The name of this superfamily has been modified since the most recent official CATH+ release (v4_4_0). At the point of the last release, this superfamily was named:
"TPP-binding domain
".
FunFam 6: 2-hydroxyacyl-CoA lyase 1
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 19 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 |
---|---|---|
Thiamine pyrophosphate binding GO:0030976
Interacting selectively and non-covalently with thiamine pyrophosphate, the diphosphoric ester of thiamine. Acts as a coenzyme of several (de)carboxylases, transketolases, and alpha-oxoacid dehydrogenases.
|
40 |
P0AFI0 (/IDA)
P0AFI0 (/IDA)
P0AFI0 (/IDA)
P0AFI0 (/IDA)
P0AFI0 (/IDA)
P0AFI0 (/IDA)
P0AFI0 (/IDA)
P0AFI0 (/IDA)
P0AFI0 (/IDA)
P0AFI0 (/IDA)
(30 more) |
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
|
39 |
P0AFI0 (/IPI)
P0AFI0 (/IPI)
P0AFI0 (/IPI)
P0AFI0 (/IPI)
P0AFI0 (/IPI)
P0AFI0 (/IPI)
P0AFI0 (/IPI)
P0AFI0 (/IPI)
P0AFI0 (/IPI)
P0AFI0 (/IPI)
(29 more) |
Magnesium ion binding GO:0000287
Interacting selectively and non-covalently with magnesium (Mg) ions.
|
37 |
P0AFI0 (/IDA)
P0AFI0 (/IDA)
P0AFI0 (/IDA)
P0AFI0 (/IDA)
P0AFI0 (/IDA)
P0AFI0 (/IDA)
P0AFI0 (/IDA)
P0AFI0 (/IDA)
P0AFI0 (/IDA)
P0AFI0 (/IDA)
(27 more) |
Oxalyl-CoA decarboxylase activity GO:0008949
Catalysis of the reaction: H(+) + oxalyl-CoA = CO(2) + formyl-CoA.
|
37 |
P0AFI0 (/IDA)
P0AFI0 (/IDA)
P0AFI0 (/IDA)
P0AFI0 (/IDA)
P0AFI0 (/IDA)
P0AFI0 (/IDA)
P0AFI0 (/IDA)
P0AFI0 (/IDA)
P0AFI0 (/IDA)
P0AFI0 (/IDA)
(27 more) |
ADP binding GO:0043531
Interacting selectively and non-covalently with ADP, adenosine 5'-diphosphate.
|
37 |
P0AFI0 (/IDA)
P0AFI0 (/IDA)
P0AFI0 (/IDA)
P0AFI0 (/IDA)
P0AFI0 (/IDA)
P0AFI0 (/IDA)
P0AFI0 (/IDA)
P0AFI0 (/IDA)
P0AFI0 (/IDA)
P0AFI0 (/IDA)
(27 more) |
Magnesium ion binding GO:0000287
Interacting selectively and non-covalently with magnesium (Mg) ions.
|
35 |
P0AFI1 (/ISS)
P0AFI1 (/ISS)
P0AFI1 (/ISS)
P0AFI1 (/ISS)
P0AFI1 (/ISS)
P0AFI1 (/ISS)
P0AFI1 (/ISS)
P0AFI1 (/ISS)
P0AFI1 (/ISS)
P0AFI1 (/ISS)
(25 more) |
Oxalyl-CoA decarboxylase activity GO:0008949
Catalysis of the reaction: H(+) + oxalyl-CoA = CO(2) + formyl-CoA.
|
35 |
P0AFI1 (/ISS)
P0AFI1 (/ISS)
P0AFI1 (/ISS)
P0AFI1 (/ISS)
P0AFI1 (/ISS)
P0AFI1 (/ISS)
P0AFI1 (/ISS)
P0AFI1 (/ISS)
P0AFI1 (/ISS)
P0AFI1 (/ISS)
(25 more) |
ADP binding GO:0043531
Interacting selectively and non-covalently with ADP, adenosine 5'-diphosphate.
|
35 |
P0AFI1 (/ISS)
P0AFI1 (/ISS)
P0AFI1 (/ISS)
P0AFI1 (/ISS)
P0AFI1 (/ISS)
P0AFI1 (/ISS)
P0AFI1 (/ISS)
P0AFI1 (/ISS)
P0AFI1 (/ISS)
P0AFI1 (/ISS)
(25 more) |
Carbon-carbon lyase activity GO:0016830
Catalysis of the cleavage of C-C bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond.
|
3 | Q8CHM7 (/IDA) Q9UJ83 (/IDA) Q9UJ83 (/IDA) |
Protein binding GO:0005515
Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules).
