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:
"FAD/NAD(P)-binding domain
".
FunFam 1: Dihydrolipoyl dehydrogenase, mitochondrial
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 35 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 |
---|---|---|
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.
|
243 |
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
(233 more) |
Dihydrolipoyl dehydrogenase activity GO:0004148
Catalysis of the reaction: protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+.
|
130 |
O81413 (/IDA)
O81413 (/IDA)
P09622 (/IDA)
P09622 (/IDA)
P09622 (/IDA)
P09624 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
(120 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).
|
127 |
O08749 (/IPI)
P09622 (/IPI)
P09622 (/IPI)
P09622 (/IPI)
P09624 (/IPI)
P0A9P0 (/IPI)
P0A9P0 (/IPI)
P0A9P0 (/IPI)
P0A9P0 (/IPI)
P0A9P0 (/IPI)
(117 more) |
Disulfide oxidoreductase activity GO:0015036
Catalysis of the reaction: substrate with reduced sulfide groups = substrate with oxidized disulfide bonds.
|
122 |
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
(112 more) |
NAD(P)+ transhydrogenase activity GO:0008746
Catalysis of the reaction: NADPH + H+ + NAD+ = NADP+ + NADH + H+.
|
120 |
P27306 (/IDA)
P27306 (/IDA)
P27306 (/IDA)
P27306 (/IDA)
P27306 (/IDA)
P27306 (/IDA)
P27306 (/IDA)
P27306 (/IDA)
P27306 (/IDA)
P27306 (/IDA)
(110 more) |
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
|
120 |
P27306 (/IDA)
P27306 (/IDA)
P27306 (/IDA)
P27306 (/IDA)
P27306 (/IDA)
P27306 (/IDA)
P27306 (/IDA)
P27306 (/IDA)
P27306 (/IDA)
P27306 (/IDA)
(110 more) |
Zinc ion binding GO:0008270
Interacting selectively and non-covalently with zinc (Zn) ions.
|
114 |
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
(104 more) |
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
|
111 |
P0A9P0 (/IPI)
P0A9P0 (/IPI)
P0A9P0 (/IPI)
P0A9P0 (/IPI)
P0A9P0 (/IPI)
P0A9P0 (/IPI)
P0A9P0 (/IPI)
P0A9P0 (/IPI)
P0A9P0 (/IPI)
P0A9P0 (/IPI)
(101 more) |
Dihydrolipoyl dehydrogenase activity GO:0004148
Catalysis of the reaction: protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+.
|
83 |
A0A0F7RGS5 (/ISS)
A0A0F7RGS5 (/ISS)
A0A1S0QYK5 (/ISS)
A0A1S0QYK5 (/ISS)
A0A1S0QYK5 (/ISS)
A0A1S0QYK5 (/ISS)
A0A1S0QYK5 (/ISS)
A0A1S0QYK5 (/ISS)
A0A1S0QYK5 (/ISS)
A0A1S0QYK5 (/ISS)
(73 more) |
NAD(P)+ transhydrogenase (B-specific) activity GO:0003957
Catalysis of the reaction: NADPH + H+ + NAD+ = NADP+ + NADH + H+, driving the transfer of a solute or solutes from one side of a membrane to the other. In the course of the reaction (left to right) one H atom is transferred from inside the cell to outside. The reaction is B-specific (i.e. the pro-S hydrogen is transferred from the 4-position of reduced nicotinamide cofactor) with respect to both NAD+ and NADP+.
|
24 |
P50529 (/ISS)
P50529 (/ISS)
P50529 (/ISS)
P50529 (/ISS)
P50529 (/ISS)
P50529 (/ISS)
P50529 (/ISS)
P50529 (/ISS)
Q5LLU3 (/ISS)
Q884I6 (/ISS)
(14 more) |
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.
|
11 |
Q8I5A0 (/IDA)
Q8I5A0 (/IDA)
Q8I5A0 (/IDA)
Q8I5A0 (/IDA)
Q8I5A0 (/IDA)
Q8I5A0 (/IDA)
Q8I5A0 (/IDA)
Q8I5A0 (/IDA)
Q8I5A0 (/IDA)
Q8I5A0 (/IDA)
(1 more) |
Oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor GO:0016655
Catalysis of an oxidation-reduction (redox) reaction in which NADH or NADPH acts as a hydrogen or electron donor and reduces a quinone or a similar acceptor molecule.
|
11 |
P9WHH9 (/IDA)
P9WHH9 (/IDA)
P9WHH9 (/IDA)
P9WHH9 (/IDA)
P9WHH9 (/IDA)
P9WHH9 (/IDA)
P9WHH9 (/IDA)
P9WHH9 (/IDA)
P9WHH9 (/IDA)
P9WHH9 (/IDA)
(1 more) |
Zymogen binding GO:0035375
Interacting selectively and non-covalently with a zymogen, an enzymatically inactive precursor of an enzyme that is often convertible to an active enzyme by proteolysis.
|
11 |
P9WHH9 (/IPI)
P9WHH9 (/IPI)
P9WHH9 (/IPI)
P9WHH9 (/IPI)
P9WHH9 (/IPI)
P9WHH9 (/IPI)
P9WHH9 (/IPI)
P9WHH9 (/IPI)
P9WHH9 (/IPI)
P9WHH9 (/IPI)
(1 more) |
Protein homodimerization activity GO:0042803
Interacting selectively and non-covalently with an identical protein to form a homodimer.
