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:
"Isopropylmalate Dehydrogenase
".
FunFam 13: Tartrate 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 6 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 |
---|---|---|
Magnesium ion binding GO:0000287
Interacting selectively and non-covalently with magnesium (Mg) ions.
|
60 |
P76251 (/IDA)
P76251 (/IDA)
P76251 (/IDA)
P76251 (/IDA)
P76251 (/IDA)
P76251 (/IDA)
P76251 (/IDA)
P76251 (/IDA)
P76251 (/IDA)
P76251 (/IDA)
(50 more) |
3-isopropylmalate dehydrogenase activity GO:0003862
Catalysis of the reaction: 3-carboxy-2-hydroxy-4-methylpentanoate + NAD+ = 3-carboxy-4-methyl-2-oxopentanoate + NADH + H+.
|
60 |
P76251 (/IDA)
P76251 (/IDA)
P76251 (/IDA)
P76251 (/IDA)
P76251 (/IDA)
P76251 (/IDA)
P76251 (/IDA)
P76251 (/IDA)
P76251 (/IDA)
P76251 (/IDA)
(50 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).
|
60 |
P76251 (/IPI)
P76251 (/IPI)
P76251 (/IPI)
P76251 (/IPI)
P76251 (/IPI)
P76251 (/IPI)
P76251 (/IPI)
P76251 (/IPI)
P76251 (/IPI)
P76251 (/IPI)
(50 more) |
Tartrate dehydrogenase activity GO:0009027
Catalysis of the reaction: tartrate + NAD+ = oxaloglycolate + NADH + H+.
|
60 |
P76251 (/IDA)
P76251 (/IDA)
P76251 (/IDA)
P76251 (/IDA)
P76251 (/IDA)
P76251 (/IDA)
P76251 (/IDA)
P76251 (/IDA)
P76251 (/IDA)
P76251 (/IDA)
(50 more) |
D-malate dehydrogenase (decarboxylating) activity GO:0046553
Catalysis of the reaction: (R)-malate + NAD(+) = CO(2) + NADH + pyruvate.
|
60 |
P76251 (/IDA)
P76251 (/IDA)
P76251 (/IDA)
P76251 (/IDA)
P76251 (/IDA)
P76251 (/IDA)
P76251 (/IDA)
P76251 (/IDA)
P76251 (/IDA)
P76251 (/IDA)
(50 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.
|
60 |
P76251 (/IDA)
P76251 (/IDA)
P76251 (/IDA)
P76251 (/IDA)
P76251 (/IDA)
P76251 (/IDA)
P76251 (/IDA)
P76251 (/IDA)
P76251 (/IDA)
P76251 (/IDA)
(50 more) |
There are 2 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 |
---|---|---|
Malate metabolic process GO:0006108
The chemical reactions and pathways involving malate, the anion of hydroxybutanedioic acid, a chiral hydroxydicarboxylic acid. The (+) enantiomer is an important intermediate in metabolism as a component of both the TCA cycle and the glyoxylate cycle.
|
60 |
P76251 (/IDA)
P76251 (/IDA)
P76251 (/IDA)
P76251 (/IDA)
P76251 (/IDA)
P76251 (/IDA)
P76251 (/IDA)
P76251 (/IDA)
P76251 (/IDA)
P76251 (/IDA)
(50 more) |
Malate metabolic process GO:0006108
The chemical reactions and pathways involving malate, the anion of hydroxybutanedioic acid, a chiral hydroxydicarboxylic acid. The (+) enantiomer is an important intermediate in metabolism as a component of both the TCA cycle and the glyoxylate cycle.
|
60 |
P76251 (/IMP)
P76251 (/IMP)
P76251 (/IMP)
P76251 (/IMP)
P76251 (/IMP)
P76251 (/IMP)
P76251 (/IMP)
P76251 (/IMP)
P76251 (/IMP)
P76251 (/IMP)
(50 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.