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:

"
FAD/NAD(P)-binding 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 334: Ferredoxin reductase

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
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).
9 P95034 (/IPI) P95034 (/IPI) P95034 (/IPI) P95034 (/IPI) P95034 (/IPI) P95034 (/IPI) P95034 (/IPI) P95034 (/IPI) P95034 (/IPI)
Ferredoxin-NAD+ reductase activity GO:0008860
Catalysis of the reaction: reduced ferredoxin + NAD+ = oxidized ferredoxin + NADH + H+.
9 P95034 (/IDA) P95034 (/IDA) P95034 (/IDA) P95034 (/IDA) P95034 (/IDA) P95034 (/IDA) P95034 (/IDA) P95034 (/IDA) P95034 (/IDA)
Electron transfer activity GO:0009055
Any molecular entity that serves as an electron acceptor and electron donor in an electron transport chain. An electron transport chain is a process in which a series of electron carriers operate together to transfer electrons from donors to any of several different terminal electron acceptors to generate a transmembrane electrochemical gradient.
9 P95034 (/IDA) P95034 (/IDA) P95034 (/IDA) P95034 (/IDA) P95034 (/IDA) P95034 (/IDA) P95034 (/IDA) P95034 (/IDA) P95034 (/IDA)
Flavin adenine dinucleotide binding GO:0050660
Interacting selectively and non-covalently with FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.
9 P95034 (/IDA) P95034 (/IDA) P95034 (/IDA) P95034 (/IDA) P95034 (/IDA) P95034 (/IDA) P95034 (/IDA) P95034 (/IDA) P95034 (/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.
9 P95034 (/IDA) P95034 (/IDA) P95034 (/IDA) P95034 (/IDA) P95034 (/IDA) P95034 (/IDA) P95034 (/IDA) P95034 (/IDA) P95034 (/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
Ferredoxin metabolic process GO:0006124
The chemical reactions and pathways involving ferredoxin, any simple, nonenzymatic iron-sulfur protein that is characterized by having equal numbers of atoms of iron and labile sulfur. Iron and sulfur atoms are present in one or two clusters of two or four atoms of each.
9 P95034 (/IDA) P95034 (/IDA) P95034 (/IDA) P95034 (/IDA) P95034 (/IDA) P95034 (/IDA) P95034 (/IDA) P95034 (/IDA) P95034 (/IDA)
Cell redox homeostasis GO:0045454
Any process that maintains the redox environment of a cell or compartment within a cell.
9 P95034 (/IDA) P95034 (/IDA) P95034 (/IDA) P95034 (/IDA) P95034 (/IDA) P95034 (/IDA) P95034 (/IDA) P95034 (/IDA) P95034 (/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.