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:
"Butyryl-CoA Dehydrogenase, subunit A, domain 3
".
FunFam 4: Acyl-CoA dehydrogenase FadE25
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 14 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 |
---|---|---|
Acyl-CoA dehydrogenase activity GO:0003995
Catalysis of the reaction: acyl-CoA + acceptor = 2,3-dehydroacyl-CoA + reduced acceptor.
|
12 |
A0A0F7R927 (/ISS)
A0A0F7R927 (/ISS)
A0A0F7R927 (/ISS)
A0A0F7R927 (/ISS)
A0A0F7R927 (/ISS)
A0A0F7R927 (/ISS)
Q81JV7 (/ISS)
Q81JV7 (/ISS)
Q81Q86 (/ISS)
Q81Q86 (/ISS)
(2 more) |
Acyl-CoA dehydrogenase activity GO:0003995
Catalysis of the reaction: acyl-CoA + acceptor = 2,3-dehydroacyl-CoA + reduced acceptor.
|
3 | P15651 (/IDA) P16219 (/IDA) P16219 (/IDA) |
Acyl-CoA dehydrogenase activity GO:0003995
Catalysis of the reaction: acyl-CoA + acceptor = 2,3-dehydroacyl-CoA + reduced acceptor.
|
2 | P16219 (/TAS) P16219 (/TAS) |
Oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor GO:0016628
Catalysis of an oxidation-reduction (redox) reaction in which a CH-CH group acts as a hydrogen or electron donor and reduces NAD or NADP.
|
2 | G3KIM8 (/IDA) H6LGM6 (/IDA) |
FAD binding GO:0071949
Interacting selectively and non-covalently with the oxidized form, FAD, of flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes.
|
2 | G3KIM8 (/IDA) H6LGM6 (/IDA) |
Fatty-acyl-CoA binding GO:0000062
Interacting selectively and non-covalently with acyl-CoA, any derivative of coenzyme A in which the sulfhydryl group is in thiolester linkage with a fatty acyl group.
|
1 | P15651 (/IDA) |
Fatty-acyl-CoA binding GO:0000062
Interacting selectively and non-covalently with acyl-CoA, any derivative of coenzyme A in which the sulfhydryl group is in thiolester linkage with a fatty acyl group.
|
1 | Q07417 (/ISO) |
Acyl-CoA dehydrogenase activity GO:0003995
Catalysis of the reaction: acyl-CoA + acceptor = 2,3-dehydroacyl-CoA + reduced acceptor.
|
1 | Q07417 (/ISO) |
Acyl-CoA dehydrogenase activity GO:0003995
Catalysis of the reaction: acyl-CoA + acceptor = 2,3-dehydroacyl-CoA + reduced acceptor.
|
1 | P15651 (/NAS) |
Butyryl-CoA dehydrogenase activity GO:0004085
Catalysis of the reaction: butanoyl-CoA + electron-transfer flavoprotein = 2-butenoyl-CoA + reduced electron-transfer flavoprotein.
|
1 | P15651 (/IDA) |
Butyryl-CoA dehydrogenase activity GO:0004085
Catalysis of the reaction: butanoyl-CoA + electron-transfer flavoprotein = 2-butenoyl-CoA + reduced electron-transfer flavoprotein.
|
1 | Q07417 (/ISO) |
Butyryl-CoA dehydrogenase activity GO:0004085
Catalysis of the reaction: butanoyl-CoA + electron-transfer flavoprotein = 2-butenoyl-CoA + reduced electron-transfer flavoprotein.
|
1 | P15651 (/TAS) |
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 | P15651 (/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 | Q07417 (/ISO) |
There are 12 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 |
---|---|---|
Fatty acid catabolic process GO:0009062
The chemical reactions and pathways resulting in the breakdown of a fatty acid, any of the aliphatic monocarboxylic acids that can be liberated by hydrolysis from naturally occurring fats and oils. Fatty acids are predominantly straight-chain acids of 4 to 24 carbon atoms, which may be saturated or unsaturated; branched fatty acids and hydroxy fatty acids also occur, and very long chain acids of over 30 carbons are found in waxes.
|
10 | A0A0F7R927 (/ISS) A0A0F7R927 (/ISS) A0A0F7R927 (/ISS) A0A0F7R927 (/ISS) A0A0F7R927 (/ISS) A0A0F7R927 (/ISS) Q81JV7 (/ISS) Q81JV7 (/ISS) Q81Q86 (/ISS) Q81Q86 (/ISS) |
Phospholipid catabolic process GO:0009395
The chemical reactions and pathways resulting in the breakdown of phospholipids, any lipid containing phosphoric acid as a mono- or diester.
