The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:
"FAD/NAD(P)-binding domain
".
FunFam 52: Electron transfer flavoprotein-ubiquinone oxidored...
Please note: GO annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.
There are 22 GO terms relating to "molecular function"
The search results have been sorted with the annotations that are found most frequently at the top of the
list. The results can be filtered by typing text into the search box at the top of the table.
GO Term | Annotations | Evidence |
---|---|---|
Electron-transferring-flavoprotein dehydrogenase activity GO:0004174
Catalysis of the reaction: reduced ETF + ubiquinone = ETF + ubiquinol.
|
3 | P55931 (/IDA) Q16134 (/IDA) Q7JWF1 (/IDA) |
Electron transfer activity GO:0009055
Any molecular entity that serves as an electron acceptor and electron donor in an electron transport chain. An electron transport chain is a process in which a series of electron carriers operate together to transfer electrons from donors to any of several different terminal electron acceptors to generate a transmembrane electrochemical gradient.
|
3 | P55931 (/IDA) Q16134 (/IDA) Q6UPE1 (/IDA) |
Electron-transferring-flavoprotein dehydrogenase activity GO:0004174
Catalysis of the reaction: reduced ETF + ubiquinone = ETF + ubiquinol.
|
2 | Q7JWF1 (/ISS) Q921G7 (/ISS) |
Oxidoreductase activity GO:0016491
Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
|
2 | P55931 (/IDA) Q16134 (/IDA) |
Oxidoreductase activity, oxidizing metal ions with flavin as acceptor GO:0043783
Catalysis of an oxidation-reduction in which the oxidation state of metal ion is altered and flavin acts as an electron acceptor.
|
2 | Q16134 (/ISS) Q921G7 (/ISS) |
Ubiquinone binding GO:0048039
Interacting selectively and non-covalently with ubiquinone, a quinone derivative with a tail of isoprene units.
|
2 | P55931 (/IDA) Q16134 (/IDA) |
Iron-sulfur cluster binding GO:0051536
Interacting selectively and non-covalently with an iron-sulfur cluster, a combination of iron and sulfur atoms.
|
2 | P55931 (/IDA) Q6UPE1 (/IDA) |
4 iron, 4 sulfur cluster binding GO:0051539
Interacting selectively and non-covalently with a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands.
|
2 | P55931 (/IDA) Q16134 (/IDA) |
Electron-transferring-flavoprotein dehydrogenase activity GO:0004174
Catalysis of the reaction: reduced ETF + ubiquinone = ETF + ubiquinol.
|
1 | Q921G7 (/ISO) |
Electron-transferring-flavoprotein dehydrogenase activity GO:0004174
Catalysis of the reaction: reduced ETF + ubiquinone = ETF + ubiquinol.
|
1 | Q16134 (/TAS) |
Electron transfer activity GO:0009055
Any molecular entity that serves as an electron acceptor and electron donor in an electron transport chain. An electron transport chain is a process in which a series of electron carriers operate together to transfer electrons from donors to any of several different terminal electron acceptors to generate a transmembrane electrochemical gradient.
|
1 | Q921G7 (/ISO) |
Electron transfer activity GO:0009055
Any molecular entity that serves as an electron acceptor and electron donor in an electron transport chain. An electron transport chain is a process in which a series of electron carriers operate together to transfer electrons from donors to any of several different terminal electron acceptors to generate a transmembrane electrochemical gradient.
|
1 | Q921G7 (/ISS) |
Oxidoreductase activity GO:0016491
Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
|
1 | Q921G7 (/ISO) |
Oxidoreductase activity GO:0016491
Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
|
1 | Q921G7 (/ISS) |
Oxidoreductase activity, oxidizing metal ions with flavin as acceptor GO:0043783
Catalysis of an oxidation-reduction in which the oxidation state of metal ion is altered and flavin acts as an electron acceptor.
|
1 | P55931 (/IDA) |
Quinone binding GO:0048038
Interacting selectively and non-covalently with a quinone, any member of a class of diketones derivable from aromatic compounds by conversion of two CH groups into CO groups with any necessary rearrangement of double bonds.
|
1 | Q16134 (/IDA) |
Quinone binding GO:0048038
Interacting selectively and non-covalently with a quinone, any member of a class of diketones derivable from aromatic compounds by conversion of two CH groups into CO groups with any necessary rearrangement of double bonds.
|
1 | Q921G7 (/ISO) |
Ubiquinone binding GO:0048039
Interacting selectively and non-covalently with ubiquinone, a quinone derivative with a tail of isoprene units.
|
1 | Q921G7 (/ISO) |
Flavin adenine dinucleotide binding GO:0050660
Interacting selectively and non-covalently with FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.
|
1 | P55931 (/IDA) |
Flavin adenine dinucleotide binding GO:0050660
Interacting selectively and non-covalently with FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.
|
1 | Q16134 (/ISS) |
Iron-sulfur cluster binding GO:0051536
Interacting selectively and non-covalently with an iron-sulfur cluster, a combination of iron and sulfur atoms.
|
1 | Q921G7 (/ISO) |
4 iron, 4 sulfur cluster binding GO:0051539
Interacting selectively and non-covalently with a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands.
|
1 | Q921G7 (/ISO) |
There are 10 GO terms relating to "biological process"
The search results have been sorted with the annotations that are found most frequently at the top of the
list. The results can be filtered by typing text into the search box at the top of the table.
