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: waiting to be named.
FunFam 1: Pyruvate dehydrogenase E1 beta subunit
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 15 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 |
---|---|---|
Pyruvate dehydrogenase (acetyl-transferring) activity GO:0004739
Catalysis of the reaction: pyruvate + lipoamide = S-acetyldihydrolipoamide + CO2.
|
71 |
A0A1S0QWD5 (/ISS)
A0A1S0QWD5 (/ISS)
A0A1S0QWD5 (/ISS)
A0A1S0QWD5 (/ISS)
A0A1S0QWD5 (/ISS)
A0A1S0QWD5 (/ISS)
A0A1S0QWD5 (/ISS)
A0A1S0QWD5 (/ISS)
A0A1S0QWD5 (/ISS)
A0A1S0QWD5 (/ISS)
(61 more) |
3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity GO:0003863
Catalysis of the reaction: 3-methyl-2-oxobutanoate + lipoamide = S-(2-methylpropanoyl)dihydrolipoamide + CO2.
|
60 |
A0A1S0QNL6 (/ISS)
A0A1S0QNL6 (/ISS)
A0A1S0QNL6 (/ISS)
A0A1S0QNL6 (/ISS)
A0A1S0QNL6 (/ISS)
A0A1S0QNL6 (/ISS)
A0A1S0QNL6 (/ISS)
A0A1S0QNL6 (/ISS)
A0A1S0QNL6 (/ISS)
A0A1S0QNL6 (/ISS)
(50 more) |
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).
|
15 |
P21953 (/IPI)
P21953 (/IPI)
P21953 (/IPI)
P75391 (/IPI)
P75391 (/IPI)
P75391 (/IPI)
P9WIS1 (/IPI)
P9WIS1 (/IPI)
P9WIS1 (/IPI)
P9WIS1 (/IPI)
(5 more) |
Fibronectin binding GO:0001968
Interacting selectively and non-covalently with a fibronectin, a group of related adhesive glycoproteins of high molecular weight found on the surface of animal cells, connective tissue matrices, and in extracellular fluids.
|
3 | P75391 (/IPI) P75391 (/IPI) P75391 (/IPI) |
3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity GO:0003863
Catalysis of the reaction: 3-methyl-2-oxobutanoate + lipoamide = S-(2-methylpropanoyl)dihydrolipoamide + CO2.
|
3 | P21953 (/TAS) P21953 (/TAS) P21953 (/TAS) |
Zinc ion binding GO:0008270
Interacting selectively and non-covalently with zinc (Zn) ions.
|
2 | O64688 (/IDA) O64688 (/IDA) |
Acetoin dehydrogenase activity GO:0019152
Catalysis of the reaction: acetoin + NAD+ = diacetyl + NADH + H+.
|
2 | A0A0F7RHX1 (/ISS) A0A0F7RHX1 (/ISS) |
Alpha-ketoacid dehydrogenase activity GO:0003826
Catalysis of an oxidation-reduction (redox) reaction involving an alpha-ketoacid.
|
1 | Q6P3A8 (/IDA) |
Alpha-ketoacid dehydrogenase activity GO:0003826
Catalysis of an oxidation-reduction (redox) reaction involving an alpha-ketoacid.
|
1 | Q8EEN7 (/ISS) |
3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity GO:0003863
Catalysis of the reaction: 3-methyl-2-oxobutanoate + lipoamide = S-(2-methylpropanoyl)dihydrolipoamide + CO2.
|
1 | Q4FKP5 (/ISA) |
Pyruvate dehydrogenase (acetyl-transferring) activity GO:0004739
Catalysis of the reaction: pyruvate + lipoamide = S-acetyldihydrolipoamide + CO2.
|
1 | Q9C6Z3 (/TAS) |
Oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor GO:0016616
Catalysis of an oxidation-reduction (redox) reaction in which a CH-OH group acts as a hydrogen or electron donor and reduces NAD+ or NADP.
|
1 | Q5LLX4 (/ISS) |
Protein-containing complex binding GO:0044877
Interacting selectively and non-covalently with a macromolecular complex.
|
1 | P35738 (/IPI) |
Protein-containing complex binding GO:0044877
Interacting selectively and non-covalently with a macromolecular complex.
|
1 | Q6P3A8 (/ISO) |
Glycosylation-dependent protein binding GO:0140032
Interacting selectively and non-covalently with a protein upon glycosylation of the target protein.
|
1 | P47515 (/IPI) |
There are 24 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 |
---|---|---|
Acetyl-CoA biosynthetic process from pyruvate GO:0006086
The chemical reactions and pathways resulting in the formation of acetyl-CoA from pyruvate.