|
11 |
Q8I5A0 (/IDA)
Q8I5A0 (/IDA)
Q8I5A0 (/IDA)
Q8I5A0 (/IDA)
Q8I5A0 (/IDA)
Q8I5A0 (/IDA)
Q8I5A0 (/IDA)
Q8I5A0 (/IDA)
Q8I5A0 (/IDA)
Q8I5A0 (/IDA)
(1 more) |
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.
|
11 |
Q8I5A0 (/IDA)
Q8I5A0 (/IDA)
Q8I5A0 (/IDA)
Q8I5A0 (/IDA)
Q8I5A0 (/IDA)
Q8I5A0 (/IDA)
Q8I5A0 (/IDA)
Q8I5A0 (/IDA)
Q8I5A0 (/IDA)
Q8I5A0 (/IDA)
(1 more) |
NADH binding GO:0070404
Interacting selectively and non-covalently with the reduced form, NADH, of nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions.
|
11 |
P9WHH9 (/IDA)
P9WHH9 (/IDA)
P9WHH9 (/IDA)
P9WHH9 (/IDA)
P9WHH9 (/IDA)
P9WHH9 (/IDA)
P9WHH9 (/IDA)
P9WHH9 (/IDA)
P9WHH9 (/IDA)
P9WHH9 (/IDA)
(1 more) |
Mercury (II) reductase activity GO:0016152
Catalysis of the reaction: H(+) + Hg + NADP(+) = Hg(2+) + NADPH.
|
4 | Q3Z8I0 (/ISS) Q5LW03 (/ISS) Q74DK1 (/ISS) Q74DK1 (/ISS) |
Dihydrolipoyl dehydrogenase activity GO:0004148
Catalysis of the reaction: protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+.
|
3 | P09622 (/TAS) P09622 (/TAS) P09622 (/TAS) |
Copper ion binding GO:0005507
Interacting selectively and non-covalently with copper (Cu) ions.
|
3 | Q9M5K2 (/IDA) Q9M5K3 (/IDA) Q9M5K3 (/IDA) |
ATP binding GO:0005524
Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
|
3 | Q9M5K2 (/IDA) Q9M5K3 (/IDA) Q9M5K3 (/IDA) |
Cobalt ion binding GO:0050897
Interacting selectively and non-covalently with a cobalt (Co) ion.
|
3 | Q9M5K2 (/IDA) Q9M5K3 (/IDA) Q9M5K3 (/IDA) |
Dihydrolipoyl dehydrogenase activity GO:0004148
Catalysis of the reaction: protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+.
|
2 | O08749 (/IMP) Q9M5K2 (/IMP) |
Dihydrolipoyl dehydrogenase activity GO:0004148
Catalysis of the reaction: protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+.
|
1 | O08749 (/ISO) |
Glycine dehydrogenase (decarboxylating) activity GO:0004375
Catalysis of the reaction: glycine + lipoylprotein = S-aminomethyldihydrolipoylprotein + CO2.
|
1 | P09624 (/IMP) |
Oxoglutarate dehydrogenase (succinyl-transferring) activity GO:0004591
Catalysis of the reaction: 2-oxoglutarate + lipoamide = S-succinyldihydrolipoamide + CO2.
|
1 | P09624 (/IMP) |
Pyruvate dehydrogenase activity GO:0004738
Catalysis of the oxidative decarboxylation of pyruvate.
|
1 | P09624 (/IMP) |
Pyruvate dehydrogenase (acetyl-transferring) activity GO:0004739
Catalysis of the reaction: pyruvate + lipoamide = S-acetyldihydrolipoamide + CO2.
|
1 | O00087 (/ISO) |
Disulfide oxidoreductase activity GO:0015036
Catalysis of the reaction: substrate with reduced sulfide groups = substrate with oxidized disulfide bonds.
|
1 | Q04933 (/ISM) |
Leghemoglobin reductase activity GO:0015043
Catalysis of the reaction: NADPH + H+ + 2 ferrileghemoglobin = NADP+ + 2 ferroleghemoglobin.
|
1 | Q9SPB1 (/IDA) |
Oxoglutarate dehydrogenase (NAD+) activity GO:0034602
Catalysis of the reaction: 2-oxoglutarate + CoA + NAD+ = succinyl-CoA + CO2 + NADH.
|
1 | Q9FEN7 (/IDA) |
Lipoamide binding GO:0043544
Interacting selectively and non-covalently with lipoamide, the functional form of lipoic acid in which the carboxyl group is attached to protein by an amide linkage to a lysine amino group.
|
1 | Q6P6R2 (/IDA) |
Lipoamide binding GO:0043544
Interacting selectively and non-covalently with lipoamide, the functional form of lipoic acid in which the carboxyl group is attached to protein by an amide linkage to a lysine amino group.
|
1 | O08749 (/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 | O08749 (/ISO) |
NAD binding GO:0051287
Interacting selectively and non-covalently with nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH.
|
1 | Q6P6R2 (/IDA) |
NAD binding GO:0051287
Interacting selectively and non-covalently with nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH.
|
1 | O08749 (/ISO) |
There are 63 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.
|
122 |
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
(112 more) |
Cell redox homeostasis GO:0045454
Any process that maintains the redox environment of a cell or compartment within a cell.
|
120 |
P27306 (/IMP)
P27306 (/IMP)
P27306 (/IMP)
P27306 (/IMP)
P27306 (/IMP)
P27306 (/IMP)
P27306 (/IMP)
P27306 (/IMP)
P27306 (/IMP)
P27306 (/IMP)
(110 more) |
Pyruvate metabolic process GO:0006090
The chemical reactions and pathways involving pyruvate, 2-oxopropanoate.
