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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.
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FunFam 286674: NADP-dependent l-serine/l-allo-threonine dehydroge...

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
3-hydroxypropionate dehydrogenase (NADP(+)). [EC: 1.1.1.298]
3-hydroxypropanoate + NADP(+) = 3-oxopropanoate + NADPH.
  • Catalyzes the reduction of 3-oxopropanoate to 3-hydroxypropanoate, a key step in the 3-hydroxypropanoate and the 3-hydroxypropanoate/4-hydroxybutyrate cycles, autotrophic CO(2) fixation pathways found in some green non-sulfur phototrophic bacteria and archaea, respectively.
  • The enzyme from Chloroflexus aurantiacus is bifunctional, and also catalyzes the upstream reaction in the pathway, EC 1.2.1.75.
  • Different from EC 1.1.1.59 by cofactor preference.
 842 A0A017IGA9 A0A017IGA9 A0A023YWW3 A0A023YWW3 A0A024KWH8 A0A024KWH8 A0A025BRU3 A0A025BRU3 A0A026V6B5 A0A026V6B5
(832 more...)
Serine 3-dehydrogenase (NADP(+)). [EC: 1.1.1.276]
L-serine + NADP(+) = 2-aminoacetaldehyde + CO(2) + NADPH.
  • NAD(+) cannot replace NADP(+) (cf. EC 1.1.1.387).
 768 A0A023YWW3 A0A023YWW3 A0A024IWM7 A0A024IWM7 A0A024KWH8 A0A024KWH8 A0A025BRU3 A0A025BRU3 A0A026V6B5 A0A026V6B5
(758 more...)
3-hydroxy acid dehydrogenase. [EC: 1.1.1.381]
L-allo-threonine + NADP(+) = aminoacetone + CO(2) + NADPH.
  • The enzyme, purified from the bacterium Escherichia coli and the yeast Saccharomyces cerevisiae, shows activity with a range of 3- and 4-carbon 3-hydroxy acids.
  • The highest activity is seen with L-allo-threonine and D-threonine.
  • The enzyme from E.coli also shows high activity with L-serine, D-serine, (S)-3-hydroxy-2-methylpropanoate and (R)-3-hydroxy-2- methylpropanoate.
  • The enzyme has no activity with NAD(+) or L-threonine (cf. EC 1.1.1.103).
 488 A0A024KWH8 A0A024KWH8 A0A026V6B5 A0A026V6B5 A0A027U5A7 A0A027U5A7 A0A027ZJZ1 A0A027ZJZ1 A0A028DVL1 A0A028DVL1
(478 more...)
Sulfoacetaldehyde reductase. [EC: 1.1.1.313]
Isethionate + NADP(+) = 2-sulfoacetaldehyde + NADPH.
  • Catalyzes the reaction only in the opposite direction.
  • Involved in taurine degradation.
  • The bacterium Chromohalobacter salexigens strain DSM 3043 possesses two enzymes that catalyze this reaction, a constitutive enzyme (encoded by isfD2) and an inducible enzyme (encoded by isfD).
  • The latter is induced by taurine, and is responsible for most of the activity observed in taurine-grown cells.
 118 A0A060UXK3 A0A060UXK3 A0A071KTD3 A0A071KTD3 A0A0B7D2W1 A0A0B7D2W1 A0A0C7KZE7 A0A0C7KZE7 A0A0D0TPI9 A0A0D0TPI9
(108 more...)
3-hydroxybutyrate dehydrogenase. [EC: 1.1.1.30]
(R)-3-hydroxybutanoate + NAD(+) = acetoacetate + NADH.
  • Also oxidizes other 3-hydroxymonocarboxylic acids.
 8 C5WG74 C5WG74 F5U4R1 F5U4R1 K4QCJ5 K4QCJ5 M4ZDT9 M4ZDT9
Phosphoribosylformylglycinamidine cyclo-ligase. [EC: 6.3.3.1]
ATP + 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole.
    		 2 A5UEU4 A5UEU4