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CATH Superfamily 3.20.20.70

Aldolase class I

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:

"
Aldolase class I
".

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 120764: Oxidoreductase, 2-nitropropane dioxygenase family

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
Nitronate monooxygenase. [EC: 1.13.12.16]
Ethylnitronate + O(2) = acetaldehyde + nitrite + other products.
  • Previously classified as EC 1.13.11.32, but it is now recognized that this was the result of the slow ionization of nitroalkanes to their nitronate (anionic) forms.
  • The enzymes from the fungus Neurospora crassa and the yeast Williopsis saturnus var. mrakii (formerly classified as Hansenula mrakii) contain non-covalently bound FMN as the cofactor.
  • Neither hydrogen peroxide nor superoxide were detected during enzyme turnover.
  • Active toward linear alkyl nitronates of lengths between 2 and 6 carbon atoms and, with lower activity, toward propyl-2-nitronate.
  • The enzyme from N.crassa can also utilize neutral nitroalkanes, but with lower activity.
  • Formerly EC 1.13.11.32.
 1688 A0A023P4L9 A0A023P4L9 A0A045H0K9 A0A045H0K9 A0A045I665 A0A045I665 A0A064C254 A0A064C254 A0A066PQF9 A0A066PQF9
(1678 more...)
Enoyl-[acyl-carrier-protein] reductase (NADH). [EC: 1.3.1.9]
An acyl-[acyl-carrier protein] + NAD(+) = a trans-2,3-dehydroacyl-[acyl- carrier protein] + NADH.
  • The enzyme catalyzes an essential step in fatty acid biosynthesis, the reduction of the 2,3-double bond in enoyl-acyl-[acyl-carrier- protein] derivatives of the elongating fatty acid moiety.
  • The enzyme from the bacterium Escherichia coli accepts substrates with carbon chain length from 4 to 18.
  • The enzyme from the bacterium Mycobacterium tuberculosis prefers substrates with carbon chain length from 12 to 24 carbons.
 936 A0A011SJC9 A0A011SJC9 A0A023DCC2 A0A023DCC2 A0A024DFS0 A0A024DFS0 A0A031WIF2 A0A031WIF2 A0A059F961 A0A059F961
(926 more...)
Transferred entry: 1.13.12.16. [EC: 1.13.11.32]
    		18 A0M3J4 A0M3J4 B2AIU5 B2AIU5 B3R8U8 B3R8U8 D3HQG4 D3HQG4 G0L1D4 G0L1D4
    (8 more...)
    3-oxoacyl-[acyl-carrier-protein] reductase. [EC: 1.1.1.100]
    (3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP(+) = 3-oxoacyl-[acyl- carrier-protein] + NADPH.
    • Exhibits a marked preference for [acyl-carrier-protein] derivatives over CoA derivatives as substrates.
    		 12 A0A0B7LC80 A0A0B7LC80 A0A0H2ZNM6 A0A0H2ZNM6 A0A1M3UIS2 A0A1M3UIS2 B2ILW4 B2ILW4 C1CCI4 C1CCI4
    (2 more...)
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