|
112 |
P09624 (/IMP)
P0A9P0 (/IMP)
P0A9P0 (/IMP)
P0A9P0 (/IMP)
P0A9P0 (/IMP)
P0A9P0 (/IMP)
P0A9P0 (/IMP)
P0A9P0 (/IMP)
P0A9P0 (/IMP)
P0A9P0 (/IMP)
(102 more) |
2-oxoglutarate metabolic process GO:0006103
The chemical reactions and pathways involving oxoglutarate, the dianion of 2-oxoglutaric acid. It is a key constituent of the TCA cycle and a key intermediate in amino-acid metabolism.
|
112 |
P09624 (/IMP)
P0A9P0 (/IMP)
P0A9P0 (/IMP)
P0A9P0 (/IMP)
P0A9P0 (/IMP)
P0A9P0 (/IMP)
P0A9P0 (/IMP)
P0A9P0 (/IMP)
P0A9P0 (/IMP)
P0A9P0 (/IMP)
(102 more) |
Pyruvate metabolic process GO:0006090
The chemical reactions and pathways involving pyruvate, 2-oxopropanoate.
|
111 |
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
(101 more) |
2-oxoglutarate metabolic process GO:0006103
The chemical reactions and pathways involving oxoglutarate, the dianion of 2-oxoglutaric acid. It is a key constituent of the TCA cycle and a key intermediate in amino-acid metabolism.
|
111 |
P0A9P0 (/IGI)
P0A9P0 (/IGI)
P0A9P0 (/IGI)
P0A9P0 (/IGI)
P0A9P0 (/IGI)
P0A9P0 (/IGI)
P0A9P0 (/IGI)
P0A9P0 (/IGI)
P0A9P0 (/IGI)
P0A9P0 (/IGI)
(101 more) |
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.
|
111 |
P0A9P0 (/IMP)
P0A9P0 (/IMP)
P0A9P0 (/IMP)
P0A9P0 (/IMP)
P0A9P0 (/IMP)
P0A9P0 (/IMP)
P0A9P0 (/IMP)
P0A9P0 (/IMP)
P0A9P0 (/IMP)
P0A9P0 (/IMP)
(101 more) |
Glycine decarboxylation via glycine cleavage system GO:0019464
The chemical reactions and pathways resulting in the breakdown of glycine by oxidative cleavage to carbon dioxide, ammonia, and a methylene group, mediated by enzymes of the glycine cleavage complex.
|
111 |
P0A9P0 (/IMP)
P0A9P0 (/IMP)
P0A9P0 (/IMP)
P0A9P0 (/IMP)
P0A9P0 (/IMP)
P0A9P0 (/IMP)
P0A9P0 (/IMP)
P0A9P0 (/IMP)
P0A9P0 (/IMP)
P0A9P0 (/IMP)
(101 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.
|
39 |
Q81M68 (/ISS)
Q81M68 (/ISS)
Q81M68 (/ISS)
Q81M68 (/ISS)
Q81M68 (/ISS)
Q81M68 (/ISS)
Q81M68 (/ISS)
Q81M68 (/ISS)
Q81M68 (/ISS)
Q81M68 (/ISS)
(29 more) |
Acetyl-CoA biosynthetic process from pyruvate GO:0006086
The chemical reactions and pathways resulting in the formation of acetyl-CoA from pyruvate.
|
20 |
A0A1S0QYK5 (/ISS)
A0A1S0QYK5 (/ISS)
A0A1S0QYK5 (/ISS)
A0A1S0QYK5 (/ISS)
A0A1S0QYK5 (/ISS)
A0A1S0QYK5 (/ISS)
A0A1S0QYK5 (/ISS)
A0A1S0QYK5 (/ISS)
A0A1S0QYK5 (/ISS)
A0A1S0QYK5 (/ISS)
(10 more) |
Pathogenesis GO:0009405
The set of specific processes that generate the ability of an organism to induce an abnormal, generally detrimental state in another organism.
|
13 |
Q9I3D1 (/IDA)
Q9I3D1 (/IDA)
Q9I3D1 (/IDA)
Q9I3D1 (/IDA)
Q9I3D1 (/IDA)
Q9I3D1 (/IDA)
Q9I3D1 (/IDA)
Q9I3D1 (/IDA)
Q9I3D1 (/IDA)
Q9I3D1 (/IDA)
(3 more) |
Evasion or tolerance of host immune response GO:0020012
Any process, either active or passive, by which an organism avoids the effects of the host organism's immune response. The host is defined as the larger of the organisms involved in a symbiotic interaction.
|
13 |
Q9I3D1 (/IDA)
Q9I3D1 (/IDA)
Q9I3D1 (/IDA)
Q9I3D1 (/IDA)
Q9I3D1 (/IDA)
Q9I3D1 (/IDA)
Q9I3D1 (/IDA)
Q9I3D1 (/IDA)
Q9I3D1 (/IDA)
Q9I3D1 (/IDA)
(3 more) |
Cell redox homeostasis GO:0045454
Any process that maintains the redox environment of a cell or compartment within a cell.
|
11 |
P9WHH9 (/IDA)
P9WHH9 (/IDA)
P9WHH9 (/IDA)
P9WHH9 (/IDA)
P9WHH9 (/IDA)
P9WHH9 (/IDA)
P9WHH9 (/IDA)
P9WHH9 (/IDA)
P9WHH9 (/IDA)
P9WHH9 (/IDA)
(1 more) |
Cell redox homeostasis GO:0045454
Any process that maintains the redox environment of a cell or compartment within a cell.
