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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)
electron transport complex subunit RsxG
RnfABCDGE type electron transport complex subunit G
The six subunit complex RnfABCDGE in Rhodobacter capsulatus encodes an apparent NADH oxidoreductase responsible for electron transport to nitrogenase, necessary for nitrogen fixation. A closely related complex in E. coli, RsxABCDGE (Reducer of SoxR), reduces the 2Fe-2S-containing superoxide sensor SoxR, active as a transcription factor when oxidized. This family of putative NADH oxidoreductase complexes exists in many of the same species as the related NQR, a Na(+)-translocating NADH-quinone reductase, but is distinct. This model describes the A subunit.
electron transport complex subunit G
electron transport complex subunit G is part of a membrane complex that may be involved in transporting electrons to nitrogenase
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