View in Gene3D

CATH Superfamily 3.20.20.70

Aldolase class I

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:

"
Aldolase class I
".

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.
« Back to all FunFams

FunFam 120901: Probable nicotinate-nucleotide pyrophosphorylase [...

There are 6 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
Nicotinate-nucleotide diphosphorylase (carboxylating). [EC: 2.4.2.19]
Beta-nicotinate D-ribonucleotide + diphosphate + CO(2) = pyridine-2,3- dicarboxylate + 5-phospho-alpha-D-ribose 1-diphosphate.
  • The reaction is catalyzed in the opposite direction.
  • Since quinolinate is synthesized from L-tryptophan in eukaryotes, but from L-aspartate in some prokaryotes, this is the first NAD(+) biosynthesis enzyme shared by both eukaryotes and prokaryotes.
 11892 A0A009F7T2 A0A009F7T2 A0A009G1X2 A0A009G1X2 A0A009H4W5 A0A009H4W5 A0A009HB10 A0A009HB10 A0A009INC8 A0A009INC8
(11882 more...)
L-aspartate oxidase. [EC: 1.4.3.16]
L-aspartate + O(2) = iminosuccinate + H(2)O(2).
  • L-aspartate oxidase catalyzes the first step in the de novo biosynthesis of NAD(+) in some bacteria.
  • O(2) can be replaced by fumarate as electron acceptor, yielding succinate.
  • The ability of the enzyme to use both O(2) and fumarate in cofactor reoxidation enables it to function under both aerobic and anaerobic conditions.
  • Iminosuccinate can either be hydrolyzed to form oxaloacetate and NH(3) or can be used by EC 2.5.1.72 in the production of quinolinate.
 54 A0A0C2J7X5 A0A0C2J7X5 A0A0E9AFC9 A0A0E9AFC9 A0A0F4KA00 A0A0F4KA00 A0A0N0AN95 A0A0N0AN95 A0A147KE11 A0A147KE11
(44 more...)
Glutarate-semialdehyde dehydrogenase. [EC: 1.2.1.20]
Glutarate semialdehyde + NAD(+) + H(2)O = glutarate + NADH.
    		 4 C4WII6 C4WII6 M5JZ41 M5JZ41
    Nicotinate phosphoribosyltransferase. [EC: 6.3.4.21]
    Nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H(2)O = beta- nicotinate D-ribonucleotide + diphosphate + ADP + phosphate.
    • The enzyme, which is involved in pyridine nucleotide recycling, can form beta-nicotinate D-ribonucleotide and diphosphate from nicotinate and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) in the absence of ATP.
    • However, when ATP is available the enzyme is phosphorylated resulting in a much lower K(m) for nicotinate.
    • The phospho-enzyme is hydrolyzed during the transferase reaction, regenerating the low affinity form.
    • The presence of ATP shifts the products/substrates equilibrium from 0.67 to 1100.
    • Formerly EC 2.4.2.11.
    		 4 A0A098AX60 A0A098AX60 G9XJE1 G9XJE1
    Phosphoglycerate kinase. [EC: 2.7.2.3]
    ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate.
      		 2 M2W0C4 M2W0C4
      Quinolinate synthase. [EC: 2.5.1.72]
      Glycerone phosphate + iminosuccinate = pyridine-2,3-dicarboxylate + 2 H(2)O + phosphate.
      • Quinolinate synthase catalyzes the second step in the de novo biosynthesis of NAD(+) from aspartate in some bacteria, with EC 1.4.3.16 catalyzing the first step and EC 2.4.2.19 the third step.
      • In Escherichia coli, two of the residues that are involved in the [4Fe-4S] cluster binding appear to undergo reversible disulfide-bond formation that regulates the activity of the enzyme.
      		 2 R5I4J2 R5I4J2
      CATH-Gene3D is a Global Biodata Core Resource Learn more...