|
2 | Q9UJ83 (/IPI) Q9UJ83 (/IPI) |
Carbon-carbon lyase activity GO:0016830
Catalysis of the cleavage of C-C bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond.
|
2 | Q7K3B7 (/ISS) Q9QXE0 (/ISS) |
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.
|
2 | Q9UJ83 (/IDA) Q9UJ83 (/IDA) |
Signaling receptor binding GO:0005102
Interacting selectively and non-covalently with one or more specific sites on a receptor molecule, a macromolecule that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function.
|
1 | Q9QXE0 (/ISO) |
Lyase activity GO:0016829
Catalysis of the cleavage of C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond. They differ from other enzymes in that two substrates are involved in one reaction direction, but only one in the other direction. When acting on the single substrate, a molecule is eliminated and this generates either a new double bond or a new ring.
|
1 | Q9QXE0 (/IDA) |
Carbon-carbon lyase activity GO:0016830
Catalysis of the cleavage of C-C bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond.
|
1 | Q9QXE0 (/ISO) |
Thiamine pyrophosphate binding GO:0030976
Interacting selectively and non-covalently with thiamine pyrophosphate, the diphosphoric ester of thiamine. Acts as a coenzyme of several (de)carboxylases, transketolases, and alpha-oxoacid dehydrogenases.
|
1 | Q9QXE0 (/ISO) |
Thiamine pyrophosphate binding GO:0030976
Interacting selectively and non-covalently with thiamine pyrophosphate, the diphosphoric ester of thiamine. Acts as a coenzyme of several (de)carboxylases, transketolases, and alpha-oxoacid dehydrogenases.
|
1 | Q9QXE0 (/ISS) |
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
|
1 | Q9QXE0 (/ISO) |
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 | Q9QXE0 (/ISO) |
There are 11 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 |
---|---|---|
Oxalate catabolic process GO:0033611
The chemical reactions and pathways resulting in the breakdown of oxalate, the organic acid ethanedioate.
|
37 |
P0AFI0 (/IDA)
P0AFI0 (/IDA)
P0AFI0 (/IDA)
P0AFI0 (/IDA)
P0AFI0 (/IDA)
P0AFI0 (/IDA)
P0AFI0 (/IDA)
P0AFI0 (/IDA)
P0AFI0 (/IDA)
P0AFI0 (/IDA)
(27 more) |
Oxalate catabolic process GO:0033611
The chemical reactions and pathways resulting in the breakdown of oxalate, the organic acid ethanedioate.
|
35 |
P0AFI1 (/ISS)
P0AFI1 (/ISS)
P0AFI1 (/ISS)
P0AFI1 (/ISS)
P0AFI1 (/ISS)
P0AFI1 (/ISS)
P0AFI1 (/ISS)
P0AFI1 (/ISS)
P0AFI1 (/ISS)
P0AFI1 (/ISS)
(25 more) |
Cellular response to acidic pH GO:0071468
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a pH stimulus with pH < 7. pH is a measure of the acidity or basicity of an aqueous solution.
|
35 |
P0AFI0 (/IMP)
P0AFI0 (/IMP)
P0AFI0 (/IMP)
P0AFI0 (/IMP)
P0AFI0 (/IMP)
P0AFI0 (/IMP)
P0AFI0 (/IMP)
P0AFI0 (/IMP)
P0AFI0 (/IMP)
P0AFI0 (/IMP)
(25 more) |
Fatty acid alpha-oxidation GO:0001561
A metabolic pathway by which 3-methyl branched fatty acids are degraded. These compounds are not degraded by the normal peroxisomal beta-oxidation pathway, because the 3-methyl blocks the dehydrogenation of the hydroxyl group by hydroxyacyl-CoA dehydrogenase. The 3-methyl branched fatty acid is converted in several steps to pristenic acid, which can then feed into the beta-oxidative pathway.
|
3 | Q8CHM7 (/IDA) Q9UJ83 (/IDA) Q9UJ83 (/IDA) |
Fatty acid alpha-oxidation GO:0001561
A metabolic pathway by which 3-methyl branched fatty acids are degraded. These compounds are not degraded by the normal peroxisomal beta-oxidation pathway, because the 3-methyl blocks the dehydrogenation of the hydroxyl group by hydroxyacyl-CoA dehydrogenase. The 3-methyl branched fatty acid is converted in several steps to pristenic acid, which can then feed into the beta-oxidative pathway.
