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 291634: Fermentative D-lactate dehydrogenase, NAD-dependen...

There are 8 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
D-lactate dehydrogenase. [EC: 1.1.1.28]
(R)-lactate + NAD(+) = pyruvate + NADH.
    		 3466 A0A010SRG4 A0A010SRG4 A0A011RQ32 A0A011RQ32 A0A015NZL7 A0A015NZL7 A0A015UAM1 A0A015UAM1 A0A015WEF4 A0A015WEF4
    (3456 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.
    		 368 A0A059N5G0 A0A059N5G0 A0A095ZX29 A0A095ZX29 A0A096ARU8 A0A096ARU8 A0A0D0ZTV3 A0A0D0ZTV3 A0A0E1CJV2 A0A0E1CJV2
    (358 more...)
    D-2-hydroxyacid dehydrogenase (NADP(+)). [EC: 1.1.1.272]
    An (R)-2-hydroxycarboxylate + NADP(+) = a 2-oxocarboxylate + NADPH.
    • This enzyme, characterized from the halophilic archaeon Haloferax mediterranei and the mold Aspergillus oryzae, catalyzes a reversible stereospecific reduction of 2-oxocarboxylic acids into the corresponding D-2-hydroxycarboxylic acids.
    • The enzyme prefers substrates with a main chain of 5 carbons (such as 4-methyl-2-oxopentanoate) to those with a shorter chain, and can use NADH with much lower efficiency.
    • cf. EC 1.1.1.345.
    		 30 A0A1B9QJ59 A0A1B9QJ59 A0Y5Z5 A0Y5Z5 A3UPL1 A3UPL1 A3XG39 A3XG39 A3XKE7 A3XKE7
    (20 more...)
    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.
    		 18 A0A1E9VL45 A0A1E9VL45 A0A1F2KLI4 A0A1F2KLI4 A0A1F2KTE8 A0A1F2KTE8 A0A1J3ZBW5 A0A1J3ZBW5 A0A1J4AYA2 A0A1J4AYA2
    (8 more...)
    Cysteine--tRNA ligase. [EC: 6.1.1.16]
    ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys).
      		 6 A0A112X8G4 A0A112X8G4 A4P0P7 A4P0P7 A5UFP9 A5UFP9
      Hydroxypyruvate reductase. [EC: 1.1.1.81]
      D-glycerate + NAD(P)(+) = hydroxypyruvate + NAD(P)H.
        		 4 D7GNA2 D7GNA2 G2KTX9 G2KTX9
        Phosphoglycerate mutase (2,3-diphosphoglycerate-dependent). [EC: 5.4.2.11]
        2-phospho-D-glycerate = 3-phospho-D-glycerate.
        • The enzymes from vertebrates, platyhelminths, mollusks, annelids, crustaceans, insects, algae, fungi, yeast and some bacteria (particularly Gram-negative) require 2,3-bisphospho-D-glycerate as a cofactor.
        • The enzyme is activated by 2,3-bisphospho-D-glycerate by transferring a phosphate to histidine (His(10) in man and Escherichia coli, His(8) in Saccharomyces cerevisiae).
        • This phosphate can be transferred to the free OH of 2-phospho-D- glycerate, followed by transfer of the phosphate already on the phosphoglycerate back to the histidine.
        • Cf. EC 5.4.2.12.
        • The enzyme has no requirement for metal ions.
        • This enzyme also catalyze, slowly, the reactions of EC 5.4.2.4.
        • Formerly EC 2.7.5.3 and EC 5.4.2.1.
        		 2 B2UQ72 B2UQ72
        D-lactate dehydrogenase (cytochrome). [EC: 1.1.2.4]
        (R)-lactate + 2 ferricytochrome c = pyruvate + 2 ferrocytochrome c + 2 H(+).
          		 2 A0A0X9TN19 A0A0X9TN19