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 1273: Glutamate 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 8 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 |
|---|---|---|
|
Glutamate dehydrogenase (NAD+) activity GO:0004352
Catalysis of the reaction: L-glutamate + H2O + NAD+ = 2-oxoglutarate + NH3 + NADH + H+.
|
1 | A3MUY9 (/IDA) |
|
Glutamate dehydrogenase (NAD+) activity GO:0004352
Catalysis of the reaction: L-glutamate + H2O + NAD+ = 2-oxoglutarate + NH3 + NADH + H+.
|
1 | Q60A41 (/ISS) |
|
Glutamate dehydrogenase (NADP+) activity GO:0004354
Catalysis of the reaction: L-glutamate + H2O + NADP+ = 2-oxoglutarate + NH3 + NADPH + H+.
|
1 | A3MWK6 (/IDA) |
|
Phenylalanine dehydrogenase activity GO:0050175
Catalysis of the reaction: L-phenylalanine + H2O + NAD+ = phenylpyruvate + NH3 + NADH.
|
1 | Q59771 (/IDA) |
|
NADP+ binding GO:0070401
Interacting selectively and non-covalently with the oxidized form, NADP+, of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions.
|
1 | A3MWK6 (/IDA) |
|
NADPH binding GO:0070402
Interacting selectively and non-covalently with the reduced form, NADPH, of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions.
|
1 | A3MWK6 (/IDA) |
|
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.
|
1 | A3MUY9 (/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.
|
1 | A3MUY9 (/IDA) |
There are 6 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 |
|---|---|---|
|
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.
|
2 | A3MUY9 (/IDA) A3MWK6 (/IDA) |
|
Glutamate metabolic process GO:0006536
The chemical reactions and pathways involving glutamate, the anion of 2-aminopentanedioic acid.
|
2 | A3MUY9 (/IDA) A3MWK6 (/IDA) |
|
Protein hexamerization GO:0034214
The formation of a protein hexamer, a macromolecular structure consisting of six noncovalently associated identical or nonidentical subunits.
|
2 | A3MUY9 (/IDA) A3MWK6 (/IDA) |
|
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 | A3MUY9 (/IDA) A3MWK6 (/IDA) |
|
Glutamate metabolic process GO:0006536
The chemical reactions and pathways involving glutamate, the anion of 2-aminopentanedioic acid.
|
1 | Q60A41 (/ISS) |
|
L-phenylalanine catabolic process GO:0006559
The chemical reactions and pathways resulting in the breakdown of phenylalanine, 2-amino-3-phenylpropanoic acid.
|
1 | Q59771 (/IDA) |
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.
