Protein Domain : Electron transfer flavoprotein alpha subunit/FixB IPR001308

Type	Family
Description	This entry includes electron transfer flavoprotein alpha subunit and the FixB protein.Electron transfer flavoproteins (ETFs) serve as specific electron acceptors for primary dehydrogenases, transferring the electrons to terminal respiratory systems. They can be functionally classified into constitutive, "housekeeping"ETFs, mainly involved in the oxidation of fatty acids (Group I), and ETFs produced by some prokaryotes under specific growth conditions, receiving electrons only from the oxidation of specific substrates (Group II) [ ]. ETFs are heterodimeric proteins composed of an alpha and beta subunit, and contain an FAD cofactor and AMP [ , , , , ]. ETF consists of three domains: domains I and II are formed by the N- and C-terminal portions of the alpha subunit, respectively, while domain III is formed by the beta subunit. Domains I and III share an almost identical α-β-alpha sandwich fold, while domain II forms an α-β-alpha sandwich similar to that of bacterial flavodoxins. FAD is bound in a cleft between domains II and III, while domain III binds the AMP molecule. Interactions between domains I and III stabilise the protein, forming a shallow bowl where domain II resides. The alpha subunit of both Group I and Group II ETFs is composed of domains I and II.Many enterobacteria are able to convert carnitine, via crotonobetaine, to gamma-butyrobetaine in the presence of carbon and nitrogen sources under anaerobic conditions [ ]. In Escherichia coli the enzymes involved in this pathway are encoded by the caiTABCDE operon []. The adjacent but divergent fixABCD operon also appears to be necessary for carnintine meatbolism []. The Fix proteins are homologous to proteins found in known electron transport pathways.
Short Name	ETF_a/FixB