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:
"NAD(P)-binding Rossmann-like Domain
".
FunFam 63: NAD(P) transhydrogenase subunit alpha
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 16 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 |
---|---|---|
NAD(P)+ transhydrogenase (AB-specific) activity GO:0008750
Catalysis of the reaction: NADPH + H+ + NAD+ = NADP+ + NADH + H+. The reaction is A-specific (i.e. the pro-R hydrogen is transferred from the 4-position of reduced nicotinamide cofactor) with respect to NAD+ and B-specific (i.e. the pro-S hydrogen is transferred) with respect to NADP+.
|
20 |
P07001 (/IDA)
P07001 (/IDA)
P07001 (/IDA)
P07001 (/IDA)
P07001 (/IDA)
P07001 (/IDA)
P07001 (/IDA)
P07001 (/IDA)
P07001 (/IDA)
P07001 (/IDA)
(10 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).
|
17 |
P07001 (/IPI)
P07001 (/IPI)
P07001 (/IPI)
P07001 (/IPI)
P07001 (/IPI)
P07001 (/IPI)
P07001 (/IPI)
P07001 (/IPI)
P07001 (/IPI)
P07001 (/IPI)
(7 more) |
Protein dimerization activity GO:0046983
The formation of a protein dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits.
|
17 |
P07001 (/IDA)
P07001 (/IDA)
P07001 (/IDA)
P07001 (/IDA)
P07001 (/IDA)
P07001 (/IDA)
P07001 (/IDA)
P07001 (/IDA)
P07001 (/IDA)
P07001 (/IDA)
(7 more) |
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.
|
17 |
P07001 (/IDA)
P07001 (/IDA)
P07001 (/IDA)
P07001 (/IDA)
P07001 (/IDA)
P07001 (/IDA)
P07001 (/IDA)
P07001 (/IDA)
P07001 (/IDA)
P07001 (/IDA)
(7 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+.
|
7 | Q9KM26 (/ISS) Q9KM26 (/ISS) Q9KM26 (/ISS) Q9KM26 (/ISS) Q9KM26 (/ISS) Q9KM26 (/ISS) Q9KM26 (/ISS) |
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.
|
6 | P0C186 (/ISS) P0C186 (/ISS) P43842 (/ISS) Q9ALA2 (/ISS) Q9ALA2 (/ISS) Q9ALA2 (/ISS) |
Protein dimerization activity GO:0046983
The formation of a protein dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits.
|
4 | P43842 (/ISS) Q9ALA2 (/ISS) Q9ALA2 (/ISS) Q9ALA2 (/ISS) |
NAD+ binding GO:0070403
Interacting selectively and non-covalently with the oxidized form, NAD, of nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions.
|
4 | P0C186 (/ISS) P0C186 (/ISS) P41077 (/ISS) P41077 (/ISS) |
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+.
|
2 | Q2RSB2 (/IDA) Q2RSB2 (/IDA) |
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+.
|
2 | Q13423 (/TAS) Q13423 (/TAS) |
NAD(P)+ transhydrogenase (AB-specific) activity GO:0008750
Catalysis of the reaction: NADPH + H+ + NAD+ = NADP+ + NADH + H+. The reaction is A-specific (i.e. the pro-R hydrogen is transferred from the 4-position of reduced nicotinamide cofactor) with respect to NAD+ and B-specific (i.e. the pro-S hydrogen is transferred) with respect to NADP+.
|
2 | P0C186 (/ISS) P0C186 (/ISS) |
NADP binding GO:0050661
Interacting selectively and non-covalently with nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH.
|
2 | Q13423 (/IDA) Q13423 (/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.
|
2 | Q13423 (/TAS) Q13423 (/TAS) |
NAD+ binding GO:0070403
Interacting selectively and non-covalently with the oxidized form, NAD, of nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions.
|
2 | Q2RSB2 (/IDA) Q2RSB2 (/IDA) |
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.
|
2 | Q2RSB2 (/IDA) Q2RSB2 (/IDA) |
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.
|
2 | P0C186 (/ISS) P0C186 (/ISS) |
There are 19 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 |
---|---|---|
NADPH regeneration GO:0006740
A metabolic process that generates a pool of NADPH by the reduction of NADP+.
|
20 |
P07001 (/IDA)
P07001 (/IDA)
P07001 (/IDA)
P07001 (/IDA)
P07001 (/IDA)
P07001 (/IDA)
P07001 (/IDA)
P07001 (/IDA)
P07001 (/IDA)
P07001 (/IDA)
(10 more) |
NADPH regeneration GO:0006740
A metabolic process that generates a pool of NADPH by the reduction of NADP+.
|
16 |
P07001 (/IMP)
P07001 (/IMP)
P07001 (/IMP)
P07001 (/IMP)
P07001 (/IMP)
P07001 (/IMP)
P07001 (/IMP)
P07001 (/IMP)
P07001 (/IMP)
P07001 (/IMP)
(6 more) |
NADH oxidation GO:0006116
A metabolic process that results in the oxidation of reduced nicotinamide adenine dinucleotide, NADH, to the oxidized form, NAD.