|
11 |
P9WHH9 (/TAS)
P9WHH9 (/TAS)
P9WHH9 (/TAS)
P9WHH9 (/TAS)
P9WHH9 (/TAS)
P9WHH9 (/TAS)
P9WHH9 (/TAS)
P9WHH9 (/TAS)
P9WHH9 (/TAS)
P9WHH9 (/TAS)
(1 more) |
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.
|
11 |
Q8I5A0 (/ISS)
Q8I5A0 (/ISS)
Q8I5A0 (/ISS)
Q8I5A0 (/ISS)
Q8I5A0 (/ISS)
Q8I5A0 (/ISS)
Q8I5A0 (/ISS)
Q8I5A0 (/ISS)
Q8I5A0 (/ISS)
Q8I5A0 (/ISS)
(1 more) |
Histone succinylation GO:0106077
The modification of a histone by the addition of an succinyl group.
|
9 | O08749 (/ISS) P09623 (/ISS) P49819 (/ISS) Q5R4B1 (/ISS) Q60HG3 (/ISS) Q60HG3 (/ISS) Q6P6R2 (/ISS) Q811C4 (/ISS) Q8CIZ7 (/ISS) |
Response to mercury ion GO:0046689
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 mercury ion stimulus.
|
4 | Q3Z8I0 (/ISS) Q5LW03 (/ISS) Q74DK1 (/ISS) Q74DK1 (/ISS) |
Mitochondrial acetyl-CoA biosynthetic process from pyruvate GO:0061732
The chemical reactions and pathways resulting in the formation of acetyl-CoA from pyruvate in the mitochondrion. The process begins with the transport of pyruvate from the cytosol to the mitochondrion where it is subsequently decarboxylated to form acetyl-CoA.
|
4 | O08749 (/IC) P09622 (/IC) P09622 (/IC) P09622 (/IC) |
Pyruvate metabolic process GO:0006090
The chemical reactions and pathways involving pyruvate, 2-oxopropanoate.
|
3 | P09622 (/TAS) P09622 (/TAS) P09622 (/TAS) |
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.
|
3 | P09622 (/TAS) P09622 (/TAS) P09622 (/TAS) |
Lysine catabolic process GO:0006554
The chemical reactions and pathways resulting in the breakdown of lysine, 2,6-diaminohexanoic acid.
|
3 | P09622 (/TAS) P09622 (/TAS) P09622 (/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 | P09622 (/TAS) P09622 (/TAS) P09622 (/TAS) |
Response to cadmium ion GO:0046686
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 cadmium (Cd) ion stimulus.
|
3 | Q9M5K2 (/IEP) Q9M5K3 (/IEP) Q9M5K3 (/IEP) |
Histone succinylation GO:0106077
The modification of a histone by the addition of an succinyl group.
|
3 | P09622 (/IDA) P09622 (/IDA) P09622 (/IDA) |
Acetyl-CoA biosynthetic process from pyruvate GO:0006086
The chemical reactions and pathways resulting in the formation of acetyl-CoA from pyruvate.
|
2 | O00087 (/ISO) O08749 (/ISO) |
Fermentation GO:0006113
The anaerobic enzymatic conversion of organic compounds, especially carbohydrates, coupling the oxidation and reduction of NAD/H and the generation of adenosine triphosphate (ATP).
|
2 | A0A0F7RGS5 (/ISS) A0A0F7RGS5 (/ISS) |
Glycine catabolic process GO:0006546
The chemical reactions and pathways resulting in the breakdown of glycine, aminoethanoic acid.
|
2 | Q54EW8 (/ISS) Q9VVL7 (/ISS) |
Filamentous growth GO:0030447
The process in which a multicellular organism, a unicellular organism or a group of unicellular organisms grow in a threadlike, filamentous shape.
|
2 | Q59RQ6 (/IMP) Q59RQ6 (/IMP) |
Filamentous growth of a population of unicellular organisms in response to biotic stimulus GO:0036180
The process in which a group of unicellular organisms grow in a threadlike, filamentous shape in response to a biotic (living) stimulus.
|
2 | Q59RQ6 (/IMP) Q59RQ6 (/IMP) |
Filamentous growth of a population of unicellular organisms GO:0044182
The process in which a group of unicellular organisms grow in a threadlike, filamentous shape.
|
2 | Q59RQ6 (/IMP) Q59RQ6 (/IMP) |
Heart contraction GO:0060047
The multicellular organismal process in which the heart decreases in volume in a characteristic way to propel blood through the body.
|
2 | Q6TNU6 (/IMP) Q803L1 (/IMP) |
Acetyl-CoA biosynthetic process from pyruvate GO:0006086
The chemical reactions and pathways resulting in the formation of acetyl-CoA from pyruvate.
|
1 | Q6P6R2 (/IDA) |
Acetyl-CoA biosynthetic process from pyruvate GO:0006086
The chemical reactions and pathways resulting in the formation of acetyl-CoA from pyruvate.
|
1 | Q5LRA7 (/TAS) |
Generation of precursor metabolites and energy GO:0006091
The chemical reactions and pathways resulting in the formation of precursor metabolites, substances from which energy is derived, and any process involved in the liberation of energy from these substances.
|
1 | O00087 (/IC) |
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.
|
1 | Q9VVL7 (/ISS) |
2-oxoglutarate metabolic process GO:0006103
The chemical reactions and pathways involving oxoglutarate, the dianion of 2-oxoglutaric acid. It is a key constituent of the TCA cycle and a key intermediate in amino-acid metabolism.