|
73 |
A0A0F7RHX1 (/ISS)
A0A0F7RHX1 (/ISS)
A0A1S0QWD5 (/ISS)
A0A1S0QWD5 (/ISS)
A0A1S0QWD5 (/ISS)
A0A1S0QWD5 (/ISS)
A0A1S0QWD5 (/ISS)
A0A1S0QWD5 (/ISS)
A0A1S0QWD5 (/ISS)
A0A1S0QWD5 (/ISS)
(63 more) |
Branched-chain amino acid catabolic process GO:0009083
The chemical reactions and pathways resulting in the breakdown of amino acids containing a branched carbon skeleton, comprising isoleucine, leucine and valine.
|
50 |
A0A1S0QNL6 (/ISS)
A0A1S0QNL6 (/ISS)
A0A1S0QNL6 (/ISS)
A0A1S0QNL6 (/ISS)
A0A1S0QNL6 (/ISS)
A0A1S0QNL6 (/ISS)
A0A1S0QNL6 (/ISS)
A0A1S0QNL6 (/ISS)
A0A1S0QNL6 (/ISS)
A0A1S0QNL6 (/ISS)
(40 more) |
Tricarboxylic acid cycle GO:0006099
A nearly universal metabolic pathway in which the acetyl group of acetyl coenzyme A is effectively oxidized to two CO2 and four pairs of electrons are transferred to coenzymes. The acetyl group combines with oxaloacetate to form citrate, which undergoes successive transformations to isocitrate, 2-oxoglutarate, succinyl-CoA, succinate, fumarate, malate, and oxaloacetate again, thus completing the cycle. In eukaryotes the tricarboxylic acid is confined to the mitochondria. See also glyoxylate cycle.
|
13 |
Q8I0X1 (/ISS)
Q8I0X1 (/ISS)
Q8I0X1 (/ISS)
Q8I0X1 (/ISS)
Q8I0X1 (/ISS)
Q8I0X1 (/ISS)
Q8I0X1 (/ISS)
Q8I0X1 (/ISS)
Q8I0X1 (/ISS)
Q8I0X1 (/ISS)
(3 more) |
Fatty acid biosynthetic process GO:0006633
The chemical reactions and pathways resulting in the formation 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.
|
9 | Q8IL09 (/TAS) Q8IL09 (/TAS) Q8IL09 (/TAS) Q8IL09 (/TAS) Q8IL09 (/TAS) Q8IL09 (/TAS) Q8IL09 (/TAS) Q8IL09 (/TAS) Q9C6Z3 (/TAS) |
Branched-chain amino acid catabolic process GO:0009083
The chemical reactions and pathways resulting in the breakdown of amino acids containing a branched carbon skeleton, comprising isoleucine, leucine and valine.
|
3 | P21953 (/IMP) P21953 (/IMP) P21953 (/IMP) |
Branched-chain amino acid catabolic process GO:0009083
The chemical reactions and pathways resulting in the breakdown of amino acids containing a branched carbon skeleton, comprising isoleucine, leucine and valine.
|
3 | P21953 (/TAS) P21953 (/TAS) P21953 (/TAS) |
Plasminogen activation GO:0031639
The process in which inactive plasminogen is processed to active plasmin. This process includes cleavage at an internal Arg-Val site to form an N-terminal A-chain and C-terminal B-chain held together by a disulfide bond, and can include further proteolytic cleavage events to remove the preactivation peptide.
|
3 | P75391 (/IDA) P75391 (/IDA) P75391 (/IDA) |
Interaction with host via substance in symbiont cell outer membrane GO:0044045
An interaction with the host organism mediated by a substance in the symbiont cell outer membrane - a lipid bilayer that forms the outermost layer of the symbiont cell envelope. The host is defined as the larger of the organisms involved in a symbiotic interaction.
|
3 | P75391 (/IMP) P75391 (/IMP) P75391 (/IMP) |
Positive regulation of fibrinolysis GO:0051919
Any process that activates, maintains or increases the frequency, rate or extent of fibrinolysis, an ongoing process that solubilizes fibrin, resulting in the removal of small blood clots.
|
3 | P75391 (/IDA) P75391 (/IDA) P75391 (/IDA) |
Catabolism by symbiont of host protein GO:0052014
The chemical reactions and pathways performed by an organism resulting in the breakdown of protein macromolecules within the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.
|
3 | P75391 (/IDA) P75391 (/IDA) P75391 (/IDA) |
Fatty-acyl-CoA biosynthetic process GO:0046949
The chemical reactions and pathways resulting in the formation of a fatty-acyl-CoA, any derivative of coenzyme A in which the sulfhydryl group is in thiolester linkage with a fatty-acyl group.
