Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyStabilizer of iron transporter SufD 8035775 3000240 SCOP2B (2022-06-29)
BSCOP2 FamilyStabilizer of iron transporter SufD 8023395 4000956 SCOP2 (2022-06-29)
BSCOP2 SuperfamilyStabilizer of iron transporter SufD 8035775 3000240 SCOP2 (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
AUPF0051e1vh4A1 A: beta duplicates or obligate multimersX: Single-stranded right-handed beta-helixH: Stabilizer of iron transporter sufD (From Topology)T: Stabilizer of iron transporter sufDF: UPF0051ECOD (1.6)
BUPF0051e1vh4B1 A: beta duplicates or obligate multimersX: Single-stranded right-handed beta-helixH: Stabilizer of iron transporter sufD (From Topology)T: Stabilizer of iron transporter sufDF: UPF0051ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B
PF01458SUF system FeS cluster assembly, SufBD core domain (SUFBD_core)SUF system FeS cluster assembly, SufBD core domainIron-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 prosth ...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] [1]. 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 [2]. SufC is an ATPase with an unorthodox ATP-binding cassette (ABC)-like component. SufA is homologous to IscA [3], 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 the core domain of SufB and SufD proteins, which are homologous, and form part of the SufBCD complex in the SUF system [4]. SufB accepts sulfur transferred from SufE [5], whereas SufD may play a role in iron acquisition [6].
Domain