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 named:

"
Dihydrofolate Reductase, subunit A
".

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 6554: Riboflavin biosynthesis protein RibD

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
NADP binding GO:0050661
Interacting selectively and non-covalently with nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH.
3 O66747 (/IDA) P25539 (/IDA) Q58085 (/IDA)
5-amino-6-(5-phosphoribosylamino)uracil reductase activity GO:0008703
Catalysis of the reaction: 5-amino-6-(5-phosphoribitylamino)uracil + NADP(+) = 5-amino-6-(5-phosphoribosylamino)uracil + H(+) + NADPH.
2 Q8EBP0 (/ISS) Q9KPU1 (/ISS)
Diaminohydroxyphosphoribosylaminopyrimidine deaminase activity GO:0008835
Catalysis of the reaction: 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + H(2)O + H(+) = 5-amino-6-(5-phosphoribosylamino)uracil + NH(4)(+).
2 Q8EBP0 (/ISS) Q9KPU1 (/ISS)
Oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor GO:0016616
Catalysis of an oxidation-reduction (redox) reaction in which a CH-OH group acts as a hydrogen or electron donor and reduces NAD+ or NADP.
2 O66747 (/IDA) Q58085 (/IDA)
Protein dimerization activity GO:0046983
The formation of a protein dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits.
2 O66747 (/IDA) Q58085 (/IDA)
5-amino-6-(5-phosphoribosylamino)uracil reductase activity GO:0008703
Catalysis of the reaction: 5-amino-6-(5-phosphoribitylamino)uracil + NADP(+) = 5-amino-6-(5-phosphoribosylamino)uracil + H(+) + NADPH.
1 P25539 (/IDA)
Diaminohydroxyphosphoribosylaminopyrimidine deaminase activity GO:0008835
Catalysis of the reaction: 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + H(2)O + H(+) = 5-amino-6-(5-phosphoribosylamino)uracil + NH(4)(+).
1 P25539 (/IDA)
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.
1 Q58085 (/IDA)

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
Riboflavin biosynthetic process GO:0009231
The chemical reactions and pathways resulting in the formation of riboflavin (vitamin B2), the precursor for the coenzymes flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD).
3 O66747 (/IDA) P25539 (/IDA) Q58085 (/IDA)
Riboflavin biosynthetic process GO:0009231
The chemical reactions and pathways resulting in the formation of riboflavin (vitamin B2), the precursor for the coenzymes flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD).
2 Q8EBP0 (/ISS) Q9KPU1 (/ISS)

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.