CATH Classification

Domain Context

CATH Clusters

Superfamily Dihydrodipicolinate Reductase; domain 2
Functional Family UDP-2-acetamido-2-deoxy-d-glucuronic acid 3-dehydrogenase, WbpB

Enzyme Information

1.1.1.335
UDP-N-acetyl-2-amino-2-deoxyglucuronate dehydrogenase.
based on mapping to UniProt G3XD23
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.

UniProtKB Entries (1)

G3XD23
WBPB_PSEAE
Pseudomonas aeruginosa PAO1
UDP-N-acetyl-2-amino-2-deoxy-D-glucuronate oxidase

PDB Structure

PDB 3OA2
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structural and Functional Studies of WlbA: A Dehydrogenase Involved in the Biosynthesis of 2,3-Diacetamido-2,3-dideoxy-d-mannuronic Acid .
Thoden, J.B., Holden, H.M.
Biochemistry