|
1 | O00087 (/IC) |
2-oxoglutarate metabolic process GO:0006103
The chemical reactions and pathways involving oxoglutarate, the dianion of 2-oxoglutaric acid. It is a key constituent of the TCA cycle and a key intermediate in amino-acid metabolism.
|
1 | Q6P6R2 (/IDA) |
2-oxoglutarate metabolic process GO:0006103
The chemical reactions and pathways involving oxoglutarate, the dianion of 2-oxoglutaric acid. It is a key constituent of the TCA cycle and a key intermediate in amino-acid metabolism.
|
1 | O08749 (/ISO) |
Mitochondrial electron transport, NADH to ubiquinone GO:0006120
The transfer of electrons from NADH to ubiquinone that occurs during oxidative phosphorylation, mediated by the multisubunit enzyme known as complex I.
|
1 | O08749 (/IMP) |
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
|
1 | O08749 (/IDA) |
Glycine catabolic process GO:0006546
The chemical reactions and pathways resulting in the breakdown of glycine, aminoethanoic acid.
|
1 | P09624 (/IMP) |
Isoleucine catabolic process GO:0006550
The chemical reactions and pathways resulting in the breakdown of isoleucine, (2R*,3R*)-2-amino-3-methylpentanoic acid.
|
1 | P09624 (/IMP) |
Isoleucine catabolic process GO:0006550
The chemical reactions and pathways resulting in the breakdown of isoleucine, (2R*,3R*)-2-amino-3-methylpentanoic acid.
|
1 | Q54EW8 (/ISS) |
Leucine catabolic process GO:0006552
The chemical reactions and pathways resulting in the breakdown of leucine, 2-amino-4-methylpentanoic acid.
|
1 | P09624 (/IMP) |
Leucine catabolic process GO:0006552
The chemical reactions and pathways resulting in the breakdown of leucine, 2-amino-4-methylpentanoic acid.
|
1 | Q54EW8 (/ISS) |
L-serine biosynthetic process GO:0006564
The chemical reactions and pathways resulting in the formation of L-serine, the L-enantiomer of serine, i.e. (2S)-2-amino-3-hydroxypropanoic acid.
|
1 | P09624 (/IMP) |
L-serine biosynthetic process GO:0006564
The chemical reactions and pathways resulting in the formation of L-serine, the L-enantiomer of serine, i.e. (2S)-2-amino-3-hydroxypropanoic acid.
|
1 | Q54EW8 (/ISS) |
Valine catabolic process GO:0006574
The chemical reactions and pathways resulting in the breakdown of valine, 2-amino-3-methylbutanoic acid.
|
1 | P09624 (/IMP) |
Valine catabolic process GO:0006574
The chemical reactions and pathways resulting in the breakdown of valine, 2-amino-3-methylbutanoic acid.
|
1 | Q54EW8 (/ISS) |
Lipoamide metabolic process GO:0006748
The chemical reactions and pathways involving lipoamide, the functional form of lipoic acid in which the carboxyl group is attached to protein by an amide linkage to a lysine amino group.
|
1 | Q9VVL7 (/ISS) |
Gastrulation GO:0007369
A complex and coordinated series of cellular movements that occurs at the end of cleavage during embryonic development of most animals. The details of gastrulation vary from species to species, but usually result in the formation of the three primary germ layers, ectoderm, mesoderm and endoderm.
|
1 | O08749 (/IMP) |
Aging GO:0007568
A developmental process that is a deterioration and loss of function over time. Aging includes loss of functions such as resistance to disease, homeostasis, and fertility, as well as wear and tear. Aging includes cellular senescence, but is more inclusive. May precede death and may succeed developmental maturation (GO:0021700).
|
1 | Q6P6R2 (/IEP) |
Lipoate metabolic process GO:0009106
The chemical reactions and pathways involving lipoate, 1,2-dithiolane-3-pentanoate, the anion derived from lipoic acid.
|
1 | Q6P6R2 (/IDA) |
Lipoate metabolic process GO:0009106
The chemical reactions and pathways involving lipoate, 1,2-dithiolane-3-pentanoate, the anion derived from lipoic acid.
|
1 | O08749 (/ISO) |
Glycine decarboxylation via glycine cleavage system GO:0019464
The chemical reactions and pathways resulting in the breakdown of glycine by oxidative cleavage to carbon dioxide, ammonia, and a methylene group, mediated by enzymes of the glycine cleavage complex.
|
1 | O00087 (/ISO) |
Regulation of membrane potential GO:0042391
Any process that modulates the establishment or extent of a membrane potential, the electric potential existing across any membrane arising from charges in the membrane itself and from the charges present in the media on either side of the membrane.
|
1 | O08749 (/IMP) |
Hydrogen peroxide metabolic process GO:0042743
The chemical reactions and pathways involving hydrogen peroxide (H2O2), a potentially harmful byproduct of aerobic cellular respiration which can cause damage to DNA.
|
1 | P09624 (/IGI) |
Hydrogen peroxide metabolic process GO:0042743
The chemical reactions and pathways involving hydrogen peroxide (H2O2), a potentially harmful byproduct of aerobic cellular respiration which can cause damage to DNA.
|
1 | P09624 (/IMP) |
Sperm capacitation GO:0048240
A process required for sperm to reach fertilization competence. Sperm undergo an incompletely understood series of morphological and molecular maturational processes, termed capacitation, involving, among other processes, protein tyrosine phosphorylation and increased intracellular calcium.
