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:

"
NAD(P)-binding Rossmann-like Domain
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 228: Putative oxidoreductase yhhX

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 5 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
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.
4 O32223 (/IDA) O32223 (/IDA) O32223 (/IDA) O32223 (/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.
4 O32223 (/IDA) O32223 (/IDA) O32223 (/IDA) O32223 (/IDA)
Scyllo-inositol dehydrogenase (NADP+) activity GO:0102497
Catalysis of the reaction: scyllo-inositol + NADP <=> 2,4,6/3,5-pentahydroxycyclohexanone + NADPH + H+
4 O32223 (/IDA) O32223 (/IDA) O32223 (/IDA) O32223 (/IDA)
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.
2 O13991 (/ISO) O42896 (/ISO)
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.
2 A0A0F7R8V3 (/ISS) A0A0F7R8V3 (/ISS)

There are 1 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+.
2 O13991 (/ISO) O42896 (/ISO)

There are 3 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
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
51 P46853 (/IDA) P46853 (/IDA) P46853 (/IDA) P46853 (/IDA) P46853 (/IDA) P46853 (/IDA) P46853 (/IDA) P46853 (/IDA) P46853 (/IDA) P46853 (/IDA)
(41 more)
Nucleus GO:0005634
A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
2 O13991 (/HDA) O42896 (/HDA)
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 O42896 (/HDA)