Fe-S cluster assembly protein SufD, a component of SufBCD complex that acts synergistically with SufE to stimulate the cysteine desulfurase activity of SufS
FeS assembly protein SufD; This protein, SufD, forms a cytosolic complex SufBCD. This complex ...
131-410
3.20e-98
FeS assembly protein SufD; This protein, SufD, forms a cytosolic complex SufBCD. This complex enhances the cysteine desulfurase of SufSE. The system, together with SufA, is believed to act in iron-sulfur cluster formation during oxidative stress. SufB and SufD are homologous. Note that SufC belongs to the family of ABC transporter ATP binding proteins, so this protein, encoded by an adjacent gene, has often been annotated as a transporter component. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273908 Cd Length: 275 Bit Score: 294.52 E-value: 3.20e-98
SUF system FeS cluster assembly, SufBD; Iron-sulphur (FeS) clusters are important cofactors ...
170-393
6.81e-88
SUF system FeS cluster assembly, SufBD; 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 mobilization 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.
Pssm-ID: 460219 [Multi-domain] Cd Length: 218 Bit Score: 266.24 E-value: 6.81e-88
FeS assembly protein SufD; This protein, SufD, forms a cytosolic complex SufBCD. This complex ...
131-410
3.20e-98
FeS assembly protein SufD; This protein, SufD, forms a cytosolic complex SufBCD. This complex enhances the cysteine desulfurase of SufSE. The system, together with SufA, is believed to act in iron-sulfur cluster formation during oxidative stress. SufB and SufD are homologous. Note that SufC belongs to the family of ABC transporter ATP binding proteins, so this protein, encoded by an adjacent gene, has often been annotated as a transporter component. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273908 Cd Length: 275 Bit Score: 294.52 E-value: 3.20e-98
SUF system FeS cluster assembly, SufBD; Iron-sulphur (FeS) clusters are important cofactors ...
170-393
6.81e-88
SUF system FeS cluster assembly, SufBD; 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 mobilization 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.
Pssm-ID: 460219 [Multi-domain] Cd Length: 218 Bit Score: 266.24 E-value: 6.81e-88
SufBD protein N-terminal region; This entry represents the N-terminal part of the SufB and ...
9-55
6.96e-05
SufBD protein N-terminal region; This entry represents the N-terminal part of the SufB and SufD proteins. It has a right handed beta helix structure. This family is associated with the C-terminal region pfam01458
Pssm-ID: 437127 Cd Length: 172 Bit Score: 43.27 E-value: 6.96e-05
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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