|
2 | Q7K3B7 (/ISS) Q9QXE0 (/ISS) |
Fatty acid alpha-oxidation GO:0001561
A metabolic pathway by which 3-methyl branched fatty acids are degraded. These compounds are not degraded by the normal peroxisomal beta-oxidation pathway, because the 3-methyl blocks the dehydrogenation of the hydroxyl group by hydroxyacyl-CoA dehydrogenase. The 3-methyl branched fatty acid is converted in several steps to pristenic acid, which can then feed into the beta-oxidative pathway.
|
2 | Q9UJ83 (/TAS) Q9UJ83 (/TAS) |
Protein targeting to peroxisome GO:0006625
The process of directing proteins towards the peroxisome, usually using signals contained within the protein.
|
2 | Q9UJ83 (/TAS) Q9UJ83 (/TAS) |
Protein complex oligomerization GO:0051259
The process of creating protein oligomers, compounds composed of a small number, usually between three and ten, of component monomers; protein oligomers may be composed of different or identical monomers. Oligomers may be formed by the polymerization of a number of monomers or the depolymerization of a large protein polymer.
|
2 | Q9UJ83 (/IDA) Q9UJ83 (/IDA) |
Fatty acid alpha-oxidation GO:0001561
A metabolic pathway by which 3-methyl branched fatty acids are degraded. These compounds are not degraded by the normal peroxisomal beta-oxidation pathway, because the 3-methyl blocks the dehydrogenation of the hydroxyl group by hydroxyacyl-CoA dehydrogenase. The 3-methyl branched fatty acid is converted in several steps to pristenic acid, which can then feed into the beta-oxidative pathway.
|
1 | Q9QXE0 (/ISO) |
Lipid metabolic process GO:0006629
The chemical reactions and pathways involving lipids, compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent. Includes fatty acids; neutral fats, other fatty-acid esters, and soaps; long-chain (fatty) alcohols and waxes; sphingoids and other long-chain bases; glycolipids, phospholipids and sphingolipids; and carotenes, polyprenols, sterols, terpenes and other isoprenoids.
|
1 | Q9QXE0 (/IDA) |
Protein complex oligomerization GO:0051259
The process of creating protein oligomers, compounds composed of a small number, usually between three and ten, of component monomers; protein oligomers may be composed of different or identical monomers. Oligomers may be formed by the polymerization of a number of monomers or the depolymerization of a large protein polymer.
|
1 | Q9QXE0 (/ISO) |
There are 9 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.
|
4 | O53639 (/HDA) O53639 (/HDA) O53639 (/HDA) O53639 (/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.
|
4 | O53639 (/HDA) O53639 (/HDA) O53639 (/HDA) O53639 (/HDA) |
Peroxisome GO:0005777
A small organelle enclosed by a single membrane, and found in most eukaryotic cells. Contains peroxidases and other enzymes involved in a variety of metabolic processes including free radical detoxification, lipid catabolism and biosynthesis, and hydrogen peroxide metabolism.
|
3 | Q8CHM7 (/IDA) Q9UJ83 (/IDA) Q9UJ83 (/IDA) |
Peroxisome GO:0005777
A small organelle enclosed by a single membrane, and found in most eukaryotic cells. Contains peroxidases and other enzymes involved in a variety of metabolic processes including free radical detoxification, lipid catabolism and biosynthesis, and hydrogen peroxide metabolism.
|
2 | Q7K3B7 (/ISS) Q9QXE0 (/ISS) |
Peroxisomal matrix GO:0005782
The volume contained within the membranes of a peroxisome; in many cells the matrix contains a crystalloid core largely composed of urate oxidase.
|
2 | Q9UJ83 (/TAS) Q9UJ83 (/TAS) |
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
|
2 | Q9UJ83 (/TAS) Q9UJ83 (/TAS) |
Peroxisome GO:0005777
A small organelle enclosed by a single membrane, and found in most eukaryotic cells. Contains peroxidases and other enzymes involved in a variety of metabolic processes including free radical detoxification, lipid catabolism and biosynthesis, and hydrogen peroxide metabolism.
|
1 | Q7K3B7 (/ISM) |
Peroxisome GO:0005777
A small organelle enclosed by a single membrane, and found in most eukaryotic cells. Contains peroxidases and other enzymes involved in a variety of metabolic processes including free radical detoxification, lipid catabolism and biosynthesis, and hydrogen peroxide metabolism.
|
1 | Q9QXE0 (/ISO) |
Peroxisome GO:0005777
A small organelle enclosed by a single membrane, and found in most eukaryotic cells. Contains peroxidases and other enzymes involved in a variety of metabolic processes including free radical detoxification, lipid catabolism and biosynthesis, and hydrogen peroxide metabolism.
|
1 | Q9QXE0 (/TAS) |