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 290048: Nucleotide sugar dehydrogenase

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
UDP-N-acetyl-D-mannosamine dehydrogenase. [EC: 1.1.1.336]
UDP-N-acetyl-alpha-D-mannosamine + 2 NAD(+) + H(2)O = UDP-N-acetyl-alpha- D-mannosaminuronate + 2 NADH.
  • Part of the pathway for acetamido sugar biosynthesis in bacteria and archaea.
  • The enzyme has no activity with NADP(+).
  • Formerly EC 1.1.1.n3.
1736 A0A014PUY1 A0A014PUY1 A0A017I4W0 A0A017I4W0 A0A022PFD9 A0A022PFD9 A0A023V3M3 A0A023V3M3 A0A023Z535 A0A023Z535
(1726 more...)
UDP-glucose 6-dehydrogenase. [EC: 1.1.1.22]
UDP-glucose + 2 NAD(+) + H(2)O = UDP-glucuronate + 2 NADH.
  • Also acts on UDP-2-deoxyglucose.
488 A0A023Z535 A0A023Z535 A0A024KLE8 A0A024KLE8 A0A025C635 A0A025C635 A0A029L8U2 A0A029L8U2 A0A029P4N9 A0A029P4N9
(478 more...)
UDP-N-acetylglucosamine 6-dehydrogenase. [EC: 1.1.1.136]
UDP-N-acetyl-alpha-D-glucosamine + 2 NAD(+) + H(2)O = UDP-2-acetamido-2- deoxy-alpha-D-glucuronate + 2 NADH.
  • This enzyme participates in the biosynthetic pathway for UDP-alpha-D- ManNAc(3)NAcA (UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-mannuronic acid), an important precursor of B-band lipopolysaccharide.
92 A0A0B0HL40 A0A0B0HL40 A0A0D6GHX8 A0A0D6GHX8 A0A0F7KW52 A0A0F7KW52 A0A0H2WYG5 A0A0H2WYG5 A0A0H2XF11 A0A0H2XF11
(82 more...)
N-acylmannosamine 1-dehydrogenase. [EC: 1.1.1.233]
N-acyl-D-mannosamine + NAD(+) = N-acyl-D-mannosaminolactone + NADH.
  • Acts on acetyl-D-mannosamine and glycolyl-D-mannosamine.
  • Highly specific.
16 A0A0D6GHX8 A0A0D6GHX8 A0A0H2WYG5 A0A0H2WYG5 A0A0H2XF11 A0A0H2XF11 A0A0H3K6C8 A0A0H3K6C8 A0A1E8XBF3 A0A1E8XBF3
(6 more...)
Homoserine dehydrogenase. [EC: 1.1.1.3]
L-homoserine + NAD(P)(+) = L-aspartate 4-semialdehyde + NAD(P)H.
  • The enzyme from Saccharomyces cerevisiae acts most rapidly with NAD(+); the Neurospora enzyme with NADP(+).
  • The enzyme from Escherichia coli is a multifunctional protein, which also catalyzes the reaction of EC 2.7.2.4.
6 A0A090IG89 A0A090IG89 W0PH63 W0PH63 W8T8I4 W8T8I4
UDP-N-acetylglucosamine 2-epimerase (non-hydrolyzing). [EC: 5.1.3.14]
UDP-N-acetyl-alpha-D-glucosamine = UDP-N-acetyl-alpha-D-mannosamine.
  • This bacterial enzyme catalyzes the reversible interconversion of UDP-GlcNAc and UDP-ManNAc.
  • The latter is used in a variety of bacterial polysaccharide biosyntheses.
  • Cf. EC 3.2.1.183.
2 A0A173KXG7 A0A173KXG7