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: waiting to be named.

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 1: Dihydrolipoyl dehydrogenase

Please note: GO annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

There are 33 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 TermAnnotationsEvidence
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).
128 O08749 (/IPI) P09622 (/IPI) P09622 (/IPI) P09622 (/IPI) P09624 (/IPI) P0A9P0 (/IPI) P0A9P0 (/IPI) P0A9P0 (/IPI) P0A9P0 (/IPI) P0A9P0 (/IPI)
(118 more)
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.
123 P0A9P0 (/IDA) P0A9P0 (/IDA) P0A9P0 (/IDA) P0A9P0 (/IDA) P0A9P0 (/IDA) P0A9P0 (/IDA) P0A9P0 (/IDA) P0A9P0 (/IDA) P0A9P0 (/IDA) P0A9P0 (/IDA)
(113 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)
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+.
84 A0A0F7RGS5 (/ISS) A0A0F7RGS5 (/ISS) A0A1S0QYK5 (/ISS) A0A1S0QYK5 (/ISS) A0A1S0QYK5 (/ISS) A0A1S0QYK5 (/ISS) A0A1S0QYK5 (/ISS) A0A1S0QYK5 (/ISS) A0A1S0QYK5 (/ISS) A0A1S0QYK5 (/ISS)
(74 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)
Showing 1 to 10 of 33 entries

There are 65 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 TermAnnotationsEvidence
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)
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)
Response to hypochlorite GO:1901530
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 hypochlorite stimulus.
14 P77212 (/IEP) P77212 (/IEP) P77212 (/IEP) P77212 (/IEP) P77212 (/IEP) P77212 (/IEP) P77212 (/IEP) P77212 (/IEP) P77212 (/IEP) P77212 (/IEP)
(4 more)
Showing 1 to 10 of 65 entries

There are 56 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 TermAnnotationsEvidence
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
122 P0A9P0 (/HDA) P0A9P0 (/HDA) P0A9P0 (/HDA) P0A9P0 (/HDA) P0A9P0 (/HDA) P0A9P0 (/HDA) P0A9P0 (/HDA) P0A9P0 (/HDA) P0A9P0 (/HDA) P0A9P0 (/HDA)
(112 more)
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
114 P0A9P0 (/IDA) P0A9P0 (/IDA) P0A9P0 (/IDA) P0A9P0 (/IDA) P0A9P0 (/IDA) P0A9P0 (/IDA) P0A9P0 (/IDA) P0A9P0 (/IDA) P0A9P0 (/IDA) P0A9P0 (/IDA)
(104 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.
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)
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.
23 A0A024R713 (/IDA) A0A024R713 (/IDA) A0A024R713 (/IDA) E9PEX6 (/IDA) E9PEX6 (/IDA) E9PEX6 (/IDA) O08749 (/IDA) O81413 (/IDA) O81413 (/IDA) P09622 (/IDA)
(13 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)
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)
Showing 1 to 10 of 56 entries
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