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CATH Superfamily 3.30.360.10

Dihydrodipicolinate Reductase; domain 2

The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:

"
Dihydrodipicolinate Reductase; domain 2
".

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 102: Similar to Oxidoreductase family

There are 1 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-2-amino-2-deoxyglucuronate dehydrogenase. [EC: 1.1.1.335]
UDP-N-acetyl-2-amino-2-deoxy-alpha-D-glucuronate + NAD(+) = UDP-2- acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate + NADH.
  • This enzyme participates in the biosynthetic pathway for UDP-alpha-D- ManNAc3NAcA (UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-mannuronic acid), an important precursor of B-band lipopolysaccharide.
  • The enzymes from Pseudomonas aeruginosa serotype O5 and Thermus thermophilus form a complex with the the enzyme catalyzing the next step the pathway (EC 2.6.1.98).
  • The enzyme also possesses an EC 1.1.99.2 activity, and utilizes the 2-oxoglutarate produced by EC 2.6.1.98 to regenerate the tightly bound NAD(+).
  • The enzymes from Bordetella pertussis and Chromobacterium violaceum do not bind NAD(+) as tightly and do not require 2-oxoglutarate to function.
 4 G3XD23 G3XD23 Q7B7A2 Q7B7A2
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