electron transfer flavoprotein (ETF) subunit alpha forms a heterodimer with subunit beta to form ETF, which serves as a specific electron acceptor for various dehydrogenases
electron transfer flavoprotein (ETF) alpha; The electron transfer flavoprotein (ETF) serves as ...
72-247
1.16e-58
electron transfer flavoprotein (ETF) alpha; The electron transfer flavoprotein (ETF) serves as a specific electron acceptor for various mitochondrial dehydrogenases. ETF transfers electrons to the main respiratory chain via ETF-ubiquinone oxidoreductase. ETF is a heterodimer, consisting of an alpha and a beta subunit, which binds one molecule of FAD per dimer. A similar system also exists in some bacteria. The homologous pair of proteins (FixA/FixB) are essential for nitrogen fixation. The alpha subunit of ETF is structurally related to the bacterial nitrogen fixation protein fixB which could play a role in a redox process and feed electrons to ferredoxin.
Pssm-ID: 467488 [Multi-domain] Cd Length: 171 Bit Score: 188.53 E-value: 1.16e-58
Electron transfer flavoprotein domain; This family includes the homologous domain shared ...
73-247
7.48e-49
Electron transfer flavoprotein domain; This family includes the homologous domain shared between the alpha and beta subunits of the electron transfer flavoprotein.
Pssm-ID: 425985 [Multi-domain] Cd Length: 178 Bit Score: 163.55 E-value: 7.48e-49
Electron transfer flavoprotein domain; Electron transfer flavoproteins (ETFs) serve as ...
77-257
1.90e-39
Electron transfer flavoprotein domain; 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 alpha-beta-alpha sandwich fold, while domain II forms an alpha-beta-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. This entry represents the N-terminal domain of both the alpha and beta subunits from Group I and Group II ETFs.
Pssm-ID: 214890 [Multi-domain] Cd Length: 185 Bit Score: 138.94 E-value: 1.90e-39
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
18-55
2.80e-03
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a membrane-associated formate hydrogenlyase system (FHL-1) in Escherichia coli that breaks down formate, produced during anaerobic fermentation, to H2 and CO2. FHL-1 consists of formate dehydrogenase H (FDH-H) and the hydrogenase 3 complex (Hyd-3). HycB is thought to code for the [4Fe-4S] ferredoxin subunit of hydrogenase 3, which functions as an intermediate electron carrier protein between hydrogenase 3 and formate dehydrogenase. HydN codes for the [4Fe-4S] ferredoxin subunit of FDH-H; a hydN in-frame deletion mutation causes only weak reduction in hydrogenase activity, but loss of more than 60% of FDH-H activity. This pathway is only active at low pH and high formate concentrations, and is thought to provide a detoxification/de-acidification system countering the buildup of formate during fermentation.
Pssm-ID: 319876 [Multi-domain] Cd Length: 149 Bit Score: 38.01 E-value: 2.80e-03
electron transfer flavoprotein (ETF) alpha; The electron transfer flavoprotein (ETF) serves as ...
72-247
1.16e-58
electron transfer flavoprotein (ETF) alpha; The electron transfer flavoprotein (ETF) serves as a specific electron acceptor for various mitochondrial dehydrogenases. ETF transfers electrons to the main respiratory chain via ETF-ubiquinone oxidoreductase. ETF is a heterodimer, consisting of an alpha and a beta subunit, which binds one molecule of FAD per dimer. A similar system also exists in some bacteria. The homologous pair of proteins (FixA/FixB) are essential for nitrogen fixation. The alpha subunit of ETF is structurally related to the bacterial nitrogen fixation protein fixB which could play a role in a redox process and feed electrons to ferredoxin.
Pssm-ID: 467488 [Multi-domain] Cd Length: 171 Bit Score: 188.53 E-value: 1.16e-58
Electron transfer flavoprotein domain; This family includes the homologous domain shared ...
73-247
7.48e-49
Electron transfer flavoprotein domain; This family includes the homologous domain shared between the alpha and beta subunits of the electron transfer flavoprotein.
Pssm-ID: 425985 [Multi-domain] Cd Length: 178 Bit Score: 163.55 E-value: 7.48e-49
Electron transfer flavoprotein domain; Electron transfer flavoproteins (ETFs) serve as ...
77-257
1.90e-39
Electron transfer flavoprotein domain; 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 alpha-beta-alpha sandwich fold, while domain II forms an alpha-beta-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. This entry represents the N-terminal domain of both the alpha and beta subunits from Group I and Group II ETFs.
Pssm-ID: 214890 [Multi-domain] Cd Length: 185 Bit Score: 138.94 E-value: 1.90e-39
Electron transfer flavoprotein FAD-binding domain; This domain found at the C-terminus of ...
273-351
1.50e-35
Electron transfer flavoprotein FAD-binding domain; This domain found at the C-terminus of electron transfer flavoprotein alpha chain and binds to FAD. The fold consists of a five-stranded parallel beta sheet as the core of the domain, flanked by alternating helices. A small part of this domain is donated by the beta chain.
Pssm-ID: 459931 [Multi-domain] Cd Length: 81 Bit Score: 125.16 E-value: 1.50e-35
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
18-55
2.80e-03
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a membrane-associated formate hydrogenlyase system (FHL-1) in Escherichia coli that breaks down formate, produced during anaerobic fermentation, to H2 and CO2. FHL-1 consists of formate dehydrogenase H (FDH-H) and the hydrogenase 3 complex (Hyd-3). HycB is thought to code for the [4Fe-4S] ferredoxin subunit of hydrogenase 3, which functions as an intermediate electron carrier protein between hydrogenase 3 and formate dehydrogenase. HydN codes for the [4Fe-4S] ferredoxin subunit of FDH-H; a hydN in-frame deletion mutation causes only weak reduction in hydrogenase activity, but loss of more than 60% of FDH-H activity. This pathway is only active at low pH and high formate concentrations, and is thought to provide a detoxification/de-acidification system countering the buildup of formate during fermentation.
Pssm-ID: 319876 [Multi-domain] Cd Length: 149 Bit Score: 38.01 E-value: 2.80e-03
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
19-69
5.27e-03
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.
Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 36.99 E-value: 5.27e-03
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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