|
1 | O08749 (/IDA) |
Dihydrolipoamide metabolic process GO:0051068
The chemical reactions and pathways involving dihydrolipoamide, the reduced form of lipoamide, produced as an intermediate in the reactions in which lipoamide acts as a cofactor.
|
1 | Q6P6R2 (/IDA) |
Dihydrolipoamide metabolic process GO:0051068
The chemical reactions and pathways involving dihydrolipoamide, the reduced form of lipoamide, produced as an intermediate in the reactions in which lipoamide acts as a cofactor.
|
1 | O08749 (/ISO) |
Mitochondrial acetyl-CoA biosynthetic process from pyruvate GO:0061732
The chemical reactions and pathways resulting in the formation of acetyl-CoA from pyruvate in the mitochondrion. The process begins with the transport of pyruvate from the cytosol to the mitochondrion where it is subsequently decarboxylated to form acetyl-CoA.
|
1 | O08749 (/ISO) |
Histone succinylation GO:0106077
The modification of a histone by the addition of an succinyl group.
|
1 | O08749 (/ISO) |
There are 53 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 |
---|---|---|
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
|
231 |
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
(221 more) |
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
|
132 |
P0A9P0 (/HDA)
P0A9P0 (/HDA)
P0A9P0 (/HDA)
P0A9P0 (/HDA)
P0A9P0 (/HDA)
P0A9P0 (/HDA)
P0A9P0 (/HDA)
P0A9P0 (/HDA)
P0A9P0 (/HDA)
P0A9P0 (/HDA)
(122 more) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
112 |
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
P0A9P0 (/IDA)
(102 more) |
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
|
111 |
P0A9P0 (/HDA)
P0A9P0 (/HDA)
P0A9P0 (/HDA)
P0A9P0 (/HDA)
P0A9P0 (/HDA)
P0A9P0 (/HDA)
P0A9P0 (/HDA)
P0A9P0 (/HDA)
P0A9P0 (/HDA)
P0A9P0 (/HDA)
(101 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.
|
39 |
Q81M68 (/ISS)
Q81M68 (/ISS)
Q81M68 (/ISS)
Q81M68 (/ISS)
Q81M68 (/ISS)
Q81M68 (/ISS)
Q81M68 (/ISS)
Q81M68 (/ISS)
Q81M68 (/ISS)
Q81M68 (/ISS)
(29 more) |
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.
|
21 |
P9WHH5 (/HDA)
P9WHH5 (/HDA)
P9WHH5 (/HDA)
P9WHH5 (/HDA)
P9WHH5 (/HDA)
P9WHH5 (/HDA)
P9WHH5 (/HDA)
P9WHH5 (/HDA)
P9WHH5 (/HDA)
P9WHH5 (/HDA)
(11 more) |
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.
|
20 |
A0A1S0QYK5 (/ISS)
A0A1S0QYK5 (/ISS)
A0A1S0QYK5 (/ISS)
A0A1S0QYK5 (/ISS)
A0A1S0QYK5 (/ISS)
A0A1S0QYK5 (/ISS)
A0A1S0QYK5 (/ISS)
A0A1S0QYK5 (/ISS)
A0A1S0QYK5 (/ISS)
A0A1S0QYK5 (/ISS)
(10 more) |
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.
|
15 |
A0A024R713 (/IDA)
A0A024R713 (/IDA)
A0A024R713 (/IDA)
O08749 (/IDA)
O81413 (/IDA)
O81413 (/IDA)
P09622 (/IDA)
P09622 (/IDA)
P09622 (/IDA)
P31023 (/IDA)
(5 more) |
Pyruvate dehydrogenase complex GO:0045254
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).
|
15 |
P09622 (/IDA)
P09622 (/IDA)
P09622 (/IDA)
P9WHH9 (/IDA)
P9WHH9 (/IDA)
P9WHH9 (/IDA)
P9WHH9 (/IDA)
P9WHH9 (/IDA)
P9WHH9 (/IDA)
P9WHH9 (/IDA)
(5 more) |
Extracellular region GO:0005576
The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.
|
11 |
P9WHH9 (/HDA)
P9WHH9 (/HDA)
P9WHH9 (/HDA)
P9WHH9 (/HDA)
P9WHH9 (/HDA)
P9WHH9 (/HDA)
P9WHH9 (/HDA)
P9WHH9 (/HDA)
P9WHH9 (/HDA)
P9WHH9 (/HDA)
(1 more) |
Extracellular region GO:0005576
The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.
|
11 |
P9WHH9 (/IDA)
P9WHH9 (/IDA)
P9WHH9 (/IDA)
P9WHH9 (/IDA)
P9WHH9 (/IDA)
P9WHH9 (/IDA)
P9WHH9 (/IDA)
P9WHH9 (/IDA)
P9WHH9 (/IDA)
P9WHH9 (/IDA)
(1 more) |
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.
|
11 |
Q8I5A0 (/IDA)
Q8I5A0 (/IDA)
Q8I5A0 (/IDA)
Q8I5A0 (/IDA)
Q8I5A0 (/IDA)
Q8I5A0 (/IDA)
Q8I5A0 (/IDA)
Q8I5A0 (/IDA)
Q8I5A0 (/IDA)
Q8I5A0 (/IDA)
(1 more) |
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
|
11 |
P9WHH9 (/TAS)
P9WHH9 (/TAS)
P9WHH9 (/TAS)
P9WHH9 (/TAS)
P9WHH9 (/TAS)
P9WHH9 (/TAS)
P9WHH9 (/TAS)
P9WHH9 (/TAS)
P9WHH9 (/TAS)
P9WHH9 (/TAS)
(1 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.
