View in Gene3D

CATH Superfamily 3.40.50.720

NAD(P)-binding Rossmann-like Domain

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:

"
NAD(P)-binding Rossmann-like 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.
« Back to all FunFams

FunFam 289693: D-3-phosphoglycerate dehydrogenase (Pgdh)

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
Phosphoglycerate dehydrogenase. [EC: 1.1.1.95]
3-phospho-D-glycerate + NAD(+) = 3-phosphonooxypyruvate + NADH.
  • Catalyzes the first committed and rate-limiting step in the phosphoserine pathway of serine biosynthesis.
  • The reaction occurs predominantly in the direction of reduction.
  • The enzyme from the bacterium Escherichia coli also catalyzes the activity of EC 1.1.1.399.
 777 A0A009H464 A0A009HNY2 A0A009KMT4 A0A009PM27 A0A009RRA2 A0A009TDZ1 A0A017I8J9 A0A022PHV0 A0A023V2Z4 A0A023Z244
(767 more...)
2-oxoglutarate reductase. [EC: 1.1.1.399]
(R)-2-hydroxyglutarate + NAD(+) = 2-oxoglutarate + NADH.
  • The enzyme catalyzes a reversible reaction.
  • The enzyme from the bacterium Peptoniphilus asaccharolyticus is specific for (R)-2-hydroxyglutarate.
  • The SerA enzyme from Escherichia coli can also accept (S)-2- hydroxyglutarate with a much higher Km, and also catalyzes the activity of EC 1.1.1.95.
 198 A0A023Z244 A0A025CCR3 A0A026S3J2 A0A026UR48 A0A027U8M0 A0A028AEQ3 A0A028DNV9 A0A029HJ06 A0A029ILA7 A0A029KEH4
(188 more...)
4-phosphoerythronate dehydrogenase. [EC: 1.1.1.290]
4-phospho-D-erythronate + NAD(+) = (3R)-3-hydroxy-2-oxo-4- phosphonooxybutanoate + NADH.
  • This enzyme catalyzes a step in a bacterial pathway for the biosynthesis of pyridoxal 5'-phosphate.
  • The enzyme contains a tightly-bound NAD(H) cofactor that is not re-oxidized by free NAD(+).
  • In order to re-oxidize the cofactor and restore enzyme activity, the enzyme catalyzes the reduction of a 2-oxo acid (such as 2-oxoglutarate, oxaloacetate, or pyruvate) to the respective (R)- hydroxy acid.
  • Cf. EC 1.1.1.399.
 8 A0A068HNX9 A0A0E0X4X5 A0A0G3S2N9 A0A0H3GYC2 A0A0J2HHL9 A0A1D8JZA0 A0A1F2I0B7 J6H206
L-2-hydroxyglutarate dehydrogenase. [EC: 1.1.99.2]
(S)-2-hydroxyglutarate + acceptor = 2-oxoglutarate + reduced acceptor.
    		 7 A0A160J357 A0A173H8T7 A5WAM0 I3UUK3 I7C1L9 N9UGN9 Q88CM5