur acceptor CsdE interactions provide insight into the trans-persulfuration. |
| Volume: |
288 |
| Issue: |
38 |
| Pages: |
27172-80 |
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•
•
•
•
•
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| Protein Domain |
| Type: |
Family |
| Description: |
Ferredoxin thioredoxin reductase is a [4FE-4S]protein present in organisms performing oxygenic photosynthesis, and plays an important role in the ferredoxin/thioredoxin regulatory chain. It converts an electron signal (photoreduced ferredoxin) to a thiol signal (reduced thioredoxin), regulating enzymes by reduction of specific disulphide groups. It catalyses the light-dependent activation of several photosynthetis enzymes. Ferredoxin thioredoxin reductase is a heterodimer of subunit alpha and subunit beta. Subunit alpha is the variable subunit, and beta is the catalytic chain [].The structure of the beta subunit has been determined and found to fold around the FeS cluster []. |
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•
•
•
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| Protein Domain |
| Type: |
Family |
| Description: |
This family contains several seemingly unrelated proteins, including human esterase D ; mycobacterial antigen 85 [], which is responsible for the high affinity of mycobacteria to fibronectin; Corynebacterium glutamicum major secreted protein PS1; and a number of proteins from Escherichia coli, yeast, mycobacteria and Haemophilus influenzae. Proteins in this entry share the typical AB hydrolase fold including esterases with broad specificity. Among them, S-formylglutathione hydrolases, such as YeiG and FrmB from bacteria ; the three related serine hydrolases Iron(III) enterobactin esterase fes (), Iron(III) salmochelin esterase iroD () and iroE () from E. coli which are esterases for the apo and Fe3-bound forms of enterobactin iroB [, ]. |
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•
•
•
•
•
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| Protein Domain |
| Type: |
Homologous_superfamily |
| Description: |
Ferredoxin thioredoxin reductase is a [4FE-4S]protein present in organisms performing oxygenic photosynthesis, and plays an important role in the ferredoxin/thioredoxin regulatory chain. It converts an electron signal (photoreduced ferredoxin) to a thiol signal (reduced thioredoxin), regulating enzymes by reduction of specific disulphide groups. It catalyses the light-dependent activation of several photosynthetis enzymes. Ferredoxin thioredoxin reductase is a heterodimer of subunit alpha and subunit beta. Subunit alpha is the variable subunit, and beta is the catalytic chain [].The structure of the beta subunit has been determined and found to fold around the FeS cluster []. |
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•
•
•
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| Protein Domain |
| Type: |
Family |
| Description: |
In Escherichia coli, three cysteine desulfurases (IscS, SufS, and CsdA) initiate the delivery of sulfur for various biological processes such as the biogenesis of Fe-S clusters. CsdA is part of the Csd system. This protein, found in Escherichia coli, Yersinia pestis, Photorhabdus luminescens, and related species, is related to SufS. It works together with and physically interacts with CsdE (a paralogue of SufE) []. CsdA has cysteine desulphurase activity that is enhanced by CsdE, a sulphur acceptor protein []. This gene pair, although involved in FeS cluster biosynthesis, is not found next to other such genes as are its paralogs from the Suf or Isc systems. |
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•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
This entry represents CsdE (formerly known as YgdK), the sulphur acceptor subunit of a cysteine desulfurase. This protein, found as a paralogue of SufE in Escherichia coli, Yersinia pestis, Photorhabdus luminescens and related species, works together and physically interacts with CsdA (a paralogue of SufS). CsdA has cysteine desulfurase activity that is enhanced by this protein, where Cys-61 (numbered as in E. coli) is a sulphur acceptor site. CsdA and CsdE, although involved in FeS cluster biosynthesis, are not encoded next to other like the paralogous Suf proteins. |
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•
|
| Publication |
| First Author: |
Lin H |
| Year: |
2005 |
| Journal: |
J Am Chem Soc |
| Title: |
In vitro characterization of salmochelin and enterobactin trilactone hydrolases IroD, IroE, and Fes. |
| Volume: |
127 |
| Issue: |
31 |
| Pages: |
11075-84 |
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•
•
|