|
11 |
Q8I5A0 (/IDA)
Q8I5A0 (/IDA)
Q8I5A0 (/IDA)
Q8I5A0 (/IDA)
Q8I5A0 (/IDA)
Q8I5A0 (/IDA)
Q8I5A0 (/IDA)
Q8I5A0 (/IDA)
Q8I5A0 (/IDA)
Q8I5A0 (/IDA)
(1 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.
|
10 | P9WHH5 (/HDA) P9WHH5 (/HDA) P9WHH5 (/HDA) P9WHH5 (/HDA) P9WHH5 (/HDA) P9WHH5 (/HDA) P9WHH5 (/HDA) P9WHH5 (/HDA) P9WHH5 (/HDA) P9WHH5 (/HDA) |
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.
|
9 | O08749 (/ISS) P09623 (/ISS) P49819 (/ISS) Q5R4B1 (/ISS) Q60HG3 (/ISS) Q60HG3 (/ISS) Q6P6R2 (/ISS) Q811C4 (/ISS) Q8CIZ7 (/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.
|
8 | P09623 (/ISS) P49819 (/ISS) Q5R4B1 (/ISS) Q5ZM32 (/ISS) Q60HG3 (/ISS) Q60HG3 (/ISS) Q811C4 (/ISS) Q8CIZ7 (/ISS) |
Oxoglutarate dehydrogenase complex GO:0045252
A complex of multiple copies of three enzymatic components: oxoglutarate dehydrogenase (lipoamide) ; EC:1.2.4.2 (E1), dihydrolipoamide S-succinyltransferase ; EC:2.3.1.61 (E2) and dihydrolipoamide dehydrogenase ; EC:1.8.1.4 (E3); catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and carbon dioxide (CO2).
|
8 | O08749 (/ISS) P09623 (/ISS) P49819 (/ISS) Q5R4B1 (/ISS) Q60HG3 (/ISS) Q60HG3 (/ISS) Q811C4 (/ISS) Q8CIZ7 (/ISS) |
Nucleoplasm GO:0005654
That part of the nuclear content other than the chromosomes or the nucleolus.
|
6 | A0A024R713 (/IDA) A0A024R713 (/IDA) A0A024R713 (/IDA) P09622 (/IDA) P09622 (/IDA) P09622 (/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.
|
6 | O00087 (/HDA) O08749 (/HDA) P09622 (/HDA) P09622 (/HDA) P09622 (/HDA) P09624 (/HDA) |
Oxoglutarate dehydrogenase complex GO:0045252
A complex of multiple copies of three enzymatic components: oxoglutarate dehydrogenase (lipoamide) ; EC:1.2.4.2 (E1), dihydrolipoamide S-succinyltransferase ; EC:2.3.1.61 (E2) and dihydrolipoamide dehydrogenase ; EC:1.8.1.4 (E3); catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and carbon dioxide (CO2).
|
4 | P09622 (/IDA) P09622 (/IDA) P09622 (/IDA) Q6P6R2 (/IDA) |
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.
|
3 | P09622 (/IDA) P09622 (/IDA) P09622 (/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 | O08749 (/ISO) Q04933 (/ISO) Q4Q4U1 (/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.
|
3 | P09622 (/TAS) P09622 (/TAS) P09622 (/TAS) |
Mitochondrial respiratory chain complex I GO:0005747
A protein complex located in the mitochondrial inner membrane that forms part of the mitochondrial respiratory chain. It contains about 25 different polypeptide subunits, including NADH dehydrogenase (ubiquinone), flavin mononucleotide and several different iron-sulfur clusters containing non-heme iron. The iron undergoes oxidation-reduction between Fe(II) and Fe(III), and catalyzes proton translocation linked to the oxidation of NADH by ubiquinone.
|
3 | Q9M5K2 (/IDA) Q9M5K3 (/IDA) Q9M5K3 (/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 | P09622 (/TAS) P09622 (/TAS) P09622 (/TAS) |
Apoplast GO:0048046
The cell membranes and intracellular regions in a plant are connected through plasmodesmata, and plants may be described as having two major compartments: the living symplast and the non-living apoplast. The apoplast is external to the plasma membrane and includes cell walls, intercellular spaces and the lumen of dead structures such as xylem vessels. Water and solutes pass freely through it.
|
3 | Q9M5K2 (/IDA) Q9M5K3 (/IDA) Q9M5K3 (/IDA) |
Mitochondrial pyruvate dehydrogenase complex GO:0005967
Complex that carries out the oxidative decarboxylation of pyruvate to form acetyl-CoA in eukaryotes; includes subunits possessing three catalytic activities: pyruvate dehydrogenase (E1), dihydrolipoamide S-acetyltransferase (E2), and dihydrolipoamide dehydrogenase (E3). The This Eukaryotic form usually contains more subunits than its bacterial counterpart; for example, one known complex contains 30 E1 dimers, 60 E2 monomers, and 6 E3 dimers as well as a few copies of pyruvate dehydrogenase kinase and pyruvate dehydrogenase phosphatase.
|
2 | O00087 (/ISS) Q54EW8 (/ISS) |
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.
|
1 | O08749 (/ISO) |
Nucleoplasm GO:0005654
That part of the nuclear content other than the chromosomes or the nucleolus.
|
1 | O08749 (/ISO) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
1 | Q04933 (/ISM) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
1 | Q4Q4U1 (/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 | Q04933 (/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 | Q04933 (/RCA) |
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 | Q54EW8 (/ISS) |
Cilium GO:0005929
A specialized eukaryotic organelle that consists of a filiform extrusion of the cell surface and of some cytoplasmic parts. Each cilium is largely bounded by an extrusion of the cytoplasmic (plasma) membrane, and contains a regular longitudinal array of microtubules, anchored to a basal body.