GO Term | Annotations | Evidence |
---|---|---|
Response to oxidative stress GO:0006979
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals.
|
3 | P55931 (/ISS) Q16134 (/ISS) Q6UPE1 (/ISS) |
Electron transport chain GO:0022900
A process in which a series of electron carriers operate together to transfer electrons from donors to any of several different terminal electron acceptors to generate a transmembrane electrochemical gradient.
|
2 | P55931 (/IDA) Q16134 (/IDA) |
Oxidative phosphorylation GO:0006119
The phosphorylation of ADP to ATP that accompanies the oxidation of a metabolite through the operation of the respiratory chain. Oxidation of compounds establishes a proton gradient across the membrane, providing the energy for ATP synthesis.
|
1 | Q7JWF1 (/ISS) |
Fatty acid beta-oxidation GO:0006635
A fatty acid oxidation process that results in the complete oxidation of a long-chain fatty acid. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and occurs by successive cycles of reactions during each of which the fatty acid is shortened by a two-carbon fragment removed as acetyl coenzyme A; the cycle continues until only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively).
|
1 | Q7JWF1 (/IMP) |
Response to oxidative stress GO:0006979
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals.
|
1 | Q921G7 (/IDA) |
Electron transport chain GO:0022900
A process in which a series of electron carriers operate together to transfer electrons from donors to any of several different terminal electron acceptors to generate a transmembrane electrochemical gradient.
|
1 | Q921G7 (/ISO) |
Respiratory electron transport chain GO:0022904
A process in which a series of electron carriers operate together to transfer electrons from donors such as NADH and FADH2 to any of several different terminal electron acceptors to generate a transmembrane electrochemical gradient.
|
1 | Q66I16 (/IMP) |
Respiratory electron transport chain GO:0022904
A process in which a series of electron carriers operate together to transfer electrons from donors such as NADH and FADH2 to any of several different terminal electron acceptors to generate a transmembrane electrochemical gradient.
|
1 | Q16134 (/TAS) |
Fatty acid beta-oxidation using acyl-CoA dehydrogenase GO:0033539
A fatty acid beta-oxidation pathway in which the initial step of each oxidation cycle, which converts an acyl-CoA to a trans-2-enoyl-CoA, is catalyzed by acyl-CoA dehydrogenase; the electrons removed by oxidation pass through the respiratory chain to oxygen and leave H2O as the product. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and ends when only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively).
|
1 | Q16134 (/IMP) |
Fatty acid beta-oxidation using acyl-CoA dehydrogenase GO:0033539
A fatty acid beta-oxidation pathway in which the initial step of each oxidation cycle, which converts an acyl-CoA to a trans-2-enoyl-CoA, is catalyzed by acyl-CoA dehydrogenase; the electrons removed by oxidation pass through the respiratory chain to oxygen and leave H2O as the product. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and ends when only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively).
|
1 | Q921G7 (/ISO) |
There are 14 GO terms relating to "cellular component"
The search results have been sorted with the annotations that are found most frequently at the top of the
list. The results can be filtered by typing text into the search box at the top of the table.
GO Term | Annotations | Evidence |
---|---|---|
Cell GO:0005623
The basic structural and functional unit of all organisms. Includes the plasma membrane and any external encapsulating structures such as the cell wall and cell envelope.
|
2 | F1NY29 (/IDA) Q5F3D8 (/IDA) |
Mitochondrion GO:0005739
A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
|
2 | Q7JWF1 (/HDA) Q921G7 (/HDA) |
Mitochondrion GO:0005739
A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
|
2 | P55931 (/IDA) Q11190 (/IDA) |
Mitochondrial membrane GO:0031966
Either of the lipid bilayers that surround the mitochondrion and form the mitochondrial envelope.
|
2 | Q16134 (/IDA) Q6UPE1 (/IDA) |
Mitochondrion GO:0005739
A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
|
1 | Q921G7 (/ISS) |
Mitochondrial inner membrane GO:0005743
The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae.
|
1 | Q921G7 (/HDA) |
Mitochondrial inner membrane GO:0005743
The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae.
|
1 | Q7JWF1 (/ISS) |
Mitochondrial matrix GO:0005759
The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation.
|
1 | Q16134 (/TAS) |
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
|
1 | P55931 (/IDA) |
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
|
1 | Q921G7 (/ISS) |
Mitochondrial electron transfer flavoprotein complex GO:0017133
A protein complex located in the mitochondrion. It contains flavin adenine dinucleotide (FAD) that, together with an acyl-CoA dehydrogenase, forms a system that oxidizes an acyl-CoA molecule and reduces ubiquinone and other acceptors in the mitochondrial electron transport system.
|
1 | Q921G7 (/TAS) |
Integral component of mitochondrial inner membrane GO:0031305
The component of the mitochondrial inner membrane consisting of the gene products having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
|
1 | Q16134 (/IDA) |
Integral component of mitochondrial inner membrane GO:0031305
The component of the mitochondrial inner membrane consisting of the gene products having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
|
1 | Q921G7 (/ISO) |
Mitochondrial membrane GO:0031966
Either of the lipid bilayers that surround the mitochondrion and form the mitochondrial envelope.
|
1 | Q921G7 (/ISO) |