|
3 | Q9ALA2 (/IDA) Q9ALA2 (/IDA) Q9ALA2 (/IDA) |
Cellular response to oxidative stress GO:0034599
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 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.
|
3 | Q9ALA2 (/IMP) Q9ALA2 (/IMP) Q9ALA2 (/IMP) |
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.
|
2 | Q13423 (/TAS) Q13423 (/TAS) |
NADPH regeneration GO:0006740
A metabolic process that generates a pool of NADPH by the reduction of NADP+.
|
2 | P0C186 (/ISS) P0C186 (/ISS) |
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.
|
2 | P0C186 (/NAS) P0C186 (/NAS) |
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.
|
2 | Q13423 (/TAS) Q13423 (/TAS) |
Reactive oxygen species metabolic process GO:0072593
The chemical reactions and pathways involving a reactive oxygen species, any molecules or ions formed by the incomplete one-electron reduction of oxygen. They contribute to the microbicidal activity of phagocytes, regulation of signal transduction and gene expression, and the oxidative damage to biopolymers.
|
2 | Q13423 (/IMP) Q13423 (/IMP) |
Proton transmembrane transport GO:1902600
The directed movement of a proton across a membrane.
|
2 | Q13423 (/TAS) Q13423 (/TAS) |
Negative regulation of protein phosphorylation GO:0001933
Any process that stops, prevents or reduces the rate of addition of phosphate groups to amino acids within a protein.
|
1 | Q5BJZ3 (/IMP) |
Positive regulation of mitochondrial membrane potential GO:0010918
Any process that activates or increases the frequency, rate or extent of establishment or extent of a mitochondrial membrane potential, the electric potential existing across any mitochondrial membrane arising from charges in the membrane itself and from the charges present in the media on either side of the membrane.
|
1 | Q5BJZ3 (/IMP) |
Oxygen homeostasis GO:0032364
A homeostatic process involved in the maintenance of an internal steady state of oxygen within an organism or cell.
|
1 | Q5BJZ3 (/IMP) |
Response to vitamin GO:0033273
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 vitamin stimulus.
|
1 | Q5BJZ3 (/IEP) |
Negative regulation of apoptotic process GO:0043066
Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process.
|
1 | Q5BJZ3 (/IMP) |
Cell redox homeostasis GO:0045454
Any process that maintains the redox environment of a cell or compartment within a cell.
|
1 | Q5BJZ3 (/IMP) |
Reactive oxygen species metabolic process GO:0072593
The chemical reactions and pathways involving a reactive oxygen species, any molecules or ions formed by the incomplete one-electron reduction of oxygen. They contribute to the microbicidal activity of phagocytes, regulation of signal transduction and gene expression, and the oxidative damage to biopolymers.
|
1 | Q61941 (/ISS) |
Cellular oxidant detoxification GO:0098869
Any process carried out at the cellular level that reduces or removes the toxicity superoxide radicals or hydrogen peroxide.
|
1 | Q5BJZ3 (/IMP) |
Positive regulation of hydrogen peroxide catabolic process GO:1903285
Any process that activates or increases the frequency, rate or extent of hydrogen peroxide catabolic process.
|
1 | Q5BJZ3 (/IMP) |
There are 10 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 |
---|---|---|
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.
|
15 |
P07001 (/IDA)
P07001 (/IDA)
P07001 (/IDA)
P07001 (/IDA)
P07001 (/IDA)
P07001 (/IDA)
P07001 (/IDA)
P07001 (/IDA)
P07001 (/IDA)
P07001 (/IDA)
(5 more) |
Integral component of plasma membrane GO:0005887
The component of the plasma membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
|
15 |
P07001 (/IDA)
P07001 (/IDA)
P07001 (/IDA)
P07001 (/IDA)
P07001 (/IDA)
P07001 (/IDA)
P07001 (/IDA)
P07001 (/IDA)
P07001 (/IDA)
P07001 (/IDA)
(5 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.
|
7 | P96832 (/HDA) P96832 (/HDA) P96832 (/HDA) P96832 (/HDA) P96832 (/HDA) P96832 (/HDA) P96832 (/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.
|
4 | Q13423 (/IDA) Q13423 (/IDA) Q18031 (/IDA) Q5BJZ3 (/IDA) |
Integral component of plasma membrane GO:0005887
The component of the plasma membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
|
4 | P43842 (/ISS) Q9ALA2 (/ISS) Q9ALA2 (/ISS) Q9ALA2 (/ISS) |
Mitochondrial inner membrane GO:0005743
The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae.
|
2 | Q13423 (/TAS) Q13423 (/TAS) |
Mitochondrial respirasome GO:0005746
The protein complexes that form the mitochondrial electron transport system (the respiratory chain), associated with the inner mitochondrial membrane. The respiratory chain complexes transfer electrons from an electron donor to an electron acceptor and are associated with a proton pump to create a transmembrane electrochemical gradient.
|
2 | Q13423 (/TAS) Q13423 (/TAS) |
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
|
2 | Q13423 (/HDA) Q13423 (/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 | Q61941 (/HDA) |
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 | Q61941 (/HDA) |