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iron-sulfur cluster biosynthesis family protein
This family is involved in iron-sulphur cluster biosynthesis [3]. Its members include proteins that are involved in nitrogen fixation such as the HesB and HesB-like proteins [1] [2]. [1]. 10217509. Organization and expression of nitrogen-fixation genes in the. aerobic nitrogen-fixing unicellular cyanobacterium Synechococcus. sp. strain RF-1.. Huang TC, Lin RF, Chu MK, Chen HM;. Microbiology 1999;145:743-753.. [2]. 12207230. The Rhizobium etli gene iscN is highly expressed in bacteroids. and required for nitrogen fixation.. Dombrecht B, Tesfay MZ, Verreth C, Heusdens C, Napoles MC,. Vanderleyden J, Michiels J;. Mol Genet Genomics 2002;267:820-828.. [3]. 11941510. Iron-sulfur cluster biosynthesis: characterization of. Schizosaccharomyces pombe Isa1.. Wu G, Mansy SS, Hemann C, Hille R, Surerus KK, Cowan JA;. J Biol Inorg Chem 2002;7:526-532. (from Pfam)
HesB/IscA family protein
HesB/IscA family protein is a scaffold protein upon which 2Fe-2S clusters are assembled and subsequently transferred to acceptor proteins; similar to iron-sulfur assembly protein IscA that is involved in the maturation of mitochondrial 4Fe-4S proteins functioning late in the iron-sulfur cluster assembly pathway
iron-sulfur cluster assembly accessory protein
Proteins in this subfamily 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 [1]. Nitrogenase includes multiple FeS clusters and many genes for their assembly. The E. coli SufA protein is associated with SufS, a NifS homolog and SufD which are involved in the FeS cluster assembly of the FhnF protein [2]. The Azotobacter protein IscA (homologs of which are also found in E.coli) is associated which IscS, another NifS homolog and IscU, a nifU homolog as well as other factors consistent with a role in FeS cluster chemistry [3]. A homolog from Geobacter contains a selenocysteine in place of an otherwise invariant cysteine, further suggesting a role in redox chemistry.
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