|
10 | A0A0F7R927 (/ISS) A0A0F7R927 (/ISS) A0A0F7R927 (/ISS) A0A0F7R927 (/ISS) A0A0F7R927 (/ISS) A0A0F7R927 (/ISS) Q81JV7 (/ISS) Q81JV7 (/ISS) Q81Q86 (/ISS) Q81Q86 (/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).
|
3 | P15651 (/TAS) P16219 (/TAS) P16219 (/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).
|
3 | P15651 (/IDA) P16219 (/IDA) P16219 (/IDA) |
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).
|
2 | Q95S48 (/ISS) Q9VGC2 (/ISS) |
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 | Q07417 (/ISO) |
Response to starvation GO:0042594
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 a starvation stimulus, deprivation of nourishment.
|
1 | P15651 (/IEP) |
Butyrate catabolic process GO:0046359
The chemical reactions and pathways resulting in the breakdown of butyrate, the anion of butyric acid.
|
1 | P15651 (/IDA) |
Butyrate catabolic process GO:0046359
The chemical reactions and pathways resulting in the breakdown of butyrate, the anion of butyric acid.
|
1 | Q07417 (/ISO) |
Protein homotetramerization GO:0051289
The formation of a protein homotetramer, a macromolecular structure consisting of four noncovalently associated identical subunits.
|
1 | P15651 (/IDA) |
Protein homotetramerization GO:0051289
The formation of a protein homotetramer, a macromolecular structure consisting of four noncovalently associated identical subunits.
|
1 | Q07417 (/ISO) |
Response to glucocorticoid GO:0051384
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 a glucocorticoid stimulus. Glucocorticoids are hormonal C21 corticosteroids synthesized from cholesterol with the ability to bind with the cortisol receptor and trigger similar effects. Glucocorticoids act primarily on carbohydrate and protein metabolism, and have anti-inflammatory effects.
|
1 | P15651 (/IEP) |
There are 15 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 wall GO:0005618
The rigid or semi-rigid envelope lying outside the cell membrane of plant, fungal, most prokaryotic cells and some protozoan parasites, maintaining their shape and protecting them from osmotic lysis. In plants it is made of cellulose and, often, lignin; in fungi it is composed largely of polysaccharides; in bacteria it is composed of peptidoglycan; in protozoan parasites such as Giardia species, it's made of carbohydrates and proteins.
|
10 | P9WQG1 (/HDA) P9WQG1 (/HDA) P9WQG1 (/HDA) P9WQG1 (/HDA) P9WQG1 (/HDA) P9WQG1 (/HDA) P9WQG1 (/HDA) P9WQG1 (/HDA) P9WQG1 (/HDA) P9WQG1 (/HDA) |
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
|
10 | P9WQG1 (/HDA) P9WQG1 (/HDA) P9WQG1 (/HDA) P9WQG1 (/HDA) P9WQG1 (/HDA) P9WQG1 (/HDA) P9WQG1 (/HDA) P9WQG1 (/HDA) P9WQG1 (/HDA) P9WQG1 (/HDA) |
Plasma membrane GO:0005886
The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
|
10 | P9WQG1 (/HDA) P9WQG1 (/HDA) P9WQG1 (/HDA) P9WQG1 (/HDA) P9WQG1 (/HDA) P9WQG1 (/HDA) P9WQG1 (/HDA) P9WQG1 (/HDA) P9WQG1 (/HDA) P9WQG1 (/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.
|
6 | E5KSD5 (/IDA) E5KSD5 (/IDA) E9PE82 (/IDA) P15651 (/IDA) P16219 (/IDA) P16219 (/IDA) |
Nucleoplasm GO:0005654
That part of the nuclear content other than the chromosomes or the nucleolus.
|
5 | E5KSD5 (/IDA) E5KSD5 (/IDA) E9PE82 (/IDA) P16219 (/IDA) P16219 (/IDA) |
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.
|
3 | P15651 (/TAS) P16219 (/TAS) P16219 (/TAS) |
Nucleus GO:0005634
A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
|
2 | P16219 (/HDA) P16219 (/HDA) |
Nucleoplasm GO:0005654
That part of the nuclear content other than the chromosomes or the nucleolus.
|
1 | Q07417 (/ISO) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
1 | G3KIM8 (/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 | Q07417 (/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.
|
1 | Q07417 (/ISO) |
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 | P15651 (/IDA) |
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 | Q07417 (/ISO) |
Mitochondrial membrane GO:0031966
Either of the lipid bilayers that surround the mitochondrion and form the mitochondrial envelope.
|
1 | P15651 (/IDA) |
Mitochondrial membrane GO:0031966
Either of the lipid bilayers that surround the mitochondrion and form the mitochondrial envelope.
|
1 | Q07417 (/ISO) |