|
1 | O08749 (/IDA) |
Mitochondrial alpha-ketoglutarate dehydrogenase complex GO:0005947
Mitochondrial complex that possesses alpha-ketoglutarate dehydrogenase activity.
|
1 | Q9VVL7 (/ISS) |
Glycine cleavage complex GO:0005960
A protein complex that catalyzes the reversible oxidation of glycine. In E. coli, it has four components: dihydrolipoamide dehydrogenase, glycine dehydrogenase (decarboxylating), lipoyl-GcvH-protein and aminomethyltransferase, also known as L, P, H, and T.
|
1 | P31023 (/IDA) |
Glycine cleavage complex GO:0005960
A protein complex that catalyzes the reversible oxidation of glycine. In E. coli, it has four components: dihydrolipoamide dehydrogenase, glycine dehydrogenase (decarboxylating), lipoyl-GcvH-protein and aminomethyltransferase, also known as L, P, H, and T.
|
1 | P09624 (/IMP) |
Glycine cleavage complex GO:0005960
A protein complex that catalyzes the reversible oxidation of glycine. In E. coli, it has four components: dihydrolipoamide dehydrogenase, glycine dehydrogenase (decarboxylating), lipoyl-GcvH-protein and aminomethyltransferase, also known as L, P, H, and T.
|
1 | O00087 (/ISO) |
Glycine cleavage complex GO:0005960
A protein complex that catalyzes the reversible oxidation of glycine. In E. coli, it has four components: dihydrolipoamide dehydrogenase, glycine dehydrogenase (decarboxylating), lipoyl-GcvH-protein and aminomethyltransferase, also known as L, P, H, and T.
|
1 | Q9VVL7 (/ISS) |
Mitochondrial pyruvate dehydrogenase complex GO:0005967
Complex that carries out the oxidative decarboxylation of pyruvate to form acetyl-CoA in eukaryotes; includes subunits possessing three catalytic activities: pyruvate dehydrogenase (E1), dihydrolipoamide S-acetyltransferase (E2), and dihydrolipoamide dehydrogenase (E3). The This Eukaryotic form usually contains more subunits than its bacterial counterpart; for example, one known complex contains 30 E1 dimers, 60 E2 monomers, and 6 E3 dimers as well as a few copies of pyruvate dehydrogenase kinase and pyruvate dehydrogenase phosphatase.
|
1 | P09624 (/IDA) |
Mitochondrial oxoglutarate dehydrogenase complex GO:0009353
A complex of multiple copies of three enzymatic components: oxoglutarate dehydrogenase (lipoamide) ; EC:1.2.4.2 (E1), dihydrolipoamide S-succinyltransferase ; EC:2.3.1.61 (E2) and dihydrolipoamide dehydrogenase ; EC:1.8.1.4 (E3); catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and carbon dioxide (CO2) within the mitochondrial matrix. An example of this complex is found in Mus musculus.
|
1 | O00087 (/IC) |
Mitochondrial oxoglutarate dehydrogenase complex GO:0009353
A complex of multiple copies of three enzymatic components: oxoglutarate dehydrogenase (lipoamide) ; EC:1.2.4.2 (E1), dihydrolipoamide S-succinyltransferase ; EC:2.3.1.61 (E2) and dihydrolipoamide dehydrogenase ; EC:1.8.1.4 (E3); catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and carbon dioxide (CO2) within the mitochondrial matrix. An example of this complex is found in Mus musculus.
|
1 | P09624 (/IDA) |
Chloroplast GO:0009507
A chlorophyll-containing plastid with thylakoids organized into grana and frets, or stroma thylakoids, and embedded in a stroma.
|
1 | Q9M5K2 (/IDA) |
Extracellular matrix GO:0031012
A structure lying external to one or more cells, which provides structural support, biochemical or biomechanical cues for cells or tissues.
|
1 | Q54EW8 (/HDA) |
Mitochondrial nucleoid GO:0042645
The region of a mitochondrion to which the DNA is confined.
|
1 | P09624 (/IDA) |
Acrosomal matrix GO:0043159
A structural framework, or 'dense core' at the interior of an acrosome. May regulate the distribution of hydrolases within the acrosome and their release during the acrosome reaction.
|
1 | O08749 (/IDA) |
Myelin sheath GO:0043209
An electrically insulating fatty layer that surrounds the axons of many neurons. It is an outgrowth of glial cells: Schwann cells supply the myelin for peripheral neurons while oligodendrocytes supply it to those of the central nervous system.
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1 | O08749 (/HDA) |
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.
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1 | Q5LRA7 (/TAS) |
Oxoglutarate dehydrogenase complex GO:0045252
A complex of multiple copies of three enzymatic components: oxoglutarate dehydrogenase (lipoamide) ; EC:1.2.4.2 (E1), dihydrolipoamide S-succinyltransferase ; EC:2.3.1.61 (E2) and dihydrolipoamide dehydrogenase ; EC:1.8.1.4 (E3); catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and carbon dioxide (CO2).
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1 | O08749 (/ISO) |
Pyruvate dehydrogenase complex GO:0045254
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).
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1 | O08749 (/ISO) |
Phagocytic vesicle GO:0045335
A membrane-bounded intracellular vesicle that arises from the ingestion of particulate material by phagocytosis.
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1 | Q54EW8 (/HDA) |