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4Fe-4S binding protein
Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. (from Pfam)
FMN-binding protein
This conserved region includes the FMN-binding site of the NqrC protein [1] as well as the NosR and NirI regulatory proteins. This domain is post-translationally flavinylated that may facilitate electron transfer, and thus, resembles multiheme cytochromes [3]. [1]. 11248234. Expression and mutagenesis of the NqrC subunit of the NQR respiratory Na(+) pump from Vibrio cholerae with covalently attached FMN. Barquera B, Hase CC, Gennis RB;. FEBS Lett 2001;492:45-49. [2]. 12625841. New Knowledge from Old: In silico discovery of novel protein domains in Streptomyces coelicolor. Yeats C, Bentley S, Bateman A;. BMC Microbiol 2003;3:3-3. [3]. 34032212. Post-translational flavinylation is associated with diverse extracytosolic redox functionalities throughout bacterial life. Meheust R, Huang S, Rivera-Lugo R, Banfield JF, Light SH;. Elife. 2021; [Epub ahead of print] (from Pfam)
NosR/NirI family protein
NosR/NirI family protein containing FMN and 4Fe-4S binding domains, similar to Paracoccus denitrificans protein NirI and Pseudomonas aeruginosa regulatory protein NosR that functions as the transcriptional activator of the nitrous-oxide reductase gene NosZ
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