The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was: waiting to be named.
FunFam 36359: Transketolase, N-terminal (Sedoheptulose-7-phospha...
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 14 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 |
|---|---|---|
|
Transketolase activity GO:0004802
Catalysis of the reversible transfer of a 2-carbon ketol group (CH2OH-CO-) from a ketose phosphate donor to an aldose phosphate acceptor.
|
3 | P29401 (/IDA) P40142 (/IDA) P50137 (/IDA) |
|
Magnesium ion binding GO:0000287
Interacting selectively and non-covalently with magnesium (Mg) ions.
|
1 | P50137 (/IDA) |
|
Transketolase activity GO:0004802
Catalysis of the reversible transfer of a 2-carbon ketol group (CH2OH-CO-) from a ketose phosphate donor to an aldose phosphate acceptor.
|
1 | P29401 (/EXP) |
|
Transketolase activity GO:0004802
Catalysis of the reversible transfer of a 2-carbon ketol group (CH2OH-CO-) from a ketose phosphate donor to an aldose phosphate acceptor.
|
1 | P40142 (/ISO) |
|
Transketolase activity GO:0004802
Catalysis of the reversible transfer of a 2-carbon ketol group (CH2OH-CO-) from a ketose phosphate donor to an aldose phosphate acceptor.
|
1 | Q6B855 (/ISS) |
|
Transketolase activity GO:0004802
Catalysis of the reversible transfer of a 2-carbon ketol group (CH2OH-CO-) from a ketose phosphate donor to an aldose phosphate acceptor.
|
1 | P51854 (/TAS) |
|
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).
|
1 | P29401 (/IPI) |
|
Carbohydrate binding GO:0030246
Interacting selectively and non-covalently with any carbohydrate, which includes monosaccharides, oligosaccharides and polysaccharides as well as substances derived from monosaccharides by reduction of the carbonyl group (alditols), by oxidation of one or more hydroxy groups to afford the corresponding aldehydes, ketones, or carboxylic acids, or by replacement of one or more hydroxy group(s) by a hydrogen atom. Cyclitols are generally not regarded as carbohydrates.
|
1 | P50137 (/IDA) |
|
Thiamine pyrophosphate binding GO:0030976
Interacting selectively and non-covalently with thiamine pyrophosphate, the diphosphoric ester of thiamine. Acts as a coenzyme of several (de)carboxylases, transketolases, and alpha-oxoacid dehydrogenases.
|
1 | P50137 (/IDA) |
|
Protein homodimerization activity GO:0042803
Interacting selectively and non-covalently with an identical protein to form a homodimer.
|
1 | P29401 (/IDA) |
|
Protein homodimerization activity GO:0042803
Interacting selectively and non-covalently with an identical protein to form a homodimer.
|
1 | P40142 (/ISO) |
|
Monosaccharide binding GO:0048029
Interacting selectively and non-covalently with any monosaccharide. Monosaccharides are the simplest carbohydrates; they are polyhydroxy aldehydes H
|
1 | P50137 (/IDA) |
|
Cofactor binding GO:0048037
Interacting selectively and non-covalently with a cofactor, a substance that is required for the activity of an enzyme or other protein. Cofactors may be inorganic, such as the metal atoms zinc, iron, and copper in certain forms, or organic, in which case they are referred to as coenzymes. Cofactors may either be bound tightly to active sites or bind loosely with the substrate.
|
1 | P29401 (/IDA) |
|
Cofactor binding GO:0048037
Interacting selectively and non-covalently with a cofactor, a substance that is required for the activity of an enzyme or other protein. Cofactors may be inorganic, such as the metal atoms zinc, iron, and copper in certain forms, or organic, in which case they are referred to as coenzymes. Cofactors may either be bound tightly to active sites or bind loosely with the substrate.
|
1 | P40142 (/ISO) |
There are 13 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 |
|---|---|---|
|
Regulation of chromatin silencing GO:0031935
Any process that affects the rate, extent or location of chromatin silencing.
|
2 | Q7KSU6 (/IMP) Q9VHN7 (/IMP) |
|
Xylulose biosynthetic process GO:0005999
The chemical reactions and pathways resulting in the formation of xylulose, the ketopentose threo-2-pentulose.
|
1 | P29401 (/TAS) |
|
Glucose catabolic process GO:0006007
The chemical reactions and pathways resulting in the breakdown of glucose, the aldohexose gluco-hexose.
|
1 | P51854 (/TAS) |
|
Pentose-phosphate shunt GO:0006098
The glucose-6-phosphate catabolic process in which, coupled to NADPH synthesis, glucose-6-P is oxidized with the formation of carbon dioxide (CO2) and ribulose 5-phosphate; ribulose 5-P then enters a series of reactions interconverting sugar phosphates. The pentose phosphate pathway is a major source of reducing equivalents for biosynthesis reactions and is also important for the conversion of hexoses to pentoses.
|
1 | P50137 (/IDA) |
|
Pentose-phosphate shunt GO:0006098
The glucose-6-phosphate catabolic process in which, coupled to NADPH synthesis, glucose-6-P is oxidized with the formation of carbon dioxide (CO2) and ribulose 5-phosphate; ribulose 5-P then enters a series of reactions interconverting sugar phosphates. The pentose phosphate pathway is a major source of reducing equivalents for biosynthesis reactions and is also important for the conversion of hexoses to pentoses.
