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:

"
Probable inorganic polyphosphate/atp-NAD kinase; domain 1
".

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 9: NAD kinase

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
NAD+ kinase activity GO:0003951
Catalysis of the reaction: ATP + NAD(+) = ADP + 2 H(+) + NADP(+).
24 O31612 (/IDA) O31612 (/IDA) O31612 (/IDA) O31612 (/IDA) O31612 (/IDA) O31612 (/IDA) O31612 (/IDA) O31612 (/IDA) O31612 (/IDA) O31612 (/IDA)
(14 more)
ATP binding GO:0005524
Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
24 O31612 (/IDA) O31612 (/IDA) O31612 (/IDA) O31612 (/IDA) O31612 (/IDA) O31612 (/IDA) O31612 (/IDA) O31612 (/IDA) O31612 (/IDA) O31612 (/IDA)
(14 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.
24 O31612 (/IDA) O31612 (/IDA) O31612 (/IDA) O31612 (/IDA) O31612 (/IDA) O31612 (/IDA) O31612 (/IDA) O31612 (/IDA) O31612 (/IDA) O31612 (/IDA)
(14 more)
NAD+ kinase activity GO:0003951
Catalysis of the reaction: ATP + NAD(+) = ADP + 2 H(+) + NADP(+).
23 Q81TQ3 (/ISS) Q81TQ3 (/ISS) Q81TQ3 (/ISS) Q81TQ3 (/ISS) Q81TQ3 (/ISS) Q81TQ3 (/ISS) Q81TQ3 (/ISS) Q81TQ3 (/ISS) Q81TQ3 (/ISS) Q81TQ3 (/ISS)
(13 more)
Polyphosphate kinase activity GO:0008976
Catalysis of the reaction: ATP + phosphate(n) = ADP + phosphate(n+1).
23 Q81TQ3 (/ISS) Q81TQ3 (/ISS) Q81TQ3 (/ISS) Q81TQ3 (/ISS) Q81TQ3 (/ISS) Q81TQ3 (/ISS) Q81TQ3 (/ISS) Q81TQ3 (/ISS) Q81TQ3 (/ISS) Q81TQ3 (/ISS)
(13 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).
15 P65779 (/IPI) P65779 (/IPI) P65779 (/IPI) P65779 (/IPI) P65779 (/IPI) P65779 (/IPI) P65779 (/IPI) P65779 (/IPI) P65779 (/IPI) P65779 (/IPI)
(5 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
NADP biosynthetic process GO:0006741
The chemical reactions and pathways resulting in the formation of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; biosynthesis may be of either the oxidized form, NADP, or the reduced form, NADPH.
24 O31612 (/IDA) O31612 (/IDA) O31612 (/IDA) O31612 (/IDA) O31612 (/IDA) O31612 (/IDA) O31612 (/IDA) O31612 (/IDA) O31612 (/IDA) O31612 (/IDA)
(14 more)
Nicotinamide metabolic process GO:0006769
The chemical reactions and pathways involving nicotinamide, pyridine-3-carboxamide, the amide of nicotinic acid. It is a member of the B complex of vitamins and occurs widely in living organisms.
23 Q81TQ3 (/ISS) Q81TQ3 (/ISS) Q81TQ3 (/ISS) Q81TQ3 (/ISS) Q81TQ3 (/ISS) Q81TQ3 (/ISS) Q81TQ3 (/ISS) Q81TQ3 (/ISS) Q81TQ3 (/ISS) Q81TQ3 (/ISS)
(13 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.