CATH Superfamily 3.30.390.30
FAD/NAD-linked reductase, C-terminal dimerisation domain
The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was: waiting to be named.
FunFam 1526: Dihydrolipoyl dehydrogenase
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 4 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 |
|---|---|---|
|
Catalytic activity GO:0003824
Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
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1 | Q8I5A0 (/IDA) |
|
Dihydrolipoyl dehydrogenase activity GO:0004148
Catalysis of the reaction: protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+.
|
1 | Q8I5A0 (/ISS) |
|
Protein homodimerization activity GO:0042803
Interacting selectively and non-covalently with an identical protein to form a homodimer.
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1 | Q8I5A0 (/IDA) |
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Cofactor binding GO:0048037
Interacting selectively and non-covalently with a cofactor, a substance that is required for the activity of an enzyme or other protein. Cofactors may be inorganic, such as the metal atoms zinc, iron, and copper in certain forms, or organic, in which case they are referred to as coenzymes. Cofactors may either be bound tightly to active sites or bind loosely with the substrate.
|
1 | Q8I5A0 (/IDA) |
There are 1 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 |
|---|---|---|
|
Oxidation-reduction process GO:0055114
A metabolic process that results in the removal or addition of one or more electrons to or from a substance, with or without the concomitant removal or addition of a proton or protons.
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1 | Q8I5A0 (/ISS) |
There are 2 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 |
|---|---|---|
|
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.
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1 | Q8I5A0 (/IDA) |
|
3-methyl-2-oxobutanoate dehydrogenase (lipoamide) complex GO:0017086
A protein complex that catalyzes the reaction 3-methyl-2-oxobutanoate + lipoamide = S-(2-methylpropanoyl)-dihydrolipoamide + carbon dioxide (CO2). This requires thiamine diphosphate; the enzyme also acts on (S)-3-methyl-2-oxopentanoate and 4-methyl-2-oxo-pentanoate.
|
1 | Q8I5A0 (/IDA) |