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:


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 5159: Hemoglobin beta chain subunit

There are 10 EC terms in this cluster

Please note: EC 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.

Note: 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.

EC Term Annotations Evidence
Nitric oxide dioxygenase. [EC:]
2 nitric oxide + 2 O(2) + NAD(P)H = 2 nitrate + NAD(P)(+) + H(+).
  • It has been proposed that FAD functions as the electron carrier from NADPH to the ferric heme prosthetic group.
2788 A0A009F3F7 A0A009I830 A0A009JED3 A0A009KPS1 A0A009KPX3 A0A009PMA9 A0A009RV24 A0A016QTS8 A0A017ICI1 A0A017T2A5
(2778 more...)
6,7-dihydropteridine reductase. [EC:]
A 5,6,7,8-tetrahydropteridine + NAD(P)(+) = a 6,7-dihydropteridine + NAD(P)H.
  • The substrate is the quinonoid form of dihydropteridine.
  • Not identical with EC
  • Formerly EC and EC
67 A0A009I830 A0A009KPX3 A0A009PMA9 A0A009RV24 A0A059ZH10 A0A062DCK2 A0A062FDP3 A0A062G4G7 A0A062ISQ1 A0A062MWY7
(57 more...)
Ferredoxin--NAD(P)(+) reductase (naphthalene dioxygenase ferredoxin- specific). [EC:]
2 reduced [2Fe-2S] ferredoxin + NAD(P)(+) + H(+) = 2 oxidized [2Fe-2S] ferredoxin + NAD(P)H.
  • The enzyme from the aerobic bacterium Ralstonia sp. U2 donates electrons to both EC and EC
  • The enzyme from Pseudomonas NCIB 9816 is specific for the ferredoxin associated with naphthalene dioxygenase.
5 A0A0U5LNB2 A0A100J5K1 A0A100JLH0 A0A178XDP2 A0A1K2FPY3
Phenol 2-monooxygenase (NADPH). [EC:]
Phenol + NADPH + O(2) = catechol + NADP(+) + H(2)O.
  • The enzyme from the fungus Trichosporon cutaneum has a broad substrate specificity, and has been reported to catalyze the hydroxylation of a variety of substituted phenols, such as fluoro-, chloro-, amino- and methyl-phenols and also dihydroxybenzenes.
  • Cf. EC
3 A0A0D8HZK7 A0A0H5P0V4 A0A1F2Q020
Ferredoxin--NADP(+) reductase. [EC:]
2 reduced ferredoxin + NADP(+) + H(+) = 2 oxidized ferredoxin + NADPH.
  • In chloroplasts and cyanobacteria the enzyme acts on plant-type [2Fe- 2S] ferredoxins, but in other bacteria it can also reduce bacterial 2[4Fe-4S] ferredoxins and flavodoxin.
  • Formerly EC and EC
2 A0A143QGS9 A0A161GMI9
Non-specific serine/threonine protein kinase. [EC:]
ATP + a protein = ADP + a phosphoprotein.
  • This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date.
  • Formerly EC and EC
1 A9GKK0
Transferred entry: [EC:]
    1 R4YTV2
    Vanillate monooxygenase. [EC:]
    Vanillate + O(2) + NADH = 3,4-dihydroxybenzoate + NAD(+) + H(2)O + formaldehyde.
    • Forms part of the vanillin degradation pathway in Arthrobacter sp.
    • Formerly EC
    1 U2EMN6
    Riboflavin reductase (NAD(P)H). [EC:]
    Reduced riboflavin + NAD(P)(+) = riboflavin + NAD(P)H.
    • Catalyzes the reduction of soluble flavins by reduced pyridine nucleotides.
    • Highest activity with riboflavin.
    • When NADH is used as acceptor, the enzyme can also utilize FMN and FAD as substrates, with lower activity than riboflavin.
    • When NADPH is used as acceptor, the enzyme has a very low activity with FMN and no activity with FAD.
    • Formerly EC and EC
    1 A0A0L1HFZ0
    Flavin reductase (NADPH). [EC:]
    Reduced riboflavin + NADP(+) = riboflavin + NADPH.
    • The enzyme from Entamoeba histolytica reduces riboflavin and galactoflavin, and, more slowly, FMN and FAD.
    • NADH is oxidized more slowly than NADPH.
    • Formerly EC
    1 A0A0L1HFZ0