|
2 | Q7PLE6 (/ISS) Q8SZ03 (/ISS) |
Pollen tube development GO:0048868
The process whose specific outcome is the progression of a pollen tube over time, from its initial formation to a mature structure.
|
2 | O64688 (/IMP) O64688 (/IMP) |
Response to nutrient GO:0007584
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 nutrient stimulus.
|
1 | P35738 (/IEP) |
Cellular amino acid catabolic process GO:0009063
The chemical reactions and pathways resulting in the breakdown of amino acids, organic acids containing one or more amino substituents.
|
1 | Q8EEN7 (/ISS) |
Cellular amino acid catabolic process GO:0009063
The chemical reactions and pathways resulting in the breakdown of amino acids, organic acids containing one or more amino substituents.
|
1 | Q6P3A8 (/TAS) |
Branched-chain amino acid catabolic process GO:0009083
The chemical reactions and pathways resulting in the breakdown of amino acids containing a branched carbon skeleton, comprising isoleucine, leucine and valine.
|
1 | Q6P3A8 (/ISO) |
Response to absence of light GO:0009646
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 an absence of light stimuli.
|
1 | Q9LDY2 (/IEP) |
Response to sucrose GO:0009744
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 sucrose stimulus.
|
1 | Q9LDY2 (/IEP) |
Cellular response to sucrose starvation GO:0043617
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 deprivation of sucrose.
|
1 | Q9LDY2 (/IEP) |
Acetoin catabolic process GO:0045150
The chemical reactions and pathways resulting in the breakdown of acetoin, 3-hydroxy-2-butanone.
|
1 | Q5LLX4 (/ISS) |
Positive regulation of fatty acid biosynthetic process GO:0045723
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of fatty acids.
|
1 | Q93619 (/IMP) |
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 | P35738 (/IEP) |
Response to cAMP GO:0051591
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 cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate) stimulus.
|
1 | P35738 (/IEP) |
Positive regulation of nematode larval development GO:0061063
Any process that increases the rate, frequency, or extent of nematode larval development, the process whose specific outcome is the progression of the nematode larva over time, from its formation to the mature structure. Nematode larval development begins with the newly hatched first-stage larva (L1) and ends with the end of the last larval stage (for example the fourth larval stage (L4) in C. elegans). Each stage of nematode larval development is characterized by proliferation of specific cell lineages and an increase in body size without alteration of the basic body plan. Nematode larval stages are separated by molts in which each stage-specific exoskeleton, or cuticle, is shed and replaced anew.
|
1 | Q93619 (/IMP) |
There are 27 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 |
---|---|---|
Cytosolic pyruvate dehydrogenase complex GO:0045250
Complex that carries out the oxidative decarboxylation of pyruvate to form acetyl-CoA; comprises subunits possessing three catalytic activities: pyruvate dehydrogenase (E1), dihydrolipoamide S-acetyltransferase (E2), and dihydrolipoamide dehydrogenase (E3). Usually contains fewer subunits than its eukaryotic counterpart; for example, the E. coli complex contains 12 E1 dimers, 8 E2 trimers, and 6 E3 dimers arranged in highly symmetric cubic order.
|
70 |
A0A1S0QWD5 (/ISS)
A0A1S0QWD5 (/ISS)
A0A1S0QWD5 (/ISS)
A0A1S0QWD5 (/ISS)
A0A1S0QWD5 (/ISS)
A0A1S0QWD5 (/ISS)
A0A1S0QWD5 (/ISS)
A0A1S0QWD5 (/ISS)
A0A1S0QWD5 (/ISS)
A0A1S0QWD5 (/ISS)
(60 more) |
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.
|
49 |
A0A1S0QNL6 (/ISS)
A0A1S0QNL6 (/ISS)
A0A1S0QNL6 (/ISS)
A0A1S0QNL6 (/ISS)
A0A1S0QNL6 (/ISS)
A0A1S0QNL6 (/ISS)
A0A1S0QNL6 (/ISS)
A0A1S0QNL6 (/ISS)
A0A1S0QNL6 (/ISS)
A0A1S0QNL6 (/ISS)
(39 more) |
Mitochondrial tricarboxylic acid cycle enzyme complex GO:0030062
Any of the heteromeric enzymes, located in the mitochondrion, that act in the tricarboxylic acid (TCA) cycle.
|
13 |
Q8I0X1 (/ISS)
Q8I0X1 (/ISS)
Q8I0X1 (/ISS)
Q8I0X1 (/ISS)
Q8I0X1 (/ISS)
Q8I0X1 (/ISS)
Q8I0X1 (/ISS)
Q8I0X1 (/ISS)
Q8I0X1 (/ISS)
Q8I0X1 (/ISS)
(3 more) |
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.
