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CATH Superfamily 3.40.50.11610

Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal domain

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:

"
Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal 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 2: 2-oxoglutarate dehydrogenase E1 component

There are 4 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
Oxoglutarate dehydrogenase (succinyl-transferring). [EC: 1.2.4.2]
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO(2).
  • It is a component of the multienzyme 2-oxoglutarate dehydrogenase complex in which multiple copies of it are bound to a core of molecules of EC 2.3.1.61, which also binds multiple copies of EC 1.8.1.4.
  • It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.61.
 467 A0A090M0Z4 A0A090M0Z4 A0A090M0Z4 A0A0E0VP15 A0A0E0VP15 A0A0E0VP15 A0A0E0VP15 A0A0E0VP15 A0A0E0VP15 A0A0E0VP15
(457 more...)
Dihydrolipoyllysine-residue succinyltransferase. [EC: 2.3.1.61]
Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)- (S-succinyldihydrolipoyl)lysine.
  • A multimer (24-mer) of this enzyme forms the core of the multienzyme complex, and binds tightly both EC 1.2.4.2 and EC 1.8.1.4.
  • The lipoyl group of this enzyme is reductively succinylated by EC 1.2.4.2, and the only observed direction catalyzed by EC 2.3.1.61 is that where this succinyl group is passed to coenzyme A.
 29 A0A0E8NQ10 A0A0E8NQ10 A0A0E8NQ10 A0A0E8NQ10 A0A0E8NQ10 A0A0H3L8Z0 A0A0H3L8Z0 A0A0H3L8Z0 A0A0H3L8Z0 A0A0H3L8Z0
(19 more...)
2-oxoglutarate decarboxylase. [EC: 4.1.1.71]
2-oxoglutarate = succinate semialdehyde + CO(2).
  • Highly specific.
 29 A0A0E8NQ10 A0A0E8NQ10 A0A0E8NQ10 A0A0E8NQ10 A0A0E8NQ10 A0A0H3L8Z0 A0A0H3L8Z0 A0A0H3L8Z0 A0A0H3L8Z0 A0A0H3L8Z0
(19 more...)
2-hydroxy-3-oxoadipate synthase. [EC: 2.2.1.5]
2-oxoglutarate + glyoxylate = 2-hydroxy-3-oxoadipate + CO(2).
  • The product decarboxylates to 5-hydroxy-4-oxopentanoate.
  • The enzyme can decarboxylate 2-oxoglutarate.
  • Acetaldehyde can replace glyoxylate.
  • Formerly EC 4.1.3.15.
 29 A0A0E8NQ10 A0A0E8NQ10 A0A0E8NQ10 A0A0E8NQ10 A0A0E8NQ10 A0A0H3L8Z0 A0A0H3L8Z0 A0A0H3L8Z0 A0A0H3L8Z0 A0A0H3L8Z0
(19 more...)
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