|
1 | P29401 (/TAS) |
|
Thiamine metabolic process GO:0006772
The chemical reactions and pathways involving thiamine (vitamin B1), a water soluble vitamin present in fresh vegetables and meats, especially liver.
|
1 | P51854 (/TAS) |
|
Pentose-phosphate shunt, non-oxidative branch GO:0009052
The branch of the pentose-phosphate shunt which does not involve oxidation reactions. It comprises a series of sugar phosphate interconversions, starting with ribulose 5-P and producing fructose 6-P and glyceraldehyde 3-P.
|
1 | P50137 (/IDA) |
|
Pentose-phosphate shunt, non-oxidative branch GO:0009052
The branch of the pentose-phosphate shunt which does not involve oxidation reactions. It comprises a series of sugar phosphate interconversions, starting with ribulose 5-P and producing fructose 6-P and glyceraldehyde 3-P.
|
1 | P29401 (/NAS) |
|
Regulation of growth GO:0040008
Any process that modulates the frequency, rate or extent of the growth of all or part of an organism so that it occurs at its proper speed, either globally or in a specific part of the organism's development.
|
1 | P40142 (/IMP) |
|
Regulation of growth GO:0040008
Any process that modulates the frequency, rate or extent of the growth of all or part of an organism so that it occurs at its proper speed, either globally or in a specific part of the organism's development.
|
1 | Q6B855 (/ISS) |
|
Glyceraldehyde-3-phosphate biosynthetic process GO:0046166
The chemical reactions and pathways resulting in the formation of glyceraldehyde-3-phosphate, an important intermediate in glycolysis.
|
1 | P29401 (/IDA) |
|
Glyceraldehyde-3-phosphate biosynthetic process GO:0046166
The chemical reactions and pathways resulting in the formation of glyceraldehyde-3-phosphate, an important intermediate in glycolysis.
|
1 | P40142 (/ISO) |
|
Ribose phosphate biosynthetic process GO:0046390
The chemical reactions and pathways resulting in the formation of ribose phosphate, any phosphorylated ribose sugar.
|
1 | P50137 (/IDA) |
There are 19 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 |
|---|---|---|
|
Nucleoplasm GO:0005654
That part of the nuclear content other than the chromosomes or the nucleolus.
|
2 | P29401 (/IDA) V9HWD9 (/IDA) |
|
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
|
2 | Q7KSU6 (/IDA) Q9VHN7 (/IDA) |
|
Nuclear body GO:0016604
Extra-nucleolar nuclear domains usually visualized by confocal microscopy and fluorescent antibodies to specific proteins.
|
2 | P29401 (/IDA) V9HWD9 (/IDA) |
|
Nuclear speck GO:0016607
A discrete extra-nucleolar subnuclear domain, 20-50 in number, in which splicing factors are seen to be localized by immunofluorescence microscopy.
|
2 | P29401 (/IDA) V9HWD9 (/IDA) |
|
Nucleoplasm GO:0005654
That part of the nuclear content other than the chromosomes or the nucleolus.
|
1 | P40142 (/ISO) |
|
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
1 | Q9H0I9 (/IDA) |
|
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
1 | Q9D4D4 (/ISO) |
|
Peroxisome GO:0005777
A small organelle enclosed by a single membrane, and found in most eukaryotic cells. Contains peroxidases and other enzymes involved in a variety of metabolic processes including free radical detoxification, lipid catabolism and biosynthesis, and hydrogen peroxide metabolism.
|
1 | P50137 (/IDA) |
|
Peroxisome GO:0005777
A small organelle enclosed by a single membrane, and found in most eukaryotic cells. Contains peroxidases and other enzymes involved in a variety of metabolic processes including free radical detoxification, lipid catabolism and biosynthesis, and hydrogen peroxide metabolism.
|
1 | P29401 (/ISS) |
|
Endoplasmic reticulum membrane GO:0005789
The lipid bilayer surrounding the endoplasmic reticulum.
|
1 | P50137 (/IDA) |
|
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
|
1 | P29401 (/TAS) |
|
Nuclear body GO:0016604
Extra-nucleolar nuclear domains usually visualized by confocal microscopy and fluorescent antibodies to specific proteins.
|
1 | P40142 (/ISO) |
|
Nuclear speck GO:0016607
A discrete extra-nucleolar subnuclear domain, 20-50 in number, in which splicing factors are seen to be localized by immunofluorescence microscopy.
|
1 | P40142 (/ISO) |
|
Vesicle GO:0031982
Any small, fluid-filled, spherical organelle enclosed by membrane.
|
1 | P29401 (/IDA) |
|
Vesicle GO:0031982
Any small, fluid-filled, spherical organelle enclosed by membrane.
|
1 | P40142 (/ISO) |
|
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.
|
1 | P40142 (/IDA) |
|
Intracellular membrane-bounded organelle GO:0043231
Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane.
|
1 | P50137 (/IDA) |
|
Extracellular exosome GO:0070062
A vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm.
|
1 | P29401 (/IDA) |
|
Extracellular exosome GO:0070062
A vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm.
|
1 | P40142 (/ISO) |