|
9 | P9WIS1 (/HDA) P9WIS1 (/HDA) P9WIS1 (/HDA) P9WIS1 (/HDA) P9WIS1 (/HDA) P9WIS1 (/HDA) P9WIS1 (/HDA) P9WIS1 (/HDA) P9WIS1 (/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.
|
9 | P9WIS1 (/HDA) P9WIS1 (/HDA) P9WIS1 (/HDA) P9WIS1 (/HDA) P9WIS1 (/HDA) P9WIS1 (/HDA) P9WIS1 (/HDA) P9WIS1 (/HDA) P9WIS1 (/HDA) |
Apicoplast GO:0020011
The plastid organelle found in apicomplexans.
|
8 | Q8IL09 (/IDA) Q8IL09 (/IDA) Q8IL09 (/IDA) Q8IL09 (/IDA) Q8IL09 (/IDA) Q8IL09 (/IDA) Q8IL09 (/IDA) Q8IL09 (/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.
|
3 | P21953 (/IMP) P21953 (/IMP) P21953 (/IMP) |
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 | P21953 (/TAS) P21953 (/TAS) P21953 (/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.
|
3 | P75391 (/IDA) P75391 (/IDA) P75391 (/IDA) |
Mitochondrial alpha-ketoglutarate dehydrogenase complex GO:0005947
Mitochondrial complex that possesses alpha-ketoglutarate dehydrogenase activity.
|
3 | P21953 (/IMP) P21953 (/IMP) P21953 (/IMP) |
Mitochondrial alpha-ketoglutarate dehydrogenase complex GO:0005947
Mitochondrial complex that possesses alpha-ketoglutarate dehydrogenase activity.
|
3 | P35738 (/ISS) Q55FN7 (/ISS) Q6P3A8 (/ISS) |
Chloroplast GO:0009507
A chlorophyll-containing plastid with thylakoids organized into grana and frets, or stroma thylakoids, and embedded in a stroma.
|
3 | O64688 (/IDA) O64688 (/IDA) Q9C6Z3 (/IDA) |
External side of plasma membrane GO:0009897
The leaflet of the plasma membrane that faces away from the cytoplasm and any proteins embedded or anchored in it or attached to its surface.
|
3 | P75391 (/IDA) P75391 (/IDA) P75391 (/IDA) |
Chloroplast envelope GO:0009941
The double lipid bilayer enclosing the chloroplast and separating its contents from the rest of the cytoplasm; includes the intermembrane space.
|
3 | O64688 (/IDA) O64688 (/IDA) Q9C6Z3 (/IDA) |
Cell surface GO:0009986
The external part of the cell wall and/or plasma membrane.
|
3 | P75391 (/IDA) P75391 (/IDA) P75391 (/IDA) |
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
|
3 | P75391 (/IDA) P75391 (/IDA) P75391 (/IDA) |
Attachment organelle membrane GO:0033111
The lipid bilayer surrounding an attachment organelle. This is a region of the cell membrane facing the environment - in mycoplasma, part of the mycolate outer membrane.
|
3 | P75391 (/IDA) P75391 (/IDA) P75391 (/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 | P35738 (/ISS) Q6P3A8 (/ISS) |
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 | Q6P3A8 (/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 | Q6P3A8 (/ISO) |
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 | Q4FKP5 (/RCA) |
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 | Q6P3A8 (/TAS) |
Mitochondrial alpha-ketoglutarate dehydrogenase complex GO:0005947
Mitochondrial complex that possesses alpha-ketoglutarate dehydrogenase activity.
|
1 | Q4FKP5 (/ISA) |
Mitochondrial alpha-ketoglutarate dehydrogenase complex GO:0005947
Mitochondrial complex that possesses alpha-ketoglutarate dehydrogenase activity.
|
1 | Q6P3A8 (/ISO) |
Chloroplast GO:0009507
A chlorophyll-containing plastid with thylakoids organized into grana and frets, or stroma thylakoids, and embedded in a stroma.
|
1 | Q9C6Z3 (/TAS) |
Chloroplast stroma GO:0009570
The space enclosed by the double membrane of a chloroplast but excluding the thylakoid space. It contains DNA, ribosomes and some temporary products of photosynthesis.
|
1 | Q9C6Z3 (/IDA) |
Plastid pyruvate dehydrogenase complex GO:0010240
Complex that carries out the oxidative decarboxylation of pyruvate to form acetyl-CoA; comprises subunits possessing three catalytic activities: pyruvate dehydrogenase (E1), dihydrolipoamide S-acetyltransferase (E2), and dihydrolipoamide dehydrogenase (E3). This complex is found in plant plastids and is distinct from the one found in mitochondria.
|
1 | Q9C6Z3 (/TAS) |