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CATH Superfamily 3.40.605.10

Aldehyde Dehydrogenase; Chain A, domain 1

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:

"
Aldehyde Dehydrogenase; Chain A, 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 17: Bifunctional protein PutA

There are 2 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
L-glutamate gamma-semialdehyde dehydrogenase. [EC: 1.2.1.88]
L-glutamate 5-semialdehyde + NAD(+) + H(2)O = L-glutamate + NADH.
  • This enzyme catalyzes the irreversible oxidation of glutamate-gamma- semialdehyde to glutamate as part of the proline degradation pathway.
  • (S)-1-pyrroline-5-carboxylate, the product of the first enzyme of the pathway (EC 1.5.5.2) is in spontaneous equilibrium with its tautomer L-glutamate gamma-semialdehyde.
  • In many bacterial species, both activities are carried out by a single bifunctional enzyme.
  • The enzyme can also oxidize other 1-pyrrolines, e.g. 3-hydroxy-1- pyrroline-5-carboxylate is converted into 4-hydroxyglutamate and (R)- 1-pyrroline-5-carboxylate is converted into D-glutamate.
  • NADP(+) can also act as acceptor, but with lower activity.
  • Formerly EC 1.5.1.12.
 242 A0A069XGW6 A0A069XGW6 A0A069XGW6 A0A069XGW6 A0A069XGW6 A0A069XGW6 A0A069XGW6 A0A069XGW6 A0A069XGW6 A0A069XGW6
(232 more...)
Proline dehydrogenase. [EC: 1.5.5.2]
L-proline + a quinone = (S)-1-pyrroline-5-carboxylate + a quinol.
  • The electrons from L-proline are transferred to the FAD cofactor, and from there to a quinone acceptor.
  • In many organisms, ranging from bacteria to mammals, proline is oxidized to glutamate in a two-step process involving this enzyme and EC 1.2.1.88.
  • Both activities are carried out by the same enzyme in enterobacteria.
  • Formerly EC 1.5.99.8.
 242 A0A069XGW6 A0A069XGW6 A0A069XGW6 A0A069XGW6 A0A069XGW6 A0A069XGW6 A0A069XGW6 A0A069XGW6 A0A069XGW6 A0A069XGW6
(232 more...)
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