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 named:
"Aldehyde Dehydrogenase; Chain A, domain 2
".
FunFam 27: Phenylacetaldehyde 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 3 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 |
---|---|---|
Phenylacetaldehyde dehydrogenase activity GO:0008957
Catalysis of the reaction: phenylacetaldehyde + NAD+ + H2O = phenylacetate + NADH + H+.
|
50 |
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
(40 more) |
Oxidoreductase activity GO:0016491
Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
|
50 |
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
(40 more) |
4-hydroxyphenylacetaldehyde dehydrogenase activity GO:0047106
Catalysis of the reaction: NAD+ + (4-hydroxyphenyl)acetaldehyde + H2O = NADH + 4-hydroxyphenylacetate.
|
50 |
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
(40 more) |
There are 4 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 |
---|---|---|
NAD biosynthetic process GO:0009435
The chemical reactions and pathways resulting in the formation of nicotinamide adenine dinucleotide, a coenzyme present in most living cells and derived from the B vitamin nicotinic acid; biosynthesis may be of either the oxidized form, NAD, or the reduced form, NADH.
|
50 |
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
(40 more) |
Phenylethylamine catabolic process GO:0019607
The chemical reactions and pathways resulting in the breakdown of phenylethylamine, an amine with pharmacological properties similar to those of amphetamine, occurs naturally as a neurotransmitter in the brain, and is present in chocolate and oil of bitter almonds.
|
50 |
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
(40 more) |
4-nitrophenol catabolic process GO:0046196
The chemical reactions and pathways resulting in the breakdown of 4-nitrophenol, a nitroaromatic compound which is used in the production of dyes, leather treatment agents, fungicides and as an intermediate in the production of the insecticide parathion.
|
50 |
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
(40 more) |
Protein homotetramerization GO:0051289
The formation of a protein homotetramer, a macromolecular structure consisting of four noncovalently associated identical subunits.
|
50 |
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
P80668 (/IDA)
(40 more) |
There are 0 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.